|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
2-391 |
4.04e-156 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 445.42 E-value: 4.04e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 2 EDSTNRAEIAQTPDLKS-----YEKFDDMNLHPDLLFGIFTYGYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTI 76
Cdd:PTZ00424 5 EQKNQSEQVASTGTIESnydeiVDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 77 GMLQRIDIGLKSPQAIILSPTRELALQTLKVVDGIGSRLKVQVAQCIGGTQVDDDIAAAQS-CHLIVATPGRLLSLLQKK 155
Cdd:PTZ00424 85 AALQLIDYDLNACQALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAgVHMVVGTPGRVYDMIDKR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 156 YVTTSNVKMVVLDEADEMLSRGFTEQIVSIMKFMNADIQIVLVSATLPPEILELTRQFMRDPVSILVKEAELTLDGIRQY 235
Cdd:PTZ00424 165 HLRVDDLKLFILDEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 236 VVELQ-DAWKTEVVEDIYKVLSVQQGVIFCNSIGRVKELAEKLKSAGHTLSCIHSELDQAERNKIMGEFRSGQTRILIAT 314
Cdd:PTZ00424 245 YVAVEkEEWKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITT 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 159117719 315 NIIARGIDVQNVSLVINYDIPREPETYLHRIGRSGRFGRKGVAINFVTDKDKQSMQAITDKFNVTTENLPEDLSSLF 391
Cdd:PTZ00424 325 DLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEVADYL 401
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
21-385 |
5.21e-149 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 428.03 E-value: 5.21e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 21 KFDDMNLHPDLLFGIFTYGYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRIDIGL-KSPQAIILSPTRE 99
Cdd:COG0513 3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRpRAPQALILAPTRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 100 LALQTLKVVDGIGSRLKVQVAQCIGGTQVDDDIAA-AQSCHLIVATPGRLLSLLQKKYVTTSNVKMVVLDEADEMLSRGF 178
Cdd:COG0513 83 LALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRAlKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 179 TEQIVSIMKFMNADIQIVLVSATLPPEILELTRQFMRDPVSILVKEAELTLDGIRQYVVELQDAWKTEVVEDIYKVLSVQ 258
Cdd:COG0513 163 IEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDEDPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 259 QGVIFCNSIGRVKELAEKLKSAGHTLSCIHSELDQAERNKIMGEFRSGQTRILIATNIIARGIDVQNVSLVINYDIPREP 338
Cdd:COG0513 243 RAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDP 322
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 159117719 339 ETYLHRIGRSGRFGRKGVAINFVTDKDKQSMQAITD--KFNVTTENLPE 385
Cdd:COG0513 323 EDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKliGQKIEEEELPG 371
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
22-385 |
4.16e-102 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 309.81 E-value: 4.16e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 22 FDDMNLHPDLLFGIFTYGYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRIDIGLKSPQAIILSPTRELA 101
Cdd:PRK11776 6 FSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTRELA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 102 LQTLKVVDGIGSRL---KVqVAQCIG---GTQVDDDIAAAqscHLIVATPGRLLSLLQKKYVTTSNVKMVVLDEADEMLS 175
Cdd:PRK11776 86 DQVAKEIRRLARFIpniKV-LTLCGGvpmGPQIDSLEHGA---HIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 176 RGFTEQIVSIMKFMNADIQIVLVSATLPPEILELTRQFMRDPVSILVkEAELTLDGIRQYVVELQDAWKTEVVEDI---Y 252
Cdd:PRK11776 162 MGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKV-ESTHDLPAIEQRFYEVSPDERLPALQRLllhH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 253 KVLSVqqgVIFCNSIGRVKELAEKLKSAGHTLSCIHSELDQAERNKIMGEFRSGQTRILIATNIIARGIDVQNVSLVINY 332
Cdd:PRK11776 241 QPESC---VVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINY 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 159117719 333 DIPREPETYLHRIGRSGRFGRKGVAINFVTDKDKQSMQAITDKFN--VTTENLPE 385
Cdd:PRK11776 318 ELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGrkLNWEPLPS 372
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
22-221 |
2.50e-94 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation factor 4A-I (DDX2A) and eukaryotic initiation factor 4A-II (DDX2B) are involved in cap recognition and are required for mRNA binding to ribosome. They are DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350804 [Multi-domain] Cd Length: 201 Bit Score: 280.87 E-value: 2.50e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 22 FDDMNLHPDLLFGIFTYGYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRIDIGLKSPQAIILSPTRELA 101
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 102 LQTLKVVDGIGSRLKVQVAQCIGGTQVDDDIAAAQS-CHLIVATPGRLLSLLQKKYVTTSNVKMVVLDEADEMLSRGFTE 180
Cdd:cd18046 81 QQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAgPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 159117719 181 QIVSIMKFMNADIQIVLVSATLPPEILELTRQFMRDPVSIL 221
Cdd:cd18046 161 QIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRIL 201
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
24-221 |
5.95e-93 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation factor-4A (eIF4A) family consists of 3 proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA. EIF4A proteins are members of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350697 [Multi-domain] Cd Length: 199 Bit Score: 277.28 E-value: 5.95e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 24 DMNLHPDLLFGIFTYGYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRIDIGLKSPQAIILSPTRELALQ 103
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 104 TLKVVDGIGSRLKVQVAQCIGGTQVDDDIAAAQS-CHLIVATPGRLLSLLQKKYVTTSNVKMVVLDEADEMLSRGFTEQI 182
Cdd:cd17939 81 IQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYgPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQI 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 159117719 183 VSIMKFMNADIQIVLVSATLPPEILELTRQFMRDPVSIL 221
Cdd:cd17939 161 YDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRIL 199
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
22-384 |
7.03e-82 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 262.48 E-value: 7.03e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 22 FDDMNLHPDLLFGIFTYGYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRIDIGLKSPQAIILSPTRELA 101
Cdd:PRK11634 8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTRELA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 102 LQTLKVVDGIGSRLK-VQVAQCIGGTQVDDDIAA-AQSCHLIVATPGRLLSLLQKKYVTTSNVKMVVLDEADEMLSRGFT 179
Cdd:PRK11634 88 VQVAEAMTDFSKHMRgVNVVALYGGQRYDVQLRAlRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 180 EQIVSIMKFMNADIQIVLVSATLPPEILELTRQFMRDPVSILVKEAELTLDGIRQYVVELQDAWKTEVVEDIYKVLSVQQ 259
Cdd:PRK11634 168 EDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVRFLEAEDFDA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 260 GVIFCNSIGRVKELAEKLKSAGHTLSCIHSELDQAERNKIMGEFRSGQTRILIATNIIARGIDVQNVSLVINYDIPREPE 339
Cdd:PRK11634 248 AIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSE 327
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 159117719 340 TYLHRIGRSGRFGRKGVAINFVTDKDKQSMQAI--TDKFNVTTENLP 384
Cdd:PRK11634 328 SYVHRIGRTGRAGRAGRALLFVENRERRLLRNIerTMKLTIPEVELP 374
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
22-221 |
3.11e-79 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor 4A-III (EIF4AIII, also known as DDX48) is part of the exon junction complex (EJC) that plays a major role in posttranscriptional regulation of mRNA. EJC consists of four proteins (eIF4AIII, Barentsz [Btz], Mago, and Y14), mRNA, and ATP. DDX48 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350803 [Multi-domain] Cd Length: 201 Bit Score: 242.37 E-value: 3.11e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 22 FDDMNLHPDLLFGIFTYGYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRIDIGLKSPQAIILSPTRELA 101
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 102 LQTLKVVDGIGSRLKVQVAQCIGGTQVDDDIAAAQS-CHLIVATPGRLLSLLQKKYVTTSNVKMVVLDEADEMLSRGFTE 180
Cdd:cd18045 81 VQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYgQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 159117719 181 QIVSIMKFMNADIQIVLVSATLPPEILELTRQFMRDPVSIL 221
Cdd:cd18045 161 QIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRIL 201
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
31-220 |
4.03e-75 |
|
DEAD-box helicase domain of 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350669 [Multi-domain] Cd Length: 196 Bit Score: 231.56 E-value: 4.03e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 31 LLFGIFTYGYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRID----IGLKSPQAIILSPTRELALQTLK 106
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLpepkKKGRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 107 VVDGIGSRLKVQVAQCIGGTQVDDDIAA-AQSCHLIVATPGRLLSLLQKKYVTTSNVKMVVLDEADEMLSRGFTEQIVSI 185
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEAlKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 159117719 186 MKFMNADIQIVLVSATLPPEILELTRQFMRDPVSI 220
Cdd:cd00268 161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
22-361 |
4.53e-73 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 234.45 E-value: 4.53e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 22 FDDMNLHPDLLFGIFTYGYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQR-IDIGLKSPQA---IILSPT 97
Cdd:PRK11192 3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHlLDFPRRKSGPpriLILTPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 98 RELALQTLKVVDGIGSRLKVQVAQCIGGTQVDDDIAAAQSCH-LIVATPGRLLSLLQKKYVTTSNVKMVVLDEADEMLSR 176
Cdd:PRK11192 83 RELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQdIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLDM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 177 GFTEQIVSIMKFMNADIQIVLVSATLPPE-ILELTRQFMRDPVSILVKEAELTLDGIRQYVVELQDA-WKTEVVEDIYKV 254
Cdd:PRK11192 163 GFAQDIETIAAETRWRKQTLLFSATLEGDaVQDFAERLLNDPVEVEAEPSRRERKKIHQWYYRADDLeHKTALLCHLLKQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 255 LSVQQGVIFCNSIGRVKELAEKLKSAGHTLSCIHSELDQAERNKIMGEFRSGQTRILIATNIIARGIDVQNVSLVINYDI 334
Cdd:PRK11192 243 PEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDM 322
|
330 340
....*....|....*....|....*..
gi 159117719 335 PREPETYLHRIGRSGRFGRKGVAINFV 361
Cdd:PRK11192 323 PRSADTYLHRIGRTGRAGRKGTAISLV 349
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
21-387 |
1.09e-72 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 234.42 E-value: 1.09e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 21 KFDDMNLHPDLLFGIFTYGYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRI-------DIGLKSPQAII 93
Cdd:PRK01297 88 RFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLlqtpppkERYMGEPRALI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 94 LSPTRELALQTLKVVDGIGSRLKVQVAQCIGGTQVDDDIAA--AQSCHLIVATPGRLLSLLQKKYVTTSNVKMVVLDEAD 171
Cdd:PRK01297 168 IAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQleARFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEAD 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 172 EMLSRGFTEQIVSIMKF--MNADIQIVLVSATLPPEILELTRQFMRDPVSILVKEAELTLDGIRQYVVELQDAWKTEVVE 249
Cdd:PRK01297 248 RMLDMGFIPQVRQIIRQtpRKEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDKYKLLY 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 250 DIYKVLSVQQGVIFCNSIGRVKELAEKLKSAGHTLSCIHSELDQAERNKIMGEFRSGQTRILIATNIIARGIDVQNVSLV 329
Cdd:PRK01297 328 NLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHV 407
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 330 INYDIPREPETYLHRIGRSGRFGRKGVAINFVTDKDKQSMQAITDKF--NVTTENLPEDL 387
Cdd:PRK01297 408 INFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLgrKISCEMPPAEL 467
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
22-361 |
6.25e-70 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 227.00 E-value: 6.25e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 22 FDDMNLHPDLLFGIFTYGYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRIDI------GLKSPQAIILS 95
Cdd:PRK10590 3 FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITrqphakGRRPVRALILT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 96 PTRELALQTLKVVDGIGSRLKVQVAQCIGGTQVDDDIAAAQS-CHLIVATPGRLLSLLQKKYVTTSNVKMVVLDEADEML 174
Cdd:PRK10590 83 PTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGgVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRML 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 175 SRGFTEQIVSIMKFMNADIQIVLVSATLPPEILELTRQFMRDPVSILVKEAELTLDGIRQYVVELQDAWKTEVVEDIYKV 254
Cdd:PRK10590 163 DMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQMIGK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 255 LSVQQGVIFCNSIGRVKELAEKLKSAGHTLSCIHSELDQAERNKIMGEFRSGQTRILIATNIIARGIDVQNVSLVINYDI 334
Cdd:PRK10590 243 GNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYEL 322
|
330 340
....*....|....*....|....*..
gi 159117719 335 PREPETYLHRIGRSGRFGRKGVAINFV 361
Cdd:PRK10590 323 PNVPEDYVHRIGRTGRAAATGEALSLV 349
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
22-220 |
2.44e-65 |
|
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or p54) participates in mRNA regulation mediated by miRNA-mediated silencing. It also plays a role in global and transcript-specific messenger RNA (mRNA) storage, translational repression, and decay. It is a member of the DEAD-box helicase family, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350698 [Multi-domain] Cd Length: 201 Bit Score: 206.77 E-value: 2.44e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 22 FDDMNLHPDLLFGIFTYGYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRIDIGLKSPQAIILSPTRELA 101
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 102 LQTLKVVDGIGSRLKVQVAQCIGGTQVDDDIA-AAQSCHLIVATPGRLLSLLQKKYVTTSNVKMVVLDEADEMLSRGFTE 180
Cdd:cd17940 81 LQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMrLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 159117719 181 QIVSIMKFMNADIQIVLVSATLPPEILELTRQFMRDPVSI 220
Cdd:cd17940 161 IIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
27-220 |
2.73e-64 |
|
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called DEAD box RNA helicase DEAD5) and DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH)) are members of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350721 [Multi-domain] Cd Length: 196 Bit Score: 203.58 E-value: 2.73e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 27 LHPDLLFGIFTYGYKIPSAIQSQAIVPIISG--KDTIAQAQSGTGKTAAFTIGMLQRIDIGLKSPQAIILSPTRELALQT 104
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 105 LKVVDGIGSRLKVQVAQCIGGTqvDDDIAAAQSCHLIVATPGRLLSLLQKKYVTTSNVKMVVLDEADEML-SRGFTEQIV 183
Cdd:cd17963 81 GEVVEKMGKFTGVKVALAVPGN--DVPRGKKITAQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLdTQGHGDQSI 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 159117719 184 SIMKFMNADIQIVLVSATLPPEILELTRQFMRDPVSI 220
Cdd:cd17963 159 RIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
22-372 |
4.24e-63 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 212.12 E-value: 4.24e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 22 FDDMNLHPDLLFGIFTYGYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRI-------DIGLKSPQAIIL 94
Cdd:PRK04537 11 FSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlsrpalaDRKPEDPRALIL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 95 SPTRELALQTLKVVDGIGSRLKVQVAQCIGGTQVDDDIAA-AQSCHLIVATPGRLLSLL-QKKYVTTSNVKMVVLDEADE 172
Cdd:PRK04537 91 APTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELlQQGVDVIIATPGRLIDYVkQHKVVSLHACEICVLDEADR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 173 MLSRGFTEQIVSIMKFM--NADIQIVLVSATLPPEILELTRQFMRDPVSILVKEAELTLDGIRQYVVELQDAWKTEVved 250
Cdd:PRK04537 171 MFDLGFIKDIRFLLRRMpeRGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADEEKQTL--- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 251 IYKVLSVQQG---VIFCNSIGRVKELAEKLKSAGHTLSCIHSELDQAERNKIMGEFRSGQTRILIATNIIARGIDVQNVS 327
Cdd:PRK04537 248 LLGLLSRSEGartMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVK 327
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 159117719 328 LVINYDIPREPETYLHRIGRSGRFGRKGVAINFVTDKDKQSMQAI 372
Cdd:PRK04537 328 YVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDI 372
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
29-366 |
1.07e-62 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 210.40 E-value: 1.07e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 29 PD-LLFGIFTYGYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRIDIG--LK---SPQAIILSPTRELAL 102
Cdd:PTZ00110 138 PDyILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQplLRygdGPIVLVLAPTRELAE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 103 QTLK--VVDGIGSRLKVQVAqcIGGTQVDDDIAA-AQSCHLIVATPGRLLSLLQKKYVTTSNVKMVVLDEADEMLSRGFT 179
Cdd:PTZ00110 218 QIREqcNKFGASSKIRNTVA--YGGVPKRGQIYAlRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFE 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 180 EQIVSIMKFMNADIQIVLVSATLPPEILELTRQFMRD-PVSILVKEAELTL-DGIRQYVVELQDAWKTEVVEDIYKVLSV 257
Cdd:PTZ00110 296 PQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDLTAcHNIKQEVFVVEEHEKRGKLKMLLQRIMR 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 258 QQG--VIFCNSIGRVKELAEKLKSAGHTLSCIHSELDQAERNKIMGEFRSGQTRILIATNIIARGIDVQNVSLVINYDIP 335
Cdd:PTZ00110 376 DGDkiLIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFP 455
|
330 340 350
....*....|....*....|....*....|..
gi 159117719 336 REPETYLHRIGRSGRFGRKGVAINFVT-DKDK 366
Cdd:PTZ00110 456 NQIEDYVHRIGRTGRAGAKGASYTFLTpDKYR 487
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
22-366 |
2.75e-57 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 195.39 E-value: 2.75e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 22 FDDMNLHPDLLFGIFTYGYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQR---IDIG----LKSPQAIIL 94
Cdd:PLN00206 123 FSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRcctIRSGhpseQRNPLAMVL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 95 SPTRELALQTLKVVDGIGSRLKVQVAQCIGGTQVDDDI-AAAQSCHLIVATPGRLLSLLQKKYVTTSNVKMVVLDEADEM 173
Cdd:PLN00206 203 TPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLyRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCM 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 174 LSRGFTEQIVSIMKFMnADIQIVLVSATLPPEILELTRQFMRDPVSILVKEAELTLDGIRQYVVELQDAWKTEVVEDIYK 253
Cdd:PLN00206 283 LERGFRDQVMQIFQAL-SQPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQKLFDILK 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 254 vlSVQQ----GVIFCNSIGRVKELAEKL-KSAGHTLSCIHSELDQAERNKIMGEFRSGQTRILIATNIIARGIDVQNVSL 328
Cdd:PLN00206 362 --SKQHfkppAVVFVSSRLGADLLANAItVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQ 439
|
330 340 350
....*....|....*....|....*....|....*...
gi 159117719 329 VINYDIPREPETYLHRIGRSGRFGRKGVAINFVTDKDK 366
Cdd:PLN00206 440 VIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDR 477
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
232-361 |
9.78e-57 |
|
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: 181.94 E-value: 9.78e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 232 IRQYVVELQDAWKTEV-VEDIYKVLSVQQGVIFCNSIGRVKELAEKLKSAGHTLSCIHSELDQAERNKIMGEFRSGQTRI 310
Cdd:cd18787 1 IKQLYVVVEEEEKKLLlLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 159117719 311 LIATNIIARGIDVQNVSLVINYDIPREPETYLHRIGRSGRFGRKGVAINFV 361
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
22-220 |
1.42e-55 |
|
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350717 [Multi-domain] Cd Length: 205 Bit Score: 181.73 E-value: 1.42e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 22 FDDMNLHPDLLFGIFTYGYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRidigLKSPQ------AIILS 95
Cdd:cd17959 3 FQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEK----LKAHSptvgarALILS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 96 PTRELALQTLKVVDGIGSRLKVQVAQCIGGTQVDDDIAAAQSC-HLIVATPGRLLSLLQKKYVTTSNVKMVVLDEADEML 174
Cdd:cd17959 79 PTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNpDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 159117719 175 SRGFTEQIVSIMKFMNADIQIVLVSATLPPEILELTRQFMRDPVSI 220
Cdd:cd17959 159 EMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
44-209 |
1.43e-55 |
|
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: 180.13 E-value: 1.43e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 44 SAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRIDIGLKSPQAIILSPTRELALQTLKVVDGIGSRLKVQVAQCI 123
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 124 GGTQVDDDIAAAQSCHLIVATPGRLLSLLQKKyVTTSNVKMVVLDEADEMLSRGFTEQIVSIMKFMNADIQIVLVSATLP 203
Cdd:pfam00270 81 GGDSRKEQLEKLKGPDILVGTPGRLLDLLQER-KLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATLP 159
|
....*.
gi 159117719 204 PEILEL 209
Cdd:pfam00270 160 RNLEDL 165
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
39-220 |
9.25e-52 |
|
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, Component Of Gems 3, Gemin-3, and SMN-Interacting Protein) interacts directly with SMN (survival of motor neurons), the spinal muscular atrophy gene product, and may play a catalytic role in the function of the SMN complex on ribonucleoproteins. Diseases associated with DDX20 include spinal muscular atrophy and muscular atrophy. DDX20 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350701 [Multi-domain] Cd Length: 192 Bit Score: 171.29 E-value: 9.25e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 39 GYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRIDIGLKSPQAIILSPTRELALQTLKVVDGIGS---RL 115
Cdd:cd17943 9 GFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKKIGKkleGL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 116 KVQVAqcIGGTQVDDDIAAAQSCHLIVATPGRLLSLLQKKYVTTSNVKMVVLDEADEMLSRGFTEQIVSIMKFMNADIQI 195
Cdd:cd17943 89 KCEVF--IGGTPVKEDKKKLKGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSSLPKNKQV 166
|
170 180
....*....|....*....|....*
gi 159117719 196 VLVSATLPPEILELTRQFMRDPVSI 220
Cdd:cd17943 167 IAFSATYPKNLDNLLARYMRKPVLV 191
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
21-360 |
4.51e-51 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 176.32 E-value: 4.51e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 21 KFDDMNLHPDLLFGIFTYGYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRI-------DIGLKSPQAII 93
Cdd:PRK04837 9 KFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLlshpapeDRKVNQPRALI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 94 LSPTRELALQTLKVVDGIGSRLKVQVAQCIGGTQVDDDIAAAQS-CHLIVATPGRLLSLLQKKYVTTSNVKMVVLDEADE 172
Cdd:PRK04837 89 MAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESgVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 173 MLSRGFTEQIVSIMKFMNADIQ--IVLVSATLPPEILELTRQFMRDPVSILVKEAELTLDGIRQyvvEL-----QDAWK- 244
Cdd:PRK04837 169 MFDLGFIKDIRWLFRRMPPANQrlNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKE---ELfypsnEEKMRl 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 245 --TEVVEDIykvlsVQQGVIFCNSIGRVKELAEKLKSAGHTLSCIHSELDQAERNKIMGEFRSGQTRILIATNIIARGID 322
Cdd:PRK04837 246 lqTLIEEEW-----PDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLH 320
|
330 340 350
....*....|....*....|....*....|....*...
gi 159117719 323 VQNVSLVINYDIPREPETYLHRIGRSGRFGRKGVAINF 360
Cdd:PRK04837 321 IPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
22-216 |
1.62e-49 |
|
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes Drosophila melanogaster Vasa, which is essential for development. DEAD box protein 3 (DDX3) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DDX3 and DDX4 are members of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350725 [Multi-domain] Cd Length: 221 Bit Score: 166.51 E-value: 1.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 22 FDDMNLHPDLLFGIFTYGYKIPSAIQSQAIvPII-SGKDTIAQAQSGTGKTAAFTIGMLQRIdigLKS------------ 88
Cdd:cd17967 2 FEEAGLRELLLENIKRAGYTKPTPVQKYAI-PIIlAGRDLMACAQTGSGKTAAFLLPIISKL---LEDgppsvgrgrrka 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 89 -PQAIILSPTRELALQ----TLKVVdgIGSRLKVQVaqCIGGTQV-DDDIAAAQSCHLIVATPGRLLSLLQKKYVTTSNV 162
Cdd:cd17967 78 yPSALILAPTRELAIQiyeeARKFS--YRSGVRSVV--VYGGADVvHQQLQLLRGCDILVATPGRLVDFIERGRISLSSI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 159117719 163 KMVVLDEADEMLSRGFTEQIVSIMKFMN----ADIQIVLVSATLPPEILELTRQFMRD 216
Cdd:cd17967 154 KFLVLDEADRMLDMGFEPQIRKIVEHPDmppkGERQTLMFSATFPREIQRLAADFLKN 211
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
22-220 |
1.13e-46 |
|
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can shuttle between the nucleus and the cytoplasm, and has an RNA-independent ATPase activity. DX47 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350712 [Multi-domain] Cd Length: 203 Bit Score: 158.63 E-value: 1.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 22 FDDMNLHPDLLFGIFTYGYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRIdigLKSPQ---AIILSPTR 98
Cdd:cd17954 2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQAL---LENPQrffALVLAPTR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 99 ELALQTLKVVDGIGSRLKVQVAQCIGGTQ-VDDDIAAAQSCHLIVATPGRLLSLLQK-KYVTTSNVKMVVLDEADEMLSR 176
Cdd:cd17954 79 ELAQQISEQFEALGSSIGLKSAVLVGGMDmMAQAIALAKKPHVIVATPGRLVDHLENtKGFSLKSLKFLVMDEADRLLNM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 159117719 177 GFTEQIVSIMKFMNADIQIVLVSATLPPEILELTRQFMRDPVSI 220
Cdd:cd17954 159 DFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
35-235 |
1.35e-46 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 158.42 E-value: 1.35e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 35 IFTYGYKIPSAIQSQAIVPIISG-KDTIAQAQSGTGKTAAFTIGMLQRIDIGlKSPQAIILSPTRELALQTLKVVDGIGS 113
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRG-KGGRVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 114 RLKVQVAQCIGGTQVDDDIAAAQS--CHLIVATPGRLLSLLQKKYVTTSNVKMVVLDEADEMLSRGFTEQIVSIMKFMNA 191
Cdd:smart00487 80 SLGLKVVGLYGGDSKREQLRKLESgkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 159117719 192 DIQIVLVSATLPPEILELTRQFMRDPVSILVKeaELTLDGIRQY 235
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFIDVG--FTPLEPIEQF 201
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
31-222 |
8.60e-44 |
|
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350715 [Multi-domain] Cd Length: 198 Bit Score: 150.82 E-value: 8.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 31 LLFGIFTYGYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRI--DIGLKSPQAIILSPTRELALQTLKVV 108
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLgkPRKKKGLRALILAPTRELASQIYREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 109 D--GIGSRLKVQVAQCIGGTQVDDDIAAAQSCHLIVATPGRLLSLLQKKYVTTSNVKMVVLDEADEMLSRGFTEQIVSIM 186
Cdd:cd17957 81 LklSKGTGLRIVLLSKSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEIL 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 159117719 187 KFM-NADIQIVLVSATLPPEILELTRQFMRDPVSILV 222
Cdd:cd17957 161 AACtNPNLQRSLFSATIPSEVEELARSVMKDPIRIIV 197
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
22-215 |
4.57e-43 |
|
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DEAD-box helicases are 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350810 [Multi-domain] Cd Length: 264 Bit Score: 150.89 E-value: 4.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 22 FDDMNLHPDLLFGIFTYGYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRI---------DIGLKSPQAI 92
Cdd:cd18052 45 FEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMmkegltassFSEVQEPQAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 93 ILSPTRELALQ----TLKVVDGIGSRLKVqvaqCIGGTQVDDDIAA-AQSCHLIVATPGRLLSLLQKKYVTTSNVKMVVL 167
Cdd:cd18052 125 IVAPTRELANQifleARKFSYGTCIRPVV----VYGGVSVGHQIRQiEKGCHILVATPGRLLDFIGRGKISLSKLKYLIL 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 159117719 168 DEADEMLSRGFTEQIVSIMKFMN----ADIQIVLVSATLPPEILELTRQFMR 215
Cdd:cd18052 201 DEADRMLDMGFGPEIRKLVSEPGmpskEDRQTLMFSATFPEEIQRLAAEFLK 252
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
31-220 |
5.25e-42 |
|
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ribosomal subunits protein 1 homolog, and probable ATP-dependent RNA helicase DDX27) is involved in the processing of 5.8S and 28S ribosomal RNAs. More specifically, the encoded protein localizes to the nucleolus, where it interacts with the PeBoW complex to ensure proper 3' end formation of 47S rRNA. DDX27 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350705 [Multi-domain] Cd Length: 196 Bit Score: 145.86 E-value: 5.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 31 LLFGIFTYGYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRI---DIGLKSPQAIILSPTRELALQTLKV 107
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLlyrPKKKAATRVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 108 VDGIGSRLKVQVAQCIGGTQVDDDIAAAQSC-HLIVATPGRLLSLLQK-KYVTTSNVKMVVLDEADEMLSRGFTEQIVSI 185
Cdd:cd17947 81 LQQLAQFTDITFALAVGGLSLKAQEAALRARpDIVIATPGRLIDHLRNsPSFDLDSIEILVLDEADRMLEEGFADELKEI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 159117719 186 MKFMNADIQIVLVSATLPPEILELTRQFMRDPVSI 220
Cdd:cd17947 161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
22-222 |
2.14e-41 |
|
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and is required for the export of mRNA out of the nucleus. DDX39B is an essential splicing factor required for association of U2 small nuclear ribonucleoprotein with pre-mRNA, and it also plays an important role in mRNA export from the nucleus to the cytoplasm. Diseases associated with DDX39A (also called UAP56-Related Helicase, 49 kDa) include gastrointestinal stromal tumor and inflammatory bowel disease 6, while diseases associated with DDX39B (also called 56 kDa U2AF65-Associated Protein) include Plasmodium vivax malaria. DDX39 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350708 [Multi-domain] Cd Length: 208 Bit Score: 144.80 E-value: 2.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 22 FDDMNLHPDLLFGIFTYGYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRIDIGLKSPQAIILSPTRELA 101
Cdd:cd17950 4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRELA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 102 LQTLKVVDGIGSRLK-VQVAQCIGGTQVDDDIAAAQS--CHLIVATPGRLLSLLQKKYVTTSNVKMVVLDEADEML-SRG 177
Cdd:cd17950 84 FQISNEYERFSKYMPnVKTAVFFGGVPIKKDIEVLKNkcPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLeQLD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 159117719 178 FTEQIVSIMKFMNADIQIVLVSATLPPEILELTRQFMRDPVSILV 222
Cdd:cd17950 164 MRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
39-220 |
5.68e-41 |
|
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) is a component of the 17S U2 snRNP complex. It plays an important role in pre-mRNA splicing and has a role in antiviral innate immunity. DDX46 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350711 [Multi-domain] Cd Length: 222 Bit Score: 144.06 E-value: 5.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 39 GYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRIDIGLKS-----PQAIILSPTRELALQTLKVVDGIGS 113
Cdd:cd17953 31 GYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVkpgegPIGLIMAPTRELALQIYVECKKFSK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 114 RLKVQVAQCIGGTQVDDDIAA-AQSCHLIVATPGRLLSLL---QKKYVTTSNVKMVVLDEADEMLSRGFTEQIVSIMKFM 189
Cdd:cd17953 111 ALGLRVVCVYGGSGISEQIAElKRGAEIVVCTPGRMIDILtanNGRVTNLRRVTYVVLDEADRMFDMGFEPQIMKIVNNI 190
|
170 180 190
....*....|....*....|....*....|.
gi 159117719 190 NADIQIVLVSATLPPEILELTRQFMRDPVSI 220
Cdd:cd17953 191 RPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
22-218 |
7.77e-41 |
|
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350713 [Multi-domain] Cd Length: 204 Bit Score: 143.13 E-value: 7.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 22 FDDMNLHPDLLFGIFTYGYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRIDIGLKSPQAIILSPTRELA 101
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 102 LQTLKVVDGIGSRLKVQVAQCIGGT-QVDDDIAAAQSCHLIVATPGRLLSLLQKKYVTT---SNVKMVVLDEADEMLSRG 177
Cdd:cd17955 81 YQIAEQFRALGAPLGLRCCVIVGGMdMVKQALELSKRPHIVVATPGRLADHLRSSDDTTkvlSRVKFLVLDEADRLLTGS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 159117719 178 FTEQIVSIMKFMNADIQIVLVSATLPPEILELTRQFMRDPV 218
Cdd:cd17955 161 FEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPF 201
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
27-215 |
1.29e-40 |
|
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350722 [Multi-domain] Cd Length: 211 Bit Score: 142.72 E-value: 1.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 27 LHPDLLFGIFTYGYKIPSAIQSQAIVPIIS-GKDTIAQAQSGTGKTAAFTIGMLQRIDIGLKSPQ-----AIILSPTREL 100
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRrsgvsALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 101 ALQTLKVVDGIGSRL-KVQVAQCIGGTQVDDDIAAAQS--CHLIVATPGRLLSLLQKKYV--TTSNVKMVVLDEADEMLS 175
Cdd:cd17964 81 ALQIAAEAKKLLQGLrKLRVQSAVGGTSRRAELNRLRRgrPDILVATPGRLIDHLENPGVakAFTDLDYLVLDEADRLLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 159117719 176 RGFTEQIVSIMKFMNA----DIQIVLVSATLPPEILELTRQFMR 215
Cdd:cd17964 161 MGFRPDLEQILRHLPEknadPRQTLLFSATVPDEVQQIARLTLK 204
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
31-220 |
2.13e-40 |
|
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor 3B-Associated 125 kDa Protein, RHELP, or RNAHP) is an NTPase with a preference for ATP, the hydrolysis of which is enhanced by various RNA substrates. It acts as a non-processive RNA helicase with protein displacement and RNA annealing activities. DDX42 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350710 [Multi-domain] Cd Length: 197 Bit Score: 141.78 E-value: 2.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 31 LLFGIFTYGYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGML-----QRIDIGLKSPQAIILSPTRELALQTL 105
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLvhimdQRELEKGEGPIAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 106 KVVDGIGSRLKVQVAQCIGGTQVDDDIAAAQS-CHLIVATPGRLLSLLQKKYVTTSNVKMVVLDEADEMLSRGFTEQIVS 184
Cdd:cd17952 81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEgAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 159117719 185 IMKFMNADIQIVLVSATLPPEILELTRQFMRDPVSI 220
Cdd:cd17952 161 IVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
31-220 |
2.40e-40 |
|
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and PRP28 homolog) is involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation. Diseases associated with DDX23 include distal hereditary motor neuropathy, type II. DDX23 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350703 [Multi-domain] Cd Length: 220 Bit Score: 142.46 E-value: 2.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 31 LLFGIFTYGYKIPSAIQSQAIvPI-ISGKDTIAQAQSGTGKTAAFTIGMLQRID--------IGLKSPQAIILSPTRELA 101
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAI-PIgLQNRDIIGIAETGSGKTAAFLIPLLVYISrlppldeeTKDDGPYALILAPTRELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 102 LQTLKVVDGIGSRLKVQVAQCIGGTQVDDD-IAAAQSCHLIVATPGRLLSLLQKKYVTTSNVKMVVLDEADEMLSRGFTE 180
Cdd:cd17945 80 QQIEEETQKFAKPLGIRVVSIVGGHSIEEQaFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 181 QIVSIMKFMNADI--------------------QIVLVSATLPPEILELTRQFMRDPVSI 220
Cdd:cd17945 160 QVTKILDAMPVSNkkpdteeaeklaasgkhryrQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
27-220 |
2.59e-40 |
|
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of infectious West Nile virus particles. New research suggests that DDX56 relocalizes to the site of virus assembly during WNV infection and that its interaction with WNV capsid in the cytoplasm may occur transiently during virion morphogenesis. DDX56 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350719 [Multi-domain] Cd Length: 206 Bit Score: 141.95 E-value: 2.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 27 LHPDLLFGIFTYGYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRI------DIGLKSPQAIILSPTREL 100
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlkakaeSGEEQGTRALILVPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 101 ALQTLKVVDG--IGSRLKVQVAQcIGGTQVDDDIAAAQSCH--LIVATPGRLLSLLQKKY-VTTSNVKMVVLDEADEMLS 175
Cdd:cd17961 81 AQQVSKVLEQltAYCRKDVRVVN-LSASSSDSVQRALLAEKpdIVVSTPARLLSHLESGSlLLLSTLKYLVIDEADLVLS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 159117719 176 RGFTEQIVSIMKFMNADIQIVLVSATLPPEILELTRQFMRDPVSI 220
Cdd:cd17961 160 YGYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPAIL 204
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
39-222 |
6.51e-40 |
|
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin gene, NUP98, by inversion 11 (p15q22) chromosome translocation is found in the patients with de novo or therapy-related myeloid malignancies. Diseases associated with DDX10 (also known as DDX10-NUP98 Fusion Protein Type 2) include myelodysplastic syndrome and leukemia, acute myeloid. DDX10 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350699 [Multi-domain] Cd Length: 198 Bit Score: 140.50 E-value: 6.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 39 GYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRI-------DIGLKspqAIILSPTRELALQTLKVVDGI 111
Cdd:cd17941 9 GFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLyrerwtpEDGLG---ALIISPTRELAMQIFEVLRKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 112 GSRLKVQVAQCIGGTQVDDDIAAAQSCHLIVATPGRLLSLLQKK-YVTTSNVKMVVLDEADEMLSRGFTEQIVSIMKFMN 190
Cdd:cd17941 86 GKYHSFSAGLIIGGKDVKEEKERINRMNILVCTPGRLLQHMDETpGFDTSNLQMLVLDEADRILDMGFKETLDAIVENLP 165
|
170 180 190
....*....|....*....|....*....|..
gi 159117719 191 ADIQIVLVSATLPPEILELTRQFMRDPVSILV 222
Cdd:cd17941 166 KSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
6-228 |
9.79e-40 |
|
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH) is a testis-specific protein essential for completion of spermatogenesis. DDX25 is also a novel negative regulator of IFN pathway and facilitates RNA virus infection. Diseases associated with DDX25 include hydrolethalus syndrome, an autosomal recessive lethal malformation syndrome characterized by multiple developmental defects of fetus.. DDX25 (also called gonadotropin-regulated testicular RNA helicase) is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350806 [Multi-domain] Cd Length: 229 Bit Score: 141.31 E-value: 9.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 6 NRAEIAQ---TPDLKSYEKFDDMNLHPDLLFGIFTYGYKIPSAIQSQAIVPIISG--KDTIAQAQSGTGKTAAFTIGMLQ 80
Cdd:cd18048 1 HRVEVLQrdpTSPLFSVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 81 RIDIGLKSPQAIILSPTRELALQTLKVVDGIGSR-LKVQVAQCIGGTQV--DDDIAAaqscHLIVATPGRLLSLLQK-KY 156
Cdd:cd18048 81 RVDALKLYPQCLCLSPTFELALQTGKVVEEMGKFcVGIQVIYAIRGNRPgkGTDIEA----QIVIGTPGTVLDWCFKlRL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 159117719 157 VTTSNVKMVVLDEADEMLS-RGFTEQIVSIMKFMNADIQIVLVSATLPPEILELTRQFMRDPVSILVKEAELT 228
Cdd:cd18048 157 IDVTNISVFVLDEADVMINvQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
31-220 |
1.11e-39 |
|
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer development by promoting DNA replication. DDX59 knockdown mice showed reduced cell proliferation, anchorage-independent cell growth, and reduction of tumor formation. Recent work shows that EGFR and Ras regulate DDX59 during lung cancer development. Diseases associated with DDX59 (also called zinc finger HIT domain-containing protein 5) include orofaciodigital syndrome V and orofaciodigital syndrome. DDX59 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350720 [Multi-domain] Cd Length: 193 Bit Score: 139.99 E-value: 1.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 31 LLFGIFTYGYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRIDIGLKSPQAIILSPTRELALQTLKVVDG 110
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 111 IGSRL-KVQVAQCIGGTQVDDDI-AAAQSCHLIVATPGRLLSLLQKKYVTTSNVKMVVLDEADEMLSRGFTEQIVSIMKF 188
Cdd:cd17962 81 LMKGLpPMKTALLVGGLPLPPQLyRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILEN 160
|
170 180 190
....*....|....*....|....*....|..
gi 159117719 189 MNADIQIVLVSATLPPEILELTRQFMRDPVSI 220
Cdd:cd17962 161 ISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
39-220 |
4.09e-39 |
|
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350718 [Multi-domain] Cd Length: 202 Bit Score: 138.48 E-value: 4.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 39 GYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRI---DIGLKSPQ--AIILSPTRELALQTLKVVDGIGS 113
Cdd:cd17960 9 GFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrKANLKKGQvgALIISPTRELATQIYEVLQSFLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 114 RLKVQVAQ--CIGGTQVDDDIAA--AQSCHLIVATPGRLLSLLQKKY--VTTSNVKMVVLDEADEMLSRGFTEQIVSIMK 187
Cdd:cd17960 89 HHLPKLKCqlLIGGTNVEEDVKKfkRNGPNILVGTPGRLEELLSRKAdkVKVKSLEVLVLDEADRLLDLGFEADLNRILS 168
|
170 180 190
....*....|....*....|....*....|...
gi 159117719 188 FMNADIQIVLVSATLPPEILELTRQFMRDPVSI 220
Cdd:cd17960 169 KLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
22-218 |
1.22e-38 |
|
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350696 [Multi-domain] Cd Length: 204 Bit Score: 137.45 E-value: 1.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 22 FDDMNLHPDLLFGIFTYGYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRIdiglkspQAIILSPTRELA 101
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV-------VALILEPSRELA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 102 LQTLKVVDGIGSRL---KVQVAQCIGGTQVDDDIAAAQS-CHLIVATPGRLLSLLQKKYVTTSNVKMVVLDEADEMLSRG 177
Cdd:cd17938 74 EQTYNCIENFKKYLdnpKLRVALLIGGVKAREQLKRLESgVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 159117719 178 FTEQIVSIMKFMNA------DIQIVLVSATL-PPEILELTRQFMRDPV 218
Cdd:cd17938 154 NLETINRIYNRIPKitsdgkRLQVIVCSATLhSFEVKKLADKIMHFPT 201
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
17-216 |
1.59e-37 |
|
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD box, X isoform, or DDX14) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. This protein has multiple conserved domains and is thought to play roles in both the nucleus and cytoplasm. Nuclear roles include transcriptional regulation, mRNP assembly, pre-mRNA splicing, and mRNA export. In the cytoplasm, this protein is thought to be involved in translation, cellular signaling, and viral replication. Misregulation of this gene has been implicated in tumorigenesis. Diseases associated with DDX3 include mental retardation, X-linked 102 and agenesis of the corpus callosum, with facial anomalies and robin sequence. DDX3 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350809 [Multi-domain] Cd Length: 249 Bit Score: 135.94 E-value: 1.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 17 KSYEKFDDMNLHPDLLFGIFTYGYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRI------------DI 84
Cdd:cd18051 18 PHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIyeqgpgeslpseSG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 85 GLKS----PQAIILSPTRELALQTLKVVDGIGSRLKVQVAQCIGGTQVDDDIA-AAQSCHLIVATPGRLLSLLQKKYVTT 159
Cdd:cd18051 98 YYGRrkqyPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRdLERGCHLLVATPGRLVDMLERGKIGL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 159117719 160 SNVKMVVLDEADEMLSRGFTEQIVSIMKFMN----ADIQIVLVSATLPPEILELTRQFMRD 216
Cdd:cd18051 178 DYCKYLVLDEADRMLDMGFEPQIRRIVEQDTmpptGERQTLMFSATFPKEIQMLARDFLDN 238
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
39-220 |
1.05e-35 |
|
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts with several spliceosomal proteins and may recognize the bacterial second messengers cyclic di-GMP and cyclic di-AMP, resulting in the induction of genes involved in the innate immune response. Diseases associated with DDX41 include "myeloproliferative/lymphoproliferative neoplasms, familial" and "Ddx41-related susceptibility to familial myeloproliferative/lymphoproliferative neoplasms". DDX41 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350709 [Multi-domain] Cd Length: 206 Bit Score: 129.77 E-value: 1.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 39 GYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGM-LQRID-------IGLKSPQAIILSPTRELALQTLKVVDG 110
Cdd:cd17951 9 GIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLiMFALEqekklpfIKGEGPYGLIVCPSRELARQTHEVIEY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 111 IGSRLK------VQVAQCIGGTQVDDDI-AAAQSCHLIVATPGRLLSLLQKKYVTTSNVKMVVLDEADEMLSRGFTEQIV 183
Cdd:cd17951 89 YCKALQeggypqLRCLLCIGGMSVKEQLeVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMIDMGFEEDIR 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 159117719 184 SIMKFMNADIQIVLVSATLPPEILELTRQFMRDPVSI 220
Cdd:cd17951 169 TIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
39-220 |
6.67e-35 |
|
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are members of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350724 [Multi-domain] Cd Length: 197 Bit Score: 127.49 E-value: 6.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 39 GYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTI---------GMLQRIDiglkSPQAIILSPTRELALQTLKVVD 109
Cdd:cd17966 9 GFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLpaivhinaqPPLERGD----GPIVLVLAPTRELAQQIQQEAN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 110 GIGSRLKVQVAQCIGGTQVDDDIAAAQ-SCHLIVATPGRLLSLLQKKYVTTSNVKMVVLDEADEMLSRGFTEQIVSIMKF 188
Cdd:cd17966 85 KFGGSSRLRNTCVYGGAPKGPQIRDLRrGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRKIVDQ 164
|
170 180 190
....*....|....*....|....*....|..
gi 159117719 189 MNADIQIVLVSATLPPEILELTRQFMRDPVSI 220
Cdd:cd17966 165 IRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
39-220 |
7.47e-32 |
|
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis antigen 13 or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 is also called cancer/testis antigen 26 or DEAD-Box Protein CAGE. Both DDX46 and DDX53 are members of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350716 [Multi-domain] Cd Length: 197 Bit Score: 119.11 E-value: 7.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 39 GYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRIDIGL------KSPQAIILSPTRELALQtlkvVDGIG 112
Cdd:cd17958 9 GFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPipreqrNGPGVLVLTPTRELALQ----IEAEC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 113 SRLKVQ--VAQCI--GGTQVDDDIAAAQSCHLIVATPGRLLSLLQKKYVTTSNVKMVVLDEADEMLSRGFTEQIVSIMKF 188
Cdd:cd17958 85 SKYSYKglKSVCVygGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIRKILLD 164
|
170 180 190
....*....|....*....|....*....|..
gi 159117719 189 MNADIQIVLVSATLPPEILELTRQFMRDPVSI 220
Cdd:cd17958 165 IRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
243-352 |
8.94e-32 |
|
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: 116.16 E-value: 8.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 243 WKTEVVEDIYKVLSVQQGVIFCNSIGRVkELAEKLKSAGHTLSCIHSELDQAERNKIMGEFRSGQTRILIATNIIARGID 322
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTL-EAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 159117719 323 VQNVSLVINYDIPREPETYLHRIGRSGRFG 352
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
39-220 |
1.30e-31 |
|
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1. DDX31 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350707 [Multi-domain] Cd Length: 214 Bit Score: 119.23 E-value: 1.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 39 GYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRIdIGLKS-------PQAIILSPTRELALQTLKVVDGI 111
Cdd:cd17949 10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRL-LSLEPrvdrsdgTLALVLVPTRELALQIYEVLEKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 112 GSRLKVQVAQCI-GGTQVDDDIAA-AQSCHLIVATPGRLLSLLQK-KYVTTSNVKMVVLDEADEMLSRGFTEQIVSIMKF 188
Cdd:cd17949 89 LKPFHWIVPGYLiGGEKRKSEKARlRKGVNILIATPGRLLDHLKNtQSFDVSNLRWLVLDEADRLLDMGFEKDITKILEL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 159117719 189 MNADI-------------QIVLVSATLPPEILELTRQFMRDPVSI 220
Cdd:cd17949 169 LDDKRskaggekskpsrrQTVLVSATLTDGVKRLAGLSLKDPVYI 213
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
20-217 |
1.19e-30 |
|
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both mRNA (mRNA) export from the nucleus into the cytoplasm and in mRNA translation. DDX19 functions in the nucleus in resolving RNA:DNA hybrids (R-loops). Activation of a DNA damage response pathway dependent upon the ATR kinase, a major regulator of replication fork progression, stimulates translocation of DDX19 from the cytoplasm into the nucleus. Only nuclear Ddx19 is competent to resolve R-loops. DDX19 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350805 [Multi-domain] Cd Length: 205 Bit Score: 116.36 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 20 EKFDDMNLHPDLLFGIFTYGYKIPSAIQSQAIVPIISG--KDTIAQAQSGTGKTAAFTIGMLQRIDIGLKSPQAIILSPT 97
Cdd:cd18047 1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 98 RELALQTLKVVDGIGSRL-KVQVAQCIGGTQVDDDIAAAQscHLIVATPGRLLS-LLQKKYVTTSNVKMVVLDEADEML- 174
Cdd:cd18047 81 YELALQTGKVIEQMGKFYpELKLAYAVRGNKLERGQKISE--QIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADVMIa 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 159117719 175 SRGFTEQIVSIMKFMNADIQIVLVSATLPPEILELTRQFMRDP 217
Cdd:cd18047 159 TQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
46-215 |
5.10e-30 |
|
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and nucleolar RNA helicase 2) is an RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II. It promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) and binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs. DDX50 (also called Gu-Beta, Nucleolar Protein Gu2, and malignant cell derived RNA helicase). DDX21 and DDX50 have similar genomic structures and are in tandem orientation on chromosome 10, suggesting that the two genes arose by gene duplication in evolution. Diseases associated with DDX21 include stomach disease and cerebral creatine deficiency syndrome 3. Diseases associated with DDX50 include rectal disease. Both are members of the DEAD-box helicases, 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. Their name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.
Pssm-ID: 350702 [Multi-domain] Cd Length: 202 Bit Score: 114.56 E-value: 5.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 46 IQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRIDIGL------KSPQAIILSPTRELALQTLKVVDGIGSRLKVqv 119
Cdd:cd17944 16 IQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQqprkrgRAPKVLVLAPTRELANQVTKDFKDITRKLSV-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 120 AQCIGGTQVDDDIAAAQS-CHLIVATPGRLLSLLQKKYVTTSNVKMVVLDEADEMLSRGFTEQIVSIM-----KFMNADI 193
Cdd:cd17944 94 ACFYGGTPYQQQIFAIRNgIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILsvsykKDSEDNP 173
|
170 180
....*....|....*....|..
gi 159117719 194 QIVLVSATLPPEILELTRQFMR 215
Cdd:cd17944 174 QTLLFSATCPDWVYNVAKKYMK 195
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
39-202 |
1.28e-28 |
|
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box protein, which shows little similarity to any of the other known human DEAD box proteins, but shows a high similarity to mouse Ddx24 at the amino acid level. MDM2 mediates nonproteolytic polyubiquitylation of the DEAD-Box RNA helicase DDX24. DDX24 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.
Pssm-ID: 350704 [Multi-domain] Cd Length: 235 Bit Score: 111.56 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 39 GYKIPSAIQSQAI-VPIISGKDTIAQAQSGTGKTAAFTIGMLQRIDIGLKS---------PQAIILSPTRELALQTLKVV 108
Cdd:cd17946 9 GFSEPTPIQALALpAAIRDGKDVIGAAETGSGKTLAFGIPILERLLSQKSSngvggkqkpLRALILTPTRELAVQVKDHL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 109 DGIGSRLKVQVAQCIGG-TQVDDDIAAAQSCHLIVATPGRLLSLLQKK-YVTTS--NVKMVVLDEADEMLSRGFTEQIVS 184
Cdd:cd17946 89 KAIAKYTNIKIASIVGGlAVQKQERLLKKRPEIVVATPGRLWELIQEGnEHLANlkSLRFLVLDEADRMLEKGHFAELEK 168
|
170 180
....*....|....*....|....*
gi 159117719 185 IMKFMNAD-------IQIVLVSATL 202
Cdd:cd17946 169 ILELLNKDragkkrkRQTFVFSATL 193
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
40-220 |
1.37e-28 |
|
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or DEAD Box Protein P82) has a wide variety of functions including regulating the alternative splicing of exons exhibiting specific features such as the inclusion of AC-rich alternative exons in CD44 transcripts, playing a role in innate immunity, and promoting mRNA degradation mediated by the antiviral zinc-finger protein ZC3HAV1 in an ATPase-dependent manner. DDX17 synergizes with DDX5 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. DDX17 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350808 [Multi-domain] Cd Length: 271 Bit Score: 112.80 E-value: 1.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 40 YKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGM---------LQRIDiglkSPQAIILSPTRELALQTLKVVDG 110
Cdd:cd18050 82 FKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAivhinhqpyLERGD----GPICLVLAPTRELAQQVQQVADD 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 111 IG--SRLKvqvAQCI-----GGTQVDDDIAAAQSChliVATPGRLLSLLQKKYVTTSNVKMVVLDEADEMLSRGFTEQIV 183
Cdd:cd18050 158 YGksSRLK---STCIyggapKGPQIRDLERGVEIC---IATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIR 231
|
170 180 190
....*....|....*....|....*....|....*..
gi 159117719 184 SIMKFMNADIQIVLVSATLPPEILELTRQFMRDPVSI 220
Cdd:cd18050 232 KIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQI 268
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
271-352 |
1.49e-28 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 106.53 E-value: 1.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 271 KELAEKLKSAGHTLSCIHSELDQAERNKIMGEFRSGQTRILIATNIIARGIDVQNVSLVINYDIPREPETYLHRIGRSGR 350
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 159117719 351 FG 352
Cdd:smart00490 81 AG 82
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
39-220 |
8.19e-28 |
|
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein and is activated by Myc protein. DDX18 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350700 [Multi-domain] Cd Length: 198 Bit Score: 108.60 E-value: 8.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 39 GYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAF---TIGMLQRIDIGLKSPQA-IILSPTRELALQTLKVVDGIGSR 114
Cdd:cd17942 9 GFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFlipAIELLYKLKFKPRNGTGvIIISPTRELALQIYGVAKELLKY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 115 LKVQVAQCIGGTQVDDDIAAAQS-CHLIVATPGRLLSLLQ-KKYVTTSNVKMVVLDEADEMLSRGFTEQIVSIMKFMNAD 192
Cdd:cd17942 89 HSQTFGIVIGGANRKAEAEKLGKgVNILVATPGRLLDHLQnTKGFLYKNLQCLIIDEADRILEIGFEEEMRQIIKLLPKR 168
|
170 180
....*....|....*....|....*....
gi 159117719 193 IQIVLVSATLPPEILELTR-QFMRDPVSI 220
Cdd:cd17942 169 RQTMLFSATQTRKVEDLARiSLKKKPLYV 197
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
21-220 |
1.60e-27 |
|
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, G17P1, or HUMP68) is involved in pathways that include the alteration of RNA structures, plays a role as a coregulator of transcription, a regulator of splicing, and in the processing of small noncoding RNAs. It synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. Dysregulation of this gene may play a role in cancer development. DDX5 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350807 [Multi-domain] Cd Length: 234 Bit Score: 108.94 E-value: 1.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 21 KFDDMNLHPDLLFGIFTYGYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIG---------MLQRIDiglkSPQA 91
Cdd:cd18049 25 NFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPaivhinhqpFLERGD----GPIC 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 92 IILSPTRELALQTLKVVD--GIGSRLKvqvAQCI-----GGTQVDDDIAAAQSChliVATPGRLLSLLQKKYVTTSNVKM 164
Cdd:cd18049 101 LVLAPTRELAQQVQQVAAeyGRACRLK---STCIyggapKGPQIRDLERGVEIC---IATPGRLIDFLEAGKTNLRRCTY 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 159117719 165 VVLDEADEMLSRGFTEQIVSIMKFMNADIQIVLVSATLPPEILELTRQFMRDPVSI 220
Cdd:cd18049 175 LVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHI 230
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
38-209 |
3.58e-27 |
|
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350706 [Multi-domain] Cd Length: 231 Bit Score: 107.84 E-value: 3.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 38 YGYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRI-------DIGLKSPQAIILSPTRELALQTLKVVDG 110
Cdd:cd17948 8 QGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLlrykllaEGPFNAPRGLVITPSRELAEQIGSVAQS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 111 IGSRLKVQVaQCIGGTQVDDDIAAAQ--SCHLIVATPGRLLSLLQKKYVTTSNVKMVVLDEADEMLSRGFTEQIVSIMK- 187
Cdd:cd17948 88 LTEGLGLKV-KVITGGRTKRQIRNPHfeEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKLSHFLRr 166
|
170 180 190
....*....|....*....|....*....|....
gi 159117719 188 ----FMNADI--------QIVLVSATLPPEILEL 209
Cdd:cd17948 167 fplaSRRSENtdgldpgtQLVLVSATMPSGVGEV 200
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
47-391 |
1.96e-20 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 93.04 E-value: 1.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 47 QSQAIVP-IISGKDTIAQAQSGTGKTAAFTIGMLQRIDIGLKspqAIILSPTRELALQTLKVVDGIGSRLKVQVAQCIGG 125
Cdd:COG1204 27 QAEALEAgLLEGKNLVVSAPTASGKTLIAELAILKALLNGGK---ALYIVPLRALASEKYREFKRDFEELGIKVGVSTGD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 126 tqVDDDIAAAQSCHLIVATPGRLLSLLQKKYVTTSNVKMVVLDEA----DEmlSRGFT-EQIVSIMKFMNADIQIVLVSA 200
Cdd:COG1204 104 --YDSDDEWLGRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAhlidDE--SRGPTlEVLLARLRRLNPEAQIVALSA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 201 TL--PPEILE-LTRQFMRD---PVsilvkeaELTLDGIRQYVVELQDAWKTEVVEDIYKVL-SVQQG---VIFCNSIGRV 270
Cdd:COG1204 180 TIgnAEEIAEwLDAELVKSdwrPV-------PLNEGVLYDGVLRFDDGSRRSKDPTLALALdLLEEGgqvLVFVSSRRDA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 271 KELAEKLKSA-----------------------------GHTLS-CI-------HSELDQAERNKIMGEFRSGQTRILIA 313
Cdd:COG1204 253 ESLAKKLADElkrrltpeereeleelaeellevseethtNEKLAdCLekgvafhHAGLPSELRRLVEDAFREGLIKVLVA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 314 T-------NIIARGIDVQNVSLVINYDIPrePETYLHRIGRSGRFGR--KGVAInfVTDKDKQSMQAITDKFnVTTEnlP 384
Cdd:COG1204 333 TptlaagvNLPARRVIIRDTKRGGMVPIP--VLEFKQMAGRAGRPGYdpYGEAI--LVAKSSDEADELFERY-ILGE--P 405
|
....*..
gi 159117719 385 EDLSSLF 391
Cdd:COG1204 406 EPIRSKL 412
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
57-201 |
1.67e-19 |
|
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: 84.38 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 57 GKDTIAQAQSGTGKTAAFTIGMLQRIDigLKSPQAIILSPTRELALQTLKVVDGIgSRLKVQVAQCIGGTQV-DDDIAAA 135
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLL--KKGKKVLVLVPTKALALQTAERLREL-FGPGIRVAVLVGGSSAeEREKNKL 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 159117719 136 QSCHLIVATPGRLL-SLLQKKYVTTSNVKMVVLDEADEMLSRGFTEQIV--SIMKFMNADIQIVLVSAT 201
Cdd:cd00046 78 GDADIIIATPDMLLnLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILdlAVRKAGLKNAQVILLSAT 146
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
47-358 |
1.71e-18 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 87.58 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 47 QSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRIdigLKSPQ--AIILSPTRELA---LQTL-KVVDGIGsrLKVQVA 120
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEAL---LEDPGatALYLYPTKALArdqLRRLrELAEALG--LGVRVA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 121 QCIGGTQVDDDIAAAQSCHLIVATPGRL-LSLL--QKKYVTT-SNVKMVVLDEADE-----------MLSRgfteqIVSI 185
Cdd:COG1205 136 TYDGDTPPEERRWIREHPDIVLTNPDMLhYGLLphHTRWARFfRNLRYVVIDEAHTyrgvfgshvanVLRR-----LRRI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 186 MKFMNADIQIVLVSATL--PPEILE-LT-RQFM--------RDPVSILVKEAELTLDGIRQY-VVELQDAWKTEVVEDIy 252
Cdd:COG1205 211 CRHYGSDPQFILASATIgnPAEHAErLTgRPVTvvdedgspRGERTFVLWNPPLVDDGIRRSaLAEAARLLADLVREGL- 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 253 kvlsvqQGVIFCNSIGRVKELAEKLKSA------GHTLSCIHSELDQAERNKIMGEFRSGQTRILIATNIIARGIDVQNV 326
Cdd:COG1205 290 ------RTLVFTRSRRGAELLARYARRAlrepdlADRVAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGL 363
|
330 340 350
....*....|....*....|....*....|..
gi 159117719 327 SLVINYDIPREPETYLHRIGRSGRFGRKGVAI 358
Cdd:COG1205 364 DAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV 395
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
37-360 |
3.04e-18 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 86.31 E-value: 3.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 37 TYGYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRIDIGLkspqaiilsptrelalqtlkVVDGIGSRLK 116
Cdd:PRK11057 20 TFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTL--------------------VVSPLISLMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 117 VQV---------AQCIGGTQV-DDDIAAAQSCH-----LIVATPGRLL--SLLQKkyVTTSNVKMVVLDEADEMLSRG-- 177
Cdd:PRK11057 80 DQVdqllangvaAACLNSTQTrEQQLEVMAGCRtgqikLLYIAPERLMmdNFLEH--LAHWNPALLAVDEAHCISQWGhd 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 178 FTEQIVSI--MKFMNADIQIVLVSATLPpeilELTRQ------FMRDPvsiLVKEAELTLDGIRQYVVElqdawKTEVVE 249
Cdd:PRK11057 158 FRPEYAALgqLRQRFPTLPFMALTATAD----DTTRQdivrllGLNDP---LIQISSFDRPNIRYTLVE-----KFKPLD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 250 DIYKVLSVQQ---GVIFCNSIGRVKELAEKLKSAGHTLSCIHSELDQAERNKIMGEFRSGQTRILIATNIIARGIDVQNV 326
Cdd:PRK11057 226 QLMRYVQEQRgksGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNV 305
|
330 340 350
....*....|....*....|....*....|....
gi 159117719 327 SLVINYDIPREPETYLHRIGRSGRFGRKGVAINF 360
Cdd:PRK11057 306 RFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLF 339
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
67-330 |
3.87e-18 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 86.23 E-value: 3.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 67 GTGKT--AAFTIGMLQRIDiglkspQAIILSPTRELALQTLKVVdgigsrLKVQVAQCIGGTQVDDDiaaaqsCHLIVAT 144
Cdd:COG1061 110 GTGKTvlALALAAELLRGK------RVLVLVPRRELLEQWAEEL------RRFLGDPLAGGGKKDSD------APITVAT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 145 PGRLLSLLQKKYVTtSNVKMVVLDEADEMLSRGFTEqivsIMKFMNADIqIVLVSAT------LPPEILELT-------- 210
Cdd:COG1061 172 YQSLARRAHLDELG-DRFGLVIIDEAHHAGAPSYRR----ILEAFPAAY-RLGLTATpfrsdgREILLFLFDgivyeysl 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 211 RQFMRD----PVSILVKEAELT--------LDGIRQYVVELQDAWKTEVVEDIY-KVLSVQQGVIFCNSIGRVKELAEKL 277
Cdd:COG1061 246 KEAIEDgylaPPEYYGIRVDLTderaeydaLSERLREALAADAERKDKILRELLrEHPDDRKTLVFCSSVDHAEALAELL 325
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 159117719 278 KSAGHTLSCIHSELDQAERNKIMGEFRSGQTRILIATNIIARGIDVQNVSLVI 330
Cdd:COG1061 326 NEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI 378
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
258-367 |
7.44e-16 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 79.03 E-value: 7.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 258 QQGVIFCNSIGRVKELAEKLKSAGHTLSCIHSELDQAERNKIMGEFRSGQTRILIATNIIARGIDVQNVSLVINYDIPRE 337
Cdd:COG0514 231 GSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKS 310
|
90 100 110
....*....|....*....|....*....|
gi 159117719 338 PETYLHRIGRSGRFGRKGVAINFVTDKDKQ 367
Cdd:COG0514 311 IEAYYQEIGRAGRDGLPAEALLLYGPEDVA 340
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
22-220 |
5.56e-15 |
|
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 (MRH4) plays an essential role during the late stages of mitochondrial ribosome or mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions. MRH4 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350723 [Multi-domain] Cd Length: 251 Bit Score: 73.95 E-value: 5.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 22 FDDMNLHPD---------LLFGIFTYGYKIPSAIQSQAIvPIISGKDTIAQ-----------------AQSGTGKTAAF- 74
Cdd:cd17965 1 FDQLKLLPSvreaiikeiLKGSNKTDEEIKPSPIQTLAI-KKLLKTLMRKVtkqtsneepklevfllaAETGSGKTLAYl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 75 --TIGMLQRIDI--------------GLKSPQAIILSPTRELALQTLKVVDGIGSRLKVQVAQC---IGGTQVDDDIAAA 135
Cdd:cd17965 80 apLLDYLKRQEQepfeeaeeeyesakDTGRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFssgFGPSYQRLQLAFK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 136 QSCHLIVATPGRLLSLLQKKYVTTSNVKMVVLDEADEMLSRGFTEQIVSIMKFMNADIQIVLVSATLPPEILELTRQFMR 215
Cdd:cd17965 160 GRIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLRKLFP 239
|
....*
gi 159117719 216 DPVSI 220
Cdd:cd17965 240 DVVRI 244
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
46-203 |
1.06e-14 |
|
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: 71.52 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 46 IQSQAIVPII-SGKDTIAQAQSGTGKTAAFTIGMLQRIdigLKSPQAII-LSPTRELALQTLKVVDGIGSRLKVQVAQCI 123
Cdd:cd17921 5 IQREALRALYlSGDSVLVSAPTSSGKTLIAELAILRAL---ATSGGKAVyIAPTRALVNQKEADLRERFGPLGKNVGLLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 124 GGTQVDddIAAAQSCHLIVATPGRLLSLLQK-KYVTTSNVKMVVLDEA----DEmlSRGFT-EQIVSIMKFMNADIQIVL 197
Cdd:cd17921 82 GDPSVN--KLLLAEADILVATPEKLDLLLRNgGERLIQDVRLVVVDEAhligDG--ERGVVlELLLSRLLRINKNARFVG 157
|
....*.
gi 159117719 198 VSATLP 203
Cdd:cd17921 158 LSATLP 163
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
42-202 |
3.75e-14 |
|
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350714 [Multi-domain] Cd Length: 231 Bit Score: 71.12 E-value: 3.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 42 IPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRIdIGLKSPQ--AIILSPTRELALQTLKVVDGIGSRLKVQV 119
Cdd:cd17956 21 IPWLLPSSKSTPPYRPGDLCVSAPTGSGKTLAYVLPIVQAL-SKRVVPRlrALIVVPTKELVQQVYKVFESLCKGTGLKV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 120 AQCIGGTQVDDDIAAAQSCH---------LIVATPGRLLS-LLQKKYVTTSNVKMVVLDEADEMLSRGFTEQIVSIMKFM 189
Cdd:cd17956 100 VSLSGQKSFKKEQKLLLVDTsgrylsrvdILVATPGRLVDhLNSTPGFTLKHLRFLVIDEADRLLNQSFQDWLETVMKAL 179
|
170 180 190
....*....|....*....|....*....|...
gi 159117719 190 NAD--------------------IQIVLVSATL 202
Cdd:cd17956 180 GRPtapdlgsfgdanllersvrpLQKLLFSATL 212
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
260-360 |
8.57e-13 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They 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: 350181 [Multi-domain] Cd Length: 134 Bit Score: 64.92 E-value: 8.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 260 GVIFCNSIGRVKELAEKLKSAGHTLSCIHSELDQAERNKIMGEFRSGQTRILIATNIIARGIDVQNVSLVINYDIPREPE 339
Cdd:cd18794 33 GIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSME 112
|
90 100
....*....|....*....|.
gi 159117719 340 TYLHRIGRSGRFGRKGVAINF 360
Cdd:cd18794 113 SYYQESGRAGRDGLPSECILF 133
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
45-203 |
3.69e-12 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs 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: 350781 [Multi-domain] Cd Length: 206 Bit Score: 65.07 E-value: 3.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 45 AIQSQAIVPII-SGKDTIAQAQSGTGKTAAFTIGMLQ----RIDIGLKSPQAIILSPTRELALQTLKVVDGIGSRLKVQV 119
Cdd:cd18023 4 RIQSEVFPDLLySDKNFVVSAPTGSGKTVLFELAILRllkeRNPLPWGNRKVVYIAPIKALCSEKYDDWKEKFGPLGLSC 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 120 AQCIGGTQVDDDiAAAQSCHLIVATPGR--LLSLLQKKYVT-TSNVKMVVLDEADEM-LSRGFT-EQIVSIMKFMN---- 190
Cdd:cd18023 84 AELTGDTEMDDT-FEIQDADIILTTPEKwdSMTRRWRDNGNlVQLVALVLIDEVHIIkENRGATlEVVVSRMKTLSssse 162
|
170
....*....|....*....
gi 159117719 191 ------ADIQIVLVSATLP 203
Cdd:cd18023 163 lrgstvRPMRFVAVSATIP 181
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
67-323 |
1.43e-11 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 65.87 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 67 GTGKT-AAFTIGMLQRIDIGLKSpqaIILS-PTRELALQTLKVVDGIG----------SRLKVQVAQCIGGTQVDDDIAA 134
Cdd:COG1203 157 GGGKTeAALLFALRLAAKHGGRR---IIYAlPFTSIINQTYDRLRDLFgedvllhhslADLDLLEEEEEYESEARWLKLL 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 135 AQSCH--LIVATPGRLL-SLLQKKyvTTSNVKM-------VVLDEADeMLSRGFTEQIVSIMKFM-NADIQIVLVSATLP 203
Cdd:COG1203 234 KELWDapVVVTTIDQLFeSLFSNR--KGQERRLhnlansvIILDEVQ-AYPPYMLALLLRLLEWLkNLGGSVILMTATLP 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 204 PEIleltRQFMRDPVSILVKEAELTLDGIRQYV---VELQDAWKT--EVVEDIYKVL-SVQQGVIFCNSIGRVKELAEKL 277
Cdd:COG1203 311 PLL----REELLEAYELIPDEPEELPEYFRAFVrkrVELKEGPLSdeELAELILEALhKGKSVLVIVNTVKDAQELYEAL 386
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 159117719 278 KSAGHTLSCI--HSELDQAER----NKIMGEFRSGQTRILIATNIIARGIDV 323
Cdd:COG1203 387 KEKLPDEEVYllHSRFCPADRseieKEIKERLERGKPCILVSTQVVEAGVDI 438
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
269-374 |
5.06e-11 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 60.44 E-value: 5.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 269 RVKELAEKLKS---AGHTLSCIHSELDQAERNKIMGEFRSGQTRILIATNIIARGIDVQNVSLVINYDIPREPETYLHRI 345
Cdd:cd18811 46 AAVAMYEYLKErfrPELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLHQL 125
|
90 100 110
....*....|....*....|....*....|....
gi 159117719 346 -GRSGRFGRKGVAINFVTDKD----KQSMQAITD 374
Cdd:cd18811 126 rGRVGRGDHQSYCLLVYKDPLtetaKQRLRVMTE 159
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
47-374 |
2.38e-10 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 62.21 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 47 QSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRIDIGLKSpqaIILSPTRELALQTLKVVDGIGSrLKVQVAQCIGgt 126
Cdd:PRK01172 27 QRMAIEQLRKGENVIVSVPTAAGKTLIAYSAIYETFLAGLKS---IYIVPLRSLAMEKYEELSRLRS-LGMRVKISIG-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 127 QVDDDIAAAQSCHLIVATPGRLLSLLQKKYVTTSNVKMVVLDE----ADEmlSRGFT-EQIVSIMKFMNADIQIVLVSAT 201
Cdd:PRK01172 101 DYDDPPDFIKRYDVVILTSEKADSLIHHDPYIINDVGLIVADEihiiGDE--DRGPTlETVLSSARYVNPDARILALSAT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 202 LP--PEILE------LTRQFMRDP--VSILVKEaELTLDGIRQYVVELQDAWKtEVVEDIYKVLsvqqgvIFCNSIGRVK 271
Cdd:PRK01172 179 VSnaNELAQwlnaslIKSNFRPVPlkLGILYRK-RLILDGYERSQVDINSLIK-ETVNDGGQVL------VFVSSRKNAE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 272 ELAEKL-------------------------KSAGHTLSCIHSELDQAERNKIMGEFRSGQTRILIATNIIARGIDVQnV 326
Cdd:PRK01172 251 DYAEMLiqhfpefndfkvssennnvyddslnEMLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLP-A 329
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 159117719 327 SLVINYDIPREPETYL---------HRIGRSGRFGRKGVAINFVTDKDKQSMQAITD 374
Cdd:PRK01172 330 RLVIVRDITRYGNGGIrylsnmeikQMIGRAGRPGYDQYGIGYIYAASPASYDAAKK 386
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
257-361 |
1.30e-09 |
|
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: 54.25 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 257 VQQGVIFCNSIGRVKELAEKLKsaghtlscihseldqaernkimgefrsgqtrILIATNIIARGIDVQNVSLVINYDIPR 336
Cdd:cd18785 3 VVKIIVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDPPS 51
|
90 100
....*....|....*....|....*.
gi 159117719 337 EPETYLHRIGRSGRFG-RKGVAINFV 361
Cdd:cd18785 52 SAASYIQRVGRAGRGGkDEGEVILFV 77
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
236-350 |
2.48e-09 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases 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: 350183 [Multi-domain] Cd Length: 150 Bit Score: 55.35 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 236 VVELQDAWKTEVVEDIYK--VLSVQQG---VIFCNSIGRVKELAEKLKSAGHTLS------CIHSELDQAERNKIMGEFR 304
Cdd:cd18796 12 VAPEIFPWAGESGADAYAevIFLLERHkstLVFTNTRSQAERLAQRLRELCPDRVppdfiaLHHGSLSRELREEVEAALK 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 159117719 305 SGQTRILIATNIIARGIDVQNVSLVINYDIPREPETYLHRIGRSGR 350
Cdd:cd18796 92 RGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
165-354 |
7.05e-09 |
|
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
Pssm-ID: 187770 [Multi-domain] Cd Length: 353 Bit Score: 57.05 E-value: 7.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 165 VVLDEADEMLS--RGFTEQIVSIMKFMnaDIQIVLVSATLPpeilELTRQFMRDPVSILVKEAELTLDGIRQYVVELQDA 242
Cdd:cd09639 127 LIFDEVHFYDEytLALILAVLEVLKDN--DVPILLMSATLP----KFLKEYAEKIGYVEENEPLDLKPNERAPFIKIESD 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 243 WK------TEVVEDIYKVLSVqqgVIFCNSIGRVKELAEKLKSAGHTLSC--IHSELDQAERNK----IMGEFRSGQTRI 310
Cdd:cd09639 201 KVgeisslERLLEFIKKGGSV---AIIVNTVDRAQEFYQQLKEKGPEEEImlIHSRFTEKDRAKkeaeLLLEFKKSEKFV 277
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 159117719 311 LIATNIIARGIDVqNVSLVINYDIPrePETYLHRIGRSGRFGRK 354
Cdd:cd09639 278 IVATQVIEASLDI-SVDVMITELAP--IDSLIQRLGRLHRYGEK 318
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
54-203 |
8.95e-09 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type 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: 350786 [Multi-domain] Cd Length: 177 Bit Score: 54.65 E-value: 8.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 54 IISGKDTIAQAQSGTGKTAAFTIGMLQRIDIGLKspqAIILSPTRELA---LQTLKVVDGIGSRLKVQVAQciggtqVDD 130
Cdd:cd18028 14 LLKGENLLISIPTASGKTLIAEMAMVNTLLEGGK---ALYLVPLRALAsekYEEFKKLEEIGLKVGISTGD------YDE 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 159117719 131 DIAAAQSCHLIVATPGRLLSLLQKKYVTTSNVKMVVLDEAdEMLS---RGFT-EQIVSIMKFMNADIQIVLVSATLP 203
Cdd:cd18028 85 DDEWLGDYDIIVATYEKFDSLLRHSPSWLRDVGVVVVDEI-HLISdeeRGPTlESIVARLRRLNPNTQIIGLSATIG 160
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
40-365 |
1.05e-08 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 57.03 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 40 YKIPSAIQSQAIVPIISGKDTIAQAQSGTGKT-AAFT---IGMLQRIDIGLKSP--QAIILSPTRELA------LQTlkV 107
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAFLpalDELARRPRPGELPDglRVLYISPLKALAndiernLRA--P 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 108 VDGIGSRLKVQVaqciggtqvdDDIAAA-------QS---------CHLIVATPGRL-LSLLQKKYVTT-SNVKMVVLDE 169
Cdd:COG1201 100 LEEIGEAAGLPL----------PEIRVGvrtgdtpASerqrqrrrpPHILITTPESLaLLLTSPDARELlRGVRTVIVDE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 170 ADEMLS--RG-----FTEQIVSIMKfmnADIQIVLVSATL--PPEILE-LTRQFMRDPVSI----LVKEAELTldgIRQY 235
Cdd:COG1201 170 IHALAGskRGvhlalSLERLRALAP---RPLQRIGLSATVgpLEEVARfLVGYEDPRPVTIvdagAGKKPDLE---VLVP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 236 VVELQDA--WKTEVVEDIYKVLS--VQQG---VIFCNS-------IGRVKELAEK--LKSAGHtlsciHSELDQAERNKI 299
Cdd:COG1201 244 VEDLIERfpWAGHLWPHLYPRVLdlIEAHrttLVFTNTrsqaerlFQRLNELNPEdaLPIAAH-----HGSLSREQRLEV 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 159117719 300 MGEFRSGQTRILIATNIIARGIDVQNVSLVINYDIPREPETYLHRIGRSG-RFGRKGVAINFVTDKD 365
Cdd:COG1201 319 EEALKAGELRAVVATSSLELGIDIGDVDLVIQVGSPKSVARLLQRIGRAGhRVGEVSKGRLVPTHRD 385
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
248-354 |
1.93e-08 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 56.44 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 248 VEDIYKVLSVQQ----GVIFCNSIGRVKELAEKLKSAGHTLSCIHSELDQAERNKIMGEFRSGQTRILIATNIIARGIDV 323
Cdd:PLN03137 667 LEDIDKFIKENHfdecGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINK 746
|
90 100 110
....*....|....*....|....*....|.
gi 159117719 324 QNVSLVINYDIPREPETYLHRIGRSGRFGRK 354
Cdd:PLN03137 747 PDVRFVIHHSLPKSIEGYHQECGRAGRDGQR 777
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
287-374 |
2.12e-08 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They 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: 350179 [Multi-domain] Cd Length: 160 Bit Score: 53.04 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 287 IHSELDQAERNKIMGEFRSGQTRILIATNIIARGIDVQNVSLVINYDIPREPETYLHRI-GRSGRFGRKGVAI------N 359
Cdd:cd18792 66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFGLSQLHQLrGRVGRGKHQSYCYllypdpK 145
|
90
....*....|....*
gi 159117719 360 FVTDKDKQSMQAITD 374
Cdd:cd18792 146 KLTETAKKRLRAIAE 160
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
259-347 |
2.00e-07 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains 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: 350189 [Multi-domain] Cd Length: 142 Bit Score: 49.90 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 259 QGVIFCNSIGRVKELAEKLKSAGHTLSCIH---------------SELDQAERNKIMGEFRSGQTRILIATNIIARGIDV 323
Cdd:cd18802 27 RGIIFVERRATAVVLSRLLKEHPSTLAFIRcgfligrgnssqrkrSLMTQRKQKETLDKFRDGELNLLIATSVLEEGIDV 106
|
90 100
....*....|....*....|....
gi 159117719 324 QNVSLVINYDIPREPETYLHRIGR 347
Cdd:cd18802 107 PACNLVIRFDLPKTLRSYIQSRGR 130
|
|
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
270-330 |
2.27e-07 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 52.74 E-value: 2.27e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 159117719 270 VKELAEKLKSA--GHTLSCIHSELDQAERNKIMGEFRSGQTRILIATNIIARGIDVQNVSL-VI 330
Cdd:COG1200 490 AEETYEELREAfpGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTVIEVGVDVPNATVmVI 553
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
291-358 |
3.07e-07 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 52.42 E-value: 3.07e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 159117719 291 LDQAERNKIMGEFRSGQTRILIATNIIARGIDVQNVSLVINYD-IPREPEtYLHRIGRSGRFGRKGVAI 358
Cdd:COG1111 395 LTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYEpVPSEIR-SIQRKGRTGRKREGRVVV 462
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
272-371 |
5.42e-07 |
|
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350177 [Multi-domain] Cd Length: 171 Bit Score: 49.17 E-value: 5.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 272 ELAEKLKSAGHTLSCIHSELDQAERNKIMGEFRSGQTRILIATNIIARGIDVQNVSLVINYDIPRE----PETYL-HRIG 346
Cdd:cd18790 42 DLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDADKEgflrSETSLiQTIG 121
|
90 100
....*....|....*....|....*
gi 159117719 347 RSGRfGRKGVAInFVTDKDKQSMQA 371
Cdd:cd18790 122 RAAR-NVNGKVI-LYADKITDSMQK 144
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
58-170 |
5.51e-07 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer 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: 350792 [Multi-domain] Cd Length: 200 Bit Score: 49.57 E-value: 5.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 58 KDTIAQAQSGTGKT--AAFTIGMLQRIDIGLKSP--QAIILSPTRELALQTLKVvdgIGSRLKVQVAQCIGGTQVDDDIA 133
Cdd:cd18034 17 RNTIVVLPTGSGKTliAVMLIKEMGELNRKEKNPkkRAVFLVPTVPLVAQQAEA---IRSHTDLKVGEYSGEMGVDKWTK 93
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 159117719 134 AAQSC-----HLIVATPGRLLSLLQKKYVTTSNVKMVVLDEA 170
Cdd:cd18034 94 ERWKEelekyDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
47-202 |
8.33e-07 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs 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: 350681 [Multi-domain] Cd Length: 182 Bit Score: 48.74 E-value: 8.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 47 QSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRIdIGLKSPQAIILSPTRELA---LQTL-KVVDGIGSRLKVQVaqC 122
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEAL-LRDPGSRALYLYPTKALAqdqLRSLrELLEQLGLGIRVAT--Y 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 123 IGGTQVDD--DIAAAQScHLIVATPGRL-LSLL---QKKYVTTSNVKMVVLDEAD----------EMLSRGFTEqivsIM 186
Cdd:cd17923 82 DGDTPREErrAIIRNPP-RILLTNPDMLhYALLphhDRWARFLRNLRYVVLDEAHtyrgvfgshvALLLRRLRR----LC 156
|
170
....*....|....*.
gi 159117719 187 KFMNADIQIVLVSATL 202
Cdd:cd17923 157 RRYGADPQFILTSATI 172
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
246-355 |
1.05e-06 |
|
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: 47.74 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 246 EVVEDIYKVLSVQQGVIfcnsigRVKEL---AEKLKSAGhtlscihseLDQAERNKIMGEFRSGQTRILIATNIIARGID 322
Cdd:cd18801 41 DSAEEIVNFLSKIRPGI------RATRFigqASGKSSKG---------MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLD 105
|
90 100 110
....*....|....*....|....*....|...
gi 159117719 323 VQNVSLVINYDIPREPETYLHRIGRSGRfGRKG 355
Cdd:cd18801 106 IGEVDLIICYDASPSPIRMIQRMGRTGR-KRQG 137
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
246-362 |
1.70e-06 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 50.22 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 246 EVVEDIY----KVLsvqqgvIFCNSIGRVKELAEKLKSAGHTLSCIHSELDQAERNKIMGEFRSGQ--TRILIATNIIAR 319
Cdd:COG0553 540 ELLEELLaegeKVL------VFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGGE 613
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 159117719 320 GIDVQNVSLVINYDIPREPETYLHRIGRSGRFG-RKGV-AINFVT 362
Cdd:COG0553 614 GLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGqTRDVqVYKLVA 658
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
271-358 |
6.97e-06 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases 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: 350184 [Multi-domain] Cd Length: 146 Bit Score: 45.33 E-value: 6.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 271 KELAEKLKSAGHTLSCIHSE---LDQAERNKIMGEFRSGQTRILIATNIIARGIDVQNVSLVINYDIPREPETYLHRIGR 347
Cdd:cd18797 53 RYLKARLVEEGPLASKVASYragYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAGYPGSLASLWQQAGR 132
|
90
....*....|.
gi 159117719 348 SGRFGRKGVAI 358
Cdd:cd18797 133 AGRRGKDSLVI 143
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
272-349 |
7.33e-06 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 47.84 E-value: 7.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 272 ELAEKLKSA--GHTLSCIHSELDQAERNKIMGEFRSGQTRILIATNIIARGIDVQNVSLVINYDiprePETY----LH-- 343
Cdd:PRK10917 494 ETYEELQEAfpELRVGLLHGRMKPAEKDAVMAAFKAGEIDILVATTVIEVGVDVPNATVMVIEN----AERFglaqLHql 569
|
....*...
gi 159117719 344 --RIGRSG 349
Cdd:PRK10917 570 rgRVGRGA 577
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
211-372 |
7.41e-06 |
|
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350197 [Multi-domain] Cd Length: 151 Bit Score: 45.41 E-value: 7.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 211 RQFMRDPVSILVKEA---ELTLDGIRQYVVELqdawktevVEDIYKVLsvqqgvifcnsiGRVKELAEKLKSAghtlsCI 287
Cdd:cd18810 3 RTYVMPYDDELIREAierELLRGGQVFYVHNR--------IESIEKLA------------TQLRQLVPEARIA-----IA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 288 HSELDQAERNKIMGEFRSGQTRILIATNIIARGIDVQNVSLVINYDIPREPETYLHRI-GRSGRFGRKGVAINFVTDKDK 366
Cdd:cd18810 58 HGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIERADKFGLAQLYQLrGRVGRSKERAYAYFLYPDQKK 137
|
....*.
gi 159117719 367 QSMQAI 372
Cdd:cd18810 138 LTEDAL 143
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
54-350 |
7.75e-06 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 47.89 E-value: 7.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 54 IISGKDTIAQAQSGTGKTAAFTIGMLQRIdigLKSP-QAIILSPTRELALQTLKVVDGiGSRLKVQVAQCIGGTQVDDDI 132
Cdd:PRK00254 36 VLEGKNLVLAIPTASGKTLVAEIVMVNKL---LREGgKAVYLVPLKALAEEKYREFKD-WEKLGLRVAMTTGDYDSTDEW 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 133 AAAQSchLIVATPGRLLSLLQKKYVTTSNVKMVVLDEADEMLSRGFTEQIVSIMKFMNADIQIVLVSATL--PPEILE-L 209
Cdd:PRK00254 112 LGKYD--IIIATAEKFDSLLRHGSSWIKDVKLVVADEIHLIGSYDRGATLEMILTHMLGRAQILGLSATVgnAEELAEwL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 210 TRQFMRD---PVSI---LVKEAELTLD--GIRQYvvelQDAWKTEVVEDIYKvlsVQQGVIFCNS--------------- 266
Cdd:PRK00254 190 NAELVVSdwrPVKLrkgVFYQGFLFWEdgKIERF----PNSWESLVYDAVKK---GKGALVFVNTrrsaekealelakki 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 267 --------IGRVKELA---------EKLKSAGHT-LSCIHSELDQAERNKIMGEFRSGQTRILIATNIIARGIDVQNVSL 328
Cdd:PRK00254 263 krfltkpeLRALKELAdsleenptnEKLKKALRGgVAFHHAGLGRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRV 342
|
330 340 350
....*....|....*....|....*....|.
gi 159117719 329 VINyDIPREPETYLHRI---------GRSGR 350
Cdd:PRK00254 343 IIR-DTKRYSNFGWEDIpvleiqqmmGRAGR 372
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
261-352 |
8.66e-06 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They 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: 350180 [Multi-domain] Cd Length: 135 Bit Score: 44.77 E-value: 8.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 261 VIFCNSIGRVKELAEKLKSAGHTLSCIHSELDQAERNKIMGEFR--SGQTRILIATNIIARGIDVQNVSLVINYDIPREP 338
Cdd:cd18793 31 LIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNedPDIRVFLLSTKAGGVGLNLTAANRVILYDPWWNP 110
|
90
....*....|....
gi 159117719 339 ETYLHRIGRSGRFG 352
Cdd:cd18793 111 AVEEQAIDRAHRIG 124
|
|
| SF2_C_priA |
cd18804 |
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ... |
298-358 |
1.96e-05 |
|
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350191 [Multi-domain] Cd Length: 238 Bit Score: 45.70 E-value: 1.96e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 159117719 298 KIMGEFRSGQTRILIATNIIARGIDVQNVSLV--INYDI----P--REPE---TYLHRI-GRSGRFGRKGVAI 358
Cdd:cd18804 135 KLLDQFERGEIDILIGTQMIAKGLDFPNVTLVgiLNADSglnsPdfRASErafQLLTQVsGRAGRGDKPGKVI 207
|
|
| ComFA |
COG4098 |
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ... |
165-350 |
6.84e-05 |
|
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, recombination and repair];
Pssm-ID: 443274 [Multi-domain] Cd Length: 451 Bit Score: 44.87 E-value: 6.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 165 VVLDEAD-------EMLSRGfteqivsIMKFMNADIQIVLVSATlPPEILEltRQFMRD--PVSILVK--------EAEL 227
Cdd:COG4098 220 LIIDEVDafpysgdPMLQYA-------VKRARKPDGKLIYLTAT-PSKALQ--RQVKRGklKVVKLPAryhghplpVPKF 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 228 TLDG-IRQYVVelQDAWKTEVVEDIYKVLSVQQGV-IFCNSIGRVKELAEKLKSAGHTLS--CIHSElDQAERNKIMgEF 303
Cdd:COG4098 290 KWLGnWKKRLR--RGKLPRKLLKWLKKRLKEGRQLlIFVPTIELLEQLVALLQKLFPEERiaGVHAE-DPERKEKVQ-AF 365
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 159117719 304 RSGQTRILIATNIIARGIDVQNVS-LVINYDiprepetylHRI----------GRSGR 350
Cdd:COG4098 366 RDGEIPILVTTTILERGVTFPNVDvAVLGAD---------HPVfteaalvqiaGRVGR 414
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
262-363 |
8.57e-05 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases 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: 350182 [Multi-domain] Cd Length: 154 Bit Score: 42.54 E-value: 8.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 262 IFCNSIGRVKELAEKLKSAG-HtlsciHSELDQAERNKIMGEFRSGQTRILIATNIIARGIdvqNV--SLVI-------N 331
Cdd:cd18795 48 VFCSSRKECEKTAKDLAGIAfH-----HAGLTREDRELVEELFREGLIKVLVATSTLAAGV---NLpaRTVIikgtqryD 119
|
90 100 110
....*....|....*....|....*....|....*.
gi 159117719 332 YDIPRE--PETYLHRIGRSGR--FGRKGVAInFVTD 363
Cdd:cd18795 120 GKGYRElsPLEYLQMIGRAGRpgFDTRGEAI-IMTK 154
|
|
| PRK05580 |
PRK05580 |
primosome assembly protein PriA; Validated |
302-358 |
1.63e-04 |
|
primosome assembly protein PriA; Validated
Pssm-ID: 235514 [Multi-domain] Cd Length: 679 Bit Score: 43.61 E-value: 1.63e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 159117719 302 EFRSGQTRILIATNIIARGIDVQNVSLV--INYDI------PREPE-TY--LHRI-GRSGRFGRKGVAI 358
Cdd:PRK05580 475 QFARGEADILIGTQMLAKGHDFPNVTLVgvLDADLglfspdFRASErTFqlLTQVaGRAGRAEKPGEVL 543
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
288-349 |
2.04e-04 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 43.76 E-value: 2.04e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 159117719 288 HSELDQAERNKIMGEFRSGQTRILIATNIIARGIDVQNVSLVINYDIPREPETYLHRIGRSG 349
Cdd:PRK09751 308 HGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
260-330 |
2.17e-04 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins 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: 350186 [Multi-domain] Cd Length: 116 Bit Score: 40.62 E-value: 2.17e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 159117719 260 GVIFCNSIGRVKELAEKLKSAGHTLSCIHSELDQAERN---KIMGEFRSGQTRILIATNIIARGIDVQNVSLVI 330
Cdd:cd18799 9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGdeaLILLFFGELKPPILVTVDLLTTGVDIPEVDNVV 82
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
57-213 |
3.09e-04 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 41.03 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 57 GKDTIAQAQSGTGKT-AAFTIGMLQRIDIGLKSPQAIILSPTRELA------LQTLkvVDGIGSRLKVQVAQciggtqvd 129
Cdd:cd17922 1 GRNVLIAAPTGSGKTeAAFLPALSSLADEPEKGVQVLYISPLKALIndqerrLEEP--LDEIDLEIPVAVRH-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 130 DDIAAAQSCHLIVATPGRLLS--------LLQKKY-VTTSNVKMVVLDEADEMLS--RGFteQIVSIM----KFMNADIQ 194
Cdd:cd17922 71 GDTSQSEKAKQLKNPPGILITtpeslellLVNKKLrELFAGLRYVVVDEIHALLGskRGV--QLELLLerlrKLTGRPLR 148
|
170
....*....|....*....
gi 159117719 195 IVLVSATLPPeiLELTRQF 213
Cdd:cd17922 149 RIGLSATLGN--LEEAAAF 165
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
244-347 |
3.79e-04 |
|
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350176 [Multi-domain] Cd Length: 153 Bit Score: 40.70 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 244 KTEVVEDIYKVLS-VQQGVIFCNSIGRVKELAEKLKSAGhtlscIHSELDQAERNKIMGEFRSGQTRILIATNIIARGID 322
Cdd:cd18789 35 KLRALEELLKRHEqGDKIIVFTDNVEALYRYAKRLLKPF-----ITGETPQSEREEILQNFREGEYNTLVVSKVGDEGID 109
|
90 100
....*....|....*....|....*....
gi 159117719 323 V--QNVSLVI--NYDIPREpetYLHRIGR 347
Cdd:cd18789 110 LpeANVAIQIsgHGGSRRQ---EAQRLGR 135
|
|
| PriA |
COG1198 |
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, ... |
297-358 |
6.16e-04 |
|
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440811 [Multi-domain] Cd Length: 728 Bit Score: 42.03 E-value: 6.16e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 159117719 297 NKIMGEFRSGQTRILIATNIIARGIDVQNVSLV--INYDI------PREPE-TY--LHRI-GRSGRFGRKGVAI 358
Cdd:COG1198 521 EKLLEAFARGEADILVGTQMLAKGHDFPNVTLVgvLDADLglnspdFRAAErTFqlLTQVaGRAGRAEKPGEVL 594
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
92-201 |
2.45e-03 |
|
DEAH-box helicase domain of FANCM; 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. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM 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: 350791 [Multi-domain] Cd Length: 182 Bit Score: 38.46 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 92 IILSPTRELALQTLKVVDGIGSRLKVQVAQCIGGTQVDDDIAAAQSCHLIVATPGRLLSLLQKKYVTTSNVKMVVLDEAD 171
Cdd:cd18033 50 VFMAPTKPLVSQQIEACYKITGIPSSQTAELTGSVPPTKRAELWASKRVFFLTPQTLENDLKEGDCDPKSIVCLVIDEAH 129
|
90 100 110
....*....|....*....|....*....|
gi 159117719 172 EMLSRGFTEQIVSIMKFMNADIQIVLVSAT 201
Cdd:cd18033 130 RATGNYAYCQVVRELMRYNSHFRILALTAT 159
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
30-218 |
2.48e-03 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 38.67 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 30 DLLFGIFtyGYKIPSAIQSQAIVPIISGKDTIAQAQSGTGKTAAFTI-GMLQRidiGLkspqAIILSPTREL------AL 102
Cdd:cd17920 2 QILKEVF--GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLpALLLD---GV----TLVVSPLISLmqdqvdRL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 103 QTLKV-VDGIGSRLKVQVAQciggtQVDDDIAAAQSCHLIVaTPGRLLS-----LLQKKYVtTSNVKMVVLDEA------ 170
Cdd:cd17920 73 QQLGIrAAALNSTLSPEEKR-----EVLLRIKNGQYKLLYV-TPERLLSpdfleLLQRLPE-RKRLALIVVDEAhcvsqw 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 159117719 171 -----DEMLsrgfteQIvSIMKFMNADIQIVLVSATLPPEILE--LTRQFMRDPV 218
Cdd:cd17920 146 ghdfrPDYL------RL-GRLRRALPGVPILALTATATPEVREdiLKRLGLRNPV 193
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
244-355 |
2.48e-03 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 39.86 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 244 KTEVVEDIYK-VLSVQQG---VIFCNSIGRVKELAEKLKSAGhtlscIHSE-------------LDQAERNKIMGEFRSG 306
Cdd:PRK13766 348 KLEKLREIVKeQLGKNPDsriIVFTQYRDTAEKIVDLLEKEG-----IKAVrfvgqaskdgdkgMSQKEQIEILDKFRAG 422
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 159117719 307 QTRILIATNIIARGIDVQNVSLVINYD-IPREPETyLHRIGRSGRfGRKG 355
Cdd:PRK13766 423 EFNVLVSTSVAEEGLDIPSVDLVIFYEpVPSEIRS-IQRKGRTGR-QEEG 470
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
47-221 |
4.79e-03 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 37.78 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 47 QSQAIVPIISG------KDTIAQAQSGTGKTAAFTIGMLQRIDIGlksPQAIILSPTRELALQTLKVVDGIGSRLKVQVA 120
Cdd:cd17918 20 QAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAALLAYKNG---KQVAILVPTEILAHQHYEEARKFLPFINVELV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 121 qcIGGTQVDDdiaaAQSCHLIVATPGRLLSLLQKKyvttsNVKMVVLDEADEMlsrgFTEQIVSIMKFMNADiqIVLVSA 200
Cdd:cd17918 97 --TGGTKAQI----LSGISLLVGTHALLHLDVKFK-----NLDLVIVDEQHRF----GVAQREALYNLGATH--FLEATA 159
|
170 180
....*....|....*....|.
gi 159117719 201 TLPPEILELTRQFMRDpVSIL 221
Cdd:cd17918 160 TPIPRTLALALSGLLD-LSVI 179
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
46-170 |
9.14e-03 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef 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: 350793 [Multi-domain] Cd Length: 181 Bit Score: 37.11 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159117719 46 IQSQAIVPIISGKDTIAQAQSGTGKTAAFTIGMLQRIDigLKSPQAIILSPTRELALQ---TLKVVdgigSRLKVQVAQC 122
Cdd:cd18035 5 LYQVLIAAVALNGNTLIVLPTGLGKTIIAILVAADRLT--KKGGKVLILAPSRPLVEQhaeNLKRV----LNIPDKITSL 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 159117719 123 IGGTQVDDDIAAAQSCHLIVATPGRLLSLLQKKYVTTSNVKMVVLDEA 170
Cdd:cd18035 79 TGEVKPEERAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEA 126
|
|
| |
