|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
1-441 |
1.09e-149 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 433.42 E-value: 1.09e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 1 MSGFAELGLSSWLVAQCRQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDPYG-IFCLVLTPT 79
Cdd:COG0513 1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRaPQALILAPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 80 RELAYQIAEQFRVLGKPLGLKDCIIVGGMDMVAQALELSRKPHVVIATPGRLADHLRSsNTFSIKKIRFLVMDEADRLLE 159
Cdd:COG0513 81 RELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIER-GALDLSGVETLVLDEADRMLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 160 QGctdFTVDLEAILAAVPARRQTLLFSATLTDTLRELQGLATNQPFFWEAQAPVSTVEQLDQRYLLVPEKVKDAYLVHLI 239
Cdd:COG0513 160 MG---FIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 240 qrfqdEHEDW-SIIIFTNTCKTCQILCMMLRKFSFPTVALHSMMKQKERFAALAKFKSSIYRILIATDVASRGLDIPTVQ 318
Cdd:COG0513 237 -----RDEDPeRAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 319 VVINHNTPGLPKIYIHRVGRTARAGRQGQAITLVTQYDIHLVYAIEEQIKKKLEEFSVEEAEVLQiltqvnvvrreceiK 398
Cdd:COG0513 312 HVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVE--------------E 377
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1622894498 399 LEAAHFDEKKEINKRKQLILEGKDPDLEAKRKAELAKIKQKNR 441
Cdd:COG0513 378 KRLERLKPKIKEKLKGKKAGRGGRPGPKGERKARRGKRRRRKR 420
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
4-208 |
1.15e-131 |
|
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: 379.26 E-value: 1.15e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 4 FAELGLSSWLVAQCRQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDPYGIFCLVLTPTRELA 83
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 84 YQIAEQFRVLGKPLGLKDCIIVGGMDMVAQALELSRKPHVVIATPGRLADHLRSSN--TFSIKKIRFLVMDEADRLLEqg 161
Cdd:cd17955 81 YQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDdtTKVLSRVKFLVLDEADRLLT-- 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622894498 162 cTDFTVDLEAILAAVPARRQTLLFSATLTDTLRELQGLATNQPFFWE 208
Cdd:cd17955 159 -GSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFFWE 204
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
1-382 |
4.42e-99 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 305.57 E-value: 4.42e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 1 MSGFAELGLSSWLVAQCRQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDPYGIFCLVLTPTR 80
Cdd:PRK11776 3 MTAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 81 ELAYQIAEQFRVLGKPL-GLKDCIIVGGMDMVAQALELSRKPHVVIATPGRLADHLRsSNTFSIKKIRFLVMDEADRLLE 159
Cdd:PRK11776 83 ELADQVAKEIRRLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLR-KGTLDLDALNTLVLDEADRMLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 160 QGctdFTVDLEAILAAVPARRQTLLFSATLTDTLRELQGLATNQPFFWEAQAPVSTvEQLDQRYLLVPEKVKDAYLVHLI 239
Cdd:PRK11776 162 MG---FQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDL-PAIEQRFYEVSPDERLPALQRLL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 240 QRFQDEhedwSIIIFTNTCKTCQILCMMLRKFSFPTVALHSMMKQKERFAALAKF--KSSiyRILIATDVASRGLDIPTV 317
Cdd:PRK11776 238 LHHQPE----SCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFanRSC--SVLVATDVAARGLDIKAL 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622894498 318 QVVINHNTPGLPKIYIHRVGRTARAGRQGQAITLVTQYDIHLVYAIEEQIKKKLEEFSVEEAEVL 382
Cdd:PRK11776 312 EAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPSLSPL 376
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
4-204 |
1.11e-94 |
|
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: 284.98 E-value: 1.11e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 4 FAELGLSSWLVAQCRQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDPYGIFCLVLTPTRELA 83
Cdd:cd17954 2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTRELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 84 YQIAEQFRVLGKPLGLKDCIIVGGMDMVAQALELSRKPHVVIATPGRLADHLRSSNTFSIKKIRFLVMDEADRLLEQgct 163
Cdd:cd17954 82 QQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKGFSLKSLKFLVMDEADRLLNM--- 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622894498 164 DFTVDLEAILAAVPARRQTLLFSATLTDTLRELQGLATNQP 204
Cdd:cd17954 159 DFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNP 199
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
4-465 |
1.09e-90 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 282.99 E-value: 1.09e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 4 FAELGLSSWLVAQCRQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSE----DPYGIFCLVLTPT 79
Cdd:PRK11192 3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDfprrKSGPPRILILTPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 80 RELAYQIAEQFRVLGKPLGLKDCIIVGGMDMVAQALELSRKPHVVIATPGRLADHLRSSNtFSIKKIRFLVMDEADRLLE 159
Cdd:PRK11192 83 RELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEEN-FDCRAVETLILDEADRMLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 160 QGctdFTVDLEAILAAVPARRQTLLFSATLT-DTLRELQGLATNQPFFWEAQAPVSTVEQLDQRYLLVPEKV-KDAYLVH 237
Cdd:PRK11192 162 MG---FAQDIETIAAETRWRKQTLLFSATLEgDAVQDFAERLLNDPVEVEAEPSRRERKKIHQWYYRADDLEhKTALLCH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 238 LIQRFQDEhedwSIIIFTNTCKTCQILCMMLRKFSFPTVALHSMMKQKERFAALAKFKSSIYRILIATDVASRGLDIPTV 317
Cdd:PRK11192 239 LLKQPEVT----RSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 318 QVVINHNTPGLPKIYIHRVGRTARAGRQGQAITLVTQYDIHLVYAIEEQIKKKLEEFSVEEaevlqiltqvnvvrrecei 397
Cdd:PRK11192 315 SHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLKARVIDE------------------- 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622894498 398 kLEAAH-FDEKKEINKrkqlilegkdpdleaKRKAELAKIKQKNRRFKEKVEETLKRQKAGRVGHKGHP 465
Cdd:PRK11192 376 -LRPKTkAPSEKKTGK---------------PSKKVLAKRAEKKEKEKEKPKVKKRHRDTKNIGKRRKP 428
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
13-196 |
1.23e-80 |
|
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: 248.51 E-value: 1.23e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 13 LVAQCRQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDPY----GIFCLVLTPTRELAYQIAE 88
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKkkgrGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 89 QFRVLGKPLGLKDCIIVGGMDMVAQALELSRKPHVVIATPGRLADHLRsSNTFSIKKIRFLVMDEADRLLEQGctdFTVD 168
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIE-RGKLDLSNVKYLVLDEADRMLDMG---FEED 156
|
170 180
....*....|....*....|....*...
gi 1622894498 169 LEAILAAVPARRQTLLFSATLTDTLREL 196
Cdd:cd00268 157 VEKILSALPKDRQTLLFSATLPEEVKEL 184
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
4-441 |
4.95e-79 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 258.24 E-value: 4.95e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 4 FAELGLSSWLVAQCRQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDPYGIFCLVLTPTRELA 83
Cdd:PRK11634 8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTRELA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 84 YQIAEQFRVLGKPL-GLKDCIIVGGMDMVAQALELSRKPHVVIATPGRLADHLRSSnTFSIKKIRFLVMDEADRLLEQGc 162
Cdd:PRK11634 88 VQVAEAMTDFSKHMrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRG-TLDLSKLSGLVLDEADEMLRMG- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 163 tdFTVDLEAILAAVPARRQTLLFSATLTDTLRELQGLATNQPFFWEAQAPVSTVEQLDQRYLLVPEKVKDAYLVhliqRF 242
Cdd:PRK11634 166 --FIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALV----RF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 243 QdEHEDW-SIIIFTNTCKTCQILCMMLRKFSFPTVALHSMMKQKERFAALAKFKSSIYRILIATDVASRGLDIPTVQVVI 321
Cdd:PRK11634 240 L-EAEDFdAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 322 NHNTPGLPKIYIHRVGRTARAGRQGQAITLVTQYDIHLVYAIEEQIKKKLEEFSVEEAEvlqILTQVNVVRRECEI--KL 399
Cdd:PRK11634 319 NYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAE---LLGKRRLEKFAAKVqqQL 395
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1622894498 400 EAAHFDEKKEINKRKQLILEGKDPDLEAkRKAELAKIKQKNR 441
Cdd:PRK11634 396 ESSDLDQYRALLAKIQPTAEGEELDLET-LAAALLKMAQGER 436
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
1-380 |
8.99e-79 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 252.81 E-value: 8.99e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 1 MSgFAELGLSSWLVAQCRQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDPYG------IFCL 74
Cdd:PRK10590 1 MS-FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHakgrrpVRAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 75 VLTPTRELAYQIAEQFRVLGKPLGLKDCIIVGGMDMVAQALELSRKPHVVIATPGRLADhLRSSNTFSIKKIRFLVMDEA 154
Cdd:PRK10590 80 ILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLD-LEHQNAVKLDQVEILVLDEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 155 DRLLEQGctdFTVDLEAILAAVPARRQTLLFSATLTDTLRELQGLATNQPFFWEAQAPVSTVEQLDQRYLLVPEKVKDAY 234
Cdd:PRK10590 159 DRMLDMG---FIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKREL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 235 LVHLIQRfqdehEDW-SIIIFTNTCKTCQILCMMLRKFSFPTVALHSMMKQKERFAALAKFKSSIYRILIATDVASRGLD 313
Cdd:PRK10590 236 LSQMIGK-----GNWqQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLD 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622894498 314 IPTVQVVINHNTPGLPKIYIHRVGRTARAGRQGQAITLVTQYDIHLVYAIEEQIKKKLEEFSVEEAE 380
Cdd:PRK10590 311 IEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRIAIPGYE 377
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
4-353 |
8.18e-74 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 242.37 E-value: 8.18e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 4 FAELGLSSWLVAQCRQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDPY-----GIFCLVLTP 78
Cdd:PTZ00110 132 FEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLlrygdGPIVLVLAP 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 79 TRELAYQIAEQFRVLGKPLGLKDCIIVGGMDMVAQALELSRKPHVVIATPGRLADHLRSSNTfSIKKIRFLVMDEADRLL 158
Cdd:PTZ00110 212 TRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVT-NLRRVTYLVLDEADRML 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 159 EQGctdFTVDLEAILAAVPARRQTLLFSATLTdtlRELQGLATNQPffweAQAPV---------STVEQLDQRYLLVPEK 229
Cdd:PTZ00110 291 DMG---FEPQIRKIVSQIRPDRQTLMWSATWP---KEVQSLARDLC----KEEPVhvnvgsldlTACHNIKQEVFVVEEH 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 230 VKDAYLVHLIQRFQDEHEdwSIIIFTNTCKTCQILCMMLRKFSFPTVALHSMMKQKERFAALAKFKSSIYRILIATDVAS 309
Cdd:PTZ00110 361 EKRGKLKMLLQRIMRDGD--KILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVAS 438
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1622894498 310 RGLDIPTVQVVINHNTPGLPKIYIHRVGRTARAGRQGQAITLVT 353
Cdd:PTZ00110 439 RGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLT 482
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
13-204 |
4.58e-69 |
|
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: 219.05 E-value: 4.58e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 13 LVAQCRQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDPYGIF---CLVLTPTRELAYQIAEQ 89
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAatrVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 90 FRVLGKPLGLKDCIIVGGMDMVAQALELSRKPHVVIATPGRLADHLRSSNTFSIKKIRFLVMDEADRLLEQGctdFTVDL 169
Cdd:cd17947 81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSFDLDSIEILVLDEADRMLEEG---FADEL 157
|
170 180 190
....*....|....*....|....*....|....*
gi 1622894498 170 EAILAAVPARRQTLLFSATLTDTLRELQGLATNQP 204
Cdd:cd17947 158 KEILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKP 192
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
26-196 |
4.06e-62 |
|
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: 199.78 E-value: 4.06e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 26 TPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDPYGIFCLVLTPTRELAYQIAEQFRVLGKPLGLKDCIIV 105
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 106 GGMDMVAQALELsRKPHVVIATPGRLADHLRSSNTFsiKKIRFLVMDEADRLLEQGctdFTVDLEAILAAVPARRQTLLF 185
Cdd:pfam00270 81 GGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERKLL--KNLKLLVLDEAHRLLDMG---FGPDLEEILRRLPKKRQILLL 154
|
170
....*....|.
gi 1622894498 186 SATLTDTLREL 196
Cdd:pfam00270 155 SATLPRNLEDL 165
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
2-204 |
1.34e-60 |
|
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: 197.14 E-value: 1.34e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 2 SGFAELGLSSWLVAQCRQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKL--SEDPYGIFCLVLTPT 79
Cdd:cd17959 1 GGFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLkaHSPTVGARALILSPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 80 RELAYQIAEQFRVLGKPLGLKDCIIVGGMDMVAQALELSRKPHVVIATPGRLADHLRSSNtFSIKKIRFLVMDEADRLLE 159
Cdd:cd17959 81 RELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMN-LKLSSVEYVVFDEADRLFE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622894498 160 QGctdFTVDLEAILAAVPARRQTLLFSATLTDTLRELQGLATNQP 204
Cdd:cd17959 160 MG---FAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEP 201
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
4-482 |
8.07e-60 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 205.95 E-value: 8.07e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 4 FAELGLSSWLVAQCRQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKL----------SEDPYGifc 73
Cdd:PRK04537 11 FSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlsrpaladrkPEDPRA--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 74 LVLTPTRELAYQIAEQFRVLGKPLGLKDCIIVGGMDMVAQALELSRKPHVVIATPGRLADHLRSSNTFSIKKIRFLVMDE 153
Cdd:PRK04537 88 LILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVVSLHACEICVLDE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 154 ADRLLEQGctdFTVDLEAILAAVPAR--RQTLLFSATLTDTLRELQGLATNQPFFWEAQAPVSTVEQLDQRYLLVPEKVK 231
Cdd:PRK04537 168 ADRMFDLG---FIKDIRFLLRRMPERgtRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADEEK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 232 DAYLVHLIQRfqdeHEDWSIIIFTNTCKTCQILCMMLRKFSFPTVALHSMMKQKERFAALAKFKSSIYRILIATDVASRG 311
Cdd:PRK04537 245 QTLLLGLLSR----SEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 312 LDIPTVQVVINHNTPGLPKIYIHRVGRTARAGRQGQAITLVTQYDIHLVYAIEEQIKKKLEEFSVeEAEVLQILTqvnvv 391
Cdd:PRK04537 321 LHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKIPVEPV-TAELLTPLP----- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 392 rRECEIKLEAAHFDEkkeinkrkqlilEGKDPDLEAKRKAELAKIKQKNRRFKEKveeTLKRQKAGRVGHKGHPPRAPPG 471
Cdd:PRK04537 395 -RPPRVPVEGEEADD------------EAGDSVGTIFREAREQRAAEEQRRGGGR---SGPGGGSRSGSVGGGGRRDGAG 458
|
490
....*....|.
gi 1622894498 472 SHSGPVPSQGP 482
Cdd:PRK04537 459 ADGKPRPRRKP 469
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
2-372 |
3.17e-58 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 199.37 E-value: 3.17e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 2 SGFAELGLSSWLVAQCRQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDPYG-------IFCL 74
Cdd:PRK01297 87 TRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPkerymgePRAL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 75 VLTPTRELAYQIAEQFRVLGKPLGLKDCIIVGGMDMVAQALEL-SRKPHVVIATPGRLADHLRSSNTFsIKKIRFLVMDE 153
Cdd:PRK01297 167 IIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLeARFCDILVATPGRLLDFNQRGEVH-LDMVEVMVLDE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 154 ADRLLEQGctdFTVDLEAILAAVP--ARRQTLLFSATLTDTLRELQGLATNQPFFWEAQAPVSTVEQLDQRYLLVPEKVK 231
Cdd:PRK01297 246 ADRMLDMG---FIPQVRQIIRQTPrkEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDK 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 232 DAYLVHLIQRfqdehEDWS-IIIFTNTCKTCQILCMMLRKFSFPTVALHSMMKQKERFAALAKFKSSIYRILIATDVASR 310
Cdd:PRK01297 323 YKLLYNLVTQ-----NPWErVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGR 397
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622894498 311 GLDIPTVQVVINHNTPGLPKIYIHRVGRTARAGRQGQAITLVTQYDIHLVYAIEEQIKKKLE 372
Cdd:PRK01297 398 GIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKIS 459
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
4-200 |
1.39e-57 |
|
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: 190.01 E-value: 1.39e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 4 FAELGLSSWLVAQCRQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDPYGI----------FC 73
Cdd:cd17967 2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSvgrgrrkaypSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 74 LVLTPTRELAYQIAEQFRVLGKPLGLKDCIIVGGMDMVAQALELSRKPHVVIATPGRLADHLrSSNTFSIKKIRFLVMDE 153
Cdd:cd17967 82 LILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFI-ERGRISLSSIKFLVLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622894498 154 ADRLLEQGctdFTVDLEAILAA----VPARRQTLLFSATLTdtlRELQGLA 200
Cdd:cd17967 161 ADRMLDMG---FEPQIRKIVEHpdmpPKGERQTLMFSATFP---REIQRLA 205
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
4-382 |
4.24e-57 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 194.66 E-value: 4.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 4 FAELGLSSWLVAQCRQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDPYGIFCLVLTPTRELA 83
Cdd:PTZ00424 30 FDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTRELA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 84 YQIAEQFRVLGKPLGLKDCIIVGGMDMVAQALELSRKPHVVIATPGRLAD-----HLRssntfsIKKIRFLVMDEADRLL 158
Cdd:PTZ00424 110 QQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDmidkrHLR------VDDLKLFILDEADEML 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 159 EQGctdFTVDLEAILAAVPARRQTLLFSATLTDTLRELQGLATNQPFFWEAQAPVSTVEQLDQRYLLVPekvKDAYLvhl 238
Cdd:PTZ00424 184 SRG---FKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVE---KEEWK--- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 239 IQRFQDEHEDWSI---IIFTNTCKTCQILCMMLRKFSFPTVALHSMMKQKERFAALAKFKSSIYRILIATDVASRGLDIP 315
Cdd:PTZ00424 255 FDTLCDLYETLTItqaIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQ 334
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622894498 316 TVQVVINHNTPGLPKIYIHRVGRTARAGRQGQAITLVTQYDIHLVYAIEEQIKKKLEEFSVEEAEVL 382
Cdd:PTZ00424 335 QVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEVADYL 401
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
20-190 |
2.88e-54 |
|
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: 181.67 E-value: 2.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 20 LGLKQPTPVQLGCIP-AILEGRDCLGCAKTGSGKTAAFVLPILQKL-----SEDPYGI----FCLVLTPTRELAYQIAEQ 89
Cdd:cd17946 8 LGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERLlsqksSNGVGGKqkplRALILTPTRELAVQVKDH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 90 FRVLGKPLGLKDCIIVGGMDMVAQALELSRKPHVVIATPGRLADHLRSSNTF--SIKKIRFLVMDEADRLLEQGCTDftv 167
Cdd:cd17946 88 LKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHlaNLKSLRFLVLDEADRMLEKGHFA--- 164
|
170 180 190
....*....|....*....|....*....|
gi 1622894498 168 DLEAILAAVPA-------RRQTLLFSATLT 190
Cdd:cd17946 165 ELEKILELLNKdragkkrKRQTFVFSATLT 194
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
19-205 |
1.95e-52 |
|
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: 176.23 E-value: 1.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 19 QLGLKQPTPVQLGCIPAILE-GRDCLGCAKTGSGKTAAFVLPILQKLSEDP-----YGIFCLVLTPTRELAYQIAEQFR- 91
Cdd:cd17964 11 RMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKpagrrSGVSALIISPTRELALQIAAEAKk 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 92 VLGKPLGLKDCIIVGGMDMVAQALELSR-KPHVVIATPGRLADHLRSS---NTFsiKKIRFLVMDEADRLLEQGctdFTV 167
Cdd:cd17964 91 LLQGLRKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLENPgvaKAF--TDLDYLVLDEADRLLDMG---FRP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622894498 168 DLEAILAAVPAR----RQTLLFSATLTDTLRELQGLATNQPF 205
Cdd:cd17964 166 DLEQILRHLPEKnadpRQTLLFSATVPDEVQQIARLTLKKDY 207
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
18-206 |
4.23e-52 |
|
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: 174.79 E-value: 4.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 18 RQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKL------SEDpyGIFCLVLTPTRELAYQIAEQFR 91
Cdd:cd17941 6 KEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLyrerwtPED--GLGALIISPTRELAMQIFEVLR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 92 VLGKPLGLKDCIIVGGMDMVAQALELSRKpHVVIATPGRLADHLRSSNTFSIKKIRFLVMDEADRLLEQGctdFTVDLEA 171
Cdd:cd17941 84 KVGKYHSFSAGLIIGGKDVKEEKERINRM-NILVCTPGRLLQHMDETPGFDTSNLQMLVLDEADRILDMG---FKETLDA 159
|
170 180 190
....*....|....*....|....*....|....*
gi 1622894498 172 ILAAVPARRQTLLFSATLTDTLRELQGLATNQPFF 206
Cdd:cd17941 160 IVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEY 194
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
219-352 |
1.55e-51 |
|
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: 170.77 E-value: 1.55e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 219 LDQRYLLVPEKVKDAYLvhlIQRFQDEHEDWSIIIFTNTCKTCQILCMMLRKFSFPTVALHSMMKQKERFAALAKFKSSI 298
Cdd:cd18787 1 IKQLYVVVEEEEKKLLL---LLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGK 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1622894498 299 YRILIATDVASRGLDIPTVQVVINHNTPGLPKIYIHRVGRTARAGRQGQAITLV 352
Cdd:cd18787 78 VRVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
18-196 |
3.83e-51 |
|
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: 172.89 E-value: 3.83e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 18 RQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDPY--------GIFCLVLTPTRELAYQIAEQ 89
Cdd:cd17945 6 RKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPldeetkddGPYALILAPTRELAQQIEEE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 90 FRVLGKPLGLKDCIIVGGMDMVAQALELSRKPHVVIATPGRLADHLrSSNTFSIKKIRFLVMDEADRLLEQGctdFTVDL 169
Cdd:cd17945 86 TQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCL-ERRLLVLNQCTYVVLDEADRMIDMG---FEPQV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622894498 170 EAILAAVP--------------------ARRQTLLFSATLTDTLREL 196
Cdd:cd17945 162 TKILDAMPvsnkkpdteeaeklaasgkhRYRQTMMFTATMPPAVEKI 208
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
21-196 |
1.07e-49 |
|
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: 168.54 E-value: 1.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 21 GLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSE--DPYGIFCLVLTPTRELAYQIAEQFRVLGKPLG 98
Cdd:cd17957 9 GYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKprKKKGLRALILAPTRELASQIYRELLKLSKGTG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 99 LKDCIIVGGM-DMVAQALELSRKPHVVIATPGRLADHLRsSNTFSIKKIRFLVMDEADRLLEQGctdFTVDLEAILAAVP 177
Cdd:cd17957 89 LRIVLLSKSLeAKAKDGPKSITKYDILVSTPLRLVFLLK-QGPIDLSSVEYLVLDEADKLFEPG---FREQTDEILAACT 164
|
170 180
....*....|....*....|
gi 1622894498 178 ARR-QTLLFSATLTDTLREL 196
Cdd:cd17957 165 NPNlQRSLFSATIPSEVEEL 184
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
18-205 |
2.12e-49 |
|
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: 168.15 E-value: 2.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 18 RQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKL------SEDPYGIFCLVLTPTRELAYQIAEQFR 91
Cdd:cd17961 10 AKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlkakaeSGEEQGTRALILVPTRELAQQVSKVLE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 92 VL----GKPLGLKDciIVGGMDMVAQALELSRKPHVVIATPGRLADHLRSSNTFSIKKIRFLVMDEADRLLEQGCTDftv 167
Cdd:cd17961 90 QLtaycRKDVRVVN--LSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLLSTLKYLVIDEADLVLSYGYEE--- 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622894498 168 DLEAILAAVPARRQTLLFSATLTDTLRELQGLATNQPF 205
Cdd:cd17961 165 DLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
20-206 |
7.26e-49 |
|
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: 166.99 E-value: 7.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 20 LGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDPY------GIFCLVLTPTRELAYQIAEQFRVL 93
Cdd:cd17949 9 MGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPrvdrsdGTLALVLVPTRELALQIYEVLEKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 94 GKP-LGLKDCIIVGGMDMVAQALELSRKPHVVIATPGRLADHLRSSNTFSIKKIRFLVMDEADRLLEQGctdFTVDLEAI 172
Cdd:cd17949 89 LKPfHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQSFDVSNLRWLVLDEADRLLDMG---FEKDITKI 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622894498 173 LAAV-------------PARRQTLLFSATLTDTLRELQGLATNQPFF 206
Cdd:cd17949 166 LELLddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDPVY 212
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
4-368 |
1.37e-48 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 172.46 E-value: 1.37e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 4 FAELGLSSWLVAQCRQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDPYGIF-------CLVL 76
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDrkvnqprALIM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 77 TPTRELAYQIAEQFRVLGKPLGLKDCIIVGGMDMVAQALELSRKPHVVIATPGRLADHLRsSNTFSIKKIRFLVMDEADR 156
Cdd:PRK04837 90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAK-QNHINLGAIQVVVLDEADR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 157 LLEQGctdFTVDLEAILAAVPA--RRQTLLFSATLTDTLRELQGLATNQPFFWEAQAPVSTVEQLdQRYLLVPEKV-KDA 233
Cdd:PRK04837 169 MFDLG---FIKDIRWLFRRMPPanQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRI-KEELFYPSNEeKMR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 234 YLVHLIQrfqdehEDW--SIIIFTNTCKTCQILCMMLRKFSFPTVALHSMMKQKERFAALAKFKSSIYRILIATDVASRG 311
Cdd:PRK04837 245 LLQTLIE------EEWpdRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARG 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622894498 312 LDIPTVQVVINHNTPGLPKIYIHRVGRTARAGRQGQAITLV-TQYDIHLVyAIEEQIK 368
Cdd:PRK04837 319 LHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLAcEEYALNLP-AIETYIG 375
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
18-206 |
4.42e-48 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 164.59 E-value: 4.42e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 18 RQLGLKQPTPVQLGCIPAILEG-RDCLGCAKTGSGKTAAFVLPILQKLSEDPYGIfCLVLTPTRELAYQIAEQFRVLGKP 96
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKGGR-VLVLVPTRELAEQWAEELKKLGPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 97 LGLKDCIIVGGMDMVAQALEL-SRKPHVVIATPGRLADHLRsSNTFSIKKIRFLVMDEADRLLEQGctdFTVDLEAILAA 175
Cdd:smart00487 81 LGLKVVGLYGGDSKREQLRKLeSGKTDILVTTPGRLLDLLE-NDKLSLSNVDLVILDEAHRLLDGG---FGDQLEKLLKL 156
|
170 180 190
....*....|....*....|....*....|.
gi 1622894498 176 VPARRQTLLFSATLTDTLRELQGLATNQPFF 206
Cdd:smart00487 157 LPKNVQLLLLSATPPEEIENLLELFLNDPVF 187
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
4-200 |
3.05e-47 |
|
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: 164.37 E-value: 3.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 4 FAELGLSSWLVAQCRQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDpyGI-----------F 72
Cdd:cd18052 45 FEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKE--GLtassfsevqepQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 73 CLVLTPTRELAYQIAEQFRVLGKPLGLKDCIIVGGMDMVAQALELSRKPHVVIATPGRLADHLrSSNTFSIKKIRFLVMD 152
Cdd:cd18052 123 ALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFI-GRGKISLSKLKYLILD 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622894498 153 EADRLLEQGctdFTVDLEAILAA--VPA--RRQTLLFSATLTDtlrELQGLA 200
Cdd:cd18052 202 EADRMLDMG---FGPEIRKLVSEpgMPSkeDRQTLMFSATFPE---EIQRLA 247
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
19-196 |
1.37e-46 |
|
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: 160.43 E-value: 1.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 19 QLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKL-----SEDPYGIFCLVLTPTRELAYQIaeqFRVL 93
Cdd:cd17960 7 ELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrkaNLKKGQVGALIISPTRELATQI---YEVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 94 GK-----PLGLKDCIIVGGMDMVAQALELSR-KPHVVIATPGRLADHLRSSNT-FSIKKIRFLVMDEADRLLEQGctdFT 166
Cdd:cd17960 84 QSflehhLPKLKCQLLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLSRKADkVKVKSLEVLVLDEADRLLDLG---FE 160
|
170 180 190
....*....|....*....|....*....|
gi 1622894498 167 VDLEAILAAVPARRQTLLFSATLTDTLREL 196
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEEL 190
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
4-205 |
1.80e-46 |
|
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: 160.16 E-value: 1.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 4 FAELGLSSWLVAQCRQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDPYGIFCLVLTPTRELA 83
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 84 YQIAEQFRVLGKPLGLKDCIIVGGMDMVAQALELSRKPHVVIATPGRLADhLRSSNTFSIKKIRFLVMDEADRLLEQgct 163
Cdd:cd17940 81 LQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILD-LAKKGVADLSHCKTLVLDEADKLLSQ--- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622894498 164 DFTVDLEAILAAVPARRQTLLFSATLTDTLRELQGLATNQPF 205
Cdd:cd17940 157 DFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPY 198
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
18-206 |
2.14e-45 |
|
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: 157.14 E-value: 2.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 18 RQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLP---ILQKLSEDPY-GIFCLVLTPTRELAYQIAEQFRVL 93
Cdd:cd17942 6 EEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPaieLLYKLKFKPRnGTGVIIISPTRELALQIYGVAKEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 94 GKPLGLKDCIIVGGMDMVAQALELSRKPHVVIATPGRLADHLRSSNTFSIKKIRFLVMDEADRLLEQGctdFTVDLEAIL 173
Cdd:cd17942 86 LKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKNLQCLIIDEADRILEIG---FEEEMRQII 162
|
170 180 190
....*....|....*....|....*....|....
gi 1622894498 174 AAVPARRQTLLFSATLTDTLRELQGLA-TNQPFF 206
Cdd:cd17942 163 KLLPKRRQTMLFSATQTRKVEDLARISlKKKPLY 196
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
4-196 |
2.39e-45 |
|
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: 157.92 E-value: 2.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 4 FAELGLSSWLVAQCRQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPIL-----QKLSEDPYGIFCLVLTP 78
Cdd:cd17953 14 WSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFrhikdQRPVKPGEGPIGLIMAP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 79 TRELAYQIAEQFRVLGKPLGLKDCIIVGGMDMVAQALELSRKPHVVIATPGRLADHLRSSN--TFSIKKIRFLVMDEADR 156
Cdd:cd17953 94 TRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNgrVTNLRRVTYVVLDEADR 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622894498 157 LLEQGctdFTVDLEAILAAVPARRQTLLFSATLTDTLREL 196
Cdd:cd17953 174 MFDMG---FEPQIMKIVNNIRPDRQTVLFSATFPRKVEAL 210
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
4-359 |
3.50e-45 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 165.35 E-value: 3.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 4 FAELGLSSWLVAQCRQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKL-------SEDPYGIFCLVL 76
Cdd:PLN00206 123 FSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCctirsghPSEQRNPLAMVL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 77 TPTRELAYQIAEQFRVLGKPLGLKDCIIVGGMDMVAQALELSRKPHVVIATPGRLADhLRSSNTFSIKKIRFLVMDEADR 156
Cdd:PLN00206 203 TPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLID-LLSKHDIELDNVSVLVLDEVDC 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 157 LLEQGctdFTVDLEAILAAVPaRRQTLLFSATLTDTLRELQGLATNQPFFWEAQAPVSTVEQLDQRYLLVPEKVKDAYLV 236
Cdd:PLN00206 282 MLERG---FRDQVMQIFQALS-QPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQKLF 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 237 HLIQRFQdeHEDWSIIIFTNTCKTCQILCMMLRKFS-FPTVALHSMMKQKERFAALAKFKSSIYRILIATDVASRGLDIP 315
Cdd:PLN00206 358 DILKSKQ--HFKPPAVVFVSSRLGADLLANAITVVTgLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLL 435
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1622894498 316 TVQVVINHNTPGLPKIYIHRVGRTARAGRQGQAITLVTQYDIHL 359
Cdd:PLN00206 436 RVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNL 479
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
13-200 |
4.88e-45 |
|
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: 156.38 E-value: 4.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 13 LVAQCRQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDPY-----GIFCLVLTPTRELAYQIA 87
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPlergdGPIVLVLAPTRELAQQIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 88 EQFRVLGKPLGLKDCIIVGGMDMVAQALELSRKPHVVIATPGRLADHLRSSNTfSIKKIRFLVMDEADRLLEQGctdFTV 167
Cdd:cd17966 81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKT-NLRRVTYLVLDEADRMLDMG---FEP 156
|
170 180 190
....*....|....*....|....*....|...
gi 1622894498 168 DLEAILAAVPARRQTLLFSATLTdtlRELQGLA 200
Cdd:cd17966 157 QIRKIVDQIRPDRQTLMWSATWP---KEVRRLA 186
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
13-196 |
4.55e-43 |
|
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: 151.03 E-value: 4.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 13 LVAQCRQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDPY-----GIFCLVLTPTRELAYQIA 87
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRElekgeGPIAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 88 EQFRVLGKPLGLKDCIIVGGMDMVAQALELSRKPHVVIATPGRLADHLRSSNTfSIKKIRFLVMDEADRLLEQGctdFTV 167
Cdd:cd17952 81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKAT-NLQRVTYLVLDEADRMFDMG---FEY 156
|
170 180
....*....|....*....|....*....
gi 1622894498 168 DLEAILAAVPARRQTLLFSATLTDTLREL 196
Cdd:cd17952 157 QVRSIVGHVRPDRQTLLFSATFKKKIEQL 185
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
13-206 |
6.59e-43 |
|
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: 151.63 E-value: 6.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 13 LVAQCRQLGLKQPTPVQLGCIPAILEG---------RDCLGCAKTGSGKTAAFVLPILQKLSEDPYG-IFCLVLTPTREL 82
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPrLRALIVVPTKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 83 AYQIAEQFRVLGKPLGLKDCIIVGGMD--------MVAQALELSRKPHVVIATPGRLADHLRSSNTFSIKKIRFLVMDEA 154
Cdd:cd17956 81 VQQVYKVFESLCKGTGLKVVSLSGQKSfkkeqkllLVDTSGRYLSRVDILVATPGRLVDHLNSTPGFTLKHLRFLVIDEA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622894498 155 DRLLEQ----------------GCTDFTVDLEAILAAVPARR-QTLLFSATLTDTLRELQGLATNQPFF 206
Cdd:cd17956 161 DRLLNQsfqdwletvmkalgrpTAPDLGSFGDANLLERSVRPlQKLLFSATLTRDPEKLSSLKLHRPRL 229
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
21-195 |
7.08e-43 |
|
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: 150.95 E-value: 7.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 21 GLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLP-ILQKLSED---PY----GIFCLVLTPTRELA---YQIAEQ 89
Cdd:cd17951 9 GIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPlIMFALEQEkklPFikgeGPYGLIVCPSRELArqtHEVIEY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 90 FRVL----GKPlGLKDCIIVGGMDMVAQALELSRKPHVVIATPGRLADHLrSSNTFSIKKIRFLVMDEADRLLEQGctdF 165
Cdd:cd17951 89 YCKAlqegGYP-QLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDML-NKKKINLDICRYLCLDEADRMIDMG---F 163
|
170 180 190
....*....|....*....|....*....|
gi 1622894498 166 TVDLEAILAAVPARRQTLLFSATLTDTLRE 195
Cdd:cd17951 164 EEDIRTIFSYFKGQRQTLLFSATMPKKIQN 193
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
25-200 |
2.06e-42 |
|
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: 150.96 E-value: 2.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 25 PTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDPYGIFC----------------LVLTPTRELAYQIAE 88
Cdd:cd18051 44 PTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQGPGESLpsesgyygrrkqyplaLVLAPTRELASQIYD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 89 QFRVLGKPLGLKDCIIVGGMDMVAQALELSRKPHVVIATPGRLADHLRSSNtFSIKKIRFLVMDEADRLLEQGctdFTVD 168
Cdd:cd18051 124 EARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGK-IGLDYCKYLVLDEADRMLDMG---FEPQ 199
|
170 180 190
....*....|....*....|....*....|....*.
gi 1622894498 169 LEAILA--AVPAR--RQTLLFSATLTdtlRELQGLA 200
Cdd:cd18051 200 IRRIVEqdTMPPTgeRQTLMFSATFP---KEIQMLA 232
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
2-194 |
5.08e-42 |
|
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: 148.65 E-value: 5.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 2 SGFAELGLSSWLVAQCRQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDPYGIFCLVLTPTRE 81
Cdd:cd17950 2 SGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 82 LAYQIAEQFRVLGKPL-GLKDCIIVGGMDMVAQALELSRK-PHVVIATPGRLADHLRsSNTFSIKKIRFLVMDEADRLLE 159
Cdd:cd17950 82 LAFQISNEYERFSKYMpNVKTAVFFGGVPIKKDIEVLKNKcPHIVVGTPGRILALVR-EKKLKLSHVKHFVLDECDKMLE 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1622894498 160 QgcTDFTVDLEAILAAVPARRQTLLFSATLTDTLR 194
Cdd:cd17950 161 Q--LDMRRDVQEIFRATPHDKQVMMFSATLSKEIR 193
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
21-196 |
3.83e-40 |
|
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: 143.17 E-value: 3.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 21 GLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDPYGIFCLVLTPTRELAYQIAEQFRVLGKPL-GL 99
Cdd:cd17943 9 GFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKKIGKKLeGL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 100 KDCIIVGGMDmVAQALELSRKPHVVIATPGRLAdHLRSSNTFSIKKIRFLVMDEADRLLEQgctDFTVDLEAILAAVPAR 179
Cdd:cd17943 89 KCEVFIGGTP-VKEDKKKLKGCHIAVGTPGRIK-QLIELGALNVSHVRLFVLDEADKLMEG---SFQKDVNWIFSSLPKN 163
|
170
....*....|....*..
gi 1622894498 180 RQTLLFSATLTDTLREL 196
Cdd:cd17943 164 KQVIAFSATYPKNLDNL 180
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
4-189 |
6.46e-39 |
|
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: 140.15 E-value: 6.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 4 FAELGLSSWLVAQCRQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSedpygifCLVLTPTRELA 83
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIVV-------ALILEPSRELA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 84 YQIAEQFRVLGKPL---GLKDCIIVGGMDMVAQALELSRKPHVVIATPGRLADhLRSSNTFSIKKIRFLVMDEADRLLEQ 160
Cdd:cd17938 74 EQTYNCIENFKKYLdnpKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLED-LIKTGKLDLSSVRFFVLDEADRLLSQ 152
|
170 180 190
....*....|....*....|....*....|....*
gi 1622894498 161 GCTDFtvdLEAILAAVPA------RRQTLLFSATL 189
Cdd:cd17938 153 GNLET---INRIYNRIPKitsdgkRLQVIVCSATL 184
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
6-196 |
7.03e-38 |
|
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: 137.07 E-value: 7.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 6 ELGLSSWLVAQCRQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDPYGIFCLVLTPTRELAYQ 85
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 86 IAEQFRVLGKPLGLKDCIIVGGMDMVAQALELSRKPHVVIATPGRLADHLrSSNTFSIKKIRFLVMDEADRLLEQGctdF 165
Cdd:cd17939 81 IQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDML-QRRSLRTDKIKMFVLDEADEMLSRG---F 156
|
170 180 190
....*....|....*....|....*....|.
gi 1622894498 166 TVDLEAILAAVPARRQTLLFSATLTDTLREL 196
Cdd:cd17939 157 KDQIYDIFQFLPPETQVVLFSATMPHEVLEV 187
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
18-196 |
6.60e-37 |
|
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: 134.51 E-value: 6.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 18 RQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDPY------GIFCLVLTPTRELAYQI-AEQF 90
Cdd:cd17958 6 KKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIpreqrnGPGVLVLTPTRELALQIeAECS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 91 RVLGKplGLKDCIIVGGMDMVAQALELSRKPHVVIATPGRLADhLRSSNTFSIKKIRFLVMDEADRLLEQGctdFTVDLE 170
Cdd:cd17958 86 KYSYK--GLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLND-LQMNNVINLKSITYLVLDEADRMLDMG---FEPQIR 159
|
170 180
....*....|....*....|....*.
gi 1622894498 171 AILAAVPARRQTLLFSATLTDTLREL 196
Cdd:cd17958 160 KILLDIRPDRQTIMTSATWPDGVRRL 185
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
21-198 |
3.04e-36 |
|
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: 132.67 E-value: 3.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 21 GLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDPYGIFCLVLTPTRELAYQIAEQFRVLGKPL-GL 99
Cdd:cd17962 9 GYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKELMKGLpPM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 100 KDCIIVGGMDMVAQALELSRKPHVVIATPGRLADHLRSSnTFSIKKIRFLVMDEADRLLEQGCTDFTVDleaILAAVPAR 179
Cdd:cd17962 89 KTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQS-SVELDNIKIVVVDEADTMLKMGFQQQVLD---ILENISHD 164
|
170
....*....|....*....
gi 1622894498 180 RQTLLFSATLTDTLRELQG 198
Cdd:cd17962 165 HQTILVSATIPRGIEQLAG 183
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
1-196 |
1.14e-35 |
|
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: 133.60 E-value: 1.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 1 MSGFAELGLSSWLVAQCRQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDPY-----GIFCLV 75
Cdd:cd18050 61 VFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYlergdGPICLV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 76 LTPTRELAYQIAEQFRVLGKPLGLKDCIIVGGMDMVAQALELSRKPHVVIATPGRLADHLRSSNTfSIKKIRFLVMDEAD 155
Cdd:cd18050 141 LAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKT-NLRRCTYLVLDEAD 219
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622894498 156 RLLEQGctdFTVDLEAILAAVPARRQTLLFSATLTDTLREL 196
Cdd:cd18050 220 RMLDMG---FEPQIRKIVDQIRPDRQTLMWSATWPKEVRQL 257
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
4-196 |
1.51e-34 |
|
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: 129.36 E-value: 1.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 4 FAELGLSSWLVAQCRQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDPY-----GIFCLVLTP 78
Cdd:cd18049 26 FYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFlergdGPICLVLAP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 79 TRELAYQIAEQFRVLGKPLGLKDCIIVGGMDMVAQALELSRKPHVVIATPGRLADHLRSSNTfSIKKIRFLVMDEADRLL 158
Cdd:cd18049 106 TRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKT-NLRRCTYLVLDEADRML 184
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622894498 159 EQGctdFTVDLEAILAAVPARRQTLLFSATLTDTLREL 196
Cdd:cd18049 185 DMG---FEPQIRKIVDQIRPDRQTLMWSATWPKEVRQL 219
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
231-343 |
5.06e-31 |
|
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: 115.39 E-value: 5.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 231 KDAYLVHLIQrfqdEHEDWSIIIFTNTCKTCQIlCMMLRKFSFPTVALHSMMKQKERFAALAKFKSSIYRILIATDVASR 310
Cdd:pfam00271 2 KLEALLELLK----KERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAER 76
|
90 100 110
....*....|....*....|....*....|...
gi 1622894498 311 GLDIPTVQVVINHNTPGLPKIYIHRVGRTARAG 343
Cdd:pfam00271 77 GLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
13-202 |
2.07e-30 |
|
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: 117.85 E-value: 2.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 13 LVAQCRQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDPY-------GIFCLVLTPTRELAYQ 85
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLlaegpfnAPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 86 IAEQFRVLGKPLGLKDCIIVGG---MDMVAQALElsrKPHVVIATPGRLADhLRSSNTFSIKKIRFLVMDEADRLLEQgc 162
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITGGrtkRQIRNPHFE---EVDILVATPGALSK-LLTSRIYSLEQLRHLVLDEADTLLDD-- 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622894498 163 tDFTVDLEAILAAVP-------------ARRQTLLFSATLTDTLRELQGLATN 202
Cdd:cd17948 155 -SFNEKLSHFLRRFPlasrrsentdgldPGTQLVLVSATMPSGVGEVLSKVID 206
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
20-196 |
4.40e-30 |
|
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: 115.75 E-value: 4.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 20 LGLKQPTPVQLGCIPAILEG--RDCLGCAKTGSGKTAAFVLPILQKLseDPYGIF--CLVLTPTRELAYQIAEQFRVLGK 95
Cdd:cd17963 12 MGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRV--DPTLKSpqALCLAPTRELARQIGEVVEKMGK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 96 PLGLKDCIIVGGMDMVAqalelsRKP---HVVIATPGRLADHLRsSNTFSIKKIRFLVMDEADRLLEQGctDFTVDLEAI 172
Cdd:cd17963 90 FTGVKVALAVPGNDVPR------GKKitaQIVIGTPGTVLDWLK-KRQLDLKKIKILVLDEADVMLDTQ--GHGDQSIRI 160
|
170 180
....*....|....*....|....
gi 1622894498 173 LAAVPARRQTLLFSATLTDTLREL 196
Cdd:cd17963 161 KRMLPRNCQILLFSATFPDSVRKF 184
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
4-189 |
5.41e-30 |
|
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: 116.01 E-value: 5.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 4 FAELGLSSWLVAQCRQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDPYGIFCLVLTPTRELA 83
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 84 YQIAEQFRVLGKPLGLKDCIIVGGMDMVAQALELSRKPHVVIATPGRLADHLrSSNTFSIKKIRFLVMDEADRLLEQGct 163
Cdd:cd18046 81 QQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMI-NRRYLRTDYIKMFVLDEADEMLSRG-- 157
|
170 180
....*....|....*....|....*.
gi 1622894498 164 dFTVDLEAILAAVPARRQTLLFSATL 189
Cdd:cd18046 158 -FKDQIYDIFQKLPPDTQVVLLSATM 182
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
262-343 |
2.45e-25 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 99.21 E-value: 2.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 262 QILCMMLRKFSFPTVALHSMMKQKERFAALAKFKSSIYRILIATDVASRGLDIPTVQVVINHNTPGLPKIYIHRVGRTAR 341
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 1622894498 342 AG 343
Cdd:smart00490 81 AG 82
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
38-462 |
4.08e-25 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 108.57 E-value: 4.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 38 EGRDCLGCAKTGSGKT--AAFvlpILQKLSEDPygiFCLVLTPTRELAYQIAEQFRVLgkplgLKDCIIVGGmdmvaqal 115
Cdd:COG1061 99 GGGRGLVVAPTGTGKTvlALA---LAAELLRGK---RVLVLVPRRELLEQWAEELRRF-----LGDPLAGGG-------- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 116 ELSRKPHVVIATPGRLADHLRSSNTFsiKKIRFLVMDEADRLLEQGctdftvdLEAILAAVPARRqTLLFSATL--TDTL 193
Cdd:COG1061 160 KKDSDAPITVATYQSLARRAHLDELG--DRFGLVIIDEAHHAGAPS-------YRRILEAFPAAY-RLGLTATPfrSDGR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 194 RELQGLATNQPF---FWEAQ-----APVSTVEQLD------QRYLLVPEKVKDAYL------VHLIQRFQDEH-EDWSII 252
Cdd:COG1061 230 EILLFLFDGIVYeysLKEAIedgylAPPEYYGIRVdltderAEYDALSERLREALAadaerkDKILRELLREHpDDRKTL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 253 IFTNTCKTCQILCMMLRKFSFPTVALHSMMKQKERFAALAKFKSSIYRILIATDVASRGLDIPTVQVVI---NHNTPGLp 329
Cdd:COG1061 310 VFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAIllrPTGSPRE- 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 330 kiYIHRVGRTARAGRQGQAITLVTQYDIH---LVYAIEEQIKKKLEEFSVEEAEVLQILTQVNVVRRECEIKLEAAHFDE 406
Cdd:COG1061 389 --FIQRLGRGLRPAPGKEDALVYDFVGNDvpvLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPALEVKGELEEELL 466
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622894498 407 KKEINKRKQLILEGKDPDLEAKRKAELAKIKQKNRRFKEKVEETLKRQKAGRVGHK 462
Cdd:COG1061 467 EELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAK 522
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
4-204 |
1.24e-23 |
|
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: 98.31 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 4 FAELGLSSWLVAQCRQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDPYGIFCLVLTPTRELA 83
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 84 YQIAEQFRVLGKPLGLKDCIIVGGMDMVAQALELSRKPHVVIATPGRLADHLRSSNtFSIKKIRFLVMDEADRLLEQGct 163
Cdd:cd18045 81 VQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRS-LRTRHIKMLVLDEADEMLNKG-- 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622894498 164 dFTVDLEAILAAVPARRQTLLFSATLTDTLRELQGLATNQP 204
Cdd:cd18045 158 -FKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDP 197
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
27-188 |
7.93e-23 |
|
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: 96.07 E-value: 7.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 27 PVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDPYGIF------CLVLTPTRELAYQIAEQFRVLGKPLGLK 100
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKrgrapkVLVLAPTRELANQVTKDFKDITRKLSVA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 101 dCiIVGGMDMVAQALELSRKPHVVIATPGRLADHLRsSNTFSIKKIRFLVMDEADRLLEQGctdFTVDLEAILAAVPARR 180
Cdd:cd17944 95 -C-FYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQ-NGRLDLTKLKHVVLDEVDQMLDMG---FAEQVEEILSVSYKKD 168
|
170
....*....|...
gi 1622894498 181 -----QTLLFSAT 188
Cdd:cd17944 169 sednpQTLLFSAT 181
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
39-188 |
9.06e-21 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 88.61 E-value: 9.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 39 GRDCLGCAKTGSGKTAAFVLPILQKLseDPYGIFCLVLTPTRELAYQIAEQFRVLGKPlGLKDCIIVGGMDMVAQALELS 118
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLL--LKKGKKVLVLVPTKALALQTAERLRELFGP-GIRVAVLVGGSSAEEREKNKL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 119 RKPHVVIATPGRLADHLRSSNTFSIKKIRFLVMDEADRLLEQGcTDFTVDLEAILAAVPARRQTLLFSAT 188
Cdd:cd00046 78 GDADIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALLIDS-RGALILDLAVRKAGLKNAQVILLSAT 146
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
4-193 |
1.38e-19 |
|
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: 87.38 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 4 FAELGLSSWLVAQCRQLGLKQPTPVQLGCIPAILEG--RDCLGCAKTGSGKTAAFVLPILQKLSEDPYGIFCLVLTPTRE 81
Cdd:cd18048 20 FEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLSPTFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 82 LAYQIAEQFRVLGK-PLGLKDCIIVGGmDMVAQALELSRKphVVIATPGRLADHLRSSNTFSIKKIRFLVMDEADRLLE- 159
Cdd:cd18048 100 LALQTGKVVEEMGKfCVGIQVIYAIRG-NRPGKGTDIEAQ--IVIGTPGTVLDWCFKLRLIDVTNISVFVLDEADVMINv 176
|
170 180 190
....*....|....*....|....*....|....
gi 1622894498 160 QGCTDFTVDLEailAAVPARRQTLLFSATLTDTL 193
Cdd:cd18048 177 QGHSDHSVRVK---RSMPKECQMLLFSATFEDSV 207
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
24-196 |
9.05e-17 |
|
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: 79.73 E-value: 9.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 24 QPTPVQLGCIPAILEGRDC----------------LGCAKTGSGKTAAFVLPILQKLSEDPYGIF--------------- 72
Cdd:cd17965 30 KPSPIQTLAIKKLLKTLMRkvtkqtsneepklevfLLAAETGSGKTLAYLAPLLDYLKRQEQEPFeeaeeeyesakdtgr 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 73 --CLVLTPTRELAYQIAEQFRVLGKPLGLKDCIIVGGMD-MVAQALELSRKP-HVVIATPGRLADhLRSSNTFSIKKIRF 148
Cdd:cd17965 110 prSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGpSYQRLQLAFKGRiDILVTTPGKLAS-LAKSRPKILSRVTH 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622894498 149 LVMDEADRLLEQgctDFTVDLEAILAAVPARRQTLLFSAT----LTDTLREL 196
Cdd:cd17965 189 LVVDEADTLFDR---SFLQDTTSIIKRAPKLKHLILCSATipkeFDKTLRKL 237
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
26-191 |
1.34e-16 |
|
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: 77.69 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 26 TPVQLGCI-PAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEdpYGIFCLVLTPTRELAYQIAEQFRVLGKPLGLKDCII 104
Cdd:cd17921 3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRALAT--SGGKAVYIAPTRALVNQKEADLRERFGPLGKNVGLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 105 VGGMDMvaqALELSRKPHVVIATPGRLADHLRSSNTFSIKKIRFLVMDEAdRLLEQGctDFTVDLEAILAAVPAR---RQ 181
Cdd:cd17921 81 TGDPSV---NKLLLAEADILVATPEKLDLLLRNGGERLIQDVRLVVVDEA-HLIGDG--ERGVVLELLLSRLLRInknAR 154
|
170
....*....|
gi 1622894498 182 TLLFSATLTD 191
Cdd:cd17921 155 FVGLSATLPN 164
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
4-193 |
5.36e-16 |
|
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: 76.68 E-value: 5.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 4 FAELGLSSWLVAQCRQLGLKQPTPVQLGCIPAILEG--RDCLGCAKTGSGKTAAFVLPILQKLSEDPYGIFCLVLTPTRE 81
Cdd:cd18047 3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 82 LAYQIAEQFRVLGKplGLKDCIIVGGMDMVAQALELSRKPHVVIATPGRLADHLRSSNTFSIKKIRFLVMDEADRLL-EQ 160
Cdd:cd18047 83 LALQTGKVIEQMGK--FYPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIaTQ 160
|
170 180 190
....*....|....*....|....*....|...
gi 1622894498 161 GCTDFTVDLEAILaavPARRQTLLFSATLTDTL 193
Cdd:cd18047 161 GHQDQSIRIQRML---PRNCQMLLFSATFEDSV 190
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
231-353 |
8.04e-16 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 80.16 E-value: 8.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 231 KDAYLVHLIQRFQDEHEDWSIIIFTNTCKTCQILCMMLRKFSFPTVAL--------HSMMKQKERFAALAKFKSSIYRIL 302
Cdd:COG1111 336 KLSKLREILKEQLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFvgqaskegDKGLTQKEQIEILERFRAGEFNVL 415
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1622894498 303 IATDVASRGLDIPTVQVVINHNtPGLPKI-YIHRVGRTARaGRQGQAITLVT 353
Cdd:COG1111 416 VATSVAEEGLDIPEVDLVIFYE-PVPSEIrSIQRKGRTGR-KREGRVVVLIA 465
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
228-354 |
5.53e-13 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 71.44 E-value: 5.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 228 EKVKDaylvhLIQRFQDEHEDWSIIIFTNTCKTCQILCMMLRKFSFPTVAL--------HSMMKQKERFAALAKFKSSIY 299
Cdd:PRK13766 350 EKLRE-----IVKEQLGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFvgqaskdgDKGMSQKEQIEILDKFRAGEF 424
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622894498 300 RILIATDVASRGLDIPTVQVVInhntpglpkIY---------IHRVGRTARaGRQGQAITLVTQ 354
Cdd:PRK13766 425 NVLVSTSVAEEGLDIPSVDLVI---------FYepvpseirsIQRKGRTGR-QEEGRVVVLIAK 478
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
12-189 |
6.43e-13 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 70.69 E-value: 6.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 12 WLVAQCRQLGLKQPTPVQLGCIPA-ILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDPYGIFclvLTPTRELAYQIAEQF 90
Cdd:COG1204 10 KVIEFLKERGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTLIAELAILKALLNGGKALY---IVPLRALASEKYREF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 91 RVLGKPLGLKDCIIVGGMDMVAQALElsrKPHVVIATPGRLaDHLRSSNTFSIKKIRFLVMDEA------DRlleqGCTd 164
Cdd:COG1204 87 KRDFEELGIKVGVSTGDYDSDDEWLG---RYDILVATPEKL-DSLLRNGPSWLRDVDLVVVDEAhliddeSR----GPT- 157
|
170 180
....*....|....*....|....*...
gi 1622894498 165 ftvdLEAILA---AVPARRQTLLFSATL 189
Cdd:COG1204 158 ----LEVLLArlrRLNPEAQIVALSATI 181
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
238-351 |
5.96e-11 |
|
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: 60.45 E-value: 5.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 238 LIQRFQDEHE--DWSIIIFTNTCKTCQILCMMLRKFSfPTVALH-----------SMMKQKERFAALAKFKSSIYRILIA 304
Cdd:cd18801 18 VKEHFKKKQEgsDTRVIIFSEFRDSAEEIVNFLSKIR-PGIRATrfigqasgkssKGMSQKEQKEVIEQFRKGGYNVLVA 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1622894498 305 TDVASRGLDIPTVQVVINHNTPGLPKIYIHRVGRTARaGRQGQAITL 351
Cdd:cd18801 97 TSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR-KRQGRVVVL 142
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
23-97 |
6.93e-11 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 64.74 E-value: 6.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 23 KQPTPVQLGCIPAILEGRDCLGCAKTGSGKT-AAFvLPILQKLSEDPY------GIFCLVLTPTRELAYQIAeqfRVLGK 95
Cdd:COG1201 23 GAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPRpgelpdGLRVLYISPLKALANDIE---RNLRA 98
|
..
gi 1622894498 96 PL 97
Cdd:COG1201 99 PL 100
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
13-379 |
1.32e-10 |
|
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: 63.70 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 13 LVAQCRQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDPyGIFCLVLTPTRELAY-QIAEqFR 91
Cdd:COG1205 45 LRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDP-GATALYLYPTKALARdQLRR-LR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 92 VLGKPLGLKDCIIV--GGMDMVAQAlELSRKPHVVIATP-----GRLADHLRSSNTFSikKIRFLVMDEA---------- 154
Cdd:COG1205 123 ELAEALGLGVRVATydGDTPPEERR-WIREHPDIVLTNPdmlhyGLLPHHTRWARFFR--NLRYVVIDEAhtyrgvfgsh 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 155 -----DRLLEqgctdftvdleaILAAVPARRQTLLFSATL---TDTLRELqglaTNQPFFW--EAQAPVSTVEqldqRYL 224
Cdd:COG1205 200 vanvlRRLRR------------ICRHYGSDPQFILASATIgnpAEHAERL----TGRPVTVvdEDGSPRGERT----FVL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 225 LVPEKVKD----------AYLV-HLIQRfqdeheDWSIIIFTNTCKTCQILCMMLRK-FSFPTVAL-----HSMMKQKER 287
Cdd:COG1205 260 WNPPLVDDgirrsalaeaARLLaDLVRE------GLRTLVFTRSRRGAELLARYARRaLREPDLADrvaayRAGYLPEER 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 288 FAALAKFKSSIYRILIATDVASRGLDIPTVQVVINHNTPGLPKIYIHRVGRTARAGRQGQAItLVTQYDihlvyAIEEQI 367
Cdd:COG1205 334 REIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV-LVAGDD-----PLDQYY 407
|
410
....*....|....*
gi 1622894498 368 KKKLEEF---SVEEA 379
Cdd:COG1205 408 VRHPEELferPPEAA 422
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
222-342 |
4.96e-09 |
|
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: 54.90 E-value: 4.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 222 RYLLVPEKVKDayLVHLIQRFQDEHEDWSIIIFTNTCKTCQILCMML----RKFSFPTVAL-----------HSMMKQKE 286
Cdd:cd18802 1 EEIVVIPKLQK--LIEILREYFPKTPDFRGIIFVERRATAVVLSRLLkehpSTLAFIRCGFligrgnssqrkRSLMTQRK 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622894498 287 RFAALAKFKSSIYRILIATDVASRGLDIPTVQVVINHNTPGLPKIYIHRVGRtARA 342
Cdd:cd18802 79 QKETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARA 133
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
39-191 |
5.83e-09 |
|
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: 55.28 E-value: 5.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 39 GRDCLGCAKTGSGKTAAFVLPILQKLSEDPY-GIFCLVLTPTRELayqIAEQFRVLGKPLglkDCIIVG-------GmDm 110
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEkGVQVLYISPLKAL---INDQERRLEEPL---DEIDLEipvavrhG-D- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 111 VAQALE---LSRKPHVVIATPGRLADHL---RSSNTFSikKIRFLVMDEADRLL--EQGCTDFTVdLEAI--LAAVPARR 180
Cdd:cd17922 73 TSQSEKakqLKNPPGILITTPESLELLLvnkKLRELFA--GLRYVVVDEIHALLgsKRGVQLELL-LERLrkLTGRPLRR 149
|
170
....*....|.
gi 1622894498 181 QTLlfSATLTD 191
Cdd:cd17922 150 IGL--SATLGN 158
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
46-373 |
1.19e-08 |
|
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: 56.67 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 46 AKTGSGKT---AAFVLPILQKLSEDPyGIFCLvltPTRELAYQIAEQFR-VLGKPLGLKDCIIVGGMDMVAQALELSR-- 119
Cdd:cd09639 6 APTGYGKTeaaLLWALHSLKSQKADR-VIIAL---PTRATINAMYRRAKeAFGETGLYHSSILSSRIKEMGDSEEFEHlf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 120 -------------------KPHVVIATPGRLADHLRSsnTFSIKKIRfLVMDEADRLLeqgctDFTvdLEAILAAVPARR 180
Cdd:cd09639 82 plyihsndtlfldpitvctIDQVLKSVFGEFGHYEFT--LASIANSL-LIFDEVHFYD-----EYT--LALILAVLEVLK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 181 QT----LLFSATLTDTLRELqGLATNQPFFWEAQaPVSTVEQLDQRYLLVPEKVKDAYLVHLIQRFQDEHedwSIIIFTN 256
Cdd:cd09639 152 DNdvpiLLMSATLPKFLKEY-AEKIGYVEENEPL-DLKPNERAPFIKIESDKVGEISSLERLLEFIKKGG---SVAIIVN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 257 TCKTCQILCMMLRK--FSFPTVALHSMMKQKERFAA----LAKFKSSIYRILIATDVASRGLDIpTVQVVINHNTPglPK 330
Cdd:cd09639 227 TVDRAQEFYQQLKEkgPEEEIMLIHSRFTEKDRAKKeaelLLEFKKSEKFVIVATQVIEASLDI-SVDVMITELAP--ID 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1622894498 331 IYIHRVGRTARAGRQGQ----AITLVTQYDIHLVYAIE--EQIKKKLEE 373
Cdd:cd09639 304 SLIQRLGRLHRYGEKNGeevyIITDAPDGKGQKPYPYDlvERTIELLEE 352
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
26-153 |
6.06e-08 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 55.28 E-value: 6.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 26 TPVQLGCIPAILEGRDCLGCAKTGSGKT-AAF--VLPILQKLSED---PYGIFCLVLTPTRELAYQIaeqFRVLGKPL-G 98
Cdd:PRK13767 34 TPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFlaIIDELFRLGREgelEDKVYCLYVSPLRALNNDI---HRNLEEPLtE 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622894498 99 LKDCIIVGGMDM----VA-----------QALeLSRKPHVVIATPGRLADHLRSSNtFS--IKKIRFLVMDE 153
Cdd:PRK13767 111 IREIAKERGEELpeirVAirtgdtssyekQKM-LKKPPHILITTPESLAILLNSPK-FRekLRTVKWVIVDE 180
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
220-347 |
6.73e-08 |
|
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: 51.44 E-value: 6.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 220 DQRYLLVPEKVKDAYLVHLIQRFQDEHEDWSIIIFTNTCKTCQILCMMLRKFSFPTVALHSMMKQKERFAALAKFKSSIY 299
Cdd:cd18794 2 PNLFYSVRPKDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKI 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1622894498 300 RILIATDVASRGLDIPTVQVVINHntpGLPKI---YIHRVGrtaRAGRQGQ 347
Cdd:cd18794 82 QVIVATVAFGMGIDKPDVRFVIHY---SLPKSmesYYQESG---RAGRDGL 126
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
18-207 |
1.41e-07 |
|
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: 51.77 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 18 RQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILqkLSEdpyGIfCLVLTPTRELayqIAEQFRVLgKPL 97
Cdd:cd17920 6 EVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPAL--LLD---GV-TLVVSPLISL---MQDQVDRL-QQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 98 GLKDCIIVGGMDM--VAQALELSRKP--HVVIATPGRLA-----DHLRSSNTFsiKKIRFLVMDEADRLLEQGcTDFTVD 168
Cdd:cd17920 76 GIRAAALNSTLSPeeKREVLLRIKNGqyKLLYVTPERLLspdflELLQRLPER--KRLALIVVDEAHCVSQWG-HDFRPD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622894498 169 ---LEAILAAVPaRRQTLLFSATLTDTLRE--LQGLATNQPFFW 207
Cdd:cd17920 153 ylrLGRLRRALP-GVPILALTATATPEVREdiLKRLGLRNPVIF 195
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
35-154 |
3.68e-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: 50.28 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 35 AILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDPyGIFCLVLTPTRELAYQIAEQFRVLGKPLGLKdcIIV----GGMDM 110
Cdd:cd17923 11 AARAGRSVVVTTGTASGKSLCYQLPILEALLRDP-GSRALYLYPTKALAQDQLRSLRELLEQLGLG--IRVatydGDTPR 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1622894498 111 VAQALELSRKPHVVIATP-----GRLADHLRSSNTFSikKIRFLVMDEA 154
Cdd:cd17923 88 EERRAIIRNPPRILLTNPdmlhyALLPHHDRWARFLR--NLRYVVLDEA 134
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
48-154 |
4.20e-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: 50.34 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 48 TGSGKTAAFVLPILQKLS----EDPYGIFCLVLTPTRELAYQiaeQFRVLGKPLGLKDCIIVGGMDMVAQA----LELSR 119
Cdd:cd18034 25 TGSGKTLIAVMLIKEMGElnrkEKNPKKRAVFLVPTVPLVAQ---QAEAIRSHTDLKVGEYSGEMGVDKWTkerwKEELE 101
|
90 100 110
....*....|....*....|....*....|....*
gi 1622894498 120 KPHVVIATPGRLADHLRSSNtFSIKKIRFLVMDEA 154
Cdd:cd18034 102 KYDVLVMTAQILLDALRHGF-LSLSDINLLIFDEC 135
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
28-194 |
4.50e-07 |
|
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: 50.43 E-value: 4.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 28 VQLGCIPAILEG-RDCLGCAKTGSGKTAAFVLPILQKLSE----DPYGIFCLVLTPTRELAYQIAEQFRVLGKPLGLKDC 102
Cdd:cd18023 5 IQSEVFPDLLYSdKNFVVSAPTGSGKTVLFELAILRLLKErnplPWGNRKVVYIAPIKALCSEKYDDWKEKFGPLGLSCA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 103 IIVGgmDMVAQALELSRKPHVVIATPGR--LADHLRSSNTFSIKKIRFLVMDEADRLLE-QGCTdftvdLEAILaavpAR 179
Cdd:cd18023 85 ELTG--DTEMDDTFEIQDADIILTTPEKwdSMTRRWRDNGNLVQLVALVLIDEVHIIKEnRGAT-----LEVVV----SR 153
|
170
....*....|....*.
gi 1622894498 180 RQTL-LFSATLTDTLR 194
Cdd:cd18023 154 MKTLsSSSELRGSTVR 169
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
212-352 |
5.95e-07 |
|
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: 49.26 E-value: 5.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 212 PVST----VEQLDQRYLLVPEKVKDAYLVHLIQRFQDEHEDWSIiiftntcKTCQILCMMLRKFSFP--TVAL-HSMMKQ 284
Cdd:cd18811 1 PITTylifHTRLDKVYEFVREEIAKGRQAYVIYPLIEESEKLDL-------KAAVAMYEYLKERFRPelNVGLlHGRLKS 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 285 KERFAALAKFKSSIYRILIATDVASRGLDIP--TVQVVINHNTPGLPKIYIHRvGRTARAGRQGQAITLV 352
Cdd:cd18811 74 DEKDAVMAEFREGEVDILVSTTVIEVGVDVPnaTVMVIEDAERFGLSQLHQLR-GRVGRGDHQSYCLLVY 142
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
6-390 |
6.38e-07 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 52.13 E-value: 6.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 6 ELGLSSWLVAQCRQLGLKQPTPVQLGCIPA-ILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDpyGIFCLVLTPTRELAY 84
Cdd:PRK00254 5 ELRVDERIKRVLKERGIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIVMVNKLLRE--GGKAVYLVPLKALAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 85 QIAEQFRVLGKpLGLKDCIIVGGMDMVAQALElsrKPHVVIATPGRLADHLRSSNTFsIKKIRFLVMDEADRLleqGCTD 164
Cdd:PRK00254 83 EKYREFKDWEK-LGLRVAMTTGDYDSTDEWLG---KYDIIIATAEKFDSLLRHGSSW-IKDVKLVVADEIHLI---GSYD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 165 FTVDLEAILAAVPARRQTLLFSATLTDTlREL-------------------QGLATNQPFFWEAQAPVSTVEQLDQRYLL 225
Cdd:PRK00254 155 RGATLEMILTHMLGRAQILGLSATVGNA-EELaewlnaelvvsdwrpvklrKGVFYQGFLFWEDGKIERFPNSWESLVYD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 226 VPEKVKDAY---------------LVHLIQRFQDEHEDWSIIIFTNTCK---TCQILCMMLRKfsfpTVAL-HSMMKQKE 286
Cdd:PRK00254 234 AVKKGKGALvfvntrrsaekealeLAKKIKRFLTKPELRALKELADSLEenpTNEKLKKALRG----GVAFhHAGLGRTE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 287 RFAALAKFKSSIYRILIATDVASRGLDIPTVQVVI-------NHNTPGLPKIYIHRVgrTARAGR-----QGQAITLVTQ 354
Cdd:PRK00254 310 RVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIrdtkrysNFGWEDIPVLEIQQM--MGRAGRpkydeVGEAIIVATT 387
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1622894498 355 YDIHLVyaIEEQIKKKLEEF-------SVEEAEVLQILTQVNV 390
Cdd:PRK00254 388 EEPSKL--MERYIFGKPEKLfsmlsneSAFRSQVLALITNFGV 428
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
27-189 |
6.82e-07 |
|
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: 49.25 E-value: 6.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 27 PVQLGCIPA-ILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDPYGIFclvLTPTRELAYQIAEQFRVLgKPLGLKDCIIV 105
Cdd:cd18028 4 PPQAEAVRAgLLKGENLLISIPTASGKTLIAEMAMVNTLLEGGKALY---LVPLRALASEKYEEFKKL-EEIGLKVGIST 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 106 GGMDMVAQALElsrKPHVVIATPGRLADHLRSSNTFsIKKIRFLVMDE----ADRllEQGCTdftvdLEAILA---AVPA 178
Cdd:cd18028 80 GDYDEDDEWLG---DYDIIVATYEKFDSLLRHSPSW-LRDVGVVVVDEihliSDE--ERGPT-----LESIVArlrRLNP 148
|
170
....*....|.
gi 1622894498 179 RRQTLLFSATL 189
Cdd:cd18028 149 NTQIIGLSATI 159
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
296-352 |
1.14e-06 |
|
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: 46.16 E-value: 1.14e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622894498 296 SSIYRILIATDVASRGLDIPTVQVVINHNTPGLPKIYIHRVGRTARAG-RQGQAITLV 352
Cdd:cd18785 20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGkDEGEVILFV 77
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
235-322 |
1.19e-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: 47.86 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 235 LVHLIQRFQDEHEdwSIIIFTNTCKTCQILCMMLRKFSFPTVALHSMMKQKERFAALAKFK--SSIYRILIATDVASRGL 312
Cdd:cd18793 16 LLELLEELREPGE--KVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNedPDIRVFLLSTKAGGVGL 93
|
90
....*....|
gi 1622894498 313 DIPTVQVVIN 322
Cdd:cd18793 94 NLTAANRVIL 103
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
226-359 |
1.41e-05 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 47.44 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 226 VPEKVKDAYLVHLIQRFQDEhedwSIIIFTNTCKTCQILCMMLRKFSFPTVALHSMMKQKERFAALAKFKSSIYRILIAT 305
Cdd:COG0514 212 KPPDDKLAQLLDFLKEHPGG----SGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT 287
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1622894498 306 dVA-SRGLDIPTVQVVINHNTPGLPKIYIHRVGRTARAGRQGQAITLVTQYDIHL 359
Cdd:COG0514 288 -IAfGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAI 341
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
43-208 |
1.81e-05 |
|
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 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: 350778 [Multi-domain] Cd Length: 199 Bit Score: 45.50 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 43 LGCAKTGSGKTAAFVLPILQKLSE--DPYGI-----FCLV-LTPTRELAYQIAEQFRVLGKPLGLKDCIIVGGMDMVAQA 114
Cdd:cd18020 21 LICAPTGAGKTNIAMLTILHEIRQhvNQGGVikkddFKIVyIAPMKALAAEMVEKFSKRLAPLGIKVKELTGDMQLTKKE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 115 LElsrKPHVVIATPGRLADHLRSSN--TFSIKKIRFLVMDEADRLLEqgctdftvDLEAILAAVPARRQTLLFSatlTDT 192
Cdd:cd18020 101 IA---ETQIIVTTPEKWDVVTRKSSgdVALSQLVRLLIIDEVHLLHD--------DRGPVIESLVARTLRQVES---TQS 166
|
170
....*....|....*.
gi 1622894498 193 LRELQGLATNQPFFWE 208
Cdd:cd18020 167 MIRIVGLSATLPNYLD 182
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
27-355 |
4.08e-05 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 46.43 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 27 PVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILqkLSEdpyGIfCLVLTPTRELayqIAEQFRVLGKPlGLKDCIIVG 106
Cdd:PLN03137 463 PNQREIINATMSGYDVFVLMPTGGGKSLTYQLPAL--ICP---GI-TLVISPLVSL---IQDQIMNLLQA-NIPAASLSA 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 107 GMDMVAQaLELSR-------KPHVVIATPGRLAD------HLRSSNTFSIKKiRFlVMDEAdRLLEQGCTDFTVDLE--A 171
Cdd:PLN03137 533 GMEWAEQ-LEILQelsseysKYKLLYVTPEKVAKsdsllrHLENLNSRGLLA-RF-VIDEA-HCVSQWGHDFRPDYQglG 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 172 ILAAVPARRQTLLFSATLTDTLRE--LQGL----------ATNQPFFWeaqapvstveqldqrYLLVPEKVKdayLVHLI 239
Cdd:PLN03137 609 ILKQKFPNIPVLALTATATASVKEdvVQALglvncvvfrqSFNRPNLW---------------YSVVPKTKK---CLEDI 670
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 240 QRFQDE-HEDWSIIIFTNTCKTCQILCMMLRKFSFPTVALHSMMKQKERFAALAKFKSSIYRILIATDVASRGLDIPTVQ 318
Cdd:PLN03137 671 DKFIKEnHFDECGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVR 750
|
330 340 350
....*....|....*....|....*....|....*..
gi 1622894498 319 VVINHNTPGLPKIYIHRVGrtaRAGRQGQAITLVTQY 355
Cdd:PLN03137 751 FVIHHSLPKSIEGYHQECG---RAGRDGQRSSCVLYY 784
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
21-357 |
4.88e-05 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 45.86 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 21 GLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQK------------LSED------PYGIF--CLVLTPTR 80
Cdd:PRK11057 22 GYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLdgltlvvsplisLMKDqvdqllANGVAaaCLNSTQTR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 81 ElayqiaEQFRVLgkplglkdciivggMDMVAQALELsrkphVVIAtPGRLA-----DHLRSSNtfsikkIRFLVMDEAd 155
Cdd:PRK11057 102 E------QQLEVM--------------AGCRTGQIKL-----LYIA-PERLMmdnflEHLAHWN------PALLAVDEA- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 156 RLLEQGCTDFTVDLEAiLAAVPARRQTLLF---SATLTDTLRE--LQGLATNQPFFWeaqapVSTVEQLDQRYLLVpEKV 230
Cdd:PRK11057 149 HCISQWGHDFRPEYAA-LGQLRQRFPTLPFmalTATADDTTRQdiVRLLGLNDPLIQ-----ISSFDRPNIRYTLV-EKF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 231 KDaylVHLIQRFQDEHEDWSIIIFTNTCKTCQILCMMLRKFSFPTVALHSMMKQKERFAALAKFKSSIYRILIATDVASR 310
Cdd:PRK11057 222 KP---LDQLMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGM 298
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1622894498 311 GLDIPTVQVVINHNTPGLPKIYIHRVGRTARAGRQGQAITLVTQYDI 357
Cdd:PRK11057 299 GINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPADM 345
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
33-156 |
5.60e-05 |
|
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: 43.66 E-value: 5.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 33 IPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEdpYGIFCLVLTPTRELAYQIAEQFR-VLGKPLglkDCIIVGGMDMV 111
Cdd:cd18035 10 IAAVALNGNTLIVLPTGLGKTIIAILVAADRLTK--KGGKVLILAPSRPLVEQHAENLKrVLNIPD---KITSLTGEVKP 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1622894498 112 AQALELSRKPHVVIATPGRLADHLRSSNtFSIKKIRFLVMDEADR 156
Cdd:cd18035 85 EERAERWDASKIIVATPQVIENDLLAGR-ITLDDVSLLIFDEAHH 128
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
364-449 |
7.49e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 7.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 364 EEQIKKKLEEFSVEEAEVLQILTQVNVVRRECEIKLEAAHfDEKKEINKRKQLI--LEGKDPDLEAKRKAELAKIKQKNR 441
Cdd:PRK03918 188 TENIEELIKEKEKELEEVLREINEISSELPELREELEKLE-KEVKELEELKEEIeeLEKELESLEGSKRKLEEKIRELEE 266
|
....*...
gi 1622894498 442 RFKEKVEE 449
Cdd:PRK03918 267 RIEELKKE 274
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
220-348 |
7.79e-05 |
|
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: 43.01 E-value: 7.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 220 DQRYLLVPEKVKDAYLVHLIQRfqdeHEDWS-IIIFTNTCKTCQILCMMLRKfsfPtvALHSMMKQKERFAALAKFKSSI 298
Cdd:cd18789 24 KRRLLAAMNPNKLRALEELLKR----HEQGDkIIVFTDNVEALYRYAKRLLK---P--FITGETPQSEREEILQNFREGE 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1622894498 299 YRILIATDVASRGLDIPTVQV-VINHNTPGLPKIYIHRVGRTARAGRQGQA 348
Cdd:cd18789 95 YNTLVVSKVGDEGIDLPEANVaIQISGHGGSRRQEAQRLGRILRPKKGGGK 145
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
23-156 |
9.55e-05 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex 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. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 43.58 E-value: 9.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 23 KQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDP--YGIFCLVLTPTRELAYQIAEQFRVLGKPLGLK 100
Cdd:cd17927 1 FKPRNYQLELAQPALKGKNTIICLPTGSGKTFVAVLICEHHLKKFPagRKGKVVFLANKVPLVEQQKEVFRKHFERPGYK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622894498 101 DCIIVGGMDMVAQALELSRKPHVVIATPGRLADHLRSSNTFSIKKIRFLVMDEADR 156
Cdd:cd17927 81 VTGLSGDTSENVSVEQIVESSDVIIVTPQILVNDLKSGTIVSLSDFSLLVFDECHN 136
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
278-352 |
1.16e-04 |
|
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: 42.64 E-value: 1.16e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622894498 278 LHSMMKQKERFAALAKFKSSIYRILIATDVASRGLDIPTVQVVI--NHNTPGLPKIYIHRvGRTARAGRQGQAITLV 352
Cdd:cd18792 66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIieDADRFGLSQLHQLR-GRVGRGKHQSYCYLLY 141
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
27-154 |
2.10e-04 |
|
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 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: 350779 [Multi-domain] Cd Length: 191 Bit Score: 42.25 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 27 PVQLGCIPAILEGRD-CLGCAKTGSGKTAAFVLPILQKLSEDPYGIfCLVLTPTRELAYQIAEQFRV-LGKPLGLKDCII 104
Cdd:cd18021 6 PIQTQVFNSLYNTDDnVFVGAPTGSGKTVCAELALLRHWRQNPKGR-AVYIAPMQELVDARYKDWRAkFGPLLGKKVVKL 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1622894498 105 VGGMdmvAQALELSRKPHVVIATPGRLaDHL--RSSNTFSIKKIRFLVMDEA 154
Cdd:cd18021 85 TGET---STDLKLLAKSDVILATPEQW-DVLsrRWKQRKNVQSVELFIADEL 132
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
18-154 |
2.84e-04 |
|
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom syndrome protein homolog or BLM) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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. Mutations in RecQ2 cause Bloom syndrome.
Pssm-ID: 350774 [Multi-domain] Cd Length: 208 Bit Score: 42.12 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 18 RQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILqkLSEdpyGIfCLVLTPTRELayqIAEQFRVLgKPL 97
Cdd:cd18016 11 KKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPAC--VSP---GV-TVVISPLRSL---IVDQVQKL-TSL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622894498 98 GLKDCIIVGGMDMVAQA---LELSRKPHVV---------IATPGRLADHLrsSNTFSIKKIRFLVMDEA 154
Cdd:cd18016 81 DIPATYLTGDKTDAEATkiyLQLSKKDPIIkllyvtpekISASNRLISTL--ENLYERKLLARFVIDEA 147
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
212-349 |
4.32e-04 |
|
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: 40.71 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 212 PVSTVEQLDQRYLLVPEKVKDAY--LVHLIQRfqdeHEdwSIIIFTNTCKTCQILCMMLRKF------SFPTVALHSMMK 283
Cdd:cd18796 6 IKVILPVAPEIFPWAGESGADAYaeVIFLLER----HK--STLVFTNTRSQAERLAQRLRELcpdrvpPDFIALHHGSLS 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622894498 284 QKERFAALAKFKSSIYRILIATDVASRGLDIPTVQVVINHNTPGLPKIYIHRVGrtaRAGRQGQAI 349
Cdd:cd18796 80 RELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLG---RSGHRPGAA 142
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
25-91 |
5.20e-04 |
|
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: 40.86 E-value: 5.20e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622894498 25 PTPVQLGCIPAIL------EGRDCLGCAKTGSGKTAAFVLPILQKLSEdpyGIFCLVLTPTRELAYQIAEQFR 91
Cdd:cd17918 16 LTKDQAQAIKDIEkdlhspEPMDRLLSGDVGSGKTLVALGAALLAYKN---GKQVAILVPTEILAHQHYEEAR 85
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
364-454 |
7.07e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 7.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 364 EEQIKKKLEEFSVEEAEVLQILTQVNvvRRECEIKLEAAHFDEKKEINKRKQliLEGKDPDLEAKRKAELAKIKQKNRRf 443
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAEELK--KAEEENKIKAAEEAKKAEEDKKKA--EEAKKAEEDEKKAAEALKKEAEEAK- 1702
|
90
....*....|.
gi 1622894498 444 keKVEETLKRQ 454
Cdd:PTZ00121 1703 --KAEELKKKE 1711
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
48-314 |
1.43e-03 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 41.22 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 48 TGSGKTAAFVLPILQKLSE-DPYGIFcLVLtPTRELAYQIAEQFR-VLGKPLGL-----------KDCIIVGGMDMVAQA 114
Cdd:COG1203 156 TGGGKTEAALLFALRLAAKhGGRRII-YAL-PFTSIINQTYDRLRdLFGEDVLLhhsladldlleEEEEYESEARWLKLL 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 115 LELSRKPhVVIATPgrlaDHL-----RSSNTFSIKKIRF----LVMDEADrlleqgctdfTVD---LEAILAAVPARRQ- 181
Cdd:COG1203 234 KELWDAP-VVVTTI----DQLfeslfSNRKGQERRLHNLansvIILDEVQ----------AYPpymLALLLRLLEWLKNl 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 182 ---TLLFSATLTDTLREL----QGLATNQPffweAQAPVSTVEQLDQRYLLVPEKVKDAYLV-HLIQRFQDEHedwSIII 253
Cdd:COG1203 299 ggsVILMTATLPPLLREElleaYELIPDEP----EELPEYFRAFVRKRVELKEGPLSDEELAeLILEALHKGK---SVLV 371
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622894498 254 FTNTCKTCQILCMMLRK--FSFPTVALHSMMKQKERFAALAK----FKSSIYRILIATDVASRGLDI 314
Cdd:COG1203 372 IVNTVKDAQELYEALKEklPDEEVYLLHSRFCPADRSEIEKEikerLERGKPCILVSTQVVEAGVDI 438
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
48-189 |
1.58e-03 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 38.83 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 48 TGSGKTAafvlpILQKLSEDPYGIFCLVLTPTRELAYQIAEQFRvlgKPLGLKDCIIVGGmdmVAQALELSRKphVVIAT 127
Cdd:cd17926 27 TGSGKTL-----TALALIAYLKELRTLIVVPTDALLDQWKERFE---DFLGDSSIGLIGG---GKKKDFDDAN--VVVAT 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622894498 128 PGRLAdhlRSSNTFSIKKIRFLVM--DEADRLleqgCTDFtvdLEAILAAVPARRQtLLFSATL 189
Cdd:cd17926 94 YQSLS---NLAEEEKDLFDQFGLLivDEAHHL----PAKT---FSEILKELNAKYR-LGLTATP 146
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
20-154 |
2.52e-03 |
|
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.
Pssm-ID: 350776 [Multi-domain] Cd Length: 201 Bit Score: 39.16 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 20 LGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDPyGIfCLVLTPTRELayqIAEQFRVLgkPLGL 99
Cdd:cd18018 8 FGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRRRGP-GL-TLVVSPLIAL---MKDQVDAL--PRAI 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622894498 100 KDCIIVGGMDM--VAQALEL--SRKPHVVIATPGRLADHLRSSNTFSIKKIRFLVMDEA 154
Cdd:cd18018 81 KAAALNSSLTReeRRRILEKlrAGEVKILYVSPERLVNESFRELLRQTPPISLLVVDEA 139
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
278-383 |
2.85e-03 |
|
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: 38.48 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 278 LHSMMKQKERFAALAKFKSSIYRILIATDVASRGLDIPTVQVVI--NHNTPGLPKIYIHRvGRTARAGRQGQAITLVtqy 355
Cdd:cd18810 57 AHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIieRADKFGLAQLYQLR-GRVGRSKERAYAYFLY--- 132
|
90 100
....*....|....*....|....*...
gi 1622894498 356 dihlvyaieeQIKKKLEEFSVEEAEVLQ 383
Cdd:cd18810 133 ----------PDQKKLTEDALKRLEAIQ 150
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
291-380 |
3.04e-03 |
|
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase 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: 350185 [Multi-domain] Cd Length: 174 Bit Score: 38.44 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 291 LAKFKSSIYRILIAT----DVASRGLDIP-TVQVVINHNTPglPKIYIHRVGRTAR--AGR--QGQAITLVTqyDIHLVY 361
Cdd:cd18798 65 LEKFEEGEIDVLIGVasyyGVLVRGIDLPeRIKYAIFYGVP--VTTYIQASGRTSRlyAGGltKGLSVVLVD--DPELFE 140
|
90
....*....|....*....
gi 1622894498 362 AIEEQIKKKLEEFSVEEAE 380
Cdd:cd18798 141 ALKKRLKLILDEFIFKELE 159
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
48-157 |
3.52e-03 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 38.04 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 48 TGSGKT---AAFVLPILQKLSEDPygifCLVLTPTRELAYQIAEQFR-VLGKPlgLKDCIIVGGMDMVAQALELsrkpHV 123
Cdd:pfam04851 32 TGSGKTltaAKLIARLFKKGPIKK----VLFLVPRKDLLEQALEEFKkFLPNY--VEIGEIISGDKKDESVDDN----KI 101
|
90 100 110
....*....|....*....|....*....|....*
gi 1622894498 124 VIATPGRLADHLRS-SNTFSIKKIRFLVMDEADRL 157
Cdd:pfam04851 102 VVTTIQSLYKALELaSLELLPDFFDVIIIDEAHRS 136
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
5-188 |
4.10e-03 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 39.94 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 5 AELGLSSWLVAQCRQLGLKQPTPVQLGCIPA-ILEGRDCLGCAKTGSGKTAAFVLPILQKLSEdpyGIFCLVLTPTRELA 83
Cdd:PRK02362 4 AELPLPEGVIEFYEAEGIEELYPPQAEAVEAgLLDGKNLLAAIPTASGKTLIAELAMLKAIAR---GGKALYIVPLRALA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 84 YQIAEQFRVLGKpLGLKDCIIVGGMDMVAQAleLSRKpHVVIATPGRlADHLRSSNTFSIKKIRFLVMDE------ADRl 157
Cdd:PRK02362 81 SEKFEEFERFEE-LGVRVGISTGDYDSRDEW--LGDN-DIIVATSEK-VDSLLRNGAPWLDDITCVVVDEvhlidsANR- 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 1622894498 158 leqGCTdftvdLEAILAAVpaRR-----QTLLFSAT 188
Cdd:PRK02362 155 ---GPT-----LEVTLAKL--RRlnpdlQVVALSAT 180
|
|
| uvrb |
TIGR00631 |
excinuclease ABC, B subunit; All proteins in this family for wich functions are known are DNA ... |
278-445 |
5.26e-03 |
|
excinuclease ABC, B subunit; All proteins in this family for wich functions are known are DNA helicases that function in the nucleotide excision repair and are endonucleases that make the 3' incision next to DNA damage. They are part of a pathway requiring UvrA, UvrB, UvrC, and UvrD homologs. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273185 [Multi-domain] Cd Length: 655 Bit Score: 39.20 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 278 LHSMMKQKERFAALAKFKSSIYRILIATDVASRGLDIPTVQVV--INHNTPGLPKIY---IHRVGRTARAGRqGQAItlv 352
Cdd:TIGR00631 472 LHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVaiLDADKEGFLRSErslIQTIGRAARNVN-GKVI--- 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 353 tqydihlVYA--IEEQIKKKLEEfsveeaevlqilTQvnvVRRECEIKLEAAHFDEKKEINKRKQLILEGKDPDLEAKRK 430
Cdd:TIGR00631 548 -------MYAdkITDSMQKAIEE------------TE---RRRKIQMAYNEEHGITPQTIRKPIRDILDIELKEKEDAAK 605
|
170
....*....|....*
gi 1622894498 431 AELAKIKQKNRRFKE 445
Cdd:TIGR00631 606 KKKKGEDLSDLSKKE 620
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
363-458 |
6.98e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 38.97 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 363 IEEQIKKKLEEFSVEEAEVLQILT-QVNVVRRECEIKLEAAHFDEKKEINKRKQLILEGKDPDLEAKRKAELAKIKQK-N 440
Cdd:pfam09731 314 IERALEKQKEELDKLAEELSARLEeVRAADEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLKDVLVEQEIElQ 393
|
90
....*....|....*...
gi 1622894498 441 RRFKEKVEETLKRQKAGR 458
Cdd:pfam09731 394 REFLQDIKEKVEEERAGR 411
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
25-137 |
8.94e-03 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members 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: 350794 [Multi-domain] Cd Length: 204 Bit Score: 37.46 E-value: 8.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 25 PTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDP---YGIFCLVLTPTRELAYQiaeQFRVLGKPL--GL 99
Cdd:cd18036 3 LRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKRRsagEKGRVVVLVNKVPLVEQ---QLEKFFKYFrkGY 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 1622894498 100 KDCIIVGGMDMVAQALELSRKPHVVIATPGRLADHLRS 137
Cdd:cd18036 80 KVTGLSGDSSHKVSFGQIVKASDVIICTPQILINNLLS 117
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
252-341 |
9.00e-03 |
|
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: 36.00 E-value: 9.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622894498 252 IIFTNTCKTCQILCMMLRKFSFPTVALHSMMKQKER---FAALAKFKSSIYRILIATDVASRGLDIPTV-QVVINHNTpG 327
Cdd:cd18799 10 LIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERgdeALILLFFGELKPPILVTVDLLTTGVDIPEVdNVVFLRPT-E 88
|
90
....*....|....
gi 1622894498 328 LPKIYIHRVGRTAR 341
Cdd:cd18799 89 SRTLFLQMLGRGLR 102
|
|
| |
