|
Name |
Accession |
Description |
Interval |
E-value |
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
1-380 |
0e+00 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 682.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 1 MSSGFETLNLHPQLKQAIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLLNNPIQGQRYRGEPR 80
Cdd:PRK01297 85 GKTRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKERYMGEPR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 81 ALILAPTRELALQIESDAKDLTKFTDLNVVTLLGGVDFDKQKSQLNKNFVDIIVATPGRLIDFVEQKEVWLDQIEFLVID 160
Cdd:PRK01297 165 ALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARFCDILVATPGRLLDFNQRGEVHLDMVEVMVLD 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 161 EADRLLDMGFIPAVKRIVRYSPRKEQRQTLMFSATFSYDVLNLAQQWLFEPVTVEIEPEKKTNADVEQRVYMVAKTDKYK 240
Cdd:PRK01297 245 EADRMLDMGFIPQVRQIIRQTPRKEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDKYK 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 241 LLEEILRDEPIEKVMIFANRRDQVRKLYDHLKRDDYKVVMLSGEIAQDKRLKMLDQFKNGKHNIMIATDVAGRGIHVDGV 320
Cdd:PRK01297 325 LLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGI 404
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2156030574 321 SHVVNFTLPEQSDDYVHRIGRTGRAGTRGVSISFLSEDDAFYLPEIEKAIGQKL-----------PLTRLD 380
Cdd:PRK01297 405 SHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKIscemppaellkPVPRKH 475
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
5-382 |
0e+00 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 533.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 5 FETLNLHPQLKQAIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLLNNPiqgqryRGEPRALIL 84
Cdd:COG0513 4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSR------PRAPQALIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 85 APTRELALQIESDAKDLTKFTDLNVVTLLGGVDFDKQKSQLNKNfVDIIVATPGRLIDFVEQKEVWLDQIEFLVIDEADR 164
Cdd:COG0513 78 APTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRG-VDIVVATPGRLLDLIERGALDLSGVETLVLDEADR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 165 LLDMGFIPAVKRIVRYSPrkEQRQTLMFSATFSYDVLNLAQQWLFEPVTVEIEPEKKTNADVEQRVYMVAKTDKYKLLEE 244
Cdd:COG0513 157 MLDMGFIEDIERILKLLP--KERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 245 ILRDEPIEKVMIFANRRDQVRKLYDHLKRDDYKVVMLSGEIAQDKRLKMLDQFKNGKHNIMIATDVAGRGIHVDGVSHVV 324
Cdd:COG0513 235 LLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVI 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2156030574 325 NFTLPEQSDDYVHRIGRTGRAGTRGVSISFLSEDDAFYLPEIEKAIGQKLPLTRLDGY 382
Cdd:COG0513 315 NYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGF 372
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
5-380 |
4.59e-140 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 405.12 E-value: 4.59e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 5 FETLNLHPQLKQAIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLLNNPIQGQRYRGEPRALIL 84
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDRKVNQPRALIM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 85 APTRELALQIESDAKDLTKFTDLNVVTLLGGVDFDKQKSQLNKNfVDIIVATPGRLIDFVEQKEVWLDQIEFLVIDEADR 164
Cdd:PRK04837 90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESG-VDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 165 LLDMGFIPAVKRIVRYSPRKEQRQTLMFSATFSYDVLNLAQQWLFEPVTVEIEPEKKTNADVEQRVYMVAKTDKYKLLEE 244
Cdd:PRK04837 169 MFDLGFIKDIRWLFRRMPPANQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYPSNEEKMRLLQT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 245 ILRDEPIEKVMIFANRRDQVRKLYDHLKRDDYKVVMLSGEIAQDKRLKMLDQFKNGKHNIMIATDVAGRGIHVDGVSHVV 324
Cdd:PRK04837 249 LIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVF 328
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2156030574 325 NFTLPEQSDDYVHRIGRTGRAGTRGVSISFLSEDDAFYLPEIEKAIGQKLPLTRLD 380
Cdd:PRK04837 329 NYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIGHSIPVSKYD 384
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
5-375 |
5.81e-121 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 361.58 E-value: 5.81e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 5 FETLNLHPQLKQAIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLLNNPIQGQRYRGEPRALIL 84
Cdd:PRK04537 11 FSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALADRKPEDPRALIL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 85 APTRELALQIESDAKDLTKFTDLNVVTLLGGVDFDKQKSQLNKNfVDIIVATPGRLIDFVEQKEV-WLDQIEFLVIDEAD 163
Cdd:PRK04537 91 APTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQG-VDVIIATPGRLIDYVKQHKVvSLHACEICVLDEAD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 164 RLLDMGFIPAVKRIVRYSPRKEQRQTLMFSATFSYDVLNLAQQWLFEPVTVEIEPEKKTNADVEQRVYMVAKTDKYKLLE 243
Cdd:PRK04537 170 RMFDLGFIKDIRFLLRRMPERGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADEEKQTLLL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 244 EILRDEPIEKVMIFANRRDQVRKLYDHLKRDDYKVVMLSGEIAQDKRLKMLDQFKNGKHNIMIATDVAGRGIHVDGVSHV 323
Cdd:PRK04537 250 GLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYV 329
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2156030574 324 VNFTLPEQSDDYVHRIGRTGRAGTRGVSISFLSEDDAFYLPEIEKAIGQKLP 375
Cdd:PRK04537 330 YNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKIP 381
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
5-374 |
8.91e-117 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 346.16 E-value: 8.91e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 5 FETLNLHPQLKQAIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLLNNPiqgQRYRGEPRALIL 84
Cdd:PRK11192 3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFP---RRKSGPPRILIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 85 APTRELALQIESDAKDLTKFTDLNVVTLLGGVDFDKQKSQLNKNfVDIIVATPGRLIDFVEQKEVWLDQIEFLVIDEADR 164
Cdd:PRK11192 80 TPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSEN-QDIVVATPGRLLQYIKEENFDCRAVETLILDEADR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 165 LLDMGFIPAVKRIVrysprKEQR---QTLMFSATF-SYDVLNLAQQWLFEPVTVEIEPEKKTNADVEQRVYMV-AKTDKY 239
Cdd:PRK11192 159 MLDMGFAQDIETIA-----AETRwrkQTLLFSATLeGDAVQDFAERLLNDPVEVEAEPSRRERKKIHQWYYRAdDLEHKT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 240 KLLEEILRDEPIEKVMIFANRRDQVRKLYDHLKRDDYKVVMLSGEIAQDKRLKMLDQFKNGKHNIMIATDVAGRGIHVDG 319
Cdd:PRK11192 234 ALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDD 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2156030574 320 VSHVVNFTLPEQSDDYVHRIGRTGRAGTRGVSISFLSEDDAFYLPEIEKAIGQKL 374
Cdd:PRK11192 314 VSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPL 368
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
1-380 |
8.81e-110 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 329.07 E-value: 8.81e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 1 MSSGFETLNLHPQLKQAIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISvindLLNNpIQGQRYRgePR 80
Cdd:PRK11776 2 SMTAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLG----LLQK-LDVKRFR--VQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 81 ALILAPTRELALQIESDAKDLTKFTD-LNVVTLLGGVDFDKQKSQLNKNfVDIIVATPGRLIDFVEQKEVWLDQIEFLVI 159
Cdd:PRK11776 75 ALVLCPTRELADQVAKEIRRLARFIPnIKVLTLCGGVPMGPQIDSLEHG-AHIIVGTPGRILDHLRKGTLDLDALNTLVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 160 DEADRLLDMGFIPAVKRIVRYSPRkeQRQTLMFSATFSYDVLNLAQQWLFEPVTVEIEpEKKTNADVEQRVYMVAKTDKY 239
Cdd:PRK11776 154 DEADRMLDMGFQDAIDAIIRQAPA--RRQTLLFSATYPEGIAAISQRFQRDPVEVKVE-STHDLPAIEQRFYEVSPDERL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 240 KLLEEILRDEPIEKVMIFANRRDQVRKLYDHLKRDDYKVVMLSGEIAQDKRLKMLDQFKNGKHNIMIATDVAGRGIHVDG 319
Cdd:PRK11776 231 PALQRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKA 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2156030574 320 VSHVVNFTLPEQSDDYVHRIGRTGRAGTRGVSISFLSEDDAFYLPEIEKAIGQKLPLTRLD 380
Cdd:PRK11776 311 LEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLP 371
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
1-382 |
5.43e-99 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 301.34 E-value: 5.43e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 1 MSsgFETLNLHPQLKQAIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLLNNPIQGQRYRgeP- 79
Cdd:PRK10590 1 MS--FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRR--Pv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 80 RALILAPTRELALQIESDAKDLTKFTDLNVVTLLGGVDFDKQKSQLnKNFVDIIVATPGRLIDFVEQKEVWLDQIEFLVI 159
Cdd:PRK10590 77 RALILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKL-RGGVDVLVATPGRLLDLEHQNAVKLDQVEILVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 160 DEADRLLDMGFIPAVKRIVRYSPRKeqRQTLMFSATFSYDVLNLAQQWLFEPVTVEIEPEKKTNADVEQRVYMVAKTDKY 239
Cdd:PRK10590 156 DEADRMLDMGFIHDIRRVLAKLPAK--RQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 240 KLLEEILRDEPIEKVMIFANRRDQVRKLYDHLKRDDYKVVMLSGEIAQDKRLKMLDQFKNGKHNIMIATDVAGRGIHVDG 319
Cdd:PRK10590 234 ELLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEE 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2156030574 320 VSHVVNFTLPEQSDDYVHRIGRTGRAGTRGVSISFLSEDDAFYLPEIEKAIGQKLPLTRLDGY 382
Cdd:PRK10590 314 LPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRIAIPGY 376
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
14-215 |
4.48e-92 |
|
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: 274.32 E-value: 4.48e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 14 LKQAIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLLNNPIQGQRyrgEPRALILAPTRELALQ 93
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGR---GPQALVLAPTRELAMQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 94 IESDAKDLTKFTDLNVVTLLGGVDFDKQKSQLNKNfVDIIVATPGRLIDFVEQKEVWLDQIEFLVIDEADRLLDMGFIPA 173
Cdd:cd00268 78 IAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKG-PDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEED 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2156030574 174 VKRIVRYSPRKeqRQTLMFSATFSYDVLNLAQQWLFEPVTVE 215
Cdd:cd00268 157 VEKILSALPKD--RQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
5-358 |
5.68e-88 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 275.88 E-value: 5.68e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 5 FETLNLHPQLKQAIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLLNNPIQgqRYRGEPRALIL 84
Cdd:PTZ00110 132 FEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLL--RYGDGPIVLVL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 85 APTRELALQIESDAKDLTKFTDLNVVTLLGGVDFDKQKSQLnKNFVDIIVATPGRLIDFVEQKEVWLDQIEFLVIDEADR 164
Cdd:PTZ00110 210 APTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYAL-RRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADR 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 165 LLDMGFIPAVKRIVrySPRKEQRQTLMFSATFSYDVLNLAQQWL-FEPVTVEIEP-EKKTNADVEQRVYMVAKTDKY--- 239
Cdd:PTZ00110 289 MLDMGFEPQIRKIV--SQIRPDRQTLMWSATWPKEVQSLARDLCkEEPVHVNVGSlDLTACHNIKQEVFVVEEHEKRgkl 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 240 -KLLEEILRDEPieKVMIFANRRDQVRKLYDHLKRDDYKVVMLSGEIAQDKRLKMLDQFKNGKHNIMIATDVAGRGIHVD 318
Cdd:PTZ00110 367 kMLLQRIMRDGD--KILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVK 444
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2156030574 319 GVSHVVNFTLPEQSDDYVHRIGRTGRAGTRGVSISFLSED 358
Cdd:PTZ00110 445 DVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPD 484
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
5-208 |
6.79e-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: 234.30 E-value: 6.79e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 5 FETLNLHPQLKQAIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLLNNPIQGQRYRG---EPRA 81
Cdd:cd17967 2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGRrkaYPSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 82 LILAPTRELALQIESDAKDLTKFTDLNVVTLLGGVDFDKQKSQLNKNfVDIIVATPGRLIDFVEQKEVWLDQIEFLVIDE 161
Cdd:cd17967 82 LILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRG-CDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2156030574 162 ADRLLDMGFIPAVKRIVRYS--PRKEQRQTLMFSATFSYDVLNLAQQWL 208
Cdd:cd17967 161 ADRMLDMGFEPQIRKIVEHPdmPPKGERQTLMFSATFPREIQRLAADFL 209
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
5-375 |
6.65e-72 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 236.28 E-value: 6.65e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 5 FETLNLHPQLKQAIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLlNNPIQGqryrgePRALIL 84
Cdd:PRK11634 8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNL-DPELKA------PQILVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 85 APTRELALQIESDAKDLTK-FTDLNVVTLLGGVDFDKQKSQLNKNfVDIIVATPGRLIDFVEQKEVWLDQIEFLVIDEAD 163
Cdd:PRK11634 81 APTRELAVQVAEAMTDFSKhMRGVNVVALYGGQRYDVQLRALRQG-PQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 164 RLLDMGFIPAVKRIVRYSPrkEQRQTLMFSATFSYDVLNLAQQWLFEPVTVEIEPEKKTNADVEQRVYMVAKTDKYKLLE 243
Cdd:PRK11634 160 EMLRMGFIEDVETIMAQIP--EGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 244 EILRDEPIEKVMIFANRRDQVRKLYDHLKRDDYKVVMLSGEIAQDKRLKMLDQFKNGKHNIMIATDVAGRGIHVDGVSHV 323
Cdd:PRK11634 238 RFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLV 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2156030574 324 VNFTLPEQSDDYVHRIGRTGRAGTRGVSISFLSEDDAFYLPEIEKAIGQKLP 375
Cdd:PRK11634 318 VNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIP 369
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
10-206 |
1.14e-68 |
|
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: 215.14 E-value: 1.14e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 10 LHPQLKQAIDALGFKEMTPIQQKVLKFTLA-GHDAIGRAQTGTGKTAAFLISVINDLLNNPIQGQRYRgePRALILAPTR 88
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSG--VSALIISPTR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 89 ELALQIESDAKDLTKF-TDLNVVTLLGGVDFDKQKSQLNKNFVDIIVATPGRLIDFVEQ--KEVWLDQIEFLVIDEADRL 165
Cdd:cd17964 79 ELALQIAAEAKKLLQGlRKLRVQSAVGGTSRRAELNRLRRGRPDILVATPGRLIDHLENpgVAKAFTDLDYLVLDEADRL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2156030574 166 LDMGFIPAVKRIVRYSP--RKEQRQTLMFSATFSYDVLNLAQQ 206
Cdd:cd17964 159 LDMGFRPDLEQILRHLPekNADPRQTLLFSATVPDEVQQIARL 201
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
5-208 |
7.91e-68 |
|
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: 214.83 E-value: 7.91e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 5 FETLNLHPQLKQAIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLLNNPIQGQRYRG--EPRAL 82
Cdd:cd18052 45 FEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEGLTASSFSEvqEPQAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 83 ILAPTRELALQIESDAKDLTKFTDLNVVTLLGGVDFDKQKSQLNKNfVDIIVATPGRLIDFVEQKEVWLDQIEFLVIDEA 162
Cdd:cd18052 125 IVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKG-CHILVATPGRLLDFIGRGKISLSKLKYLILDEA 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2156030574 163 DRLLDMGFIPAVKRIVRYS--PRKEQRQTLMFSATFSYDVLNLAQQWL 208
Cdd:cd18052 204 DRMLDMGFGPEIRKLVSEPgmPSKEDRQTLMFSATFPEEIQRLAAEFL 251
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
5-368 |
1.28e-67 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 218.93 E-value: 1.28e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 5 FETLNLHPQLKQAIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLLNNPIQGQryrgeprALIL 84
Cdd:PTZ00424 30 FDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQ-------ALIL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 85 APTRELALQIESDAKDLTKFTDLNVVTLLGGVDFDKQKSQLnKNFVDIIVATPGRLIDFVEQKEVWLDQIEFLVIDEADR 164
Cdd:PTZ00424 103 APTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKL-KAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 165 LLDMGFIPAVKRIVRYSPrkEQRQTLMFSATFSYDVLNLAQQWLFEPVTVEIEPEKKTNADVEQrVYMVAKTDKYKL--L 242
Cdd:PTZ00424 182 MLSRGFKGQIYDVFKKLP--PDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQ-FYVAVEKEEWKFdtL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 243 EEILRDEPIEKVMIFANRRDQVRKLYDHLKRDDYKVVMLSGEIAQDKRLKMLDQFKNGKHNIMIATDVAGRGIHVDGVSH 322
Cdd:PTZ00424 259 CDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSL 338
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2156030574 323 VVNFTLPEQSDDYVHRIGRTGRAGTRGVSISFLSEDDAFYLPEIEK 368
Cdd:PTZ00424 339 VINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIER 384
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
5-215 |
5.05e-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: 200.62 E-value: 5.05e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 5 FETLNLHPQLKQAIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLLNNPiqgQRYrgepRALIL 84
Cdd:cd17954 2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENP---QRF----FALVL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 85 APTRELALQIESDAKDLTKFTDLNVVTLLGGVDFDKQKSQLNKNfVDIIVATPGRLIDFVEQ-KEVWLDQIEFLVIDEAD 163
Cdd:cd17954 75 APTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKK-PHVIVATPGRLVDHLENtKGFSLKSLKFLVMDEAD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2156030574 164 RLLDMGFIPAVKRIVRYSPRkeQRQTLMFSATFSYDVLNLAQQWLFEPVTVE 215
Cdd:cd17954 154 RLLNMDFEPEIDKILKVIPR--ERTTYLFSATMTTKVAKLQRASLKNPVKIE 203
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
17-214 |
3.05e-61 |
|
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: 196.39 E-value: 3.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 17 AIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLLNNPIQGQRYRGE-PRALILAPTRELALQIE 95
Cdd:cd17945 4 VIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDEETKDDgPYALILAPTRELAQQIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 96 SDAKDLTKFTDLNVVTLLGGVDFDKQKSQLnKNFVDIIVATPGRLIDFVEQKEVWLDQIEFLVIDEADRLLDMGFIPAVK 175
Cdd:cd17945 84 EETQKFAKPLGIRVVSIVGGHSIEEQAFSL-RNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQVT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2156030574 176 RIVRYSP------------------RKEQRQTLMFSATFSYDVLNLAQQWLFEPVTV 214
Cdd:cd17945 163 KILDAMPvsnkkpdteeaeklaasgKHRYRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
3-214 |
8.67e-61 |
|
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: 194.83 E-value: 8.67e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 3 SGFETLNLHPQLKQAIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLlnnpiQGQRYRGEPRAL 82
Cdd:cd17959 1 GGFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKL-----KAHSPTVGARAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 83 ILAPTRELALQIESDAKDLTKFTDLNVVTLLGGVDFDKQKSQLNKNfVDIIVATPGRLIDFVEQKEVWLDQIEFLVIDEA 162
Cdd:cd17959 76 ILSPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASN-PDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2156030574 163 DRLLDMGFIPAVKRIVRYSPrkEQRQTLMFSATFSYDVLNLAQQWLFEPVTV 214
Cdd:cd17959 155 DRLFEMGFAEQLHEILSRLP--ENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
14-214 |
9.52e-61 |
|
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: 194.40 E-value: 9.52e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 14 LKQAIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLLNNPiqgqRYRGEPRALILAPTRELALQ 93
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRP----KKKAATRVLVLVPTRELAMQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 94 IESDAKDLTKFTDLNVVTLLGGVDFDKQKSQLNKNfVDIIVATPGRLIDFVEQ-KEVWLDQIEFLVIDEADRLLDMGFIP 172
Cdd:cd17947 77 CFSVLQQLAQFTDITFALAVGGLSLKAQEAALRAR-PDIVIATPGRLIDHLRNsPSFDLDSIEILVLDEADRMLEEGFAD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2156030574 173 AVKRIVRYSPRkeQRQTLMFSATFSYDVLNLAQQWLFEPVTV 214
Cdd:cd17947 156 ELKEILRLCPR--TRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
5-375 |
1.42e-59 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 201.17 E-value: 1.42e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 5 FETLNLHPQLKQAIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLLNNPIQGQRYRGEPRALIL 84
Cdd:PLN00206 123 FSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTIRSGHPSEQRNPLAMVL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 85 APTRELALQIESDAKDLTKFTDLNVVTLLGGvdfDKQKSQLN--KNFVDIIVATPGRLIDFVEQKEVWLDQIEFLVIDEA 162
Cdd:PLN00206 203 TPTRELCVQVEDQAKVLGKGLPFKTALVVGG---DAMPQQLYriQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEV 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 163 DRLLDMGFIPAVKRIVRYSPrkeQRQTLMFSATFSYDVLNLAQQWLFEPVTVEIEPEKKTNADVEQRVYMVAKTDKYKLL 242
Cdd:PLN00206 280 DCMLERGFRDQVMQIFQALS---QPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQKL 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 243 EEILRDEPIEK--VMIFANRRDQVRKLYDHL-KRDDYKVVMLSGEIAQDKRLKMLDQFKNGKHNIMIATDVAGRGIHVDG 319
Cdd:PLN00206 357 FDILKSKQHFKppAVVFVSSRLGADLLANAItVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLR 436
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2156030574 320 VSHVVNFTLPEQSDDYVHRIGRTGRAGTRGVSISFLSEDDAFYLPE---IEKAIGQKLP 375
Cdd:PLN00206 437 VRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPElvaLLKSSGAAIP 495
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
27-203 |
2.79e-55 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 179.36 E-value: 2.79e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 27 TPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLLNNPiqgqryrGEPRALILAPTRELALQIESDAKDLTKFTD 106
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLD-------NGPQALVLAPTRELAEQIYEELKKLGKGLG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 107 LNVVTLLGGVDFDKQKSQLNKnfVDIIVATPGRLIDFVEQKEVwLDQIEFLVIDEADRLLDMGFIPAVKRIVRYSPrkEQ 186
Cdd:pfam00270 74 LKVASLLGGDSRKEQLEKLKG--PDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDMGFGPDLEEILRRLP--KK 148
|
170
....*....|....*..
gi 2156030574 187 RQTLMFSATFSYDVLNL 203
Cdd:pfam00270 149 RQILLLSATLPRNLEDL 165
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
226-355 |
2.10e-54 |
|
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: 175.77 E-value: 2.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 226 VEQRVYMVAKTDKY-KLLEEILRDEPIEKVMIFANRRDQVRKLYDHLKRDDYKVVMLSGEIAQDKRLKMLDQFKNGKHNI 304
Cdd:cd18787 1 IKQLYVVVEEEEKKlLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2156030574 305 MIATDVAGRGIHVDGVSHVVNFTLPEQSDDYVHRIGRTGRAGTRGVSISFL 355
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
18-214 |
4.43e-54 |
|
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: 177.18 E-value: 4.43e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 18 IDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLLNNPIqgqRYRGE-PRALILAPTRELALQIES 96
Cdd:cd17966 5 LKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPP---LERGDgPIVLVLAPTRELAQQIQQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 97 DAKDLTKFTDLNVVTLLGGVDFDKQKSQLNKNfVDIIVATPGRLIDFVEQKEVWLDQIEFLVIDEADRLLDMGFIPAVKR 176
Cdd:cd17966 82 EANKFGGSSRLRNTCVYGGAPKGPQIRDLRRG-VEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 2156030574 177 IVrySPRKEQRQTLMFSATFSYDVLNLAQQWLFEPVTV 214
Cdd:cd17966 161 IV--DQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
5-208 |
1.30e-52 |
|
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: 175.23 E-value: 1.30e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 5 FETLNLHPQLKQAIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLLN-----NPIQGQRYRGE- 78
Cdd:cd18051 23 FSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEqgpgeSLPSESGYYGRr 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 79 ---PRALILAPTRELALQIESDAKDLTKFTDLNVVTLLGGVDFDKQKSQLNKNfVDIIVATPGRLIDFVEQKEVWLDQIE 155
Cdd:cd18051 103 kqyPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERG-CHLLVATPGRLVDMLERGKIGLDYCK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2156030574 156 FLVIDEADRLLDMGFIPAVKRIVRYS--PRKEQRQTLMFSATFSYDVLNLAQQWL 208
Cdd:cd18051 182 YLVLDEADRMLDMGFEPQIRRIVEQDtmPPTGERQTLMFSATFPKEIQMLARDFL 236
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
14-214 |
3.47e-52 |
|
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: 172.38 E-value: 3.47e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 14 LKQAIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLLNNPIQGQryRGEPRALILAPTRELALQ 93
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLK--KGQVGALIISPTRELATQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 94 IESDAKDLTKFTDLNVVTLL--GGVDFDKQKSQLNKNFVDIIVATPGRLIDFVEQKEVWLD--QIEFLVIDEADRLLDMG 169
Cdd:cd17960 79 IYEVLQSFLEHHLPKLKCQLliGGTNVEEDVKKFKRNGPNILVGTPGRLEELLSRKADKVKvkSLEVLVLDEADRLLDLG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2156030574 170 FIPAVKRIVRYSPRkeQRQTLMFSATFSYDVLNLAQQWLFEPVTV 214
Cdd:cd17960 159 FEADLNRILSKLPK--QRRTGLFSATQTDAVEELIKAGLRNPVRV 201
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
18-229 |
3.30e-51 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 169.98 E-value: 3.30e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 18 IDALGFKEMTPIQQKVLKFTLAG-HDAIGRAQTGTGKTAAFLISVINDLLNNPiqgqryrgEPRALILAPTRELALQIES 96
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGK--------GGRVLVLVPTRELAEQWAE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 97 DAKDLTKFTDLNVVTLLGGVDFDKQKSQLNKNFVDIIVATPGRLIDFVEQKEVWLDQIEFLVIDEADRLLDMGFIPAVKR 176
Cdd:smart00487 73 ELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2156030574 177 IVRYSPRKeqRQTLMFSATFSYDVLNLAQQWLFEPvtVEIEPEKKTNADVEQR 229
Cdd:smart00487 153 LLKLLPKN--VQLLLLSATPPEEIENLLELFLNDP--VFIDVGFTPLEPIEQF 201
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
14-214 |
7.58e-51 |
|
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: 168.75 E-value: 7.58e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 14 LKQAIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLLNNPiqgQRYRGE-PRALILAPTRELAL 92
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQR---ELEKGEgPIAVIVAPTRELAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 93 QIESDAKDLTKFTDLNVVTLLGGVDFDKQKSQLNKNfVDIIVATPGRLIDFVEQKEVWLDQIEFLVIDEADRLLDMGFIP 172
Cdd:cd17952 78 QIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEG-AEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEY 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2156030574 173 AVKRIVRYSprKEQRQTLMFSATFSYDVLNLAQQWLFEPVTV 214
Cdd:cd17952 157 QVRSIVGHV--RPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
14-214 |
1.44e-50 |
|
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: 168.24 E-value: 1.44e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 14 LKQAidalGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLLNNpiQGQRYRGEPrALILAPTRELALQ 93
Cdd:cd17941 5 LKEA----GFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRE--RWTPEDGLG-ALIISPTRELAMQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 94 IESDAKDLTKFTDLNVVTLLGGVDFDKQKSQLNKnfVDIIVATPGRLIDFVEQkEVWLD--QIEFLVIDEADRLLDMGFI 171
Cdd:cd17941 78 IFEVLRKVGKYHSFSAGLIIGGKDVKEEKERINR--MNILVCTPGRLLQHMDE-TPGFDtsNLQMLVLDEADRILDMGFK 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2156030574 172 PAVKRIVRYSPRKeqRQTLMFSATFSYDVLNLAQQWLFEPVTV 214
Cdd:cd17941 155 ETLDAIVENLPKS--RQTLLFSATQTKSVKDLARLSLKNPEYI 195
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
5-214 |
2.48e-50 |
|
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: 167.86 E-value: 2.48e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 5 FETLNLHPQLKQAIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVIN--DLLNNPIQgqryrgeprAL 82
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEkiDPKKDVIQ---------AL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 83 ILAPTRELALQIESDAKDLTKFTDLNVVTLLGGVDFDKQKSQLNkNFVDIIVATPGRLIDFVEQKEVWLDQIEFLVIDEA 162
Cdd:cd17940 72 ILVPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLY-QTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2156030574 163 DRLLDMGFIPAVKRIVRYSPRkeQRQTLMFSATFSYDVLNLAQQWLFEPVTV 214
Cdd:cd17940 151 DKLLSQDFQPIIEKILNFLPK--ERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
13-214 |
5.30e-50 |
|
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: 167.55 E-value: 5.30e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 13 QLKQAIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDllnnpIQGQRYRGE---PRALILAPTRE 89
Cdd:cd17953 22 KVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRH-----IKDQRPVKPgegPIGLIMAPTRE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 90 LALQIESDAKDLTKFTDLNVVTLLGGVDFDKQKSQLnKNFVDIIVATPGRLIDFV---EQKEVWLDQIEFLVIDEADRLL 166
Cdd:cd17953 97 LALQIYVECKKFSKALGLRVVCVYGGSGISEQIAEL-KRGAEIVVCTPGRMIDILtanNGRVTNLRRVTYVVLDEADRMF 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2156030574 167 DMGFIPAVKRIVRySPRKEqRQTLMFSATFSYDVLNLAQQWLFEPVTV 214
Cdd:cd17953 176 DMGFEPQIMKIVN-NIRPD-RQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
5-215 |
1.14e-49 |
|
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: 166.25 E-value: 1.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 5 FETLNLHPQLKQAIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVIndllnnpiqgQRYRGEPR---A 81
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPIL----------QRLSEDPYgifA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 82 LILAPTRELALQIESDAKDLTKFTDLNVVTLLGGVDFDKQKSQLNKNfVDIIVATPGRLIDFVE---QKEVWLDQIEFLV 158
Cdd:cd17955 71 LVLTPTRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKR-PHIVVATPGRLADHLRssdDTTKVLSRVKFLV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2156030574 159 IDEADRLLDMGFIPAVKRIVRYSPRKeqRQTLMFSATFSYDVLNLAQQWLFEPVTVE 215
Cdd:cd17955 150 LDEADRLLTGSFEDDLATILSALPPK--RQTLLFSATLTDALKALKELFGNKPFFWE 204
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
14-216 |
1.75e-49 |
|
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350715 [Multi-domain] Cd Length: 198 Bit Score: 165.45 E-value: 1.75e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 14 LKQAIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLLNnpiqgQRYRGEPRALILAPTRELALQ 93
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGK-----PRKKKGLRALILAPTRELASQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 94 IESDAKDLTKFTDLNVVtLLGGVDFDKQKSQLN-KNFVDIIVATPGRLIDFVEQKEVWLDQIEFLVIDEADRLLDMGFIP 172
Cdd:cd17957 76 IYRELLKLSKGTGLRIV-LLSKSLEAKAKDGPKsITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFRE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2156030574 173 AVKRIVRY--SPRKeqrQTLMFSATFSYDVLNLAQQWLFEPVTVEI 216
Cdd:cd17957 155 QTDEILAActNPNL---QRSLFSATIPSEVEELARSVMKDPIRIIV 197
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
14-199 |
3.88e-49 |
|
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: 165.88 E-value: 3.88e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 14 LKQAIDALGFKEMTPIQQKVLKFTLA-GHDAIGRAQTGTGKTAAFLISVINDLL-----NNPIQGQRYrgePRALILAPT 87
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLLsqkssNGVGGKQKP---LRALILTPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 88 RELALQIESDAKDLTKFTDLNVVTLLGGVDFDKQKSQLNKNfVDIIVATPGRLIDFVEQKE---VWLDQIEFLVIDEADR 164
Cdd:cd17946 78 RELAVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKR-PEIVVATPGRLWELIQEGNehlANLKSLRFLVLDEADR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2156030574 165 LLDMGFIPAVKRIVR--YSPR---KEQRQTLMFSATFSYD 199
Cdd:cd17946 157 MLEKGHFAELEKILEllNKDRagkKRKRQTFVFSATLTLD 196
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
10-214 |
2.60e-48 |
|
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: 162.75 E-value: 2.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 10 LHPQLKQAIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLLNNPIQGQRYRGePRALILAPTRE 89
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGEEQG-TRALILVPTRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 90 LALQIESDAKDLTKFT--DLNVVTLLGGVDFDKQKSQLNKNfVDIIVATPGRLIDFVEQKEVWL-DQIEFLVIDEADRLL 166
Cdd:cd17961 80 LAQQVSKVLEQLTAYCrkDVRVVNLSASSSDSVQRALLAEK-PDIVVSTPARLLSHLESGSLLLlSTLKYLVIDEADLVL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2156030574 167 DMGFIPAVKRIVRYSPRKeqRQTLMFSATFSYDVLNLAQQWLFEPVTV 214
Cdd:cd17961 159 SYGYEEDLKSLLSYLPKN--YQTFLMSATLSEDVEALKKLVLHNPAIL 204
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
16-214 |
3.00e-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: 162.25 E-value: 3.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 16 QAIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLLNNPIQGQRyRGEPRALILAPTRELALQIE 95
Cdd:cd17958 3 KEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPREQ-RNGPGVLVLTPTRELALQIE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 96 SDAKDLtKFTDLNVVTLLGGVDFDKQKSQLNKNfVDIIVATPGRLIDFVEQKEVWLDQIEFLVIDEADRLLDMGFIPAVK 175
Cdd:cd17958 82 AECSKY-SYKGLKSVCVYGGGNRNEQIEDLSKG-VDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 2156030574 176 RIVRYSprKEQRQTLMFSATFSYDVLNLAQQWLFEPVTV 214
Cdd:cd17958 160 KILLDI--RPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
21-214 |
3.63e-45 |
|
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: 154.67 E-value: 3.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 21 LGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLLNNPIQGQRYRGePRALILAPTRELALQIESDAKD 100
Cdd:cd17949 9 MGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDRSDG-TLALVLVPTRELALQIYEVLEK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 101 LTK-FTDLNVVTLLGGVDFDKQKSQLNKNfVDIIVATPGRLIDFVEQKEVW-LDQIEFLVIDEADRLLDMGFIPAVKRIV 178
Cdd:cd17949 88 LLKpFHWIVPGYLIGGEKRKSEKARLRKG-VNILIATPGRLLDHLKNTQSFdVSNLRWLVLDEADRLLDMGFEKDITKIL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2156030574 179 RY-----------SPRKEQRQTLMFSATFSYDVLNLAQQWLFEPVTV 214
Cdd:cd17949 167 ELlddkrskaggeKSKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
15-204 |
6.62e-44 |
|
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: 150.97 E-value: 6.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 15 KQAIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVInDLLNnpiqgqRYRGEPR----ALILAPTREL 90
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAI-ELLY------KLKFKPRngtgVIIISPTREL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 91 ALQIESDAKDLTKFTDLNVVTLLGGVDfDKQKSQLNKNFVDIIVATPGRLIDFVEQKEVWL-DQIEFLVIDEADRLLDMG 169
Cdd:cd17942 75 ALQIYGVAKELLKYHSQTFGIVIGGAN-RKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLyKNLQCLIIDEADRILEIG 153
|
170 180 190
....*....|....*....|....*....|....*
gi 2156030574 170 FIPAVKRIVRYSPRkeQRQTLMFSATFSYDVLNLA 204
Cdd:cd17942 154 FEEEMRQIIKLLPK--RRQTMLFSATQTRKVEDLA 186
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
7-212 |
2.04e-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: 147.09 E-value: 2.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 7 TLNLHPQLKQAIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLLNNPIQGQryrgeprALILAP 86
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQ-------ALVLAP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 87 TRELALQIESDAKDLTKFTDLNVVTLLGGVDFDKQKSQLNKNfVDIIVATPGRLIDFVEQKEVWLDQIEFLVIDEADRLL 166
Cdd:cd17939 74 TRELAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYG-PHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEML 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2156030574 167 DMGFIPAVKRIVRYSPRKEqrQTLMFSATFSYDVLNLAQQWLFEPV 212
Cdd:cd17939 153 SRGFKDQIYDIFQFLPPET--QVVLFSATMPHEVLEVTKKFMRDPV 196
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
5-216 |
4.43e-41 |
|
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: 144.77 E-value: 4.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 5 FETLNLHPQLKQAIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLLNNPIQgQRYRGePRALIL 84
Cdd:cd18049 26 FYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFL-ERGDG-PICLVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 85 APTRELALQIESDAKDLTKFTDLNVVTLLGGVDFDKQKSQLNKNfVDIIVATPGRLIDFVEQKEVWLDQIEFLVIDEADR 164
Cdd:cd18049 104 APTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERG-VEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADR 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2156030574 165 LLDMGFIPAVKRIVrySPRKEQRQTLMFSATFSYDVLNLAQQWLFEPVTVEI 216
Cdd:cd18049 183 MLDMGFEPQIRKIV--DQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINI 232
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
23-216 |
7.15e-41 |
|
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: 145.15 E-value: 7.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 23 FKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLLNNPIQgqrYRGE-PRALILAPTRELALQIESDAKDL 101
Cdd:cd18050 82 FKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYL---ERGDgPICLVLAPTRELAQQVQQVADDY 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 102 TKFTDLNVVTLLGGVDFDKQKSQLNKNfVDIIVATPGRLIDFVEQKEVWLDQIEFLVIDEADRLLDMGFIPAVKRIVryS 181
Cdd:cd18050 159 GKSSRLKSTCIYGGAPKGPQIRDLERG-VEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIV--D 235
|
170 180 190
....*....|....*....|....*....|....*
gi 2156030574 182 PRKEQRQTLMFSATFSYDVLNLAQQWLFEPVTVEI 216
Cdd:cd18050 236 QIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINI 270
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
22-214 |
1.80e-40 |
|
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: 142.09 E-value: 1.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 22 GFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLLNNPIQGQRYRGE-PRALILAPTRELALQ----IES 96
Cdd:cd17951 9 GIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEKKLPFIKGEgPYGLIVCPSRELARQthevIEY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 97 DAKDLTK--FTDLNVVTLLGGVDFDKQkSQLNKNFVDIIVATPGRLIDFVEQKEVWLDQIEFLVIDEADRLLDMGFIPAV 174
Cdd:cd17951 89 YCKALQEggYPQLRCLLCIGGMSVKEQ-LEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMIDMGFEEDI 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2156030574 175 KRIVRYSprKEQRQTLMFSATFSYDVLNLAQQWLFEPVTV 214
Cdd:cd17951 168 RTIFSYF--KGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
14-214 |
3.93e-40 |
|
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: 140.76 E-value: 3.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 14 LKQAIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVIndllnnpIQGQRYRGEPRALILAPTRELALQ 93
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVI-------IRCLTEHRNPSALILTPTRELAVQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 94 IESDAKDLTK-FTDLNVVTLLGGVDFDKQKSQLNKNfVDIIVATPGRLIDFVEQKEVWLDQIEFLVIDEADRLLDMGFIP 172
Cdd:cd17962 74 IEDQAKELMKgLPPMKTALLVGGLPLPPQLYRLQQG-VKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQ 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2156030574 173 AVKRIVRYSPRkeQRQTLMFSATFSYDVLNLAQQWLFEPVTV 214
Cdd:cd17962 153 QVLDILENISH--DHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
2-216 |
4.60e-40 |
|
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: 4.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 2 SSGFETLNLHPQLKQAIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLLNNPiqgqryrGEPRA 81
Cdd:cd17950 1 SSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVD-------GQVSV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 82 LILAPTRELALQIESDAKDLTKF-TDLNVVTLLGGVDFDKQKSQLNKNFVDIIVATPGRLIDFVEQKEVWLDQIEFLVID 160
Cdd:cd17950 74 LVICHTRELAFQISNEYERFSKYmPNVKTAVFFGGVPIKKDIEVLKNKCPHIVVGTPGRILALVREKKLKLSHVKHFVLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2156030574 161 EADRL---LDMGfiPAVKRIVRYSPRkeQRQTLMFSATFSYDVLNLAQQWLFEPVTVEI 216
Cdd:cd17950 154 ECDKMleqLDMR--RDVQEIFRATPH--DKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
5-215 |
1.18e-39 |
|
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350696 [Multi-domain] Cd Length: 204 Bit Score: 139.76 E-value: 1.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 5 FETLNLHPQLKQAIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLlnnpiqgqryrgepRALIL 84
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV--------------VALIL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 85 APTRELALQIESDAKDLTKFTD---LNVVTLLGGVDFDKQKSQLNKNfVDIIVATPGRLIDFVEQKEVWLDQIEFLVIDE 161
Cdd:cd17938 67 EPSRELAEQTYNCIENFKKYLDnpkLRVALLIGGVKAREQLKRLESG-VDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDE 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2156030574 162 ADRLLDMGFIPAVKRIVRYSPR---KEQR-QTLMFSATF-SYDVLNLAQQWLFEPVTVE 215
Cdd:cd17938 146 ADRLLSQGNLETINRIYNRIPKitsDGKRlQVIVCSATLhSFEVKKLADKIMHFPTWVD 204
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
10-206 |
1.28e-38 |
|
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: 136.94 E-value: 1.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 10 LHPQLKQAIDALGFKEMTPIQQKVLKFTLAG--HDAIGRAQTGTGKTAAFLISVIN--DLLNNpiqgqryrgEPRALILA 85
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSrvDPTLK---------SPQALCLA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 86 PTRELALQIESDAKDLTKFTDLNVVTLLGGVDFDKqksqlNKNFVD-IIVATPGRLIDFVEQKEVWLDQIEFLVIDEADR 164
Cdd:cd17963 72 PTRELARQIGEVVEKMGKFTGVKVALAVPGNDVPR-----GKKITAqIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADV 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2156030574 165 LLDM-GFIPAVKRIVRYSPRkeQRQTLMFSATFSYDVLNLAQQ 206
Cdd:cd17963 147 MLDTqGHGDQSIRIKRMLPR--NCQILLFSATFPDSVRKFAEK 187
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
5-214 |
8.20e-38 |
|
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: 134.88 E-value: 8.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 5 FETLNLHPQLKQAIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLLNNpiqgqryRGEPRALIL 84
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTS-------LKATQALVL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 85 APTRELALQIESDAKDLTKFTDLNVVTLLGGVDF--DKQKSQLNknfVDIIVATPGRLIDFVEQKEVWLDQIEFLVIDEA 162
Cdd:cd18046 74 APTRELAQQIQKVVMALGDYMGIKCHACIGGTSVrdDAQKLQAG---PHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2156030574 163 DRLLDMGFIPAVKRIVRYSPrkEQRQTLMFSATFSYDVLNLAQQWLFEPVTV 214
Cdd:cd18046 151 DEMLSRGFKDQIYDIFQKLP--PDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
14-211 |
9.35e-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: 135.84 E-value: 9.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 14 LKQAIDALGFKEMTPIQQKVLKFTLAG--HDAIGR-------AQTGTGKTAAFLISVINDLLnnpiqgQRYRGEPRALIL 84
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskSTPPYRpgdlcvsAPTGSGKTLAYVLPIVQALS------KRVVPRLRALIV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 85 APTRELALQIESDAKDLTKFTDLNVVTLLGGVDFDKQKSQLNK-------NFVDIIVATPGRLIDFVEQKEVW-LDQIEF 156
Cdd:cd17956 75 VPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVdtsgrylSRVDILVATPGRLVDHLNSTPGFtLKHLRF 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2156030574 157 LVIDEADRLLDMGF-----------------IPAVKRIVRYSPRKEQR-QTLMFSATFSYDVLNLAQQWLFEP 211
Cdd:cd17956 155 LVIDEADRLLNQSFqdwletvmkalgrptapDLGSFGDANLLERSVRPlQKLLFSATLTRDPEKLSSLKLHRP 227
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
16-208 |
3.91e-37 |
|
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: 133.43 E-value: 3.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 16 QAIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLLNNpiQGQRYRGE-PRALILAPTRELALQI 94
Cdd:cd17944 3 KLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQED--QQPRKRGRaPKVLVLAPTRELANQV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 95 ESDAKDLTKftDLNVVTLLGGVDFDKQKSQLnKNFVDIIVATPGRLIDFVEQKEVWLDQIEFLVIDEADRLLDMGFIPAV 174
Cdd:cd17944 81 TKDFKDITR--KLSVACFYGGTPYQQQIFAI-RNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQV 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 2156030574 175 KRIVRYSPRK---EQRQTLMFSATFSYDVLNLAQQWL 208
Cdd:cd17944 158 EEILSVSYKKdseDNPQTLLFSATCPDWVYNVAKKYM 194
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
5-214 |
4.31e-35 |
|
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: 127.97 E-value: 4.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 5 FETLNLHPQLKQAIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINdLLNNPIQgqryrgEPRALIL 84
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQ-CLDIQVR------ETQALIL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 85 APTRELALQIESDAKDLTKFTDLNVVTLLGGVDFDKQKSQLNKNfVDIIVATPGRLIDFVEQKEVWLDQIEFLVIDEADR 164
Cdd:cd18045 74 SPTRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYG-QHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2156030574 165 LLDMGFIPAVKRIVRYSPRKEqrQTLMFSATFSYDVLNLAQQWLFEPVTV 214
Cdd:cd18045 153 MLNKGFKEQIYDVYRYLPPAT--QVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
17-215 |
6.96e-34 |
|
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: 124.30 E-value: 6.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 17 AIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLLnnpiqgqRYRGEPRALILAPTRELALQIES 96
Cdd:cd17943 4 GLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLD-------LERRHPQVLILAPTREIAVQIHD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 97 DAKDL-TKFTDLNVVTLLGGVDFDKQKSQLNKnfVDIIVATPGRLIDFVEQKEVWLDQIEFLVIDEADRLLDMGFIPAVK 175
Cdd:cd17943 77 VFKKIgKKLEGLKCEVFIGGTPVKEDKKKLKG--CHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2156030574 176 RIvrYSPRKEQRQTLMFSATFSYDVLNLAQQWLFEPVTVE 215
Cdd:cd17943 155 WI--FSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
237-346 |
7.18e-32 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 116.16 E-value: 7.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 237 DKYKLLEEILRDEPIEKVMIFANRRDQVRKLYdHLKRDDYKVVMLSGEIAQDKRLKMLDQFKNGKHNIMIATDVAGRGIH 316
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLEAEL-LLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 2156030574 317 VDGVSHVVNFTLPEQSDDYVHRIGRTGRAG 346
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
14-196 |
8.01e-29 |
|
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: 112.07 E-value: 8.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 14 LKQAIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLLNNPIQGQRYRGEPRALILAPTRELALQ 93
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPFNAPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 94 IESDAKDLTKFTDLNVVTLLGGvdfDKQKSQLNKNF--VDIIVATPGRLIDFVEQKEVWLDQIEFLVIDEADRLLDMGFI 171
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITGG---RTKRQIRNPHFeeVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFN 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 2156030574 172 PAVKRIVRYSPRKEQR-----------QTLMFSATF 196
Cdd:cd17948 158 EKLSHFLRRFPLASRRsentdgldpgtQLVLVSATM 193
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
5-222 |
1.02e-24 |
|
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: 100.87 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 5 FETLNLHPQLKQAIDALGFKEMTPIQQKVLKFTLAG--HDAIGRAQTGTGKTAAFLISVINDLLNNpiqgQRYrgePRAL 82
Cdd:cd18048 20 FEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDAL----KLY---PQCL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 83 ILAPTRELALQIESDAKDLTKF-TDLNVVTLLGGVDFDKqKSQLNKNfvdIIVATPGRLIDFV-EQKEVWLDQIEFLVID 160
Cdd:cd18048 93 CLSPTFELALQTGKVVEEMGKFcVGIQVIYAIRGNRPGK-GTDIEAQ---IVIGTPGTVLDWCfKLRLIDVTNISVFVLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2156030574 161 EADRLLDM-GFIPAVKRIVRYSPRkeQRQTLMFSATFSYDVLNLAQQWLFEPVTVEIEPEKKT 222
Cdd:cd18048 169 EADVMINVqGHSDHSVRVKRSMPK--ECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
265-346 |
2.37e-24 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 95.36 E-value: 2.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 265 RKLYDHLKRDDYKVVMLSGEIAQDKRLKMLDQFKNGKHNIMIATDVAGRGIHVDGVSHVVNFTLPEQSDDYVHRIGRTGR 344
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 2156030574 345 AG 346
Cdd:smart00490 81 AG 82
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
5-195 |
4.86e-24 |
|
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: 99.37 E-value: 4.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 5 FETLNLHPQ----LKQAIDALGFKEM-----TPIQQKVLK-----------------------FTLAghdaigrAQTGTG 52
Cdd:cd17965 1 FDQLKLLPSvreaIIKEILKGSNKTDeeikpSPIQTLAIKkllktlmrkvtkqtsneepklevFLLA-------AETGSG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 53 KTAAFLISVINDL----------LNNPIQGQRYRGEPRALILAPTRELALQIESDAKDLTKFTDLNVVTLLGGVDFDKQK 122
Cdd:cd17965 74 KTLAYLAPLLDYLkrqeqepfeeAEEEYESAKDTGRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGPSYQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2156030574 123 SQL-NKNFVDIIVATPGRLIDFVEQKEVWLDQIEFLVIDEADRLLDMGFIPAVKRIVRYSPRKEQrqtLMF-SAT 195
Cdd:cd17965 154 LQLaFKGRIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKH---LILcSAT 225
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
49-324 |
5.33e-23 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 100.48 E-value: 5.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 49 TGTGKT--AAFLIsvindllnnpiqgQRYRGEPRALILAPTRELALQIesdAKDLTKFTDLnvvTLLGGVDFDKQKsqln 126
Cdd:COG1061 109 TGTGKTvlALALA-------------AELLRGKRVLVLVPRRELLEQW---AEELRRFLGD---PLAGGGKKDSDA---- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 127 knfvDIIVATPGRLIDFVEQKEVwLDQIEFLVIDEADRLLDMGFipavKRIVRYSPRKEqrqTLMFSAT----------- 195
Cdd:COG1061 166 ----PITVATYQSLARRAHLDEL-GDRFGLVIIDEAHHAGAPSY----RRILEAFPAAY---RLGLTATpfrsdgreill 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 196 ---------FSYDVLnLAQQWL----FEPVTVEIEPEKKTNADVEQRV---YMVAKTDKYKLLEEILRDEP-IEKVMIFA 258
Cdd:COG1061 234 flfdgivyeYSLKEA-IEDGYLappeYYGIRVDLTDERAEYDALSERLreaLAADAERKDKILRELLREHPdDRKTLVFC 312
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2156030574 259 NRRDQVRKLYDHLKRDDYKVVMLSGEIAQDKRLKMLDQFKNGKHNIMIATDVAGRGIHVDGVSHVV 324
Cdd:COG1061 313 SSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI 378
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
240-362 |
6.46e-17 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 82.47 E-value: 6.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 240 KLLEEILRDEPIEKVMIFANRRDQVRKLYDHLKRDDYKVVMLSGEIA--------QDKRLKMLDQFKNGKHNIMIATDVA 311
Cdd:COG1111 342 EILKEQLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQASkegdkgltQKEQIEILERFRAGEFNVLVATSVA 421
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2156030574 312 GRGIHVDGVSHVVNFTLPEQSDDYVHRIGRTGRAGTrG---VSISFLSEDDAFY 362
Cdd:COG1111 422 EEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGRKRE-GrvvVLIAKGTRDEAYY 474
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
5-211 |
2.12e-16 |
|
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both mRNA (mRNA) export from the nucleus into the cytoplasm and in mRNA translation. DDX19 functions in the nucleus in resolving RNA:DNA hybrids (R-loops). Activation of a DNA damage response pathway dependent upon the ATR kinase, a major regulator of replication fork progression, stimulates translocation of DDX19 from the cytoplasm into the nucleus. Only nuclear Ddx19 is competent to resolve R-loops. DDX19 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350805 [Multi-domain] Cd Length: 205 Bit Score: 77.07 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 5 FETLNLHPQLKQAIDALGFKEMTPIQQKVLKFTLAG--HDAIGRAQTGTGKTAAFLISVINDLlnNPIQGQRyrgepRAL 82
Cdd:cd18047 3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV--EPANKYP-----QCL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 83 ILAPTRELALQIESDAKDLTKFtdLNVVTLLGGVDFDKQKSQLNKNfVDIIVATPGRLIDF-VEQKEVWLDQIEFLVIDE 161
Cdd:cd18047 76 CLSPTYELALQTGKVIEQMGKF--YPELKLAYAVRGNKLERGQKIS-EQIVIGTPGTVLDWcSKLKFIDPKKIKVFVLDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2156030574 162 ADRLL-DMGFIPAVKRIVRYSPRKeqRQTLMFSATFSYDVLNLAQQWLFEP 211
Cdd:cd18047 153 ADVMIaTQGHQDQSIRIQRMLPRN--CQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
238-340 |
3.36e-13 |
|
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: 65.96 E-value: 3.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 238 KYKLLEEILRD--EPIEKVMIFANRRDQVRKLYDHLKRDDYKVVMLSGEIAQDKRLKMLDQFKNGKHN--IMIATDVAGR 313
Cdd:cd18793 12 KLEALLELLEElrEPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGV 91
|
90 100 110
....*....|....*....|....*....|...
gi 2156030574 314 GIHVDGVSHVVNFTLP------EQSDDYVHRIG 340
Cdd:cd18793 92 GLNLTAANRVILYDPWwnpaveEQAIDRAHRIG 124
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
235-362 |
4.45e-13 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 70.67 E-value: 4.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 235 KTDKYK-LLEEILRDEPIEKVMIFANRRDQVRKLYDHLKRDDYKVVMLSGE--------IAQDKRLKMLDQFKNGKHNIM 305
Cdd:PRK13766 348 KLEKLReIVKEQLGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGQaskdgdkgMSQKEQIEILDKFRAGEFNVL 427
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2156030574 306 IATDVAGRGIHVDGVSHVVnFTLPEQSD-DYVHRIGRTGRA-----------GTRgvsisflseDDAFY 362
Cdd:PRK13766 428 VSTSVAEEGLDIPSVDLVI-FYEPVPSEiRSIQRKGRTGRQeegrvvvliakGTR---------DEAYY 486
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
238-342 |
2.59e-12 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 68.33 E-value: 2.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 238 KYKLLEEILRD--EPIEKVMIFANRRDQVRKLYDHLKRDDYKVVMLSGEIAQDKRLKMLDQFKNGKHN--IMIATDVAGR 313
Cdd:COG0553 534 KLEALLELLEEllAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEApvFLISLKAGGE 613
|
90 100 110
....*....|....*....|....*....|....*
gi 2156030574 314 GIHVDGVSHVVNFTLP------EQSDDYVHRIGRT 342
Cdd:COG0553 614 GLNLTAADHVIHYDLWwnpaveEQAIDRAHRIGQT 648
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
40-195 |
6.40e-12 |
|
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: 62.81 E-value: 6.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 40 GHDAIGRAQTGTGKTAAFLISVINDLLNNpiqgqryrgEPRALILAPTRELALQIESDAKDLtkFTDLNVVTLLGGVDFD 119
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLKK---------GKKVLVLVPTKALALQTAERLREL--FGPGIRVAVLVGGSSA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 120 KQKSQLNKNFVDIIVATPGRLIDFVEQKE-VWLDQIEFLVIDEADRLLDMGFipaVKRIVRYSPRKEQR---QTLMFSAT 195
Cdd:cd00046 70 EEREKNKLGDADIIIATPDMLLNLLLREDrLFLKDLKLIIVDEAHALLIDSR---GALILDLAVRKAGLknaQVILLSAT 146
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
25-162 |
4.01e-11 |
|
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: 61.51 E-value: 4.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 25 EMTPIQQKVLK-FTLAGHDAIGRAQTGTGKTAAFLISVINDLLnnpiqgqryRGEPRALILAPTRELALQIESDAKDLTK 103
Cdd:cd17921 1 LLNPIQREALRaLYLSGDSVLVSAPTSSGKTLIAELAILRALA---------TSGGKAVYIAPTRALVNQKEADLRERFG 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2156030574 104 FTDLNVVTLLGGVDFDKQKSQLNknfvDIIVATP----GRLIDFveqKEVWLDQIEFLVIDEA 162
Cdd:cd17921 72 PLGKNVGLLTGDPSVNKLLLAEA----DILVATPekldLLLRNG---GERLIQDVRLVVVDEA 127
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
49-162 |
3.24e-10 |
|
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: 59.20 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 49 TGTGKTaafLISV--INDLLNnpIQGQRYRGEPRALILAPTRELALQiesDAKDLTKFTDLNVVTLLGGVDFDKQKSQLN 126
Cdd:cd18034 25 TGSGKT---LIAVmlIKEMGE--LNRKEKNPKKRAVFLVPTVPLVAQ---QAEAIRSHTDLKVGEYSGEMGVDKWTKERW 96
|
90 100 110
....*....|....*....|....*....|....*....
gi 2156030574 127 KNFV---DIIVATPGRLIDFVEQKEVWLDQIEFLVIDEA 162
Cdd:cd18034 97 KEELekyDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
238-345 |
5.48e-10 |
|
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: 57.22 E-value: 5.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 238 KYKLLEEILRDE----PIEKVMIFANRRDQVRKLYDHLK-----RDDYKVVML--SGEIAQDKRLKM--------LDQFK 298
Cdd:cd18802 8 KLQKLIEILREYfpktPDFRGIIFVERRATAVVLSRLLKehpstLAFIRCGFLigRGNSSQRKRSLMtqrkqketLDKFR 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2156030574 299 NGKHNIMIATDVAGRGIHVDGVSHVVNFTLPEQSDDYVHRIGRtGRA 345
Cdd:cd18802 88 DGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARA 133
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
14-275 |
7.18e-10 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 60.29 E-value: 7.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 14 LKQAIDALGFKEMTPIQQKVL-KFTLAGHDAIGRAQTGTGKTAAFLISVINDLLNNPiqgqryrgepRALILAPTRELAL 92
Cdd:COG1204 11 VIEFLKERGIEELYPPQAEALeAGLLEGKNLVVSAPTASGKTLIAELAILKALLNGG----------KALYIVPLRALAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 93 QIESDAKDLtkFTDLNV-VTLLGGvDFDKQKSQLNKNfvDIIVATPGRLIDFVEQKEVWLDQIEFLVIDEA------DR- 164
Cdd:COG1204 81 EKYREFKRD--FEELGIkVGVSTG-DYDSDDEWLGRY--DILVATPEKLDSLLRNGPSWLRDVDLVVVDEAhliddeSRg 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 165 -LLDMgfipAVKRIVRYSPRKeqrQTLMFSATFSydvlNLAQ--QWL-FEPVTVEIEPekktnadVEQRVYMVAK----- 235
Cdd:COG1204 156 pTLEV----LLARLRRLNPEA---QIVALSATIG----NAEEiaEWLdAELVKSDWRP-------VPLNEGVLYDgvlrf 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2156030574 236 TDKY--------KLLEEILRDEpiEKVMIFANRRDQV----RKLYDHLKRDD 275
Cdd:COG1204 218 DDGSrrskdptlALALDLLEEG--GQVLVFVSSRRDAeslaKKLADELKRRL 267
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
303-352 |
7.15e-09 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 51.94 E-value: 7.15e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2156030574 303 NIMIATDVAGRGIHVDGVSHVVNFTLPEQSDDYVHRIGRTGRAGTRGVSI 352
Cdd:cd18785 24 EILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEV 73
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
28-196 |
8.68e-09 |
|
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: 53.85 E-value: 8.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 28 PIQQKVLKFTLAgHDAIGRAQ----TGTGKTA-AFLISvindllnnpiqgqRYRGEPRALILAPTRELALQIesdAKDLT 102
Cdd:cd17926 3 PYQEEALEAWLA-HKNNRRGIlvlpTGSGKTLtALALI-------------AYLKELRTLIVVPTDALLDQW---KERFE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 103 KFTDLNVVTLLGGVDFDKQKSQlnknfvDIIVATPGRLIDFVEQKEVWLDQIEFLVIDEADRlldmgfIPAV--KRIVRY 180
Cdd:cd17926 66 DFLGDSSIGLIGGGKKKDFDDA------NVVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHH------LPAKtfSEILKE 133
|
170
....*....|....*.
gi 2156030574 181 SPRKEQrqtLMFSATF 196
Cdd:cd17926 134 LNAKYR---LGLTATP 146
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
229-354 |
1.05e-08 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350181 [Multi-domain] Cd Length: 134 Bit Score: 53.37 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 229 RVYMVAKTD-KYKLLEEILRDEPIEKVMIFANRRDQVRKLYDHLKRD-----DYKVVMLSGEiaqdkRLKMLDQFKNGKH 302
Cdd:cd18794 7 SVRPKDKKDeKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKgisaaAYHAGLEPSD-----RRDVQRKWLRDKI 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2156030574 303 NIMIATDVAGRGIHVDGVSHVVNFTLPEQSDDYVHRIGRTGRAGTRGVSISF 354
Cdd:cd18794 82 QVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILF 133
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
9-162 |
1.33e-08 |
|
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: 56.77 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 9 NLHPQLKQAIDALGFKEMTPIQQKVLKFTLAGHDAIGRAQTGTGKTAAFLISVINDLLNNPiqgqryrgEPRALILAPTR 88
Cdd:COG1205 40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDP--------GATALYLYPTK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 89 elALqiesdAKD-LTKFTDLNVVTLLG---GVdFD-----KQKSQLNKNfVDIIVATPgrliDFV-----EQKEVW---L 151
Cdd:COG1205 112 --AL-----ARDqLRRLRELAEALGLGvrvAT-YDgdtppEERRWIREH-PDIVLTNP----DMLhygllPHHTRWarfF 178
|
170
....*....|.
gi 2156030574 152 DQIEFLVIDEA 162
Cdd:COG1205 179 RNLRYVVIDEA 189
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
8-196 |
6.77e-08 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 51.52 E-value: 6.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 8 LNLHPQLKQAIDALgfKEMTPIQQKVLKFTLAghdaigraqTGTGKT--AAFLIsvinDLLNnpiqgqRYRGEPRALILA 85
Cdd:pfam04851 2 LELRPYQIEAIENL--LESIKNGQKRGLIVMA---------TGSGKTltAAKLI----ARLF------KKGPIKKVLFLV 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 86 PTRELALQIESDAKDLTKFTDlNVVTLLGGvdfDKQKSQLNKNfvDIIVATPGRL--IDFVEQKEVWLDQIEFLVIDEAD 163
Cdd:pfam04851 61 PRKDLLEQALEEFKKFLPNYV-EIGEIISG---DKKDESVDDN--KIVVTTIQSLykALELASLELLPDFFDVIIIDEAH 134
|
170 180 190
....*....|....*....|....*....|...
gi 2156030574 164 RLLDmgfiPAVKRIVRYSPRKEQrqtLMFSATF 196
Cdd:pfam04851 135 RSGA----SSYRNILEYFKPAFL---LGLTATP 160
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
24-308 |
1.31e-07 |
|
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: 53.55 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 24 KEMTPIQQKVLKFTLAGHDAIGR-----AQTGTGKT-AAFLISvindlLNNPIQGQRYRgepraLILA-PTRELALQIES 96
Cdd:COG1203 126 TPINPLQNEALELALEAAEEEPGlfiltAPTGGGKTeAALLFA-----LRLAAKHGGRR-----IIYAlPFTSIINQTYD 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 97 DAKDLTKF--------TDLNVVTLLGGVDFDKQKSQLNKNFVD--IIVATPGRLIDFVEQK----EVWLDQIE--FLVID 160
Cdd:COG1203 196 RLRDLFGEdvllhhslADLDLLEEEEEYESEARWLKLLKELWDapVVVTTIDQLFESLFSNrkgqERRLHNLAnsVIILD 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 161 EADrLLDMGFIPAVKRIVRYSprKEQRQTLMF-SATF-SYDVLNLAQQWLFEPvTVEIEPEKKTNADVEQRV-YMVAKTD 237
Cdd:COG1203 276 EVQ-AYPPYMLALLLRLLEWL--KNLGGSVILmTATLpPLLREELLEAYELIP-DEPEELPEYFRAFVRKRVeLKEGPLS 351
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2156030574 238 KYKLLEEILRD-EPIEKVMIFANRRDQVRKLYDHLK--RDDYKVVMLSGEIAQDKRLKMLDQ----FKNGKHNIMIAT 308
Cdd:COG1203 352 DEELAELILEAlHKGKSVLVIVNTVKDAQELYEALKekLPDEEVYLLHSRFCPADRSEIEKEikerLERGKPCILVST 429
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
238-344 |
4.59e-07 |
|
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: 48.89 E-value: 4.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 238 KYKLLEEILRD-------EPIEKVMIFANRRDQVRKLYDHLKR--DDYKVVMLSGE--------IAQDKRLKMLDQFKNG 300
Cdd:cd18801 10 KLEKLEEIVKEhfkkkqeGSDTRVIIFSEFRDSAEEIVNFLSKirPGIRATRFIGQasgksskgMSQKEQKEVIEQFRKG 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2156030574 301 KHNIMIATDVAGRGIHVDGVSHVVNFTLPEQSDDYVHRIGRTGR 344
Cdd:cd18801 90 GYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
39-162 |
6.70e-07 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 49.12 E-value: 6.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 39 AGHDAIGRAQTGTGKTAAFLISVINDLLNNPiqgqryrgEPRALILAPTRELAL-QIESdakdLTKFTDlnvvTLLGGVD 117
Cdd:cd17923 14 AGRSVVVTTGTASGKSLCYQLPILEALLRDP--------GSRALYLYPTKALAQdQLRS----LRELLE----QLGLGIR 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2156030574 118 FD--------KQKSQLNKNFVDIIVATPGRL----IDFVEQKEVWLDQIEFLVIDEA 162
Cdd:cd17923 78 VAtydgdtprEERRAIIRNPPRILLTNPDMLhyalLPHHDRWARFLRNLRYVVLDEA 134
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
237-383 |
3.13e-06 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 48.98 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 237 DKYKLLEEILRDEPIEKVMIFANRRDQVRKLYDHLKRDDYKVVMLSGEIAQDKRLKMLDQFKNGKHNIMIATdVA-GRGI 315
Cdd:COG0514 216 DKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGI 294
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2156030574 316 HVDGVSHVVNFTLPEQSDDYVHRIGRTGRAGTRGVSISFLSEDDAF---------YLPEIEKAIGQKLpLTRLDGYC 383
Cdd:COG0514 295 DKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAiqrffieqsPPDEERKRVERAK-LDAMLAYA 370
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
6-161 |
1.37e-05 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 47.12 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 6 ETLNLHPQLKQAIDALGFKEMTPIQQKVLKF-TLAGHDAIGRAQTGTGKTAAFLISVINDLLnnpiqgqryRGEPRALIL 84
Cdd:PRK00254 4 DELRVDERIKRVLKERGIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIVMVNKLL---------REGGKAVYL 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2156030574 85 APTRELALQIESDAKDLTKFtDLNVVTLLGgvDFDKQKSQLNKnfVDIIVATPGRLIDFVEQKEVWLDQIEFLVIDE 161
Cdd:PRK00254 75 VPLKALAEEKYREFKDWEKL-GLRVAMTTG--DYDSTDEWLGK--YDIIIATAEKFDSLLRHGSSWIKDVKLVVADE 146
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
47-164 |
5.23e-05 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 43.66 E-value: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 47 AQTGTGKTAAFLIsVINDLLnnpiqgQRYRGepRALILAPTRELALQIESDAKDLTKFTDLnVVTLLGGVDFDKQKSQLN 126
Cdd:cd18035 23 LPTGLGKTIIAIL-VAADRL------TKKGG--KVLILAPSRPLVEQHAENLKRVLNIPDK-ITSLTGEVKPEERAERWD 92
|
90 100 110
....*....|....*....|....*....|....*...
gi 2156030574 127 KNfvDIIVATPGRLIDFVEQKEVWLDQIEFLVIDEADR 164
Cdd:cd18035 93 AS--KIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
49-197 |
2.23e-04 |
|
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: 41.55 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 49 TGTGKTAAFLISVINDLLNNPiqgqryrgepRALILAPTRELALQiesdakDLTKFTDLNVVTLLGGV---DFDKQKSQL 125
Cdd:cd18028 26 TASGKTLIAEMAMVNTLLEGG----------KALYLVPLRALASE------KYEEFKKLEEIGLKVGIstgDYDEDDEWL 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2156030574 126 NKNfvDIIVATPGRLIDFVEQKEVWLDQIEFLVIDEADRLLDMGFIP----AVKRIVRYSPRkeqRQTLMFSATFS 197
Cdd:cd18028 90 GDY--DIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPtlesIVARLRRLNPN---TQIIGLSATIG 160
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
46-348 |
1.09e-03 |
|
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: 40.88 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 46 RAQTGTGKTAAFLIsvindLLNNPIQGQRyrgEPRALILAPTRELALQIESDAKDLtkFTDLNVVTLLGGV--------- 116
Cdd:cd09639 5 EAPTGYGKTEAALL-----WALHSLKSQK---ADRVIIALPTRATINAMYRRAKEA--FGETGLYHSSILSsrikemgds 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 117 -DFDK-----QKSQLNKNFVDIIVATPGRLIDF----VEQKEVWLDQI--EFLVIDEADRLLD--MGFIPAVKRIVRYsp 182
Cdd:cd09639 75 eEFEHlfplyIHSNDTLFLDPITVCTIDQVLKSvfgeFGHYEFTLASIanSLLIFDEVHFYDEytLALILAVLEVLKD-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 183 rKEQRQTLMfSATFSYDVLNLAQQwlFEPVTVEIEPEKKTNadveqRVYMVAKTDKYKLLEEILRDEPIE------KVMI 256
Cdd:cd09639 153 -NDVPILLM-SATLPKFLKEYAEK--IGYVEENEPLDLKPN-----ERAPFIKIESDKVGEISSLERLLEfikkggSVAI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 257 FANRRDQVRKLYDHLKRD--DYKVVMLSGEIAQDKRLK----MLDQFKNGKHNIMIATDVAGRGIHVDgvshvVNFTLPE 330
Cdd:cd09639 224 IVNTVDRAQEFYQQLKEKgpEEEIMLIHSRFTEKDRAKkeaeLLLEFKKSEKFVIVATQVIEASLDIS-----VDVMITE 298
|
330 340
....*....|....*....|
gi 2156030574 331 QS--DDYVHRIGRTGRAGTR 348
Cdd:cd09639 299 LApiDSLIQRLGRLHRYGEK 318
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
237-378 |
1.25e-03 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 40.85 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 237 DKYKLLEEILR---DEPIEKVMIFANRRDQVRKLYDHLKRDDYKVVMLSGEIAQDKRLKMLDQFKNGKHNIMIATDVAGR 313
Cdd:PRK11057 219 EKFKPLDQLMRyvqEQRGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGM 298
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2156030574 314 GIHVDGVSHVVNFTLPEQSDDYVHRIGRTGRAGTRGVSISFLSEDDAFYLPEI--EKAIGQKLPLTR 378
Cdd:PRK11057 299 GINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPADMAWLRRCleEKPAGQQQDIER 365
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
241-357 |
1.42e-03 |
|
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: 38.78 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 241 LLEEILRDEpieKVMIFANRRDQVRKLYDHLKRDDYKVVMLS------GEIAQDKRLKMLDQFKNGKHNIMIATDVAGRG 314
Cdd:cd18796 31 VIFLLERHK---STLVFTNTRSQAERLAQRLRELCPDRVPPDfialhhGSLSRELREEVEAALKRGDLKVVVATSSLELG 107
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2156030574 315 IHVDGVSHVVNFTLPEQSDDYVHRIGRTGRAGTRGVSISFLSE 357
Cdd:cd18796 108 IDIGDVDLVIQIGSPKSVARLLQRLGRSGHRPGAASKGRLVPT 150
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
40-208 |
3.75e-03 |
|
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: 37.95 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 40 GHDAIGRAQTGTGKTAAFLISVINDLLNNPIQGQryrgepRALILAPTRELALQIESDAKDLTKFTDLNV-VTLLGGVDF 118
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGV------QVLYISPLKALINDQERRLEEPLDEIDLEIpVAVRHGDTS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 119 DKQKSQLNKNFVDIIVATPGRLIDFVEQKEVW--LDQIEFLVIDEADRLLD----MGFIPAVKRIVRYSPRKEQRQTLmf 192
Cdd:cd17922 75 QSEKAKQLKNPPGILITTPESLELLLVNKKLRelFAGLRYVVVDEIHALLGskrgVQLELLLERLRKLTGRPLRRIGL-- 152
|
170
....*....|....*.
gi 2156030574 193 SATFSYdvLNLAQQWL 208
Cdd:cd17922 153 SATLGN--LEEAAAFL 166
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
30-164 |
4.05e-03 |
|
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: 38.18 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 30 QQKVLKFTLAGHDAIGRAQTGTGKT-AAFLISviNDLLNNPIQGQRyrgePRALILAPTRELALQIESDAKDLTKFTDLN 108
Cdd:cd17927 7 QLELAQPALKGKNTIICLPTGSGKTfVAVLIC--EHHLKKFPAGRK----GKVVFLANKVPLVEQQKEVFRKHFERPGYK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2156030574 109 VVTLLGGVDFDKQKSQLNKNFvDIIVATPGRLI-DFVEQKEVWLDQIEFLVIDEADR 164
Cdd:cd17927 81 VTGLSGDTSENVSVEQIVESS-DVIIVTPQILVnDLKSGTIVSLSDFSLLVFDECHN 136
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
232-359 |
4.24e-03 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 39.49 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 232 MVAKTDKykLLEEIlrDEPI------EKVMIFANRRDQVRKLYDHLKRDDYKVVMLSGEIAQDKRLKMLDQFKNGKHNIM 305
Cdd:PLN03137 659 VVPKTKK--CLEDI--DKFIkenhfdECGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINII 734
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2156030574 306 IATDVAGRGIHVDGVSHVVNFTLPEQSDDYVHRIGRTGRAGTRGVSISFLSEDD 359
Cdd:PLN03137 735 CATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGRAGRDGQRSSCVLYYSYSD 788
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
49-164 |
5.06e-03 |
|
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: 37.54 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156030574 49 TGTGKT--AAFLISVIndllnnpiqgQRYRGEPRALILAPTRELALQIESDAKDLTKFTDLNVVTLLGGVDFDKqksqln 126
Cdd:cd18032 29 TGTGKTytAAFLIKRL----------LEANRKKRILFLAHREELLEQAERSFKEVLPDGSFGNLKGGKKKPDDA------ 92
|
90 100 110
....*....|....*....|....*....|....*...
gi 2156030574 127 knfvDIIVATPGRLIDFVEQKEVWLDQIEFLVIDEADR 164
Cdd:cd18032 93 ----RVVFATVQTLNKRKRLEKFPPDYFDLIIIDEAHH 126
|
|
| |
