|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
1-422 |
0e+00 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 590.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 1 MNFSELGLNPLLAKAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLVEASAAkgyGPRILVLT 80
Cdd:COG0513 2 MSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPR---APQALILA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 81 PTRELAQQVEKAARTYGSELrKLRTASLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHMERGKIDFARLEVLVLDEADRM 160
Cdd:COG0513 79 PTRELALQVAEELRKLAKYL-GLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 161 LDMGFIDDIKAIVAKTPAERQTLLFSATLDGVVGDLARQLTRDAQRIEVARKEESAAKIEQKLHFFDDMqHKMRLLDALV 240
Cdd:COG0513 158 LDMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKR-DKLELLRRLL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 241 RDAAIQQAVVFTATKAGAEELTDELRDRGFLAEALHGDMPQHKRNRTLDRVRTGRVQFLVATDVAARGIDVAGISHVINY 320
Cdd:COG0513 237 RDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 321 DPPRQAEDYVHRIGRTGRAGRSGTAVTLVGFRERHLVRNIERYTGQAIEVVTIPGLEPTIKPRPEGGNKRPwsdKPGYKG 400
Cdd:COG0513 317 DLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPKI---KEKLKG 393
|
410 420
....*....|....*....|..
gi 1590033848 401 KRPGGEWKGKPGGGWKEGQGKP 422
Cdd:COG0513 394 KKAGRGGRPGPKGERKARRGKR 415
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
1-391 |
3.98e-146 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 424.35 E-value: 3.98e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 1 MNFSELGLNPLLAKAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLVEASAAKGYGPRILVLT 80
Cdd:PRK11192 1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRKSGPPRILILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 81 PTRELAQQVEKAARTYGSELrKLRTASLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHMERGKIDFARLEVLVLDEADRM 160
Cdd:PRK11192 81 PTRELAMQVADQARELAKHT-HLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 161 LDMGFIDDIKAIVAKTPAERQTLLFSATLDG-VVGDLARQLTRDAQRIEVA--RKEEsaAKIEQKLHFFDDMQHKMRLLD 237
Cdd:PRK11192 160 LDMGFAQDIETIAAETRWRKQTLLFSATLEGdAVQDFAERLLNDPVEVEAEpsRRER--KKIHQWYYRADDLEHKTALLC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 238 ALVRDAAIQQAVVFTATKAGAEELTDELRDRGFLAEALHGDMPQHKRNRTLDRVRTGRVQFLVATDVAARGIDVAGISHV 317
Cdd:PRK11192 238 HLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHV 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590033848 318 INYDPPRQAEDYVHRIGRTGRAGRSGTAVTLVgfrERH---LVRNIERYTGQAIEVVTIPGLEPTIKPRPEGGNKRP 391
Cdd:PRK11192 318 INFDMPRSADTYLHRIGRTGRAGRKGTAISLV---EAHdhlLLGKIERYIEEPLKARVIDELRPKTKAPSEKKTGKP 391
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
3-391 |
1.53e-129 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 383.00 E-value: 1.53e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 3 FSELGLNPLLAKAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLveasAAKGYGPRILVLTPT 82
Cdd:PRK11776 6 FSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL----DVKRFRVQALVLCPT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 83 RELAQQVEKaartygsELRKLRTA-------SLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHMERGKIDFARLEVLVLD 155
Cdd:PRK11776 82 RELADQVAK-------EIRRLARFipnikvlTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 156 EADRMLDMGFIDDIKAIVAKTPAERQTLLFSATLDGVVGDLARQLTRDAQRIEVARKEEsAAKIEQklHFFD-DMQHKMR 234
Cdd:PRK11776 155 EADRMLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHD-LPAIEQ--RFYEvSPDERLP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 235 LLDALVRDAAIQQAVVFTATKAGAEELTDELRDRGFLAEALHGDMPQHKRNRTLDRVRTGRVQFLVATDVAARGIDVAGI 314
Cdd:PRK11776 232 ALQRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKAL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 315 SHVINYDPPRQAEDYVHRIGRTGRAGRSGTAVTLVGFRERHLVRNIERYTGQAIEVVTIPGLEPTIKPRPE--------- 385
Cdd:PRK11776 312 EAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPSLSPLSGVPLLpemvtlcid 391
|
....*....
gi 1590033848 386 GGNK---RP 391
Cdd:PRK11776 392 GGKKdklRP 400
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
1-452 |
6.47e-129 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 381.08 E-value: 6.47e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 1 MNFSELGLNPLLAKAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLVEASA-AKGYGP-RILV 78
Cdd:PRK10590 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPhAKGRRPvRALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 79 LTPTRELAQQVEKAARTYGSELRkLRTASLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHMERGKIDFARLEVLVLDEAD 158
Cdd:PRK10590 81 LTPTRELAAQIGENVRDYSKYLN-IRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 159 RMLDMGFIDDIKAIVAKTPAERQTLLFSATLDGVVGDLARQLTRDAQRIEVARKEESAAKIEQKLHFFDDmQHKMRLLDA 238
Cdd:PRK10590 160 RMLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDK-KRKRELLSQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 239 LVRDAAIQQAVVFTATKAGAEELTDELRDRGFLAEALHGDMPQHKRNRTLDRVRTGRVQFLVATDVAARGIDVAGISHVI 318
Cdd:PRK10590 239 MIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 319 NYDPPRQAEDYVHRIGRTGRAGRSGTAVTLVGFRERHLVRNIERYTGQAIEVVTIPGLEP--TIKPRP--EGGNKRPWSD 394
Cdd:PRK10590 319 NYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRIAIPGYEPdpSIKAEPiqNGRQQRGGGG 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1590033848 395 KPGYKGKRPGGEWKGKPGGGWKEGQGKPWGDKPGQRGGGDKPAYKGNGDRPHAAAGQQ 452
Cdd:PRK10590 399 RGQGGGRGQQQGQPRRGEGGAKSASAKPAEKPSRRLGDAKPAGEQQRRRRPRKPAAAQ 456
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
1-377 |
9.52e-106 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 327.19 E-value: 9.52e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 1 MNFSELGLNPLLAKAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLVEASAAkgygPRILVLT 80
Cdd:PRK11634 6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKA----PQILVLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 81 PTRELAQQVEKAARTYGSELRKLRTASLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHMERGKIDFARLEVLVLDEADRM 160
Cdd:PRK11634 82 PTRELAVQVAEAMTDFSKHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 161 LDMGFIDDIKAIVAKTPAERQTLLFSATLDGVVGDLARQLTRDAQRIEVARKEESAAKIEQKLHffddMQHKMRLLDALV 240
Cdd:PRK11634 162 LRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYW----TVWGMRKNEALV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 241 R-------DAAIqqavVFTATKAGAEELTDELRDRGFLAEALHGDMPQHKRNRTLDRVRTGRVQFLVATDVAARGIDVAG 313
Cdd:PRK11634 238 RfleaedfDAAI----IFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVER 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1590033848 314 ISHVINYDPPRQAEDYVHRIGRTGRAGRSGTAVTLVGFRERHLVRNIERYTGQAIEVVTIPGLE 377
Cdd:PRK11634 314 ISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAE 377
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
3-404 |
1.18e-102 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 312.68 E-value: 1.18e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 3 FSELGLNPLLAKAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLVEASAAKGY---GPRILVL 79
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDRkvnQPRALIM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 80 TPTRELAQQVEKAARTYgSELRKLRTASLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHMERGKIDFARLEVLVLDEADR 159
Cdd:PRK04837 90 APTRELAVQIHADAEPL-AQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 160 MLDMGFIDDIKAIVAKTPA--ERQTLLFSATLDGVVGDLARQLTRDAQRIEVARKEESAAKIEQKLhFFDDMQHKMRLLD 237
Cdd:PRK04837 169 MFDLGFIKDIRWLFRRMPPanQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEEL-FYPSNEEKMRLLQ 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 238 ALVRDAAIQQAVVFTATKAGAEELTDELRDRGFLAEALHGDMPQHKRNRTLDRVRTGRVQFLVATDVAARGIDVAGISHV 317
Cdd:PRK04837 248 TLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 318 INYDPPRQAEDYVHRIGRTGRAGRSGTAVTLVGfrERHlVRN---IERYTGQAIEVVT---------IPGLEPTIKPRPE 385
Cdd:PRK04837 328 FNYDLPDDCEDYVHRIGRTGRAGASGHSISLAC--EEY-ALNlpaIETYIGHSIPVSKydsdalltdLPKPLRLTRPRTG 404
|
410
....*....|....*....
gi 1590033848 386 GGNKRPWSDKPGYKGKRPG 404
Cdd:PRK04837 405 NGPRRSGAPRNRRRRKRSG 423
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
12-208 |
1.43e-99 |
|
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: 296.66 E-value: 1.43e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 12 LAKAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLVEASAAKGYGPRILVLTPTRELAQQVEK 91
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 92 AARTYGSELRkLRTASLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHMERGKIDFARLEVLVLDEADRMLDMGFIDDIKA 171
Cdd:cd00268 81 VARKLGKGTG-LKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 1590033848 172 IVAKTPAERQTLLFSATLDGVVGDLARQLTRDAQRIE 208
Cdd:cd00268 160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
3-414 |
3.00e-98 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 305.54 E-value: 3.00e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 3 FSELGLNPLLAKAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCR-LVEASAAKGYGPRILVLTP 81
Cdd:PTZ00110 132 FEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHiNAQPLLRYGDGPIVLVLAP 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 82 TRELAQQVEKAARTYGSELrKLRTASLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHMERGKIDFARLEVLVLDEADRML 161
Cdd:PTZ00110 212 TRELAEQIREQCNKFGASS-KIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRML 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 162 DMGFIDDIKAIVAKTPAERQTLLFSATLDGVVGDLARQLTRDAQ-RIEVARKEESAAK-IEQKLHFFDDMQHKMRL---L 236
Cdd:PTZ00110 291 DMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEEPvHVNVGSLDLTACHnIKQEVFVVEEHEKRGKLkmlL 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 237 DALVRDAAiqQAVVFTATKAGAEELTDELRDRGFLAEALHGDMPQHKRNRTLDRVRTGRVQFLVATDVAARGIDVAGISH 316
Cdd:PTZ00110 371 QRIMRDGD--KILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKY 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 317 VINYDPPRQAEDYVHRIGRTGRAGRSGTAVTLV---GFR-ERHLVRnIERYTGQAIEvvtiPGLEPTIKPRPEGGNKRPW 392
Cdd:PTZ00110 449 VINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLtpdKYRlARDLVK-VLREAKQPVP----PELEKLSNERSNGTERRRW 523
|
410 420
....*....|....*....|..
gi 1590033848 393 sdkpgYKGKRPGGEWKGKPGGG 414
Cdd:PTZ00110 524 -----GGYGRFSNNVNNIPLGG 540
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
3-374 |
9.34e-96 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 296.82 E-value: 9.34e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 3 FSELGLNPLLAKAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLVEASAAKGY---GPRILVL 79
Cdd:PRK01297 89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKERymgEPRALII 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 80 TPTRELAQQVEKAARTYgSELRKLRTASLVGGAPYGPQLKLL-SQPVDVVVATPGRLMDHMERGKIDFARLEVLVLDEAD 158
Cdd:PRK01297 169 APTRELVVQIAKDAAAL-TKYTGLNVMTFVGGMDFDKQLKQLeARFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEAD 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 159 RMLDMGFIDDIKAIVAKTP--AERQTLLFSATLDGVVGDLARQLTRDAQRIEVARKEESAAKIEQKLHFFDDmQHKMRLL 236
Cdd:PRK01297 248 RMLDMGFIPQVRQIIRQTPrkEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAG-SDKYKLL 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 237 DALVRDAAIQQAVVFTATKAGAEELTDELRDRGFLAEALHGDMPQHKRNRTLDRVRTGRVQFLVATDVAARGIDVAGISH 316
Cdd:PRK01297 327 YNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISH 406
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1590033848 317 VINYDPPRQAEDYVHRIGRTGRAGRSGTAVTLVGFRERHLVRNIERYTGQAIEVVTIP 374
Cdd:PRK01297 407 VINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKISCEMPP 464
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
1-460 |
7.44e-94 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 294.94 E-value: 7.44e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 1 MNFSELGLNPLLAKAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLVEASA---AKGYGPRIL 77
Cdd:PRK04537 9 LTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPAladRKPEDPRAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 78 VLTPTRELAQQVEKAARTYGSELrKLRTASLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHMERGKIDFARL-EVLVLDE 156
Cdd:PRK04537 89 ILAPTRELAIQIHKDAVKFGADL-GLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVVSLHAcEICVLDE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 157 ADRMLDMGFIDDIKAIVAKTP--AERQTLLFSATLDGVVGDLARQLTRDAQRIEVARKEESAAKIEQKLHFFDDmQHKMR 234
Cdd:PRK04537 168 ADRMFDLGFIKDIRFLLRRMPerGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPAD-EEKQT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 235 LLDALVRDAAIQQAVVFTATKAGAEELTDELRDRGFLAEALHGDMPQHKRNRTLDRVRTGRVQFLVATDVAARGIDVAGI 314
Cdd:PRK04537 247 LLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 315 SHVINYDPPRQAEDYVHRIGRTGRAGRSGTAVTLVGFRERHLVRNIERYTGQAIEVVTIPGLEPTIKPRPE--------- 385
Cdd:PRK04537 327 KYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKIPVEPVTAELLTPLPRPPrvpvegeea 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 386 --GGNKRPWSDKPGYKGKRPGGEW-KGKPGGGWKEGQGKPWGDKPGQRGGgdkPAYKGNGDRP-------HAAAGQQQAH 455
Cdd:PRK04537 407 ddEAGDSVGTIFREAREQRAAEEQrRGGGRSGPGGGSRSGSVGGGGRRDG---AGADGKPRPRrkprvegEADAAAAGAE 483
|
....*
gi 1590033848 456 KPKRA 460
Cdd:PRK04537 484 TPVVA 488
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
3-369 |
2.11e-78 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 249.74 E-value: 2.11e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 3 FSELGLNPLLAKAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLVEASAAkgygPRILVLTPT 82
Cdd:PTZ00424 30 FDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNA----CQALILAPT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 83 RELAQQVEKAARTYGSELrKLRTASLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHMERGKIDFARLEVLVLDEADRMLD 162
Cdd:PTZ00424 106 RELAQQIQKVVLALGDYL-KVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 163 MGFIDDIKAIVAKTPAERQTLLFSATLDGVVGDLARQLTRDAQRIEVARKEESAAKIEQKLHFFDDMQHKMRLLDALVRD 242
Cdd:PTZ00424 185 RGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLYET 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 243 AAIQQAVVFTATKAGAEELTDELRDRGFLAEALHGDMPQHKRNRTLDRVRTGRVQFLVATDVAARGIDVAGISHVINYDP 322
Cdd:PTZ00424 265 LTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDL 344
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1590033848 323 PRQAEDYVHRIGRTGRAGRSGTAVTLVGFRERHLVRNIERYTGQAIE 369
Cdd:PTZ00424 345 PASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIE 391
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
3-203 |
1.20e-76 |
|
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: 238.54 E-value: 1.20e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 3 FSELGLNPLLAKAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLVEASAAKGYG------PRI 76
Cdd:cd17967 2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRgrrkayPSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 77 LVLTPTRELAQQVEKAAR--TYGSelrKLRTASLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHMERGKIDFARLEVLVL 154
Cdd:cd17967 82 LILAPTRELAIQIYEEARkfSYRS---GVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1590033848 155 DEADRMLDMGFIDDIKAIVAKT----PAERQTLLFSATLDGVVGDLARQLTRD 203
Cdd:cd17967 159 DEADRMLDMGFEPQIRKIVEHPdmppKGERQTLMFSATFPREIQRLAADFLKN 211
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
1-356 |
9.49e-74 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 240.85 E-value: 9.49e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 1 MNFSELGLNPLLAKAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLP-----SLCRLVEASAAKgyGPR 75
Cdd:PLN00206 121 LSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPiisrcCTIRSGHPSEQR--NPL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 76 ILVLTPTRELAQQVEKAARTYGSELrKLRTASLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHMERGKIDFARLEVLVLD 155
Cdd:PLN00206 199 AMVLTPTRELCVQVEDQAKVLGKGL-PFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLD 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 156 EADRMLDMGFIDDIKAIVaKTPAERQTLLFSATLDGVVGDLARQLTRDAQRIEVARKEESAAKIEQKLHFFDDMQHKMRL 235
Cdd:PLN00206 278 EVDCMLERGFRDQVMQIF-QALSQPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQKL 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 236 LDALVRDAAIQ-QAVVFTATKAGAEELTDELR-DRGFLAEALHGDMPQHKRNRTLDRVRTGRVQFLVATDVAARGIDVAG 313
Cdd:PLN00206 357 FDILKSKQHFKpPAVVFVSSRLGADLLANAITvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLR 436
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1590033848 314 ISHVINYDPPRQAEDYVHRIGRTGRAGRSGTAVTLVGFRERHL 356
Cdd:PLN00206 437 VRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNL 479
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
12-198 |
1.36e-64 |
|
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: 206.72 E-value: 1.36e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 12 LAKAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLVEASAAKGYgPRILVLTPTRELAQQVEK 91
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAA-TRVLVLVPTRELAMQCFS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 92 AARTYgSELRKLRTASLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHMERGK-IDFARLEVLVLDEADRMLDMGFIDDIK 170
Cdd:cd17947 80 VLQQL-AQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGFADELK 158
|
170 180
....*....|....*....|....*...
gi 1590033848 171 AIVAKTPAERQTLLFSATLDGVVGDLAR 198
Cdd:cd17947 159 EILRLCPRTRQTMLFSATMTDEVKDLAK 186
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
1-200 |
1.48e-64 |
|
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: 209.05 E-value: 1.48e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 1 MNFSELGLNPLLAKAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRL----VEASAAKGYG-PR 75
Cdd:cd18052 43 LTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMmkegLTASSFSEVQePQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 76 ILVLTPTRELAQQVEKAAR--TYGSelrKLRTASLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHMERGKIDFARLEVLV 153
Cdd:cd18052 123 ALIVAPTRELANQIFLEARkfSYGT---CIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLI 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1590033848 154 LDEADRMLDMGFIDDIKAIVAK--TPA--ERQTLLFSATLDGVVGDLARQL 200
Cdd:cd18052 200 LDEADRMLDMGFGPEIRKLVSEpgMPSkeDRQTLMFSATFPEEIQRLAAEF 250
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
12-207 |
3.82e-64 |
|
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: 205.68 E-value: 3.82e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 12 LAKAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRL-VEASAAKGYGPRILVLTPTRELAQQVE 90
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHInAQPPLERGDGPIVLVLAPTRELAQQIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 91 KAARTYGSELRkLRTASLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHMERGKIDFARLEVLVLDEADRMLDMGFIDDIK 170
Cdd:cd17966 81 QEANKFGGSSR-LRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 1590033848 171 AIVAKTPAERQTLLFSATLDGVVGDLARQLTRDAQRI 207
Cdd:cd17966 160 KIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
8-199 |
1.27e-63 |
|
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: 204.74 E-value: 1.27e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 8 LNPLLAKAVEKTGYNEPTPVQSQAIPAAL-TGADLLVSAQTGSGKTAAFLLPSLCRLVE-ASAAKGYGPRILVLTPTREL 85
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPAIQSLLNtKPAGRRSGVSALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 86 AQQVEKAARTYGSELRKLRTASLVGGAPYGPQLK-LLSQPVDVVVATPGRLMDHME--RGKIDFARLEVLVLDEADRMLD 162
Cdd:cd17964 81 ALQIAAEAKKLLQGLRKLRVQSAVGGTSRRAELNrLRRGRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRLLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1590033848 163 MGFIDDIKAIVAKTPA----ERQTLLFSATLDGVVGDLARQ 199
Cdd:cd17964 161 MGFRPDLEQILRHLPEknadPRQTLLFSATVPDEVQQIARL 201
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
3-208 |
1.31e-63 |
|
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: 204.47 E-value: 1.31e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 3 FSELGLNPLLAKAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLVEAsaakgygPR---ILVL 79
Cdd:cd17954 2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLEN-------PQrffALVL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 80 TPTRELAQQVEKAARTYGSELrKLRTASLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHMERGK-IDFARLEVLVLDEAD 158
Cdd:cd17954 75 APTRELAQQISEQFEALGSSI-GLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLKFLVMDEAD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1590033848 159 RMLDMGFIDDIKAIVAKTPAERQTLLFSATLDGVVGDLARQLTRDAQRIE 208
Cdd:cd17954 154 RLLNMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKIE 203
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
3-199 |
1.75e-62 |
|
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: 201.68 E-value: 1.75e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 3 FSELGLNPLLAKAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLveasAAKGYGPRILVLTPT 82
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRL----SEDPYGIFALVLTPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 83 RELAQQVEKAARTYGSELrKLRTASLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHME---RGKIDFARLEVLVLDEADR 159
Cdd:cd17955 77 RELAYQIAEQFRALGAPL-GLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEADR 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1590033848 160 MLDMGFIDDIKAIVAKTPAERQTLLFSATLDGVVGDLARQ 199
Cdd:cd17955 156 LLTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKEL 195
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
219-349 |
1.49e-61 |
|
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: 196.57 E-value: 1.49e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 219 IEQKLHFFDDMQHKMRLLDALVRDAAIQQAVVFTATKAGAEELTDELRDRGFLAEALHGDMPQHKRNRTLDRVRTGRVQF 298
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1590033848 299 LVATDVAARGIDVAGISHVINYDPPRQAEDYVHRIGRTGRAGRSGTAVTLV 349
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
25-196 |
4.00e-61 |
|
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: 196.69 E-value: 4.00e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 25 TPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLVEasaaKGYGPRILVLTPTRELAQQVEKAARTYGSELrKLR 104
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDK----LDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 105 TASLVGGAPYGPQLKLLSQPvDVVVATPGRLMDHMERGKIdFARLEVLVLDEADRMLDMGFIDDIKAIVAKTPAERQTLL 184
Cdd:pfam00270 76 VASLLGGDSRKEQLEKLKGP-DILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILL 153
|
170
....*....|..
gi 1590033848 185 FSATLDGVVGDL 196
Cdd:pfam00270 154 LSATLPRNLEDL 165
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
2-198 |
1.17e-59 |
|
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: 194.45 E-value: 1.17e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 2 NFSELGLNPLLAKAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLVEASAAKGYgpRILVLTP 81
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVGA--RALILSP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 82 TRELAQQVEKaartYGSELRK---LRTASLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHMERGKIDFARLEVLVLDEAD 158
Cdd:cd17959 80 TRELALQTLK----VTKELGKftdLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEAD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1590033848 159 RMLDMGFIDDIKAIVAKTPAERQTLLFSATLDGVVGDLAR 198
Cdd:cd17959 156 RLFEMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAK 195
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
12-198 |
2.22e-58 |
|
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: 191.38 E-value: 2.22e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 12 LAKAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLVEASAAKGY----GPRILVLTPTRELAQ 87
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDEEtkddGPYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 88 QVEKAARTYGSELRkLRTASLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHMERGKIDFARLEVLVLDEADRMLDMGFID 167
Cdd:cd17945 81 QIEEETQKFAKPLG-IRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1590033848 168 DIKAIVAKTP--------------------AERQTLLFSATLDGVVGDLAR 198
Cdd:cd17945 160 QVTKILDAMPvsnkkpdteeaeklaasgkhRYRQTMMFTATMPPAVEKIAK 210
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
12-209 |
1.48e-57 |
|
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: 188.57 E-value: 1.48e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 12 LAKAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLVEASaaKGYGPRILVLTPTRELAQQVEK 91
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPR--KKKGLRALILAPTRELASQIYR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 92 AAR--TYGSELR-KLRTASLVGGAPYGPQlklLSQPVDVVVATPGRLMDHMERGKIDFARLEVLVLDEADRMLDMGFIDD 168
Cdd:cd17957 79 ELLklSKGTGLRiVLLSKSLEAKAKDGPK---SITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQ 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1590033848 169 IKAIV-AKTPAERQTLLFSATLDGVVGDLARQLTRDAQRIEV 209
Cdd:cd17957 156 TDEILaACTNPNLQRSLFSATIPSEVEELARSVMKDPIRIIV 197
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
1-210 |
1.86e-57 |
|
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: 189.84 E-value: 1.86e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 1 MNFSELGLNPLLAKAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLV-EASAAKGYGPRILVL 79
Cdd:cd18049 24 LNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINhQPFLERGDGPICLVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 80 TPTRELAQQVEKAARTYGSELRkLRTASLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHMERGKIDFARLEVLVLDEADR 159
Cdd:cd18049 104 APTRELAQQVQQVAAEYGRACR-LKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADR 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1590033848 160 MLDMGFIDDIKAIVAKTPAERQTLLFSATLDGVVGDLARQLTRDAQRIEVA 210
Cdd:cd18049 183 MLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIG 233
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
12-207 |
4.76e-57 |
|
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: 186.99 E-value: 4.76e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 12 LAKAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLVEASAAkgygPRILVLTPTRELAQQVEK 91
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRN----PSALILTPTRELAVQIED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 92 AARTYGSELRKLRTASLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHMERGKIDFARLEVLVLDEADRMLDMGFIDDIKA 171
Cdd:cd17962 77 QAKELMKGLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLD 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 1590033848 172 IVAKTPAERQTLLFSATLDGVVGDLARQLTRDAQRI 207
Cdd:cd17962 157 ILENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
2-198 |
5.69e-56 |
|
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: 186.40 E-value: 5.69e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 2 NFSELGLNPLLAKAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLVE-------ASAAKGYG- 73
Cdd:cd18051 22 TFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEqgpgeslPSESGYYGr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 74 ----PRILVLTPTRELAQQVEKAAR--TYGSelrKLRTASLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHMERGKIDFA 147
Cdd:cd18051 102 rkqyPLALVLAPTRELASQIYDEARkfAYRS---RVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1590033848 148 RLEVLVLDEADRMLDMGFIDDIKAIVAK----TPAERQTLLFSATLDGVVGDLAR 198
Cdd:cd18051 179 YCKYLVLDEADRMLDMGFEPQIRRIVEQdtmpPTGERQTLMFSATFPKEIQMLAR 233
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
3-189 |
5.71e-56 |
|
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: 184.83 E-value: 5.71e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 3 FSELGLNPLLAKAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLcRLVEAsaakgygpriLVLTPT 82
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL-QIVVA----------LILEPS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 83 RELAQQVEKAARTYGSELR--KLRTASLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHMERGKIDFARLEVLVLDEADRM 160
Cdd:cd17938 70 RELAEQTYNCIENFKKYLDnpKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRL 149
|
170 180 190
....*....|....*....|....*....|....*
gi 1590033848 161 LDMGFIDDIKAIVAKTP-----AER-QTLLFSATL 189
Cdd:cd17938 150 LSQGNLETINRIYNRIPkitsdGKRlQVIVCSATL 184
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
14-198 |
1.26e-55 |
|
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: 183.65 E-value: 1.26e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 14 KAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLVEASAAKGYGPRILVLTPTRELAQQVEKAA 93
Cdd:cd17941 3 KGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTPEDGLGALIISPTRELAMQIFEVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 94 RTYGSeLRKLRTASLVGGAPYGPQLKLLSQpVDVVVATPGRLMDHM-ERGKIDFARLEVLVLDEADRMLDMGFIDDIKAI 172
Cdd:cd17941 83 RKVGK-YHSFSAGLIIGGKDVKEEKERINR-MNILVCTPGRLLQHMdETPGFDTSNLQMLVLDEADRILDMGFKETLDAI 160
|
170 180
....*....|....*....|....*.
gi 1590033848 173 VAKTPAERQTLLFSATLDGVVGDLAR 198
Cdd:cd17941 161 VENLPKSRQTLLFSATQTKSVKDLAR 186
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
12-207 |
1.24e-54 |
|
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: 181.07 E-value: 1.24e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 12 LAKAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLVEASA-AKGYGPRILVLTPTRELAQQVE 90
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRElEKGEGPIAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 91 KAARTYGsELRKLRTASLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHMERGKIDFARLEVLVLDEADRMLDMGFIDDIK 170
Cdd:cd17952 81 LEAKKFG-KAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 1590033848 171 AIVAKTPAERQTLLFSATLDGVVGDLARQLTRDAQRI 207
Cdd:cd17952 160 SIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
14-198 |
1.55e-53 |
|
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: 178.15 E-value: 1.55e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 14 KAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLVEASA-AKGYGPRILVLTPTRELAQQVEKA 92
Cdd:cd17960 3 DVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKAnLKKGQVGALIISPTRELATQIYEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 93 ARTYGS-ELRKLRTASLVGG-APYGPQLKLLSQPVDVVVATPGRLMDHMER--GKIDFARLEVLVLDEADRMLDMGFIDD 168
Cdd:cd17960 83 LQSFLEhHLPKLKCQLLIGGtNVEEDVKKFKRNGPNILVGTPGRLEELLSRkaDKVKVKSLEVLVLDEADRLLDLGFEAD 162
|
170 180 190
....*....|....*....|....*....|
gi 1590033848 169 IKAIVAKTPAERQTLLFSATLDGVVGDLAR 198
Cdd:cd17960 163 LNRILSKLPKQRRTGLFSATQTDAVEELIK 192
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
21-210 |
2.53e-53 |
|
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: 180.21 E-value: 2.53e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 21 YNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLV-EASAAKGYGPRILVLTPTRELAQQVEKAARTYGSE 99
Cdd:cd18050 82 FKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINhQPYLERGDGPICLVLAPTRELAQQVQQVADDYGKS 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 100 LRkLRTASLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHMERGKIDFARLEVLVLDEADRMLDMGFIDDIKAIVAKTPAE 179
Cdd:cd18050 162 SR-LKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPD 240
|
170 180 190
....*....|....*....|....*....|.
gi 1590033848 180 RQTLLFSATLDGVVGDLARQLTRDAQRIEVA 210
Cdd:cd18050 241 RQTLMWSATWPKEVRQLAEDFLRDYVQINIG 271
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
2-203 |
2.02e-51 |
|
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: 173.33 E-value: 2.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 2 NFSELGLNPLLAKAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLVEASAAK-GYGPRILVLT 80
Cdd:cd17953 13 KWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVKpGEGPIGLIMA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 81 PTRELAQQVEKAARTYGSELrKLRTASLVGGAPYGPQLKLLSQPVDVVVATPGRLMD--HMERGKI-DFARLEVLVLDEA 157
Cdd:cd17953 93 PTRELALQIYVECKKFSKAL-GLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDilTANNGRVtNLRRVTYVVLDEA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1590033848 158 DRMLDMGFIDDIKAIVAKTPAERQTLLFSATLDGVVGDLARQLTRD 203
Cdd:cd17953 172 DRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHK 217
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
16-222 |
3.67e-51 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 171.91 E-value: 3.67e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 16 VEKTGYNEPTPVQSQAIPAALTGA-DLLVSAQTGSGKTAAFLLPSLCRLveasaAKGYGPRILVLTPTRELAQQVEKAAR 94
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEAL-----KRGKGGRVLVLVPTRELAEQWAEELK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 95 TYGSELRkLRTASLVGGAPYGPQL-KLLSQPVDVVVATPGRLMDHMERGKIDFARLEVLVLDEADRMLDMGFIDDIKAIV 173
Cdd:smart00487 76 KLGPSLG-LKVVGLYGGDSKREQLrKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1590033848 174 AKTPAERQTLLFSATLDGVVGDLARQLTRDAQRIEVarKEESAAKIEQK 222
Cdd:smart00487 155 KLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDV--GFTPLEPIEQF 201
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
8-204 |
6.68e-51 |
|
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: 171.61 E-value: 6.68e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 8 LNPLLAKAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLVEASAAKG--YGPRILVLTPTREL 85
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGeeQGTRALILVPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 86 AQQVEKAAR---TYGSelRKLRTASLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHMERGKI-DFARLEVLVLDEADRML 161
Cdd:cd17961 81 AQQVSKVLEqltAYCR--KDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLlLLSTLKYLVIDEADLVL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1590033848 162 DMGFIDDIKAIVAKTPAERQTLLFSATLDGVVGDLARQLTRDA 204
Cdd:cd17961 159 SYGYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNP 201
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
14-198 |
1.91e-50 |
|
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: 169.85 E-value: 1.91e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 14 KAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPslcrLVEASAAKGYGPR----ILVLTPTRELAQQV 89
Cdd:cd17942 3 KAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIP----AIELLYKLKFKPRngtgVIIISPTRELALQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 90 EKAARtygsELRKLRTAS---LVGGAPYGPQLKLLSQPVDVVVATPGRLMDHMERGK-IDFARLEVLVLDEADRMLDMGF 165
Cdd:cd17942 79 YGVAK----ELLKYHSQTfgiVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKgFLYKNLQCLIIDEADRILEIGF 154
|
170 180 190
....*....|....*....|....*....|...
gi 1590033848 166 IDDIKAIVAKTPAERQTLLFSATLDGVVGDLAR 198
Cdd:cd17942 155 EEEMRQIIKLLPKRRQTMLFSATQTRKVEDLAR 187
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
3-207 |
2.43e-48 |
|
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: 164.78 E-value: 2.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 3 FSELGLNPLLAKAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLveasAAKGYGPRILVLTPT 82
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKI----DPKKDVIQALILVPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 83 RELAQQVEKAARTYGSELrKLRTASLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHMERGKIDFARLEVLVLDEADRMLD 162
Cdd:cd17940 77 RELALQTSQVCKELGKHM-GVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1590033848 163 MGFIDDIKAIVAKTPAERQTLLFSATLDGVVGDLARQLTRDAQRI 207
Cdd:cd17940 156 QDFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
14-199 |
3.02e-48 |
|
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: 164.43 E-value: 3.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 14 KAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLVEASA----AKGYGPRILVLTPTRELAQQV 89
Cdd:cd17951 3 KGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEKklpfIKGEGPYGLIVCPSRELARQT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 90 EKAARTYGSELRK-----LRTASLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHMERGKIDFARLEVLVLDEADRMLDMG 164
Cdd:cd17951 83 HEVIEYYCKALQEggypqLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMIDMG 162
|
170 180 190
....*....|....*....|....*....|....*
gi 1590033848 165 FIDDIKAIVAKTPAERQTLLFSATLDGVVGDLARQ 199
Cdd:cd17951 163 FEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKS 197
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
16-207 |
8.13e-48 |
|
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: 163.53 E-value: 8.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 16 VEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRL--VEASAAKGYGPRILVLTPTRELAQQVEKAA 93
Cdd:cd17949 6 KSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLlsLEPRVDRSDGTLALVLVPTRELALQIYEVL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 94 RTYGSELRKLRTASLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHMERGK-IDFARLEVLVLDEADRMLDMGFIDDIKAI 172
Cdd:cd17949 86 EKLLKPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQsFDVSNLRWLVLDEADRLLDMGFEKDITKI 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1590033848 173 V-------------AKTPAERQTLLFSATLDGVVGDLARQLTRDAQRI 207
Cdd:cd17949 166 LellddkrskaggeKSKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
12-204 |
8.41e-48 |
|
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: 163.02 E-value: 8.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 12 LAKAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLVEASAAKGY--GPRILVLTPTRELAQQV 89
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPREQrnGPGVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 90 EKAARTYgsELRKLRTASLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHMERGKIDFARLEVLVLDEADRMLDMGFIDDI 169
Cdd:cd17958 81 EAECSKY--SYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQI 158
|
170 180 190
....*....|....*....|....*....|....*
gi 1590033848 170 KAIVAKTPAERQTLLFSATLDGVVGDLARQLTRDA 204
Cdd:cd17958 159 RKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDP 193
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
14-228 |
1.31e-47 |
|
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: 163.95 E-value: 1.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 14 KAVEKTGYNEPTPVQSQAIPAALT-GADLLVSAQTGSGKTAAFLLPSLCRLVEASAAKGY-----GPRILVLTPTRELAQ 87
Cdd:cd17946 3 RALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLLSQKSSNGVggkqkPLRALILTPTRELAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 88 QVE---KAARTYGSelrkLRTASLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHMERGK---IDFARLEVLVLDEADRML 161
Cdd:cd17946 83 QVKdhlKAIAKYTN----IKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNehlANLKSLRFLVLDEADRML 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590033848 162 DMGFIDDIKAIVAKTPAE-------RQTLLFSATLDGVVGDLARQLTRdaqriEVARKEESAAKIE---QKLHFFDD 228
Cdd:cd17946 159 EKGHFAELEKILELLNKDragkkrkRQTFVFSATLTLDHQLPLKLNSK-----KKKKKKEKKQKLElliEKVGFRKK 230
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
26-202 |
8.18e-43 |
|
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: 150.00 E-value: 8.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 26 PVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLVEASA--AKGYGPRILVLTPTRELAQQVekaARTYGSELRKL 103
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQprKRGRAPKVLVLAPTRELANQV---TKDFKDITRKL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 104 RTASLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHMERGKIDFARLEVLVLDEADRMLDMGFIDDIKAIVA---KTPAER 180
Cdd:cd17944 92 SVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSvsyKKDSED 171
|
170 180
....*....|....*....|....
gi 1590033848 181 --QTLLFSATLDGVVGDLARQLTR 202
Cdd:cd17944 172 npQTLLFSATCPDWVYNVAKKYMK 195
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
5-207 |
3.32e-42 |
|
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: 148.24 E-value: 3.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 5 ELGLNPLLAKAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLvEASAAKgygPRILVLTPTRE 84
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRI-DTTVRE---TQALVLAPTRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 85 LAQQVEKAARTYGSELrKLRTASLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHMERGKIDFARLEVLVLDEADRMLDMG 164
Cdd:cd17939 77 LAQQIQKVVKALGDYM-GVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRG 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1590033848 165 FIDDIKAIVAKTPAERQTLLFSATLDGVVGDLARQLTRDAQRI 207
Cdd:cd17939 156 FKDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
8-207 |
9.89e-42 |
|
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: 146.95 E-value: 9.89e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 8 LNPLLAKAVEKTGYNEPTPVQSQAIPAALTG--ADLLVSAQTGSGKTAAFLLPSLCRLVEASAAkgygPRILVLTPTREL 85
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKS----PQALCLAPTREL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 86 AQQVEKAARTYGSeLRKLRTASLVGGAPYGPQLKLLSQpvdVVVATPGRLMDHMERGKIDFARLEVLVLDEADRMLDM-G 164
Cdd:cd17963 77 ARQIGEVVEKMGK-FTGVKVALAVPGNDVPRGKKITAQ---IVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqG 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1590033848 165 FIDDIKAIVAKTPAERQTLLFSATLDGVVGDLARQLTRDAQRI 207
Cdd:cd17963 153 HGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
14-202 |
2.99e-41 |
|
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: 145.48 E-value: 2.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 14 KAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLVEASAakgyGPRILVLTPTRELAQQVEKAA 93
Cdd:cd17943 3 EGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERR----HPQVLILAPTREIAVQIHDVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 94 RTYGSELRKLRTASLVGGAPYGPQLKLLSQPvDVVVATPGRLMDHMERGKIDFARLEVLVLDEADRMLDMGFIDDIKAIV 173
Cdd:cd17943 79 KKIGKKLEGLKCEVFIGGTPVKEDKKKLKGC-HIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIF 157
|
170 180
....*....|....*....|....*....
gi 1590033848 174 AKTPAERQTLLFSATLDgvvGDLARQLTR 202
Cdd:cd17943 158 SSLPKNKQVIAFSATYP---KNLDNLLAR 183
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
3-209 |
1.93e-39 |
|
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: 141.33 E-value: 1.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 3 FSELGLNPLLAKAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLpSLCRLVEASAAKgygPRILVLTPT 82
Cdd:cd17950 4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVL-STLQQLEPVDGQ---VSVLVICHT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 83 RELAQQVEKAARTYGSELRKLRTASLVGGAPYGPQLKLLSQPV-DVVVATPGRLMDHMERGKIDFARLEVLVLDEADRM- 160
Cdd:cd17950 80 RELAFQISNEYERFSKYMPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMl 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1590033848 161 --LDMGfiDDIKAIVAKTPAERQTLLFSATLDGVVGDLARQLTRDAQRIEV 209
Cdd:cd17950 160 eqLDMR--RDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
12-207 |
2.69e-38 |
|
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: 138.92 E-value: 2.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 12 LAKAVEKTGYNEPTPVQSQAIPAALTGA---------DLLVSAQTGSGKTAAFLLPSLCRLVEASAakgygPRI--LVLT 80
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSSkstppyrpgDLCVSAPTGSGKTLAYVLPIVQALSKRVV-----PRLraLIVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 81 PTRELAQQVEKAARTYGSELrKLRTASLVGGA---------PYGPQLKLLSqPVDVVVATPGRLMDHMERGK-IDFARLE 150
Cdd:cd17956 76 PTKELVQQVYKVFESLCKGT-GLKVVSLSGQKsfkkeqkllLVDTSGRYLS-RVDILVATPGRLVDHLNSTPgFTLKHLR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590033848 151 VLVLDEADRMLDMGFID-------------------DIKAIVAKTPAER-QTLLFSATldgvvgdlarqLTRDAQRI 207
Cdd:cd17956 154 FLVIDEADRLLNQSFQDwletvmkalgrptapdlgsFGDANLLERSVRPlQKLLFSAT-----------LTRDPEKL 219
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
3-207 |
1.10e-36 |
|
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: 133.73 E-value: 1.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 3 FSELGLNPLLAKAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLVEASAAkgygPRILVLTPT 82
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKA----TQALVLAPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 83 RELAQQVEKAARTYGsELRKLRTASLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHMERGKIDFARLEVLVLDEADRMLD 162
Cdd:cd18046 77 RELAQQIQKVVMALG-DYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1590033848 163 MGFIDDIKAIVAKTPAERQTLLFSATLDGVVGDLARQLTRDAQRI 207
Cdd:cd18046 156 RGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
232-340 |
5.88e-34 |
|
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: 123.09 E-value: 5.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 232 KMRLLDALVRDAAIQQAVVFTATKAGAEEltDELRDR-GFLAEALHGDMPQHKRNRTLDRVRTGRVQFLVATDVAARGID 310
Cdd:pfam00271 2 KLEALLELLKKERGGKVLIFSQTKKTLEA--ELLLEKeGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 1590033848 311 VAGISHVINYDPPRQAEDYVHRIGRTGRAG 340
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
3-207 |
5.93e-34 |
|
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: 126.43 E-value: 5.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 3 FSELGLNPLLAKAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLpSLCRLVEASAAKgygPRILVLTPT 82
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSI-SVLQCLDIQVRE---TQALILSPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 83 RELAQQVEKAARTYGSELrKLRTASLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHMERGKIDFARLEVLVLDEADRMLD 162
Cdd:cd18045 77 RELAVQIQKVLLALGDYM-NVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1590033848 163 MGFIDDIKAIVAKTPAERQTLLFSATLDGVVGDLARQLTRDAQRI 207
Cdd:cd18045 156 KGFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
12-196 |
9.55e-33 |
|
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: 124.02 E-value: 9.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 12 LAKAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLVEASAAKGYG---PRILVLTPTRELAQQ 88
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPfnaPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 89 VEKAARTYGSELrKLRTASLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHMERGKIDFARLEVLVLDEADRMLDMGFIDD 168
Cdd:cd17948 81 IGSVAQSLTEGL-GLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1590033848 169 IKAIVAKTP-AER------------QTLLFSATLDGVVGDL 196
Cdd:cd17948 160 LSHFLRRFPlASRrsentdgldpgtQLVLVSATMPSGVGEV 200
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
259-340 |
3.51e-30 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 111.92 E-value: 3.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 259 EELTDELRDRGFLAEALHGDMPQHKRNRTLDRVRTGRVQFLVATDVAARGIDVAGISHVINYDPPRQAEDYVHRIGRTGR 338
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 1590033848 339 AG 340
Cdd:smart00490 81 AG 82
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
2-214 |
3.26e-27 |
|
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: 108.96 E-value: 3.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 2 NFSELGLNPLLAKAVEKTGYNEPTPVQSQAIPAALTG--ADLLVSAQTGSGKTAAFLLPSLCRLveaSAAKGYgPRILVL 79
Cdd:cd18048 19 SFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRV---DALKLY-PQCLCL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 80 TPTRELAQQVEKAARTYGSELRKLRTASLVGGAPYGPQLKLLSQpvdVVVATPGRLMDHMERGK-IDFARLEVLVLDEAD 158
Cdd:cd18048 95 SPTFELALQTGKVVEEMGKFCVGIQVIYAIRGNRPGKGTDIEAQ---IVIGTPGTVLDWCFKLRlIDVTNISVFVLDEAD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1590033848 159 RMLDM-GFIDDIKAIVAKTPAERQTLLFSATLDGVVGDLARQLTRDAQRIEVaRKEE 214
Cdd:cd18048 172 VMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKL-KKEE 227
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
3-189 |
3.64e-26 |
|
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: 106.69 E-value: 3.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 3 FSELGLNPLLAKAVEK---------TGYNEPTPVQSQAIPAaLTGADL-----------------LVSAQTGSGKTAAFL 56
Cdd:cd17965 1 FDQLKLLPSVREAIIKeilkgsnktDEEIKPSPIQTLAIKK-LLKTLMrkvtkqtsneepklevfLLAAETGSGKTLAYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 57 LPSLCRLVEASAA------------KGYG-PRILVLTPTRELAQQV-EKAARTygSELRKLRTA--SLVGGAPYGPQLKL 120
Cdd:cd17965 80 APLLDYLKRQEQEpfeeaeeeyesaKDTGrPRSVILVPTHELVEQVySVLKKL--SHTVKLGIKtfSSGFGPSYQRLQLA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 121 LSQPVDVVVATPGRLMDHME-RGKIdFARLEVLVLDEADRMLDMGFIDDIKAIVAKTPAERQTLLFSATL 189
Cdd:cd17965 158 FKGRIDILVTTPGKLASLAKsRPKI-LSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATI 226
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
41-370 |
3.80e-23 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 102.41 E-value: 3.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 41 LLVSAqTGSGKTAAFLlpslcrlvEASAAKGYGPRILVLTPTRELAQQvekAARtygsELRKLRTASLVGGAPYGPQLkl 120
Cdd:COG1061 104 LVVAP-TGTGKTVLAL--------ALAAELLRGKRVLVLVPRRELLEQ---WAE----ELRRFLGDPLAGGGKKDSDA-- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 121 lsqpvDVVVATPGRLMDHMERGKIDfARLEVLVLDEADRMLDMGFiddiKAIVAKTPAERqTLLFSAT------------ 188
Cdd:COG1061 166 -----PITVATYQSLARRAHLDELG-DRFGLVIIDEAHHAGAPSY----RRILEAFPAAY-RLGLTATpfrsdgreillf 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 189 -LDGVV-----GDLARQ--LT-------RDAQRIEVARKEESAAKIEQKLhfFDDMQHKMRLLDALVRD-AAIQQAVVFT 252
Cdd:COG1061 235 lFDGIVyeyslKEAIEDgyLAppeyygiRVDLTDERAEYDALSERLREAL--AADAERKDKILRELLREhPDDRKTLVFC 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 253 ATKAGAEELTDELRDRGFLAEALHGDMPQHKRNRTLDRVRTGRVQFLVATDVAARGIDVAGISHVINYDP---PRQaedY 329
Cdd:COG1061 313 SSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPtgsPRE---F 389
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1590033848 330 VHRIGRTGRAGRSGTAVTLVGF------RERHLVRNIERYTGQAIEV 370
Cdd:COG1061 390 IQRLGRGLRPAPGKEDALVYDFvgndvpVLEELAKDLRDLAGYRVEF 436
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
7-373 |
8.44e-22 |
|
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: 98.75 E-value: 8.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 7 GLNPLLAKAVEKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLVEASAAkgygpRILVLTPTRELA 86
Cdd:COG1205 40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPGA-----TALYLYPTKALA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 87 Q-QVEKAARTYGSELRKLRTASLVGGAPYGPQLKLLSQPvDVVVATP-----GrLMDHMERGKIDFARLEVLVLDEA--- 157
Cdd:COG1205 115 RdQLRRLRELAEALGLGVRVATYDGDTPPEERRWIREHP-DIVLTNPdmlhyG-LLPHHTRWARFFRNLRYVVIDEAhty 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 158 ------------DRMldmgfiddiKAIVAKTPAERQTLLFSATLDGvVGDLARQLT-RDAQRIEvarkEESAAKieQKLH 224
Cdd:COG1205 193 rgvfgshvanvlRRL---------RRICRHYGSDPQFILASATIGN-PAEHAERLTgRPVTVVD----EDGSPR--GERT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 225 FF-------DDMQHKMRLLDA--LVRDAAIQ--QAVVFTATKAGAEELTDELRDR------GFLAEALHGDMPQHKRNRT 287
Cdd:COG1205 257 FVlwnpplvDDGIRRSALAEAarLLADLVREglRTLVFTRSRRGAELLARYARRAlrepdlADRVAAYRAGYLPEERREI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 288 LDRVRTGRVQFLVATDVAARGIDVAGISHVINYDPPRQAEDYVHRIGRTGRAGRSGTAVTLVGFR--ERHLVRNIERYTG 365
Cdd:COG1205 337 ERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVLVAGDDplDQYYVRHPEELFE 416
|
....*...
gi 1590033848 366 QAIEVVTI 373
Cdd:COG1205 417 RPPEAAVI 424
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
3-208 |
3.53e-21 |
|
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: 91.32 E-value: 3.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 3 FSELGLNPLLAKAVEKTGYNEPTPVQSQAIPAALTG--ADLLVSAQTGSGKTAAFLLPSLCRLVEASAAKgygpRILVLT 80
Cdd:cd18047 3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYP----QCLCLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 81 PTRELAQQVEKAARTYGSELRKLRTASLVGGAPYGPQLKLLSQpvdVVVATPGRLMDHMERGK-IDFARLEVLVLDEADR 159
Cdd:cd18047 79 PTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISEQ---IVIGTPGTVLDWCSKLKfIDPKKIKVFVLDEADV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1590033848 160 ML-DMGFIDDIKAIVAKTPAERQTLLFSATLDGVVGDLARQLTRDAQRIE 208
Cdd:cd18047 156 MIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
20-358 |
6.06e-21 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 95.21 E-value: 6.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 20 GYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRlveasaaKGYGpriLVLTPTRELAQ-QVEkAARTYG- 97
Cdd:COG0514 14 GYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLL-------PGLT---LVVSPLIALMKdQVD-ALRAAGi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 98 ------SEL----RKLRTASLVGGapygpQLKLLsqpvdvVVAtPGRLM-----DHMERGKIDFarlevLVLDEA----- 157
Cdd:COG0514 83 raaflnSSLsaeeRREVLRALRAG-----ELKLL------YVA-PERLLnprflELLRRLKISL-----FAIDEAhcisq 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 158 ---DrmldmgF------IDDIKAIVAKTPaerqTLLFSATLDG-VVGDLARQL-TRDAQ-----------RIEVARKEEs 215
Cdd:COG0514 146 wghD------FrpdyrrLGELRERLPNVP----VLALTATATPrVRADIAEQLgLEDPRvfvgsfdrpnlRLEVVPKPP- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 216 AAKIEQKLHFfddmqhkmrlLDALVRDAAIqqavVFTATKAGAEELTDELRDRGFLAEALHGDMPQHKRNRTLDRVRTGR 295
Cdd:COG0514 215 DDKLAQLLDF----------LKEHPGGSGI----VYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDE 280
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1590033848 296 VQFLVATdVA-ARGIDVAGISHVINYDPPRQAEDYVHRIGRTGRAGRSGTAVTLVGFRERHLVR 358
Cdd:COG0514 281 VDVIVAT-IAfGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQR 343
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
38-188 |
5.38e-19 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 83.22 E-value: 5.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 38 GADLLVSAQTGSGKTAAFLLPSLCRLVEAsaakgyGPRILVLTPTRELAQQVEKAARTYGSelRKLRTASLVGGAPYGPQ 117
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLKK------GKKVLVLVPTKALALQTAERLRELFG--PGIRVAVLVGGSSAEER 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1590033848 118 LKLLSQPVDVVVATPGRL-MDHMERGKIDFARLEVLVLDEADRMLDMGFIDDIK--AIVAKTPAERQTLLFSAT 188
Cdd:cd00046 73 EKNKLGDADIIIATPDMLlNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILdlAVRKAGLKNAQVILLSAT 146
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1-340 |
3.48e-18 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 86.87 E-value: 3.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 1 MNFSELGLnPLLAKAVEKTGYNEPTPVQSQAIPAAL-TGADLLVSAQTGSGKTA-AFLLpsLCRLVEAsaakgyGPRILV 78
Cdd:COG1204 1 MKVAELPL-EKVIEFLKERGIEELYPPQAEALEAGLlEGKNLVVSAPTASGKTLiAELA--ILKALLN------GGKALY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 79 LTPTRELAQQVEkaartygSELRK------LRTASLVGgaPYGPQLKLLSQPvDVVVATPGRlMDHMERGKIDF-ARLEV 151
Cdd:COG1204 72 IVPLRALASEKY-------REFKRdfeelgIKVGVSTG--DYDSDDEWLGRY-DILVATPEK-LDSLLRNGPSWlRDVDL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 152 LVLDEADrmldmgFIDD------IKAIVAK---TPAERQTLLFSATLDGVvGDLARQLtrDAQRIE-----VARKEesAA 217
Cdd:COG1204 141 VVVDEAH------LIDDesrgptLEVLLARlrrLNPEAQIVALSATIGNA-EEIAEWL--DAELVKsdwrpVPLNE--GV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 218 KIEQKLHFFDDMQHKMRLLDALVRDAAIQ--QAVVFTATKAGAE-----------------------ELTDELRDRG--- 269
Cdd:COG1204 210 LYDGVLRFDDGSRRSKDPTLALALDLLEEggQVLVFVSSRRDAEslakkladelkrrltpeereeleELAEELLEVSeet 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 270 ----FLAEAL-------HGDMPQHKRNRTLDRVRTGRVQFLVATDVAArgidvAGI----SHVINYDPPRQAE------D 328
Cdd:COG1204 290 htneKLADCLekgvafhHAGLPSELRRLVEDAFREGLIKVLVATPTLA-----AGVnlpaRRVIIRDTKRGGMvpipvlE 364
|
410
....*....|..
gi 1590033848 329 YVHRIGRTGRAG 340
Cdd:COG1204 365 FKQMAGRAGRPG 376
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
232-334 |
3.38e-16 |
|
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: 74.82 E-value: 3.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 232 KMRLLDALVRDAAIQQ--AVVFTATKAGAEELTDELRDRGFLAEALHGDMPQHKRNRTLDRVRTGR--VQFLVATDVAAR 307
Cdd:cd18793 12 KLEALLELLEELREPGekVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdiRVFLLSTKAGGV 91
|
90 100 110
....*....|....*....|....*....|...
gi 1590033848 308 GIDVAGISHVINYDPP------RQAEDYVHRIG 334
Cdd:cd18793 92 GLNLTAANRVILYDPWwnpaveEQAIDRAHRIG 124
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
23-337 |
6.55e-15 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 77.45 E-value: 6.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 23 EPTPVQSQAIPAALTGADLLVSAQTGSGKT-AAFlLPSLCRLVEASAAKGYGPRILVL--TPTRELAQQVEKA------- 92
Cdd:COG1201 24 APTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPRPGELPDGLRVLyiSPLKALANDIERNlraplee 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 93 -ARTYGSELRKLRTASLVGGAPYGPQLKLLSQPVDVVVATP-----------GRLMdhmergkidFARLEVLVLDEadrm 160
Cdd:COG1201 103 iGEAAGLPLPEIRVGVRTGDTPASERQRQRRRPPHILITTPeslallltspdAREL---------LRGVRTVIVDE---- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 161 ldmgfiddIKAIVA-KtpaeRQTLLfSATLDgvvgDLARQLTRDAQRI----------EVAR--------------KEES 215
Cdd:COG1201 170 --------IHALAGsK----RGVHL-ALSLE----RLRALAPRPLQRIglsatvgpleEVARflvgyedprpvtivDAGA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 216 AAKIEQK-LHFFDDMQHKM--------RLLDALVrdAAIQQA---VVFTATKAGAEELTDELRDR----GFLAEALHGDM 279
Cdd:COG1201 233 GKKPDLEvLVPVEDLIERFpwaghlwpHLYPRVL--DLIEAHrttLVFTNTRSQAERLFQRLNELnpedALPIAAHHGSL 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1590033848 280 PQHKRNRTLDRVRTGRVQFLVAT---DVaarGIDVAGISHVINYDPPRQAEDYVHRIGRTG 337
Cdd:COG1201 311 SREQRLEVEEALKAGELRAVVATsslEL---GIDIGDVDLVIQVGSPKSVARLLQRIGRAG 368
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
248-348 |
5.98e-13 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350181 [Multi-domain] Cd Length: 134 Bit Score: 65.69 E-value: 5.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 248 AVVFTATKAGAEELTDELRDRGFLAEALHGDMPQHKRNRTLDRVRTGRVQFLVATDVAARGIDVAGISHVINYDPPRQAE 327
Cdd:cd18794 33 GIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSME 112
|
90 100
....*....|....*....|.
gi 1590033848 328 DYVHRIGRTGRAGRSGTAVTL 348
Cdd:cd18794 113 SYYQESGRAGRDGLPSECILF 133
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
28-157 |
9.53e-13 |
|
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: 66.45 E-value: 9.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 28 QSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLVEASaakgyGPRILVLTPTRELAQ-QVEKAARTYGSELRKLRTA 106
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDP-----GSRALYLYPTKALAQdQLRSLRELLEQLGLGIRVA 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1590033848 107 SLVGGAPYGPQLKLLSQPVDVVVATPGRL---MDHMERGKIDFAR-LEVLVLDEA 157
Cdd:cd17923 80 TYDGDTPREERRAIIRNPPRILLTNPDMLhyaLLPHHDRWARFLRnLRYVVLDEA 134
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
228-349 |
1.14e-12 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 70.14 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 228 DMQH-KMRLLDALVRDA----AIQQAVVFTATKAGAEELTDELRDRGFLAEALHGD--------MPQHKRNRTLDRVRTG 294
Cdd:COG1111 331 DIEHpKLSKLREILKEQlgtnPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQaskegdkgLTQKEQIEILERFRAG 410
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1590033848 295 RVQFLVATDVAARGIDVAGISHVINYDPPRQAEDYVHRIGRTGRaGRSGTAVTLV 349
Cdd:COG1111 411 EFNVLVATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGR-KREGRVVVLI 464
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
232-336 |
1.43e-12 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 69.87 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 232 KMRLLDALVRDAAIQQ--AVVFTATKAGAEELTDELRDRGFLAEALHGDMPQHKRNRTLDRVRTGR--VQFLVATDVAAR 307
Cdd:COG0553 534 KLEALLELLEELLAEGekVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGGE 613
|
90 100 110
....*....|....*....|....*....|....*
gi 1590033848 308 GIDVAGISHVINYDPP------RQAEDYVHRIGRT 336
Cdd:COG0553 614 GLNLTAADHVIHYDLWwnpaveEQAIDRAHRIGQT 648
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
245-349 |
4.90e-12 |
|
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: 61.18 E-value: 4.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 245 IQQAVVFTATKAGAEELTDELrdrgflaealhgdmpqhkrnrtldrvrtgrvQFLVATDVAARGIDVAGISHVINYDPPR 324
Cdd:cd18785 3 VVKIIVFTNSIEHAEEIASSL-------------------------------EILVATNVLGEGIDVPSLDTVIFFDPPS 51
|
90 100
....*....|....*....|....*.
gi 1590033848 325 QAEDYVHRIGRTGRAG-RSGTAVTLV 349
Cdd:cd18785 52 SAASYIQRVGRAGRGGkDEGEVILFV 77
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
4-310 |
1.97e-11 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 66.45 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 4 SELGLNPLLAKAVEKTGyNEPTPVQSQAIPAALT-GADLLVSAQTGSGKTaafLLPSLCRLVEASAAKGygpRILVLTPT 82
Cdd:COG1202 191 DDLDLPPELKDLLEGRG-EELLPVQSLAVENGLLeGKDQLVVSATATGKT---LIGELAGIKNALEGKG---KMLFLVPL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 83 RELA-QQVEKAARTYGselRKLRTASLVG-------GAPYGPQlkllsqpVDVVVAT-PGrlMDHMER-GK--------- 143
Cdd:COG1202 264 VALAnQKYEDFKDRYG---DGLDVSIRVGasrirddGTRFDPN-------ADIIVGTyEG--IDHALRtGRdlgdigtvv 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 144 IDfarlEVLVLDEADR--MLDmGFIDDIKAIVAKTpaerQTLLFSATLdGVVGDLARQLtrDAQRIEVarkEESAAKIEQ 221
Cdd:COG1202 332 ID----EVHMLEDPERghRLD-GLIARLKYYCPGA----QWIYLSATV-GNPEELAKKL--GAKLVEY---EERPVPLER 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 222 KLHFFDDMQhKMRLLDALVRDAAIQ--------QAVVFTATKAGAEELTDELrdrGFLAEALHGDMPQHKRNRTLDRVRT 293
Cdd:COG1202 397 HLTFADGRE-KIRIINKLVKREFDTksskgyrgQTIIFTNSRRRCHEIARAL---GYKAAPYHAGLDYGERKKVERRFAD 472
|
330
....*....|....*..
gi 1590033848 294 GRVQFLVATDVAARGID 310
Cdd:COG1202 473 QELAAVVTTAALAAGVD 489
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
1-348 |
3.80e-11 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 65.12 E-value: 3.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 1 MNFSELGLNPLLAKAV--EKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKtaafllpSLCRLVEASAAKGYgprILV 78
Cdd:PRK11057 1 MAQAEVLNLESLAKQVlqETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGK-------SLCYQIPALVLDGL---TLV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 79 LTPTRELAQ-QVEK------AARTYGSELRKLRTASLVGGAPYGpQLKLLsqpvdvvVATPGRLM--DHMERgkIDFARL 149
Cdd:PRK11057 71 VSPLISLMKdQVDQllangvAAACLNSTQTREQQLEVMAGCRTG-QIKLL-------YIAPERLMmdNFLEH--LAHWNP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 150 EVLVLDEA--------DRMLDMGFIDDIKAIVAKTPaerqTLLFSATLDGVV-GDLARQLTRDAQRIEVARkeesaakie 220
Cdd:PRK11057 141 ALLAVDEAhcisqwghDFRPEYAALGQLRQRFPTLP----FMALTATADDTTrQDIVRLLGLNDPLIQISS--------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 221 qklhfFD------DMQHKMRLLDALVRDAAIQQ---AVVFTATKAGAEELTDELRDRGFLAEALHGDMPQHKRNRTLDRV 291
Cdd:PRK11057 208 -----FDrpniryTLVEKFKPLDQLMRYVQEQRgksGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAF 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1590033848 292 RTGRVQFLVATDVAARGIDVAGISHVINYDPPRQAEDYVHRIGRTGRAGRSGTAVTL 348
Cdd:PRK11057 283 QRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLF 339
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
233-339 |
6.79e-11 |
|
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: 59.91 E-value: 6.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 233 MRLLDALV---RDAAIQQAVVFTATKAGA----------EELTDELR-----DRGFLAEALHGDMPQHKRNRTLDRVRTG 294
Cdd:cd18802 10 QKLIEILReyfPKTPDFRGIIFVERRATAvvlsrllkehPSTLAFIRcgfliGRGNSSQRKRSLMTQRKQKETLDKFRDG 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1590033848 295 RVQFLVATDVAARGIDVAGISHVINYDPPRQAEDYVHRIGRtGRA 339
Cdd:cd18802 90 ELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARA 133
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
197-349 |
2.84e-10 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 62.58 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 197 ARQLTRDAQRIEVARKEESaakieqklhfFDDMQHKMRLLDALVRDAAIQQ----AVVFTATKAGAEELTDELRDRGFLA 272
Cdd:PRK13766 323 SKRLVEDPRFRKAVRKAKE----------LDIEHPKLEKLREIVKEQLGKNpdsrIIVFTQYRDTAEKIVDLLEKEGIKA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 273 EALHGD--------MPQHKRNRTLDRVRTGRVQFLVATDVAARGIDVAGISHVINYDPPRQAEDYVHRIGRTGRaGRSGT 344
Cdd:PRK13766 393 VRFVGQaskdgdkgMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEPVPSEIRSIQRKGRTGR-QEEGR 471
|
....*
gi 1590033848 345 AVTLV 349
Cdd:PRK13766 472 VVVLI 476
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
25-202 |
1.37e-09 |
|
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: 57.27 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 25 TPVQSQAIPAA-LTGADLLVSAQTGSGKTAAFLlpslcrLVEASAAKGYGPRILVLTPTRELAQQVEkaartygSELRKL 103
Cdd:cd17921 3 NPIQREALRALyLSGDSVLVSAPTSSGKTLIAE------LAILRALATSGGKAVYIAPTRALVNQKE-------ADLRER 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 104 RTAS-----LVGGAPYgPQLKLLSQPvDVVVATPGRLmDHMERGKID--FARLEVLVLDEADrmldmgFIDD------IK 170
Cdd:cd17921 70 FGPLgknvgLLTGDPS-VNKLLLAEA-DILVATPEKL-DLLLRNGGErlIQDVRLVVVDEAH------LIGDgergvvLE 140
|
170 180 190
....*....|....*....|....*....|....*
gi 1590033848 171 AIVAKTPA---ERQTLLFSATLDGvVGDLARQLTR 202
Cdd:cd17921 141 LLLSRLLRinkNARFVGLSATLPN-AEDLAEWLGV 174
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
38-156 |
3.93e-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: 55.67 E-value: 3.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 38 GADLLVSAQTGSGKTAAFLLPSLCRLVEASAAKGYgprILVLTPTRELAQQVEKAARTYGSELRK-LRTASLVGGAPYGP 116
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGVQ---VLYISPLKALINDQERRLEEPLDEIDLeIPVAVRHGDTSQSE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1590033848 117 QLKLLSQPVDVVVATPGRL--MDHMERGKIDFARLEVLVLDE 156
Cdd:cd17922 78 KAKQLKNPPGILITTPESLelLLVNKKLRELFAGLRYVVVDE 119
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
250-338 |
1.27e-08 |
|
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: 53.81 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 250 VFTATKAGAEELTDELRDR------GFLAEALHGDMPQHKRNRTLDRVRTGRVQFLVATDVAARGIDVAGISHVINYDPP 323
Cdd:cd18796 43 VFTNTRSQAERLAQRLRELcpdrvpPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSP 122
|
90
....*....|....*
gi 1590033848 324 RQAEDYVHRIGRTGR 338
Cdd:cd18796 123 KSVARLLQRLGRSGH 137
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
2-311 |
1.40e-08 |
|
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: 57.01 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 2 NFSELGLNPLLAKAVEK--TGYNEPT----PVQSQAIPAALTGADL-----LVSAQTGSGKT-AAFllpslcRLVEASAA 69
Cdd:COG1203 100 DMARQALDHLLAERLERllPKKSKPRtpinPLQNEALELALEAAEEepglfILTAPTGGGKTeAAL------LFALRLAA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 70 KGYGPRILVLTPTRELAQQ-----------------------VEKAARTYGSELRKLRTASlvggapygpqlKLLSQPvd 126
Cdd:COG1203 174 KHGGRRIIYALPFTSIINQtydrlrdlfgedvllhhsladldLLEEEEEYESEARWLKLLK-----------ELWDAP-- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 127 VVVATPGRLMDHME-RGKIDFARLE-----VLVLDEADrMLDmgfIDDIKAIVA--------KTPAerqtLLFSATL--- 189
Cdd:COG1203 241 VVVTTIDQLFESLFsNRKGQERRLHnlansVIILDEVQ-AYP---PYMLALLLRllewlknlGGSV----ILMTATLppl 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 190 ---------------DGVVGDLARQLTRDaqRIEVARK----EESAAKIEQKLHffddmQHKmrlldalvrdaaiqQAVV 250
Cdd:COG1203 313 lreelleayelipdePEELPEYFRAFVRK--RVELKEGplsdEELAELILEALH-----KGK--------------SVLV 371
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590033848 251 FTATKAGAEELTDELRDRGFLAEA--LHGDMPQHKRNRTLDRVRT----GRVQFLVATDVAARGIDV 311
Cdd:COG1203 372 IVNTVKDAQELYEALKEKLPDEEVylLHSRFCPADRSEIEKEIKErlerGKPCILVSTQVVEAGVDI 438
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
23-160 |
1.64e-08 |
|
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: 53.96 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 23 EPTPVQSQAIPAALTG------ADLLVSAQTGSGKTAAFLLPslcrlveASAAKGYGPRILVLTPTRELAQQVEKAARTY 96
Cdd:cd17918 15 SLTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGA-------ALLAYKNGKQVAILVPTEILAHQHYEEARKF 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1590033848 97 GSELRKLrtasLVGGapyGPQLKLLSQPvDVVVATPGRLmdHMERGKIDFArleVLVLDEADRM 160
Cdd:cd17918 88 LPFINVE----LVTG---GTKAQILSGI-SLLVGTHALL--HLDVKFKNLD---LVIVDEQHRF 138
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
246-348 |
5.52e-08 |
|
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: 51.59 E-value: 5.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 246 QQAVVFTATKAGAEELTDEL-------RDRGFLAEA----LHGdMPQHKRNRTLDRVRTGRVQFLVATDVAARGIDVAGI 314
Cdd:cd18801 31 TRVIIFSEFRDSAEEIVNFLskirpgiRATRFIGQAsgksSKG-MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEV 109
|
90 100 110
....*....|....*....|....*....|....
gi 1590033848 315 SHVINYDPPRQAEDYVHRIGRTGRaGRSGTAVTL 348
Cdd:cd18801 110 DLIICYDASPSPIRMIQRMGRTGR-KRQGRVVVL 142
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
247-343 |
1.26e-07 |
|
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: 51.10 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 247 QAVVFTATKAGAEELTdelrdRGFLAEALHGDMPQHKRNRTLDRVRTGRVQFLVATDVAARGIDV--AGISHVI--NYDP 322
Cdd:cd18789 51 KIIVFTDNVEALYRYA-----KRLLKPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLpeANVAIQIsgHGGS 125
|
90 100
....*....|....*....|.
gi 1590033848 323 PRQaedYVHRIGRTGRAGRSG 343
Cdd:cd18789 126 RRQ---EAQRLGRILRPKKGG 143
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
26-189 |
2.99e-07 |
|
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: 49.61 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 26 PVQSQAIPAAL---TGADLLVSAQTGSGKTA-AFLLPSLCrlveasaakgYGPRILVLTPTRELAQQVEKaartygsELR 101
Cdd:cd17926 3 PYQEEALEAWLahkNNRRGILVLPTGSGKTLtALALIAYL----------KELRTLIVVPTDALLDQWKE-------RFE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 102 KLRTASLVGGAPYGPQLKLLSQPVdvVVATPGRLMDHMERGKIDFARLEVLVLDEADRMLDMGFiddiKAIVAKTPAERQ 181
Cdd:cd17926 66 DFLGDSSIGLIGGGKKKDFDDANV--VVATYQSLSNLAEEEKDLFDQFGLLIVDEAHHLPAKTF----SEILKELNAKYR 139
|
....*...
gi 1590033848 182 tLLFSATL 189
Cdd:cd17926 140 -LGLTATP 146
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
23-159 |
3.30e-07 |
|
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: 50.51 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 23 EPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLVEASAakGYGPRILVLTPTRELAQQVEKAARTYgSELRK 102
Cdd:cd17927 2 KPRNYQLELAQPALKGKNTIICLPTGSGKTFVAVLICEHHLKKFPA--GRKGKVVFLANKVPLVEQQKEVFRKH-FERPG 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1590033848 103 LRTASLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHMERG-KIDFARLEVLVLDEADR 159
Cdd:cd17927 79 YKVTGLSGDTSENVSVEQIVESSDVIIVTPQILVNDLKSGtIVSLSDFSLLVFDECHN 136
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
47-157 |
5.58e-07 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 49.96 E-value: 5.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 47 TGSGKT--AAFLLPSLCRLVEASAAKGygPRILVLTPTRELAQQVEKAARTY-GSELRKLRTASLVGGAPYGPQLKLLSQ 123
Cdd:cd18034 25 TGSGKTliAVMLIKEMGELNRKEKNPK--KRAVFLVPTVPLVAQQAEAIRSHtDLKVGEYSGEMGVDKWTKERWKEELEK 102
|
90 100 110
....*....|....*....|....*....|....
gi 1590033848 124 PvDVVVATPGRLMDHMERGKIDFARLEVLVLDEA 157
Cdd:cd18034 103 Y-DVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
27-156 |
4.61e-06 |
|
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: 47.35 E-value: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 27 VQSQAIPAAL-TGADLLVSAQTGSGKTAAFLLPSLCRLVEASAAKGYGPRILVLTPTRELAQQVEKAARTYGSELrKLRT 105
Cdd:cd18023 5 IQSEVFPDLLySDKNFVVSAPTGSGKTVLFELAILRLLKERNPLPWGNRKVVYIAPIKALCSEKYDDWKEKFGPL-GLSC 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1590033848 106 ASLVGGAPYGPQLKLlsQPVDVVVATPGRLmDHMERGKID----FARLEVLVLDE 156
Cdd:cd18023 84 AELTGDTEMDDTFEI--QDADIILTTPEKW-DSMTRRWRDngnlVQLVALVLIDE 135
|
|
| DinG |
COG1199 |
Rad3-related DNA helicase DinG [Replication, recombination and repair]; |
34-292 |
5.83e-06 |
|
Rad3-related DNA helicase DinG [Replication, recombination and repair];
Pssm-ID: 440812 [Multi-domain] Cd Length: 629 Bit Score: 48.77 E-value: 5.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 34 AALTGADLLVSAQTGSGKTAAFLLPSLCrlveasAAKGYGPRILVLTPTRELAQQVEKaartygSELRKLRtaslvggap 113
Cdd:COG1199 29 ALAEGRHLLIEAGTGTGKTLAYLVPALL------AARETGKKVVISTATKALQEQLVE------KDLPLLR--------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 114 ygpqlKLLSQPVDVVVATpGRlmdhmeRGKIDFARLEVLVLDEADRMLDMGFIDDIKAIVAKTpaerQTLLFSATLDGVV 193
Cdd:COG1199 88 -----KALGLPLRVALLK-GR------SNYLCLRRLEQALQEGDDLDDEELLLARILAWASET----WTGDRDELPLPED 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 194 GDLARQLTRDAQR-------------IEVARKEESAAKIeqkL-----HFFDDMQHKMRLLDAlvrdaaiQQAVVF---- 251
Cdd:COG1199 152 DELWRQVTSDADNclgrrcpyygvcpYELARRLAREADV---VvvnhhLLFADLALGEELLPE-------DDVLIIdeah 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1590033848 252 ----TATKAGAEELT----DELRDRgflAEALHGDMPQHKRNRTLDRVR 292
Cdd:COG1199 222 nlpdRARDMFSAELSsrslLRLLRE---LRKLGLRPGLKKLLDLLERLR 267
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
26-200 |
6.03e-06 |
|
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: 46.56 E-value: 6.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 26 PVQSQAIPAAL-TGADLLVSAQTGSGKTAAFLLPSLCRLVEasaakgyGPRILVLTPTRELAQQVEKAARTYgsELRKLR 104
Cdd:cd18028 4 PPQAEAVRAGLlKGENLLISIPTASGKTLIAEMAMVNTLLE-------GGKALYLVPLRALASEKYEEFKKL--EEIGLK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 105 TASLVGGapYGPQLKLLSQpVDVVVATPGRLmDHMERGKIDFAR-LEVLVLDEadrmldMGFIDD------IKAIVAK-- 175
Cdd:cd18028 75 VGISTGD--YDEDDEWLGD-YDIIVATYEKF-DSLLRHSPSWLRdVGVVVVDE------IHLISDeergptLESIVARlr 144
|
170 180
....*....|....*....|....*.
gi 1590033848 176 -TPAERQTLLFSATLdGVVGDLARQL 200
Cdd:cd18028 145 rLNPNTQIIGLSATI-GNPDELAEWL 169
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
40-341 |
1.67e-05 |
|
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: 46.65 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 40 DLLVSAQTGSGKTAAFLLPSLCRLVEASAAKGygprILVLtPTRELAQ-QVEKAARTYGSE-----LRKLRTASLVGGAP 113
Cdd:cd09639 1 LLVIEAPTGYGKTEAALLWALHSLKSQKADRV----IIAL-PTRATINaMYRRAKEAFGETglyhsSILSSRIKEMGDSE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 114 YGPQL-KLLSQPVDVVVATPGRL--MDHM------ERGKIDFARLE----VLVLDEADRMLD--MGFIddIKAIVAKTPA 178
Cdd:cd09639 76 EFEHLfPLYIHSNDTLFLDPITVctIDQVlksvfgEFGHYEFTLASiansLLIFDEVHFYDEytLALI--LAVLEVLKDN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 179 ERQTLLFSATldgvvgdLARQLTRDAQRIEVARKEESAAKIEQKLHFF----DDMQHKMRLLDALVR--DAAIQQAVVFT 252
Cdd:cd09639 154 DVPILLMSAT-------LPKFLKEYAEKIGYVEENEPLDLKPNERAPFikieSDKVGEISSLERLLEfiKKGGSVAIIVN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 253 ATKAgAEELTDELRDRGFLAEA--LHGDMPQ----HKRNRTLDRVRTGRVQFLVATDVAARGIDvagISHVINYDPPRQA 326
Cdd:cd09639 227 TVDR-AQEFYQQLKEKGPEEEImlIHSRFTEkdraKKEAELLLEFKKSEKFVIVATQVIEASLD---ISVDVMITELAPI 302
|
330
....*....|....*
gi 1590033848 327 EDYVHRIGRTGRAGR 341
Cdd:cd09639 303 DSLIQRLGRLHRYGE 317
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
258-350 |
2.86e-05 |
|
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: 44.26 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 258 AEELTDELRDRGFLAeALHGDMPQHKRNRTLDRVRTGRVQFLVATDVAARGIDVAGISHVINYDPPRQAEDYVHRI-GRT 336
Cdd:cd18811 51 YEYLKERFRPELNVG-LLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLHQLrGRV 129
|
90
....*....|....
gi 1590033848 337 GRAGRSGTAVTLVG 350
Cdd:cd18811 130 GRGDHQSYCLLVYK 143
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
17-200 |
4.78e-05 |
|
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: 44.06 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 17 EKTGYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRlveasaakgyGPRILVLTPTRELAQ-QVEKAARt 95
Cdd:cd17920 6 EVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLL----------DGVTLVVSPLISLMQdQVDRLQQ- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 96 ygselRKLRTASLVGGAPYGPQ----LKLLSQPVDVVVATPGRLMDHMERGKID----FARLEVLVLDEA--------DR 159
Cdd:cd17920 75 -----LGIRAAALNSTLSPEEKrevlLRIKNGQYKLLYVTPERLLSPDFLELLQrlpeRKRLALIVVDEAhcvsqwghDF 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1590033848 160 MLDMGFIDDIKAIVAKTPaerqTLLFSATLD-GVVGDLARQL 200
Cdd:cd17920 150 RPDYLRLGRLRRALPGVP----ILALTATATpEVREDILKRL 187
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
21-56 |
1.03e-04 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 44.88 E-value: 1.03e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1590033848 21 YNEPTPVQSQAIPAALTGADLLVSAQTGSGKT-AAFL 56
Cdd:PRK13767 30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFL 66
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
41-159 |
1.16e-04 |
|
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs 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: 350790 [Multi-domain] Cd Length: 163 Bit Score: 42.55 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 41 LLVSAqTGSGKT--AAFLLPslcRLVEASAAKgygpRILVLTPTRELAQQVEKAARTYgselrkLRTASLVGgapygpqL 118
Cdd:cd18032 24 LLVMA-TGTGKTytAAFLIK---RLLEANRKK----RILFLAHREELLEQAERSFKEV------LPDGSFGN-------L 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1590033848 119 KLLSQPV---DVVVATPGRLMDHMERGKIDFARLEVLVLDEADR 159
Cdd:cd18032 83 KGGKKKPddaRVVFATVQTLNKRKRLEKFPPDYFDLIIIDEAHH 126
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
41-159 |
1.50e-04 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 42.27 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 41 LLVSAqTGSGKT--AAFllpslcrLVEASAAKGYGPRILVLTPTRELAQQVEKAARTYGSELRKlrtaslVGGAPYGPQL 118
Cdd:pfam04851 27 LIVMA-TGSGKTltAAK-------LIARLFKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYVE------IGEIISGDKK 92
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1590033848 119 KLLSQPVDVVVATPGRLMDHMERGKIDFARLE--VLVLDEADR 159
Cdd:pfam04851 93 DESVDDNKIVVTTIQSLYKALELASLELLPDFfdVIIIDEAHR 135
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
27-159 |
3.46e-04 |
|
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: 41.35 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 27 VQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLVEasaakgYGPRILVLTPTRELAQQVEKAARTYGSELRKLrtA 106
Cdd:cd18035 5 LYQVLIAAVALNGNTLIVLPTGLGKTIIAILVAADRLTK------KGGKVLILAPSRPLVEQHAENLKRVLNIPDKI--T 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1590033848 107 SLVGGAPYGPQLKLLSQpVDVVVATPGRLMDHMERGKIDFARLEVLVLDEADR 159
Cdd:cd18035 77 SLTGEVKPEERAERWDA-SKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
|
|
| DEAHc_XPD-like |
cd17915 |
DEAH-box helicase domain of XPD family DEAD-like helicases; The xeroderma pigmentosum group D ... |
47-157 |
4.12e-04 |
|
DEAH-box helicase domain of XPD family DEAD-like helicases; The xeroderma pigmentosum group D (XPD)-like family members 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: 350673 [Multi-domain] Cd Length: 138 Bit Score: 40.49 E-value: 4.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 47 TGSGKTAAFLLPSLCRLVEASAAKgygprILVLTPT-RELAQQVEkaartygsELRKLRTASLVggapygPQLKLLSQPV 125
Cdd:cd17915 10 TGSGKTLSLLCSALSYQREFHKTK-----VLYCSRThSQIEQIIR--------ELRKLLEKRKI------RALALSSRDA 70
|
90 100 110
....*....|....*....|....*....|...
gi 1590033848 126 DVVVATPGRLMDHMERGKID-FARLEVLVLDEA 157
Cdd:cd17915 71 DIVVLPYPYLLDARIREFIGiDLREQVVIIDEA 103
|
|
| PRP |
smart00157 |
Major prion protein; The prion protein is a major component of scrapie-associated fibrils in ... |
401-455 |
4.79e-04 |
|
Major prion protein; The prion protein is a major component of scrapie-associated fibrils in Creutzfeldt-Jakob disease, kuru, Gerstmann-Straussler syndrome and bovine spongiform encephalopathy.
Pssm-ID: 197548 [Multi-domain] Cd Length: 218 Bit Score: 41.39 E-value: 4.79e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1590033848 401 KRPggewkgKPGGGWKE------GQGKPWGDK-PGQRGGGDKPaYKGNGDRPHAAAGQQQAH 455
Cdd:smart00157 2 KRP------KPGGGWNTggsrypGQGSPGGNRyPPQGGGWGQP-HGGGWGQPHGGGWGQPHG 56
|
|
| RecB |
COG1074 |
3#-5# helicase subunit RecB of the DNA repair enzyme RecBCD (exonuclease V) [Replication, ... |
22-281 |
5.69e-04 |
|
3#-5# helicase subunit RecB of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];
Pssm-ID: 440692 [Multi-domain] Cd Length: 866 Bit Score: 42.64 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 22 NEPTPVQSQAIPAALTGADLLVSAQTGSGKTaaFLLPSLC-RLVeasAAKGYGP-RILVLTPTRelaqqveKAArtygSE 99
Cdd:COG1074 2 SEPPWTDAQRRALDPLGGSVLVEASAGSGKT--YTLVARYlRLL---LERGLDPeEILVVTFTR-------AAA----AE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 100 LR-----KLRTAsLVGGAPYGPQLKLLSQPVDVVVATPGR-------------LMDHMERGKIDFA-----------RLE 150
Cdd:COG1074 66 MRerireRLAEA-ADLEDPDLEELARARRRLARALENLDRaaistihsfcqrlLREFAFEAGLDPNfellddaeallLEE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 151 VL--VLDEADRMLDMGFIDDIKAIVAKTPaerqtllfsATLDGVVGDLARQLTRDAQRIEVARKEESAAKIEQKLhfFDD 228
Cdd:COG1074 145 AVddLLREAYAPLDALALARLLDAFGRDD---------DSLEELLLALYKLRSRPDWLEELAELDEALEALREAL--LKA 213
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1590033848 229 MQHKMRLLDALVRDAAIQQAVVFTATKAGAEELTDELRDRG---------FLAEALHGDMPQ 281
Cdd:COG1074 214 KEALAALREALAAAAAPLLAALLRLLAAVLARYERRKRERGlldfddllhRALRLLRDEDAP 275
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
26-357 |
5.74e-04 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 42.58 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 26 PVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSL-CrlveasaakgygPRI-LVLTPTRELAQ-QVEKAARTygselrK 102
Cdd:PLN03137 463 PNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALiC------------PGItLVISPLVSLIQdQIMNLLQA------N 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 103 LRTASLVGGAPYGPQLKLLSQ------PVDVVVATPGR------LMDHME----RGKIdfARLevlVLDEADRMLDMG-- 164
Cdd:PLN03137 525 IPAASLSAGMEWAEQLEILQElsseysKYKLLYVTPEKvaksdsLLRHLEnlnsRGLL--ARF---VIDEAHCVSQWGhd 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 165 FIDD------IKAIVAKTPAERQTLLFSATL-DGVVGDLA-------RQ-LTRDAQRIEVARKEESAakieqklhfFDDm 229
Cdd:PLN03137 600 FRPDyqglgiLKQKFPNIPVLALTATATASVkEDVVQALGlvncvvfRQsFNRPNLWYSVVPKTKKC---------LED- 669
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 230 qhkmrlLDALVRDAAIQQ-AVVFTATKAGAEELTDELRDRGFLAEALHGDMPQHKRNRTLDRVRTGRVQFLVATDVAARG 308
Cdd:PLN03137 670 ------IDKFIKENHFDEcGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMG 743
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1590033848 309 IDVAGISHVINYDPPRQAEDYVHRIGRTGRAGRSGTAVTLVGF----RERHLV 357
Cdd:PLN03137 744 INKPDVRFVIHHSLPKSIEGYHQECGRAGRDGQRSSCVLYYSYsdyiRVKHMI 796
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
246-338 |
8.08e-04 |
|
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350177 [Multi-domain] Cd Length: 171 Bit Score: 40.31 E-value: 8.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 246 QQAVVFTATKAGAEELTDELRDRGFLAEALHGDMPQHKRNRTLDRVRTGRVQFLVATDVAARGIDVAGISHVINYDP--- 322
Cdd:cd18790 28 ERVLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDAdke 107
|
90
....*....|....*...
gi 1590033848 323 --PRQAEDYVHRIGRTGR 338
Cdd:cd18790 108 gfLRSETSLIQTIGRAAR 125
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
23-156 |
8.17e-04 |
|
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: 40.54 E-value: 8.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 23 EPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRLVEASAAkGYGPRILVLTPTRELAQQVEKAartygsELRK 102
Cdd:cd18036 2 ELRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKRRSA-GEKGRVVVLVNKVPLVEQQLEK------FFKY 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1590033848 103 LRTASLVGGAPYGPQLKLLSQPV----DVVVATPGRLMDHMERGKIDfARLEV-----LVLDE 156
Cdd:cd18036 75 FRKGYKVTGLSGDSSHKVSFGQIvkasDVIICTPQILINNLLSGREE-ERVYLsdfslLIFDE 136
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
258-350 |
1.06e-03 |
|
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: 39.56 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 258 AEELTDELRDRgfLAEA----LHGDMPQHKRNRTLDRVRTGRVQFLVATDVAARGIDVAGISHVINYDPPRQAEDYVHRI 333
Cdd:cd18792 47 IEALAEELKEL--VPEArvalLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFGLSQLHQL 124
|
90
....*....|....*...
gi 1590033848 334 -GRTGRAGRSGTAVTLVG 350
Cdd:cd18792 125 rGRVGRGKHQSYCYLLYP 142
|
|
| UvrD |
COG0210 |
Superfamily I DNA or RNA helicase [Replication, recombination and repair]; |
25-116 |
1.37e-03 |
|
Superfamily I DNA or RNA helicase [Replication, recombination and repair];
Pssm-ID: 439980 [Multi-domain] Cd Length: 721 Bit Score: 41.07 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 25 TPVQSQAIpAALTGAdLLVSAQTGSGKT------AAFLLpslcrlveasAAKGYGP-RILVLTPTRelaqqveKAARtyg 97
Cdd:COG0210 8 NPEQRAAV-EHPEGP-LLVLAGAGSGKTrvlthrIAYLI----------AEGGVDPeQILAVTFTN-------KAAR--- 65
|
90
....*....|....*....
gi 1590033848 98 sELRKlRTASLVGGAPYGP 116
Cdd:COG0210 66 -EMRE-RIEALLGRLARGL 82
|
|
| PRP |
smart00157 |
Major prion protein; The prion protein is a major component of scrapie-associated fibrils in ... |
386-433 |
1.94e-03 |
|
Major prion protein; The prion protein is a major component of scrapie-associated fibrils in Creutzfeldt-Jakob disease, kuru, Gerstmann-Straussler syndrome and bovine spongiform encephalopathy.
Pssm-ID: 197548 [Multi-domain] Cd Length: 218 Bit Score: 39.47 E-value: 1.94e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1590033848 386 GGNKRPwsDKPGYKGKRPGGEWKGKPGGGWKEGQGKPWGDKPGQRGGG 433
Cdd:smart00157 24 GGNRYP--PQGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQ 69
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
20-157 |
2.18e-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: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 20 GYNEPTPVQSQAIPAALTGADLLVSAQTGSGKTAAFLLPSLCRlveasAAKGYGPrILVLTPTRELAQ-QVE------KA 92
Cdd:cd18018 9 GHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLL-----RRRGPGL-TLVVSPLIALMKdQVDalpraiKA 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1590033848 93 ARTYGSELRKLRTASLVggapygpqlKLLSQPVDVVVATPGRLMDHM------ERGKIDFarlevLVLDEA 157
Cdd:cd18018 83 AALNSSLTREERRRILE---------KLRAGEVKILYVSPERLVNESfrellrQTPPISL-----LVVDEA 139
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
42-159 |
2.40e-03 |
|
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350791 [Multi-domain] Cd Length: 182 Bit Score: 38.84 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 42 LVSAQTGSGKT--AAFLLPSLCRLVEASaakgygpRILVLTPTREL-AQQVEKAARTYGseLRKLRTASLVGGAPYGPQL 118
Cdd:cd18033 20 LVALPTGLGKTfiAAVVMLNYYRWFPKG-------KIVFMAPTKPLvSQQIEACYKITG--IPSSQTAELTGSVPPTKRA 90
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1590033848 119 KLLSQPvDVVVATPGRLMDHMERGKIDFARLEVLVLDEADR 159
Cdd:cd18033 91 ELWASK-RVFFLTPQTLENDLKEGDCDPKSIVCLVIDEAHR 130
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
43-337 |
3.14e-03 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 40.29 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 43 VSAQTGSGKTAAFLLPSLCRLVEASAA------KGYGPRILVLTPTRELAQQVEKAART----YGSELRK-------LRT 105
Cdd:PRK09751 1 VIAPTGSGKTLAAFLYALDRLFREGGEdtreahKRKTSRILYISPIKALGTDVQRNLQIplkgIADERRRrgetevnLRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 106 ASLVGGAPYGPQLKLLSQPVDVVVATPGRLMDHM-ERGKIDFARLEVLVLDE----------ADRMLDMGFIDDIkaivA 174
Cdd:PRK09751 81 GIRTGDTPAQERSKLTRNPPDILITTPESLYLMLtSRARETLRGVETVIIDEvhavagskrgAHLALSLERLDAL----L 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 175 KTPAERQTLlfSATLDGvVGDLARQLTRD---------AQR---IEVARKEESAAKIEQKLHFFDDMQHKMR-------- 234
Cdd:PRK09751 157 HTSAQRIGL--SATVRS-ASDVAAFLGGDrpvtvvnppAMRhpqIRIVVPVANMDDVSSVASGTGEDSHAGRegsiwpyi 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 235 ---LLDALVRDAAiqqAVVFTATKAGAEELTDEL------------------------------RDRG---FLAEALHGD 278
Cdd:PRK09751 234 etgILDEVLRHRS---TIVFTNSRGLAEKLTARLnelyaarlqrspsiavdaahfestsgatsnRVQSsdvFIARSHHGS 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1590033848 279 MPQHKRNRTLDRVRTGRVQFLVATDVAARGIDVAGISHVINYDPPRQAEDYVHRIGRTG 337
Cdd:PRK09751 311 VSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
234-346 |
3.41e-03 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 38.01 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 234 RLLDALVRDAAiqQAVVFTATKAGAEELTDELRDR----GFLAEAL---HGDMPQHKRNRTLDRVRTGRVQFLVATDVAA 306
Cdd:cd18797 26 RLFADLVRAGV--KTIVFCRSRKLAELLLRYLKARlveeGPLASKVasyRAGYLAEDRREIEAELFNGELLGVVATNALE 103
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1590033848 307 RGIDVAGISHVINYDPPRQAEDYVHRIGRTGRAGRSGTAV 346
Cdd:cd18797 104 LGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKDSLVI 143
|
|
| PRP |
smart00157 |
Major prion protein; The prion protein is a major component of scrapie-associated fibrils in ... |
381-453 |
3.71e-03 |
|
Major prion protein; The prion protein is a major component of scrapie-associated fibrils in Creutzfeldt-Jakob disease, kuru, Gerstmann-Straussler syndrome and bovine spongiform encephalopathy.
Pssm-ID: 197548 [Multi-domain] Cd Length: 218 Bit Score: 38.70 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 381 KPRPE-------GGNKRPWSDKPGYKGKRPGGEWKGKPGGGWkegqgkpWGdkpGQRGGGDKPAYKGNGDRPHAAAGQQQ 453
Cdd:smart00157 1 KKRPKpgggwntGGSRYPGQGSPGGNRYPPQGGGWGQPHGGG-------WG---QPHGGGWGQPHGGGWGQPHGGGWGQG 70
|
|
| PRP |
smart00157 |
Major prion protein; The prion protein is a major component of scrapie-associated fibrils in ... |
381-455 |
4.02e-03 |
|
Major prion protein; The prion protein is a major component of scrapie-associated fibrils in Creutzfeldt-Jakob disease, kuru, Gerstmann-Straussler syndrome and bovine spongiform encephalopathy.
Pssm-ID: 197548 [Multi-domain] Cd Length: 218 Bit Score: 38.70 E-value: 4.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1590033848 381 KPRPEGGNKRPWSDKPGykgkrpggewKGKPGGGWKEGQGKPWGdkpGQRGGGDKPAYKGNGDRPHAAAGQQQAH 455
Cdd:smart00157 3 RPKPGGGWNTGGSRYPG----------QGSPGGNRYPPQGGGWG---QPHGGGWGQPHGGGWGQPHGGGWGQPHG 64
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
248-311 |
4.05e-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: 37.15 E-value: 4.05e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590033848 248 AVVFTATKAGAEELTDELRDRGFLAEALHGDMPQHKRNR---TLDRVRTGRVQFLVATDVAARGIDV 311
Cdd:cd18799 9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDealILLFFGELKPPILVTVDLLTTGVDI 75
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
41-189 |
4.49e-03 |
|
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 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: 350688 [Multi-domain] Cd Length: 186 Bit Score: 38.04 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 41 LLVSAQTGSGKTAAFLLPSLcrlveASAAKGYGPRILVLTPTRELAQQ----VEKAARTYGSEL----------RKLRTA 106
Cdd:cd17930 4 VILEAPTGSGKTEAALLWAL-----KLAARGGKRRIIYALPTRATINQmyerIREILGRLDDEDkvlllhskaaLELLES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 107 SLVGGAPYGPQLKLLSQPV-----DVVVATPGRLMDHMERGKIDFARL-----EVLVLDEA----DRMLDMgFIDDIKAI 172
Cdd:cd17930 79 DEEPDDDPVEAVDWALLLKrswlaPIVVTTIDQLLESLLKYKHFERRLhglanSVVVLDEVqaydPEYMAL-LLKALLEL 157
|
170
....*....|....*....
gi 1590033848 173 VAK--TPAerqtLLFSATL 189
Cdd:cd17930 158 LGElgGPV----VLMTATL 172
|
|
| VirD4 |
COG3505 |
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ... |
42-97 |
5.56e-03 |
|
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442728 [Multi-domain] Cd Length: 402 Bit Score: 38.81 E-value: 5.56e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1590033848 42 LVSAQTGSGKTAAFLLPSLCRLveasaAKGYGprILVLTPTRELAQQVEKAARTYG 97
Cdd:COG3505 3 LVIGPTGSGKTVGLVIPNLTQL-----ARGES--VVVTDPKGDLAELTAGFRRRAG 51
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
1-94 |
9.23e-03 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 38.40 E-value: 9.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 1 MNFSELGLNPLLAKAVEKTGYNEPTPVQSQAIPAALT-GADLLVSAQTGSGKTaafLLPSLCRLVEASAakgyGPRILVL 79
Cdd:PRK02362 1 MKIAELPLPEGVIEFYEAEGIEELYPPQAEAVEAGLLdGKNLLAAIPTASGKT---LIAELAMLKAIAR----GGKALYI 73
|
90
....*....|....*
gi 1590033848 80 TPTRELAQqvEKAAR 94
Cdd:PRK02362 74 VPLRALAS--EKFEE 86
|
|
| DEXQc_UvrD |
cd17932 |
DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch ... |
25-112 |
9.23e-03 |
|
DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch repair, nucleotide excision repair, and recombinational repair. It plays a critical role in maintaining genomic stability and facilitating DNA lesion repair in many prokaryotic species including Helicobacter pylori and Escherichia coli. UvrD 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: 350690 [Multi-domain] Cd Length: 189 Bit Score: 37.11 E-value: 9.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590033848 25 TPVQSQAIPAalTGADLLVSAQTGSGKTA------AFLLpsLCRLVEASaakgygpRILVLTPTRelaqqveKAARtygs 98
Cdd:cd17932 1 NPEQREAVTH--PDGPLLVLAGAGSGKTRvlthriAYLI--LEGGVPPE-------RILAVTFTN-------KAAK---- 58
|
90
....*....|....
gi 1590033848 99 ELRKlRTASLVGGA 112
Cdd:cd17932 59 EMRE-RLRKLLGEQ 71
|
|
| |
