|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
2-420 |
0e+00 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 977.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 2 SKTHLTEQKFSDFALHPKVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLLSHPAIADRK 81
Cdd:PRK04837 1 SKTHLTEQKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 82 VNQPRALIMAPTRELAVQIHADAEPLAEATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQV 161
Cdd:PRK04837 81 VNQPRALIMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 162 VVLDEADRMYDLGFIKDIRWLFRRMPPANQRLNMLFSATLSYRVRELAFEQMNNAEYIEVEPEQKTGHRIKEELFYPSNE 241
Cdd:PRK04837 161 VVLDEADRMFDLGFIKDIRWLFRRMPPANQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYPSNE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 242 EKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILDEFTRGDLDILVATDVAARGLH 321
Cdd:PRK04837 241 EKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 322 IPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIGHSIPVSKYNPDALMTDLPKPLRLTR 401
Cdd:PRK04837 321 IPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIGHSIPVSKYDSDALLTDLPKPLRLTR 400
|
410
....*....|....*....
gi 445969644 402 PRTGNGPRRTGAPRNRRRS 420
Cdd:PRK04837 401 PRTGNGPRRSGAPRNRRRR 419
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
10-419 |
0e+00 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 523.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 10 KFSDFALHPKVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLLSHPAiadrkvNQPRALI 89
Cdd:COG0513 3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP------RAPQALI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 90 MAPTRELAVQIHADAEPLAEATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADR 169
Cdd:COG0513 77 LAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 170 MYDLGFIKDIRWLFRRMPPanQRLNMLFSATLSYRVRELAFEQMNNAEYIEVEPEQKTGHRIKEELFYPSNEEKMRLLQT 249
Cdd:COG0513 157 MLDMGFIEDIERILKLLPK--ERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 250 LIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILDEFTRGDLDILVATDVAARGLHIPAVTHVF 329
Cdd:COG0513 235 LLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 330 NYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIGHSIPVSKynPDALMTDLPKPLRLTRPRTGNGPR 409
Cdd:COG0513 315 NYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEE--LPGFEPVEEKRLERLKPKIKEKLK 392
|
410
....*....|
gi 445969644 410 RTGAPRNRRR 419
Cdd:COG0513 393 GKKAGRGGRP 402
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
1-405 |
3.14e-169 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 486.38 E-value: 3.14e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 1 MSKTHLTEQKFSDFALHPKVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLLSHPAIADR 80
Cdd:PRK04537 1 MSDKPLTDLTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALADR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 81 KVNQPRALIMAPTRELAVQIHADAEPLAEATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHI-NLGAI 159
Cdd:PRK04537 81 KPEDPRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVvSLHAC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 160 QVVVLDEADRMYDLGFIKDIRWLFRRMPPANQRLNMLFSATLSYRVRELAFEQMNNAEYIEVEPEQKTGHRIKEELFYPS 239
Cdd:PRK04537 161 EICVLDEADRMFDLGFIKDIRFLLRRMPERGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 240 NEEKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILDEFTRGDLDILVATDVAARG 319
Cdd:PRK04537 241 DEEKQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 320 LHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIGHSIPVSKYNPDaLMTDLPKPLRL 399
Cdd:PRK04537 321 LHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKIPVEPVTAE-LLTPLPRPPRV 399
|
....*.
gi 445969644 400 TRPRTG 405
Cdd:PRK04537 400 PVEGEE 405
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
10-395 |
7.43e-133 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 390.43 E-value: 7.43e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 10 KFSDFALHPKVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLLSHPAIADRKVNQPRALI 89
Cdd:PRK01297 88 RFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKERYMGEPRALI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 90 MAPTRELAVQIHADAEPLAEATGLKLGLAYGGDGYDKQLKVLESG-VDILIGTTGRLIDYAKQNHINLGAIQVVVLDEAD 168
Cdd:PRK01297 168 IAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEAD 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 169 RMYDLGFIKDIRWLFRRMPPANQRLNMLFSATLSYRVRELAFEQMNNAEYIEVEPEQKTGHRIKEELFYPSNEEKMRLLQ 248
Cdd:PRK01297 248 RMLDMGFIPQVRQIIRQTPRKEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDKYKLLY 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 249 TLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILDEFTRGDLDILVATDVAARGLHIPAVTHV 328
Cdd:PRK01297 328 NLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHV 407
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445969644 329 FNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIGHSIPvSKYNPDALMTDLPK 395
Cdd:PRK01297 408 INFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKIS-CEMPPAELLKPVPR 473
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
11-376 |
1.90e-110 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 331.52 E-value: 1.90e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 11 FSDFALHPKVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLLSHPAiadRKVNQPRALIM 90
Cdd:PRK11192 3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPR---RKSGPPRILIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 91 APTRELAVQIHADAEPLAEATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRM 170
Cdd:PRK11192 80 TPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 171 YDLGFIKDI-------RWlfrrmppanQRLNMLFSATLSYR-VRELAFEQMNNAEYIEVEPEQKtgHRIKEELFY---PS 239
Cdd:PRK11192 160 LDMGFAQDIetiaaetRW---------RKQTLLFSATLEGDaVQDFAERLLNDPVEVEAEPSRR--ERKKIHQWYyraDD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 240 NEEKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILDEFTRGDLDILVATDVAARG 319
Cdd:PRK11192 229 LEHKTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARG 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 445969644 320 LHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIG 376
Cdd:PRK11192 309 IDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIE 365
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
11-394 |
1.46e-94 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 291.70 E-value: 1.46e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 11 FSDFALHPKVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAF-LTstfhyLLSHpaiADRKVNQPRALI 89
Cdd:PRK11776 6 FSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFgLG-----LLQK---LDVKRFRVQALV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 90 MAPTRELAVQIHADAEPLAEAT-GLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEAD 168
Cdd:PRK11776 78 LCPTRELADQVAKEIRRLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEAD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 169 RMYDLGFIKDIRWLFRRMPPanQRLNMLFSATLSYRVRELAFEQMNNAEYIEVEpEQKTGHRIkEELFYP-SNEEKMRLL 247
Cdd:PRK11776 158 RMLDMGFQDAIDAIIRQAPA--RRQTLLFSATYPEGIAAISQRFQRDPVEVKVE-STHDLPAI-EQRFYEvSPDERLPAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 248 QTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILDEFTRGDLDILVATDVAARGLHIPAVTH 327
Cdd:PRK11776 234 QRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEA 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445969644 328 VFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIGHSIPVSKYNPDALMTDLP 394
Cdd:PRK11776 314 VINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPSLSPLSGVP 380
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
11-421 |
1.68e-92 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 286.32 E-value: 1.68e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 11 FSDFALHPKVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLLSHPAIAdrKVNQP-RALI 89
Cdd:PRK10590 3 FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHA--KGRRPvRALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 90 MAPTRELAVQIHADAEPLAEATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADR 169
Cdd:PRK10590 81 LTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 170 MYDLGFIKDIRWLFRRMPPanQRLNMLFSATLSYRVRELAFEQMNNAEYIEVEPEQKTGHRIKEELFYPSNEEKMRLLQT 249
Cdd:PRK10590 161 MLDMGFIHDIRRVLAKLPA--KRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 250 LIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILDEFTRGDLDILVATDVAARGLHIPAVTHVF 329
Cdd:PRK10590 239 MIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 330 NYDLPDDCEDYVHRIGRTGRAGASGHSISLAC-EEYALnLPAIETYIGHSIP---VSKYNPDALMTDLP----KPLRLTR 401
Cdd:PRK10590 319 NYELPNVPEDYVHRIGRTGRAAATGEALSLVCvDEHKL-LRDIEKLLKKEIPriaIPGYEPDPSIKAEPiqngRQQRGGG 397
|
410 420
....*....|....*....|
gi 445969644 402 PRTGNGPRRTGAPRNRRRSG 421
Cdd:PRK10590 398 GRGQGGGRGQQQGQPRRGEG 417
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
20-220 |
5.12e-87 |
|
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: 262.76 E-value: 5.12e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 20 VVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLLSHPAiadRKVNQPRALIMAPTRELAVQ 99
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPK---KKGRGPQALVLAPTRELAMQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 100 IHADAEPLAEATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMYDLGFIKDI 179
Cdd:cd00268 78 IAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 445969644 180 RWLFRRMPPANQRlnMLFSATLSYRVRELAFEQMNNAEYIE 220
Cdd:cd00268 158 EKILSALPKDRQT--LLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
11-358 |
1.39e-79 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 255.47 E-value: 1.39e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 11 FSDFalhpkVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLLSHPAIadRKVNQPRALIM 90
Cdd:PTZ00110 137 FPDY-----ILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLL--RYGDGPIVLVL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 91 APTRELAVQIHADAEPLAEATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRM 170
Cdd:PTZ00110 210 APTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRM 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 171 YDLGFIKDIRWLFRRMPPANQRLnmLFSATLSYRVRELAfEQMNNAEYIEVEP---EQKTGHRIKEELFYPSNEEK---- 243
Cdd:PTZ00110 290 LDMGFEPQIRKIVSQIRPDRQTL--MWSATWPKEVQSLA-RDLCKEEPVHVNVgslDLTACHNIKQEVFVVEEHEKrgkl 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 244 MRLLQTLIEEEwpDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILDEFTRGDLDILVATDVAARGLHIP 323
Cdd:PTZ00110 367 KMLLQRIMRDG--DKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVK 444
|
330 340 350
....*....|....*....|....*....|....*
gi 445969644 324 AVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSIS 358
Cdd:PTZ00110 445 DVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYT 479
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
7-357 |
5.90e-76 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 248.22 E-value: 5.90e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 7 TEQKFSDFALHPKVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLlshpaiaDRKVNQPR 86
Cdd:PRK11634 4 FETTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNL-------DPELKAPQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 87 ALIMAPTRELAVQIhadAEPLAEAT----GLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVV 162
Cdd:PRK11634 77 ILVLAPTRELAVQV---AEAMTDFSkhmrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 163 VLDEADRMYDLGFIKDIRWLFRRMPPANQrlNMLFSATLSYRVRELAFEQMNNAEYIEVEPEQKTGHRIKEELFYPSNEE 242
Cdd:PRK11634 154 VLDEADEMLRMGFIEDVETIMAQIPEGHQ--TALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 243 KMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILDEFTRGDLDILVATDVAARGLHI 322
Cdd:PRK11634 232 KNEALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDV 311
|
330 340 350
....*....|....*....|....*....|....*
gi 445969644 323 PAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSI 357
Cdd:PRK11634 312 ERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRAL 346
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
11-219 |
8.61e-65 |
|
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: 206.95 E-value: 8.61e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 11 FSDFALHPKVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLLSHPAIA---DRKVNQPRA 87
Cdd:cd17967 2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSvgrGRRKAYPSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 88 LIMAPTRELAVQIHADAEPLAEATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEA 167
Cdd:cd17967 82 LILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDEA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 445969644 168 DRMYDLGFIKDIRWLFRR--MPPANQRLNMLFSATLSYRVRELAFEQMNNaeYI 219
Cdd:cd17967 162 DRMLDMGFEPQIRKIVEHpdMPPKGERQTLMFSATFPREIQRLAADFLKN--YI 213
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
11-374 |
9.36e-61 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 202.36 E-value: 9.36e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 11 FSDFALHPKVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFhyllshpAIADRKVNQPRALIM 90
Cdd:PTZ00424 30 FDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAAL-------QLIDYDLNACQALIL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 91 APTRELAVQIHADAEPLAEATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRM 170
Cdd:PTZ00424 103 APTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEM 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 171 YDLGFIKDIRWLFRRMPPANQRlnMLFSATLSYRVRELAFEQMNNAEYIEVEPEQKTGHRIKEelFY---PSNEEKMRLL 247
Cdd:PTZ00424 183 LSRGFKGQIYDVFKKLPPDVQV--ALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQ--FYvavEKEEWKFDTL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 248 QTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILDEFTRGDLDILVATDVAARGLHIPAVTH 327
Cdd:PTZ00424 259 CDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSL 338
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 445969644 328 VFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETY 374
Cdd:PTZ00424 339 VINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERH 385
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
238-359 |
7.11e-56 |
|
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: 180.78 E-value: 7.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 238 PSNEEKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILDEFTRGDLDILVATDVAA 317
Cdd:cd18787 9 EEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVATDVAA 88
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 445969644 318 RGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 359
Cdd:cd18787 89 RGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITF 130
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
11-219 |
3.58e-54 |
|
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: 180.93 E-value: 3.58e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 11 FSDFALHPKVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLLSH--PAIADRKVNQPRAL 88
Cdd:cd18052 45 FEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEglTASSFSEVQEPQAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 89 IMAPTRELAVQIHADAEPLAEATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEAD 168
Cdd:cd18052 125 IVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEAD 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 445969644 169 RMYDLGFIKDIRWL--FRRMPPANQRLNMLFSATLSYRVRELAFEQMnNAEYI 219
Cdd:cd18052 205 RMLDMGFGPEIRKLvsEPGMPSKEDRQTLMFSATFPEEIQRLAAEFL-KEDYL 256
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
20-215 |
2.04e-53 |
|
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: 176.68 E-value: 2.04e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 20 VVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLLSHPaiadRKVNQPRALIMAPTRELAVQ 99
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRP----KKKAATRVLVLVPTRELAMQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 100 IHADAEPLAEATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNH-INLGAIQVVVLDEADRMYDLGFIKD 178
Cdd:cd17947 77 CFSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGFADE 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 445969644 179 IRWLFRRMPPANQrlNMLFSATLSYRVRELAFEQMNN 215
Cdd:cd17947 157 LKEILRLCPRTRQ--TMLFSATMTDEVKDLAKLSLNK 191
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
33-208 |
3.75e-53 |
|
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: 174.74 E-value: 3.75e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 33 TPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLlshpaiaDRKVNQPRALIMAPTRELAVQIHADAEPLAEATG 112
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAL-------DKLDNGPQALVLAPTRELAEQIYEELKKLGKGLG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 113 LKLGLAYGGDGYDKQLKVLEsGVDILIGTTGRLIDYAKQNHiNLGAIQVVVLDEADRMYDLGFIKDIRWLFRRMPPANQR 192
Cdd:pfam00270 74 LKVASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQI 151
|
170
....*....|....*.
gi 445969644 193 lnMLFSATLSYRVREL 208
Cdd:pfam00270 152 --LLLSATLPRNLEDL 165
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
9-209 |
7.02e-53 |
|
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: 176.03 E-value: 7.02e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 9 QKFSDFALHPKVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLLSHPAIADRKvnQPRAL 88
Cdd:cd17953 12 QKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVKPGE--GPIGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 89 IMAPTRELAVQIHADAEPLAEATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNH---INLGAIQVVVLD 165
Cdd:cd17953 90 IMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNgrvTNLRRVTYVVLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 445969644 166 EADRMYDLGFIKDIRWLFRRMPPANQRLnmLFSATLSYRVRELA 209
Cdd:cd17953 170 EADRMFDMGFEPQIMKIVNNIRPDRQTV--LFSATFPRKVEALA 211
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
11-363 |
1.20e-52 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 183.84 E-value: 1.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 11 FSDFALHPKVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLT------STFHyllSHPAIADRKvnq 84
Cdd:PLN00206 123 FSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVpiisrcCTIR---SGHPSEQRN--- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 85 PRALIMAPTRELAVQIHADAEPLAEATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVL 164
Cdd:PLN00206 197 PLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVL 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 165 DEADRMYDLGFIKDIRWLFRRMPpanQRLNMLFSATLSYRVRELAFEQMNNAEYIEVEPEQKTGHRIKE-ELFYPSNEEK 243
Cdd:PLN00206 277 DEVDCMLERGFRDQVMQIFQALS---QPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQlAIWVETKQKK 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 244 MRLLQTLI-EEEWPDRAIIFANTKhrceeiwghLAAD----------GHRVGLLTGDVAQKKRLRILDEFTRGDLDILVA 312
Cdd:PLN00206 354 QKLFDILKsKQHFKPPAVVFVSSR---------LGADllanaitvvtGLKALSIHGEKSMKERREVMKSFLVGEVPVIVA 424
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 445969644 313 TDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEE 363
Cdd:PLN00206 425 TGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEE 475
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
11-201 |
3.19e-52 |
|
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: 173.64 E-value: 3.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 11 FSDFALHPKVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLLSHPAIadrkvNQPRALIM 90
Cdd:cd17959 3 FQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPT-----VGARALIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 91 APTRELAVQIHADAEPLAEATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRM 170
Cdd:cd17959 78 SPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRL 157
|
170 180 190
....*....|....*....|....*....|.
gi 445969644 171 YDLGFIKDIRWLFRRMPPANQRLnmLFSATL 201
Cdd:cd17959 158 FEMGFAEQLHEILSRLPENRQTL--LFSATL 186
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
16-220 |
2.46e-50 |
|
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: 168.92 E-value: 2.46e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 16 LHPKVVEALEKKGFHNCTPIQALALPLTLA-GRDVAGQAQTGTGKTMAFLTSTFHYLLSHPaiADRKVNQPRALIMAPTR 94
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTK--PAGRRSGVSALIISPTR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 95 ELAVQIHADAEPLAE-ATGLKLGLAYGGDGYDKQLKVLES-GVDILIGTTGRLIDYAKQNH--INLGAIQVVVLDEADRM 170
Cdd:cd17964 79 ELALQIAAEAKKLLQgLRKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLENPGvaKAFTDLDYLVLDEADRL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 445969644 171 YDLGFIKDIRWLFRRMPPAN--QRLNMLFSATLSYRVRELAFEQMN-NAEYIE 220
Cdd:cd17964 159 LDMGFRPDLEQILRHLPEKNadPRQTLLFSATVPDEVQQIARLTLKkDYKFID 211
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
20-209 |
4.57e-49 |
|
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: 165.28 E-value: 4.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 20 VVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLLSHPAIadRKVNQPRALIMAPTRELAVQ 99
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQREL--EKGEGPIAVIVAPTRELAQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 100 IHADAEPLAEATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMYDLGFIKDI 179
Cdd:cd17952 79 IYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQV 158
|
170 180 190
....*....|....*....|....*....|
gi 445969644 180 RWLFRRMPPANQRLnmLFSATLSYRVRELA 209
Cdd:cd17952 159 RSIVGHVRPDRQTL--LFSATFKKKIEQLA 186
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
20-219 |
3.16e-48 |
|
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: 164.03 E-value: 3.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 20 VVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLLSHPAIADRKVNQ-PRALIMAPTRELAV 98
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDEETKDDgPYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 99 QIHADAEPLAEATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMYDLGFIKD 178
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 445969644 179 IRWLFRRMPPAN------------------QRLNMLFSATLSYRVRELAFEQMNNAEYI 219
Cdd:cd17945 161 VTKILDAMPVSNkkpdteeaeklaasgkhrYRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
20-221 |
3.67e-48 |
|
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: 162.92 E-value: 3.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 20 VVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLLSHPAIadRKVNQPRALIMAPTRELAVQ 99
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPL--ERGDGPIVLVLAPTRELAQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 100 IHADAEPLAEATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMYDLGFIKDI 179
Cdd:cd17966 79 IQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 445969644 180 RWLFRRMPPanQRLNMLFSATLSYRVRELAFEQMNnaEYIEV 221
Cdd:cd17966 159 RKIVDQIRP--DRQTLMWSATWPKEVRRLAEDFLK--DYIQV 196
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
20-209 |
1.08e-47 |
|
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: 161.97 E-value: 1.08e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 20 VVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLLShpAIADRKVNQPRALIMAPTRELAVQ 99
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLK--RKANLKKGQVGALIISPTRELATQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 100 IHADAEPLAEATGLKL--GLAYGGDGYDKQLKVL-ESGVDILIGTTGRLIDY--AKQNHINLGAIQVVVLDEADRMYDLG 174
Cdd:cd17960 79 IYEVLQSFLEHHLPKLkcQLLIGGTNVEEDVKKFkRNGPNILVGTPGRLEELlsRKADKVKVKSLEVLVLDEADRLLDLG 158
|
170 180 190
....*....|....*....|....*....|....*
gi 445969644 175 FIKDIRWLFRRMPpaNQRLNMLFSATLSYRVRELA 209
Cdd:cd17960 159 FEADLNRILSKLP--KQRRTGLFSATQTDAVEELI 191
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
24-234 |
1.23e-46 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 159.19 E-value: 1.23e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 24 LEKKGFHNCTPIQALALPLTLAG-RDVAGQAQTGTGKTMAFLTSTFHYLLSHPAiadrkvnqPRALIMAPTRELAVQIHA 102
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKG--------GRVLVLVPTRELAEQWAE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 103 DAEPLAEATGLKLGLAYGGDGYDKQLKVLESGV-DILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMYDLGFIKDIRW 181
Cdd:smart00487 73 ELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 445969644 182 LFRRMPPANQRLnmLFSATLSYRVRELAFEQMNNaeYIEVEPEQKTGHRIKEE 234
Cdd:smart00487 153 LLKLLPKNVQLL--LLSATPPEEIENLLELFLND--PVFIDVGFTPLEPIEQF 201
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
11-208 |
8.74e-46 |
|
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can shuttle between the nucleus and the cytoplasm, and has an RNA-independent ATPase activity. DX47 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350712 [Multi-domain] Cd Length: 203 Bit Score: 157.09 E-value: 8.74e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 11 FSDFALHPKVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLLSHPaiadrkvnQP-RALI 89
Cdd:cd17954 2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENP--------QRfFALV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 90 MAPTRELAVQIHADAEPLAEATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQ-NHINLGAIQVVVLDEAD 168
Cdd:cd17954 74 LAPTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENtKGFSLKSLKFLVMDEAD 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 445969644 169 RMYDLGFIKDIRWLFRRMPpaNQRLNMLFSATLSYRVREL 208
Cdd:cd17954 154 RLLNMDFEPEIDKILKVIP--RERTTYLFSATMTTKVAKL 191
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
24-215 |
5.65e-45 |
|
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: 154.67 E-value: 5.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 24 LEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLLSHpaiadRKVNQPRALIMAPTRELAVQIHAD 103
Cdd:cd17957 5 LEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKP-----RKKKGLRALILAPTRELASQIYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 104 AEPLAEATGLKLGLAYGGDGyDKQLKVLESG--VDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMYDLGFIKDIRW 181
Cdd:cd17957 80 LLKLSKGTGLRIVLLSKSLE-AKAKDGPKSItkYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDE 158
|
170 180 190
....*....|....*....|....*....|....
gi 445969644 182 LFRRMPPANQRLnMLFSATLSYRVRELAFEQMNN 215
Cdd:cd17957 159 ILAACTNPNLQR-SLFSATIPSEVEELARSVMKD 191
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
20-216 |
4.35e-44 |
|
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: 152.23 E-value: 4.35e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 20 VVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLLSHPAIADRKvNQPRALIMAPTRELAVQ 99
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPREQR-NGPGVLVLTPTRELALQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 100 IHADAEPLAEaTGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMYDLGFIKDI 179
Cdd:cd17958 80 IEAECSKYSY-KGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQI 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 445969644 180 RWLFRRMPPanQRLNMLFSATLSYRVRELAFEQMNNA 216
Cdd:cd17958 159 RKILLDIRP--DRQTIMTSATWPDGVRRLAQSYLKDP 193
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
10-219 |
6.39e-42 |
|
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD box, X isoform, or DDX14) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. This protein has multiple conserved domains and is thought to play roles in both the nucleus and cytoplasm. Nuclear roles include transcriptional regulation, mRNP assembly, pre-mRNA splicing, and mRNA export. In the cytoplasm, this protein is thought to be involved in translation, cellular signaling, and viral replication. Misregulation of this gene has been implicated in tumorigenesis. Diseases associated with DDX3 include mental retardation, X-linked 102 and agenesis of the corpus callosum, with facial anomalies and robin sequence. DDX3 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350809 [Multi-domain] Cd Length: 249 Bit Score: 148.26 E-value: 6.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 10 KFSDFALHPKVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFL----TSTFH-----YLLSHPAIADR 80
Cdd:cd18051 22 TFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLlpilSQIYEqgpgeSLPSESGYYGR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 81 KVNQPRALIMAPTRELAVQIHADAEPLAEATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQ 160
Cdd:cd18051 102 RKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYCK 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445969644 161 VVVLDEADRMYDLGFIKDIRWLFRR--MPPANQRLNMLFSATLSYRVRELAFEQMNNaeYI 219
Cdd:cd18051 182 YLVLDEADRMLDMGFEPQIRRIVEQdtMPPTGERQTLMFSATFPKEIQMLARDFLDN--YI 240
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
20-202 |
1.53e-40 |
|
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: 144.30 E-value: 1.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 20 VVEALEKKGFHNCTPIQALALPLTLA-GRDVAGQAQTGTGKTMAFLTSTFHYLLSH--PAIADRKVNQPRALIMAPTREL 96
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLLSQksSNGVGGKQKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 97 AVQI--HADAepLAEATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNH---INLGAIQVVVLDEADRMY 171
Cdd:cd17946 81 AVQVkdHLKA--IAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNehlANLKSLRFLVLDEADRML 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 445969644 172 DLGFIKDIRWLFRRMP-----PANQRLNMLFSATLS 202
Cdd:cd17946 159 EKGHFAELEKILELLNkdragKKRKRQTFVFSATLT 194
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
20-220 |
2.38e-40 |
|
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, Component Of Gems 3, Gemin-3, and SMN-Interacting Protein) interacts directly with SMN (survival of motor neurons), the spinal muscular atrophy gene product, and may play a catalytic role in the function of the SMN complex on ribonucleoproteins. Diseases associated with DDX20 include spinal muscular atrophy and muscular atrophy. DDX20 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350701 [Multi-domain] Cd Length: 192 Bit Score: 142.40 E-value: 2.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 20 VVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLlshpaiaDRKVNQPRALIMAPTRELAVQ 99
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESL-------DLERRHPQVLILAPTREIAVQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 100 IHADAEPLAEA-TGLKLGLAYGGDGYDKQLKVLeSGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMYDLGFIKD 178
Cdd:cd17943 74 IHDVFKKIGKKlEGLKCEVFIGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 445969644 179 IRWLFRRMPpaNQRLNMLFSATLSYRVRELAFEQMNNAEYIE 220
Cdd:cd17943 153 VNWIFSSLP--KNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
10-221 |
1.32e-39 |
|
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: 141.69 E-value: 1.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 10 KFSDFALHPKVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLLSHPAIadRKVNQPRALI 89
Cdd:cd18049 25 NFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFL--ERGDGPICLV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 90 MAPTRELAVQIHADAEPLAEATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADR 169
Cdd:cd18049 103 LAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADR 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 445969644 170 MYDLGFIKDIRWLFRRMPPANQRLnmLFSATLSYRVRELAFEQMNnaEYIEV 221
Cdd:cd18049 183 MLDMGFEPQIRKIVDQIRPDRQTL--MWSATWPKEVRQLAEDFLK--DYIHI 230
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
23-222 |
3.25e-39 |
|
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: 139.35 E-value: 3.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 23 ALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLLSHPAIADRKVNqprALIMAPTRELAVQIHA 102
Cdd:cd17941 4 GLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTPEDGLG---ALIISPTRELAMQIFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 103 DAEPLAEATGLKLGLAYGGDGYDKQLKVLeSGVDILIGTTGRLIDYAKQN-HINLGAIQVVVLDEADRMYDLGFIKDIRW 181
Cdd:cd17941 81 VLRKVGKYHSFSAGLIIGGKDVKEEKERI-NRMNILVCTPGRLLQHMDETpGFDTSNLQMLVLDEADRILDMGFKETLDA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 445969644 182 LFRRMPPanQRLNMLFSATLSYRVRELAFEQMNNAEYIEVE 222
Cdd:cd17941 160 IVENLPK--SRQTLLFSATQTKSVKDLARLSLKNPEYISVH 198
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
11-220 |
1.28e-38 |
|
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350696 [Multi-domain] Cd Length: 204 Bit Score: 138.22 E-value: 1.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 11 FSDFALHPKVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFltstfhyllSHPAIadrkvNQPRALIM 90
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAF---------CLPVL-----QIVVALIL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 91 APTRELAVQIHADAEPLA---EATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEA 167
Cdd:cd17938 67 EPSRELAEQTYNCIENFKkylDNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 445969644 168 DRMYDLGFIKDIRWLFRRMP---PANQRLNM-LFSATL-SYRVRELAFEQMNNAEYIE 220
Cdd:cd17938 147 DRLLSQGNLETINRIYNRIPkitSDGKRLQViVCSATLhSFEVKKLADKIMHFPTWVD 204
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
20-209 |
1.57e-38 |
|
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: 140.15 E-value: 1.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 20 VVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLLSHPAIadRKVNQPRALIMAPTRELAVQ 99
Cdd:cd18050 73 VMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYL--ERGDGPICLVLAPTRELAQQ 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 100 IHADAEPLAEATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMYDLGFIKDI 179
Cdd:cd18050 151 VQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQI 230
|
170 180 190
....*....|....*....|....*....|
gi 445969644 180 RWLFRRMPPANQRLnmLFSATLSYRVRELA 209
Cdd:cd18050 231 RKIVDQIRPDRQTL--MWSATWPKEVRQLA 258
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
20-209 |
2.70e-38 |
|
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: 137.47 E-value: 2.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 20 VVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLL-SHPAIADRKVNQPRALIMAPTRELAV 98
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALeQEKKLPFIKGEGPYGLIVCPSRELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 99 QIHADAEPLAEA------TGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMYD 172
Cdd:cd17951 81 QTHEVIEYYCKAlqeggyPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 445969644 173 LGFIKDIRWLFRRMppANQRLNMLFSATLSYRVRELA 209
Cdd:cd17951 161 MGFEEDIRTIFSYF--KGQRQTLLFSATMPKKIQNFA 195
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
11-220 |
3.45e-38 |
|
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: 136.97 E-value: 3.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 11 FSDFALHPKVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLLSHP-AIAdrkvnqprALI 89
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPyGIF--------ALV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 90 MAPTRELAVQIHADAEPLAEATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQN---HINLGAIQVVVLDE 166
Cdd:cd17955 73 LTPTRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSddtTKVLSRVKFLVLDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 445969644 167 ADRMYDLGFIKDIRWLFRRMPPanQRLNMLFSATLSYRVRELAFEQMNNAEYIE 220
Cdd:cd17955 153 ADRLLTGSFEDDLATILSALPP--KRQTLLFSATLTDALKALKELFGNKPFFWE 204
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
20-219 |
5.25e-38 |
|
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: 136.95 E-value: 5.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 20 VVEALEKK-GFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLLSHPAIADRKVNqPRALIMAPTRELAV 98
Cdd:cd17949 1 LVSHLKSKmGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDRSDG-TLALVLVPTRELAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 99 QIHADAEPLAE-ATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQ-NHINLGAIQVVVLDEADRMYDLGFI 176
Cdd:cd17949 80 QIYEVLEKLLKpFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNtQSFDVSNLRWLVLDEADRLLDMGFE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 445969644 177 KDIRWLFRRM-----------PPANQRLNMLFSATLSYRVRELAFEQMNNAEYI 219
Cdd:cd17949 160 KDITKILELLddkrskaggekSKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
21-209 |
6.55e-37 |
|
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: 133.25 E-value: 6.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 21 VEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLLshpaiadrKVN-QPR----ALIMAPTRE 95
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLY--------KLKfKPRngtgVIIISPTRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 96 LAVQIHADAEPLAEATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAkQN-----HINLgaiQVVVLDEADRM 170
Cdd:cd17942 74 LALQIYGVAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHL-QNtkgflYKNL---QCLIIDEADRI 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 445969644 171 YDLGFIKDIRWLFRRMPpaNQRLNMLFSATLSYRVRELA 209
Cdd:cd17942 150 LEIGFEEEMRQIIKLLP--KRRQTMLFSATQTRKVEDLA 186
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
11-215 |
8.34e-37 |
|
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: 133.19 E-value: 8.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 11 FSDFALHPKVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLlshpaiaDRKVNQPRALIM 90
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKI-------DPKKDVIQALIL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 91 APTRELAVQIHADAEPLAEATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRM 170
Cdd:cd17940 74 VPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 445969644 171 YDLGFIKDIRWLFRRMPPANQrlNMLFSATLSYRVRELAFEQMNN 215
Cdd:cd17940 154 LSQDFQPIIEKILNFLPKERQ--ILLFSATFPLTVKNFMDRHMHN 196
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
24-209 |
8.86e-37 |
|
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: 133.06 E-value: 8.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 24 LEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTstfhyllshPAI--ADRKVNQPRALIMAPTRELAVQIH 101
Cdd:cd17962 5 LKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLL---------PVIirCLTEHRNPSALILTPTRELAVQIE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 102 ADAEPLAEAT-GLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMYDLGFIKDIR 180
Cdd:cd17962 76 DQAKELMKGLpPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVL 155
|
170 180
....*....|....*....|....*....
gi 445969644 181 WLFRRMPPANQRLnmLFSATLSYRVRELA 209
Cdd:cd17962 156 DILENISHDHQTI--LVSATIPRGIEQLA 182
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
16-209 |
9.15e-36 |
|
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: 130.39 E-value: 9.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 16 LHPKVVEALEKKGFHNCTPIQALALPLTLAG--RDVAGQAQTGTGKTMAF-LTStfhylLSHpaiADRKVNQPRALIMAP 92
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFvLAM-----LSR---VDPTLKSPQALCLAP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 93 TRELAVQIHADAEPLAEATGLKLGLAY-GGDGYDKQlkvlESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMY 171
Cdd:cd17963 73 TRELARQIGEVVEKMGKFTGVKVALAVpGNDVPRGK----KITAQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVML 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 445969644 172 DL-GFIKDIRWLFRRMPPANQRLnmLFSATLSYRVRELA 209
Cdd:cd17963 149 DTqGHGDQSIRIKRMLPRNCQIL--LFSATFPDSVRKFA 185
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
242-351 |
9.92e-35 |
|
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: 124.63 E-value: 9.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 242 EKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWgHLAADGHRVGLLTGDVAQKKRLRILDEFTRGDLDILVATDVAARGLH 321
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLEAEL-LLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 445969644 322 IPAVTHVFNYDLPDDCEDYVHRIGRTGRAG 351
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
13-215 |
1.41e-34 |
|
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: 127.06 E-value: 1.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 13 DFALHPKVVEALEKKGFHNCTPIQALA-LPLTLaGRDVAGQAQTGTGKTMAFLTSTFHYLlshpaiaDRKVNQPRALIMA 91
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAiVPIIK-GRDVIAQAQSGTGKTATFSIGALQRI-------DTTVRETQALVLA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 92 PTRELAVQIHADAEPLAEATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMY 171
Cdd:cd17939 73 PTRELAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEML 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 445969644 172 DLGFIKDIRWLFRRMPPANQRlnMLFSATLSYRVRELAFEQMNN 215
Cdd:cd17939 153 SRGFKDQIYDIFQFLPPETQV--VLFSATMPHEVLEVTKKFMRD 194
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
28-215 |
1.23e-33 |
|
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: 124.89 E-value: 1.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 28 GFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTStfhyLLShpaIADRKVNQPRALIMAPTRELAVQIHADAEPL 107
Cdd:cd18045 18 GFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSIS----VLQ---CLDIQVRETQALILSPTRELAVQIQKVLLAL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 108 AEATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMYDLGFIKDIRWLFRRMP 187
Cdd:cd18045 91 GDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKEQIYDVYRYLP 170
|
170 180
....*....|....*....|....*...
gi 445969644 188 PANQrlNMLFSATLSYRVRELAFEQMNN 215
Cdd:cd18045 171 PATQ--VVLVSATLPQDILEMTNKFMTD 196
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
16-208 |
3.06e-33 |
|
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: 123.85 E-value: 3.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 16 LHPKVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLLSHPAIaDRKVNQPRALIMAPTRE 95
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAE-SGEEQGTRALILVPTRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 96 LAVQIHADAEPLAEATGLKLG-LAYGGDGYDKQLKVLESGV-DILIGTTGRLIDYAKQ-NHINLGAIQVVVLDEADRMYD 172
Cdd:cd17961 80 LAQQVSKVLEQLTAYCRKDVRvVNLSASSSDSVQRALLAEKpDIVVSTPARLLSHLESgSLLLLSTLKYLVIDEADLVLS 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 445969644 173 LGFIKDIRWLFRRMPPANQRLNMlfSATLSYRVREL 208
Cdd:cd17961 160 YGYEEDLKSLLSYLPKNYQTFLM--SATLSEDVEAL 193
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
11-221 |
7.31e-33 |
|
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: 122.84 E-value: 7.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 11 FSDFALHPKVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLLSHPaiadrkvNQPRALIM 90
Cdd:cd17950 4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVD-------GQVSVLVI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 91 APTRELAVQIHADAEPLAE-ATGLKLGLAYGGDGYDKQLKVLESGV-DILIGTTGRLIDYAKQNHINLGAIQVVVLDEAD 168
Cdd:cd17950 77 CHTRELAFQISNEYERFSKyMPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 445969644 169 RMY-DLGFIKDIRWLFRRMPPANQRlnMLFSATLSYRVRELAFEQMNNAEYIEV 221
Cdd:cd17950 157 KMLeQLDMRRDVQEIFRATPHDKQV--MMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
11-215 |
1.29e-32 |
|
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: 122.17 E-value: 1.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 11 FSDFALHPKVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLlshpaiaDRKVNQPRALIM 90
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQI-------DTSLKATQALVL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 91 APTRELAVQIHADAEPLAEATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRM 170
Cdd:cd18046 74 APTRELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEM 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 445969644 171 YDLGFIKDIRWLFRRMPPANQRLnmLFSATLSYRVRELAFEQMNN 215
Cdd:cd18046 154 LSRGFKDQIYDIFQKLPPDTQVV--LLSATMPNDVLEVTTKFMRD 196
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
21-222 |
4.66e-32 |
|
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: 120.72 E-value: 4.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 21 VEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLlsHPAIADRKVNQ-PRALIMAPTRELAVQ 99
Cdd:cd17944 2 IKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKL--QEDQQPRKRGRaPKVLVLAPTRELANQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 100 IHADAEPLAEAtgLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMYDLGF---I 176
Cdd:cd17944 80 VTKDFKDITRK--LSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFaeqV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 445969644 177 KDIRWLFRRMPPANQRLNMLFSATLSYRVRELAFEQMnNAEYIEVE 222
Cdd:cd17944 158 EEILSVSYKKDSEDNPQTLLFSATCPDWVYNVAKKYM-KSQYEQVD 202
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
20-208 |
2.62e-30 |
|
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350706 [Multi-domain] Cd Length: 231 Bit Score: 116.70 E-value: 2.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 20 VVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLLSHPAIADRKVNQPRALIMAPTRELAVQ 99
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPFNAPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 100 IHADAEPLAEATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMYDLGFIKDI 179
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 445969644 180 RWLFRRMPPANQRLN-----------MLFSATLSYRVREL 208
Cdd:cd17948 161 SHFLRRFPLASRRSEntdgldpgtqlVLVSATMPSGVGEV 200
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
20-209 |
3.10e-28 |
|
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: 111.18 E-value: 3.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 20 VVEALEKKGFHNCTPIQALALPLTLAG---------RDVAGQAQTGTGKTMAfltstfhYLLshP---AIADRKVNQPRA 87
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLA-------YVL--PivqALSKRVVPRLRA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 88 LIMAPTRELAVQIHADAEPLAEATGLKLGLAYGG-DGYDKQLKVL-------ESGVDILIGTTGRLIDYAKQN-HINLGA 158
Cdd:cd17956 72 LIVVPTKELVQQVYKVFESLCKGTGLKVVSLSGQkSFKKEQKLLLvdtsgryLSRVDILVATPGRLVDHLNSTpGFTLKH 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445969644 159 IQVVVLDEADRMYDLGFIKdirWL------FRRMPPANQRLN---------------MLFSATLSYRVRELA 209
Cdd:cd17956 152 LRFLVIDEADRLLNQSFQD---WLetvmkaLGRPTAPDLGSFgdanllersvrplqkLLFSATLTRDPEKLS 220
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
11-202 |
2.56e-26 |
|
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 (MRH4) plays an essential role during the late stages of mitochondrial ribosome or mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions. MRH4 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350723 [Multi-domain] Cd Length: 251 Bit Score: 106.31 E-value: 2.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 11 FSDFALHPKVVEALEK---KGFHNC------TPIQALALPL---TLAGRDVAGQ-------------AQTGTGKTMAFLT 65
Cdd:cd17965 1 FDQLKLLPSVREAIIKeilKGSNKTdeeikpSPIQTLAIKKllkTLMRKVTKQTsneepklevfllaAETGSGKTLAYLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 66 STFHYL---------LSHPAIADRKVN-QPRALIMAPTRELAVQIHADAEPLAEATGLKLGLAYGGDG--YDKQLKVLES 133
Cdd:cd17965 81 PLLDYLkrqeqepfeEAEEEYESAKDTgRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGpsYQRLQLAFKG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445969644 134 GVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMYDLGFIKDIRWLFRRMPPANQRLnmLFSATLS 202
Cdd:cd17965 161 RIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLI--LCSATIP 227
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
270-351 |
5.95e-26 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 99.98 E-value: 5.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 270 EEIWGHLAADGHRVGLLTGDVAQKKRLRILDEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGR 349
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 445969644 350 AG 351
Cdd:smart00490 81 AG 82
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
35-329 |
2.39e-20 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 93.17 E-value: 2.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 35 IQALALPLTLAGRDVAGQAQTGTGKTMAFLtstfhyllshpAIADRKVNQPRALIMAPTRELAVQIHADAEPLaeatglk 114
Cdd:COG1061 89 LEALLAALERGGGRGLVVAPTGTGKTVLAL-----------ALAAELLRGKRVLVLVPRRELLEQWAEELRRF------- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 115 LGLAYGGDGYDkqlkvlESGVDILIGTTGRLIDYAKQNHINlGAIQVVVLDEADRMYDLGFIKDIRWL---FR------- 184
Cdd:COG1061 151 LGDPLAGGGKK------DSDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHHAGAPSYRRILEAFpaaYRlgltatp 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 185 -RMPPANQRLNMLFSATLSYRVRELAFEQM-NNAEYIEV----EPEQKTGHRIKEELFY---PSNEEKMRLLQTLIEEE- 254
Cdd:COG1061 224 fRSDGREILLFLFDGIVYEYSLKEAIEDGYlAPPEYYGIrvdlTDERAEYDALSERLREalaADAERKDKILRELLREHp 303
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445969644 255 WPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILDEFTRGDLDILVATDVAARGLHIPAVTHVF 329
Cdd:COG1061 304 DDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI 378
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
9-227 |
3.01e-19 |
|
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH) is a testis-specific protein essential for completion of spermatogenesis. DDX25 is also a novel negative regulator of IFN pathway and facilitates RNA virus infection. Diseases associated with DDX25 include hydrolethalus syndrome, an autosomal recessive lethal malformation syndrome characterized by multiple developmental defects of fetus.. DDX25 (also called gonadotropin-regulated testicular RNA helicase) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350806 [Multi-domain] Cd Length: 229 Bit Score: 86.23 E-value: 3.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 9 QKFSDFALHPKVVEALEKKGFHNCTPIQALALPLTLAG--RDVAGQAQTGTGKTMAFLTStfhyLLSHpaiADRKVNQPR 86
Cdd:cd18048 18 KSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLA----MLSR---VDALKLYPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 87 ALIMAPTRELAVQIHADAEPLAE-ATGLKLGLAYGGDGYDKQLKVLESgvdILIGTTGRLIDYA-KQNHINLGAIQVVVL 164
Cdd:cd18048 91 CLCLSPTFELALQTGKVVEEMGKfCVGIQVIYAIRGNRPGKGTDIEAQ---IVIGTPGTVLDWCfKLRLIDVTNISVFVL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445969644 165 DEADRMYDL-GFIKDIRWLFRRMPPANQRLnmLFSATLSYRVRELAFEQMNNAEYIEVEPEQKT 227
Cdd:cd18048 168 DEADVMINVqGHSDHSVRVKRSMPKECQML--LFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
9-209 |
1.72e-17 |
|
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: 80.53 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 9 QKFSDFALHPKVVEALEKKGFHNCTPIQALALPLTLAG--RDVAGQAQTGTGKTMAFLTStfhyLLSHpaiADRKVNQPR 86
Cdd:cd18047 1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLA----MLSQ---VEPANKYPQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 87 ALIMAPTRELAVQIHADAEPLAEATGlKLGLAYGGDGYDkqlkvLESGV----DILIGTTGRLIDYA-KQNHINLGAIQV 161
Cdd:cd18047 74 CLCLSPTYELALQTGKVIEQMGKFYP-ELKLAYAVRGNK-----LERGQkiseQIVIGTPGTVLDWCsKLKFIDPKKIKV 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 445969644 162 VVLDEADRMYDLGFIKDIRWLFRRMPPANQRLnMLFSATLSYRVRELA 209
Cdd:cd18047 148 FVLDEADVMIATQGHQDQSIRIQRMLPRNCQM-LLFSATFEDSVWKFA 194
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
244-352 |
1.48e-15 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 78.62 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 244 MRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVA--------QKKRLRILDEFTRGDLDILVATDV 315
Cdd:COG1111 341 REILKEQLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQASkegdkgltQKEQIEILERFRAGEFNVLVATSV 420
|
90 100 110
....*....|....*....|....*....|....*...
gi 445969644 316 AARGLHIPAVTHVFNYDL-PDDCEdYVHRIGRTGRAGA 352
Cdd:COG1111 421 AEEGLDIPEVDLVIFYEPvPSEIR-SIQRKGRTGRKRE 457
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
244-357 |
1.45e-13 |
|
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: 67.62 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 244 MRLLQTLIEEEWPD---RAIIFANTKHRC-------EEIWGHLaaDGHRVGLLTG----------DVAQKKRLRILDEFT 303
Cdd:cd18802 10 QKLIEILREYFPKTpdfRGIIFVERRATAvvlsrllKEHPSTL--AFIRCGFLIGrgnssqrkrsLMTQRKQKETLDKFR 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 445969644 304 RGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRtGRAGASGHSI 357
Cdd:cd18802 88 DGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARAPNSKYIL 140
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
243-345 |
1.01e-12 |
|
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: 64.81 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 243 KMRLLQTLIEE--EWPDRAIIFANTK---HRCEEiwgHLAADGHRVGLLTGDVAQKKRLRILDEFTR--GDLDILVATDV 315
Cdd:cd18793 12 KLEALLELLEElrEPGEKVLIFSQFTdtlDILEE---ALRERGIKYLRLDGSTSSKERQKLVDRFNEdpDIRVFLLSTKA 88
|
90 100 110
....*....|....*....|....*....|....*.
gi 445969644 316 AARGLHIPAVTHVFNYDLP------DDCEDYVHRIG 345
Cdd:cd18793 89 GGVGLNLTAANRVILYDPWwnpaveEQAIDRAHRIG 124
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
241-363 |
5.04e-12 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 67.47 E-value: 5.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 241 EEKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILDEFTRGDLDILVATdvAARGL 320
Cdd:COG0514 215 DDKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT--IAFGM 292
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 445969644 321 HI--PAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEE 363
Cdd:COG0514 293 GIdkPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPE 337
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
231-347 |
3.92e-11 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 64.86 E-value: 3.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 231 IKEELFYPSNEEKMRLLQTLIEE--EWPDRAIIFanTKHR--CEEIWGHLAADGHRVGLLTGDVAQKKRLRILDEFTRGD 306
Cdd:COG0553 522 LEEGAELSGRSAKLEALLELLEEllAEGEKVLVF--SQFTdtLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGP 599
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 445969644 307 --LDILVATDVAARGLHIPAVTHVFNYDLP------DDCEDYVHRIGRT 347
Cdd:COG0553 600 eaPVFLISLKAGGEGLNLTAADHVIHYDLWwnpaveEQAIDRAHRIGQT 648
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
235-357 |
1.50e-10 |
|
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: 58.76 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 235 LFY---PSNEEKMRLLQTLIEEEWP--DRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILDEFTRGDLDI 309
Cdd:cd18794 4 LFYsvrPKDKKDEKLDLLKRIKVEHlgGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQV 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 445969644 310 LVATdvAARGLHI--PAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSI 357
Cdd:cd18794 84 IVAT--VAFGMGIdkPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECI 131
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
15-313 |
4.86e-10 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 61.39 E-value: 4.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 15 ALHPKVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLLSHPaiadrkvnQPRALIMAPTR 94
Cdd:COG1205 40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDP--------GATALYLYPTK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 95 ELAvqihAD----AEPLAEATGLKLGLA-YGGD--GYDKQlKVLESGvDILIgTTGRLIDYA-KQNHIN----LGAIQVV 162
Cdd:COG1205 112 ALA----RDqlrrLRELAEALGLGVRVAtYDGDtpPEERR-WIREHP-DIVL-TNPDMLHYGlLPHHTRwarfFRNLRYV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 163 VLDEAdRMYDLGFIKDIRWLFRRMppanQRL------NMLF---SATLSyRVRELAfEQMNNAEYIEVE----------- 222
Cdd:COG1205 185 VIDEA-HTYRGVFGSHVANVLRRL----RRIcrhygsDPQFilaSATIG-NPAEHA-ERLTGRPVTVVDedgsprgertf 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 223 -----PEQKTGHRikeelfYPSNEEKMRLLQTLIEEEWpdRAIIFANTKHRCEEIWGHlAADGHRVGLLTGDVAQ----- 292
Cdd:COG1205 258 vlwnpPLVDDGIR------RSALAEAARLLADLVREGL--RTLVFTRSRRGAELLARY-ARRALREPDLADRVAAyragy 328
|
330 340
....*....|....*....|...
gi 445969644 293 --KKRLRILDEFTRGDLDILVAT 313
Cdd:COG1205 329 lpEERREIERGLRSGELLGVVST 351
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
243-352 |
3.40e-09 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 58.73 E-value: 3.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 243 KMRLLQTLIEEEW---PD-RAIIFANTKHRCEEIWGHLAADGHRVGLLTGD--------VAQKKRLRILDEFTRGDLDIL 310
Cdd:PRK13766 348 KLEKLREIVKEQLgknPDsRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGQaskdgdkgMSQKEQIEILDKFRAGEFNVL 427
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 445969644 311 VATDVAARGLHIPAVthvfnydlpddceDYV-------------HRIGRTGRAGA 352
Cdd:PRK13766 428 VSTSVAEEGLDIPSV-------------DLVifyepvpseirsiQRKGRTGRQEE 469
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
10-329 |
8.41e-09 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 57.59 E-value: 8.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 10 KFSDFALHPKVVEALEKKGfHNCTPIQALALP--LtLAGRDVAGQAQTGTGKT----MAFLTSTFHyllshpaiadrkvN 83
Cdd:COG1202 189 PVDDLDLPPELKDLLEGRG-EELLPVQSLAVEngL-LEGKDQLVVSATATGKTligeLAGIKNALE-------------G 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 84 QPRALIMAPTRELAVQIHADAEplaeatglklgLAYGgDGYDKQLKVLES-----------GVDILIGT-TGrlIDYAKQ 151
Cdd:COG1202 254 KGKMLFLVPLVALANQKYEDFK-----------DRYG-DGLDVSIRVGASrirddgtrfdpNADIIVGTyEG--IDHALR 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 152 NHINLGAIQVVVLDE------ADRMYDL-GFIKDIRWLFrrmpPANQrlnMLF-SATLSyRVRELAfEQMNnAEYIEVEp 223
Cdd:COG1202 320 TGRDLGDIGTVVIDEvhmledPERGHRLdGLIARLKYYC----PGAQ---WIYlSATVG-NPEELA-KKLG-AKLVEYE- 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 224 eqktgHR---IKEELFYPSNEEKMRLLQTLIEEEWPDRA--------IIFANTKHRCEEIWGHL---AADGHrVGLltgd 289
Cdd:COG1202 389 -----ERpvpLERHLTFADGREKIRIINKLVKREFDTKSskgyrgqtIIFTNSRRRCHEIARALgykAAPYH-AGL---- 458
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 445969644 290 vAQKKRLRILDEFTRGDLDILVATDVAARGLHIPAVTHVF 329
Cdd:COG1202 459 -DYGERKKVERRFADQELAAVVTTAALAAGVDFPASQVIF 497
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
231-349 |
8.84e-09 |
|
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: 53.90 E-value: 8.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 231 IKEELFYPsneeKM-RLLQTLIE-----EEWPD-RAIIFANTKHRCEEIWGHLAAD----------GHRVGLLTGDVAQK 293
Cdd:cd18801 2 RKVEKIHP----KLeKLEEIVKEhfkkkQEGSDtRVIIFSEFRDSAEEIVNFLSKIrpgiratrfiGQASGKSSKGMSQK 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 445969644 294 KRLRILDEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGR 349
Cdd:cd18801 78 EQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
46-200 |
1.13e-08 |
|
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: 53.56 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 46 GRDVAGQAQTGTGKTMAFLtstfhyllsHPAIADRKVNQPRALIMAPTRELAVQIHADAEPLAeATGLKLGLAYGGDGYD 125
Cdd:cd00046 1 GENVLITAPTGSGKTLAAL---------LAALLLLLKKGKKVLVLVPTKALALQTAERLRELF-GPGIRVAVLVGGSSAE 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445969644 126 KQLKVLESGVDILIGTTGRLIDYAKQNH-INLGAIQVVVLDEADRMYDLGF---IKDIRWLFRRMPPANQrlnMLFSAT 200
Cdd:cd00046 71 EREKNKLGDADIIIATPDMLLNLLLREDrLFLKDLKLIIVDEAHALLIDSRgalILDLAVRKAGLKNAQV---ILLSAT 146
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
260-351 |
2.33e-08 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 56.26 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 260 IIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILDEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCED 339
Cdd:PRK11057 240 IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIES 319
|
90
....*....|..
gi 445969644 340 YVHRIGRTGRAG 351
Cdd:PRK11057 320 YYQETGRAGRDG 331
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
307-351 |
3.61e-08 |
|
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: 50.40 E-value: 3.61e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 445969644 307 LDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAG 351
Cdd:cd18785 23 LEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGG 67
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
55-167 |
9.02e-08 |
|
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: 52.27 E-value: 9.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 55 TGTGKTM--AFLTSTFHYLLSHPAIADRkvnqpRALIMAPTRELAVQihaDAEPLAEATGLKLGLAYGGDGYDKQ----L 128
Cdd:cd18034 25 TGSGKTLiaVMLIKEMGELNRKEKNPKK-----RAVFLVPTVPLVAQ---QAEAIRSHTDLKVGEYSGEMGVDKWtkerW 96
|
90 100 110
....*....|....*....|....*....|....*....
gi 445969644 129 KVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEA 167
Cdd:cd18034 97 KEELEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
213-355 |
1.47e-07 |
|
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350176 [Multi-domain] Cd Length: 153 Bit Score: 50.71 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 213 MNNAEYIEVEpeQKTGHRIKEELfYPSNEEKMRLLQTLIEEEWP-DRAIIFANTKHRCEEIwghlaADGHRVGLLTGDVA 291
Cdd:cd18789 8 MTPEFYREYL--GLGAHRKRRLL-AAMNPNKLRALEELLKRHEQgDKIIVFTDNVEALYRY-----AKRLLKPFITGETP 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445969644 292 QKKRLRILDEFTRGDLDILVATDVAARGLhipavthvfnyDLPD-DC-----------EDYVHRIGRTGRAGASGH 355
Cdd:cd18789 80 QSEREEILQNFREGEYNTLVVSKVGDEGI-----------DLPEaNVaiqisghggsrRQEAQRLGRILRPKKGGG 144
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
53-313 |
2.64e-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: 52.78 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 53 AQTGTGKTMAFLtsTFHYLLSHPAIADRkvnqpraLIMA-PTRELAVQIHADaepLAEATGLKLGLAYG--GDGYDKQLK 129
Cdd:COG1203 154 APTGGGKTEAAL--LFALRLAAKHGGRR-------IIYAlPFTSIINQTYDR---LRDLFGEDVLLHHSlaDLDLLEEEE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 130 VLESGV------------DILIGTTGRLID--YAKQNH--INLGAIQ--VVVLDEADrMYDLGFIKDIRWLFRRMppanQ 191
Cdd:COG1203 222 EYESEArwlkllkelwdaPVVVTTIDQLFEslFSNRKGqeRRLHNLAnsVIILDEVQ-AYPPYMLALLLRLLEWL----K 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 192 RLN---MLFSATLSYRVREL---AFEQMNNAEYIEVE-PEQKTGHRIKEELFYPSNEEKMRLLQTLIEEEwpDRAIIFAN 264
Cdd:COG1203 297 NLGgsvILMTATLPPLLREElleAYELIPDEPEELPEyFRAFVRKRVELKEGPLSDEELAELILEALHKG--KSVLVIVN 374
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 445969644 265 TKHRCEEIWGHLAADGHRVG--LLTGDVAQKKRLRILDE----FTRGDLDILVAT 313
Cdd:COG1203 375 TVKDAQELYEALKEKLPDEEvyLLHSRFCPADRSEIEKEikerLERGKPCILVST 429
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
52-324 |
4.07e-07 |
|
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: 51.66 E-value: 4.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 52 QAQTGTGKTMAFLTSTFHYLlsHPAIADRkvnqpraLIMA-PTRELAVQIHADAEPLAEATGLKLGLAYGGDGYDK-QLK 129
Cdd:cd09639 5 EAPTGYGKTEAALLWALHSL--KSQKADR-------VIIAlPTRATINAMYRRAKEAFGETGLYHSSILSSRIKEMgDSE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 130 VLESGVDILIGTTGRL---------IDYA--------KQNHINLGAIQ--VVVLDEADRM--YDLGFIKDIRWLFRRMpp 188
Cdd:cd09639 76 EFEHLFPLYIHSNDTLfldpitvctIDQVlksvfgefGHYEFTLASIAnsLLIFDEVHFYdeYTLALILAVLEVLKDN-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 189 aNQRLnMLFSATLSYRVRELaFEQMNNAEYIEVEP-----EQKTGHRIKEELFypsneeKMRLLQTLIEE-EWPDRAIIF 262
Cdd:cd09639 154 -DVPI-LLMSATLPKFLKEY-AEKIGYVEENEPLDlkpneRAPFIKIESDKVG------EISSLERLLEFiKKGGSVAII 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445969644 263 ANTKHRCEEIWGHLAADGHRVG--LLTGDVAQ----KKRLRILDEFTRGDLDILVATDVAARGLHIPA 324
Cdd:cd09639 225 VNTVDRAQEFYQQLKEKGPEEEimLIHSRFTEkdraKKEAELLLEFKKSEKFVIVATQVIEASLDISV 292
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
36-186 |
5.13e-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: 49.51 E-value: 5.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 36 QALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLLSHPaiadrkvnQPRALIMAPTRELAV-QIHADAEpLAEATGLK 114
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDP--------GSRALYLYPTKALAQdQLRSLRE-LLEQLGLG 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445969644 115 LGLA-YGGD-GYDKQLKVLESGVDILIgTTGRLIDYA-----KQNHINLGAIQVVVLDEAdRMYDLGFIKDIRWLFRRM 186
Cdd:cd17923 76 IRVAtYDGDtPREERRAIIRNPPRILL-TNPDMLHYAllphhDRWARFLRNLRYVVLDEA-HTYRGVFGSHVALLLRRL 152
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
33-202 |
5.79e-07 |
|
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: 49.57 E-value: 5.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 33 TPIQALAL-PLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLLSHPaiadrkvnqPRALIMAPTRELAVQIHADAEPLAEAT 111
Cdd:cd17921 3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRALATSG---------GKAVYIAPTRALVNQKEADLRERFGPL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 112 GLKLGLAYGGDGYDKQlkvLESGVDILIGTTGRLIDYAKQNHINLG-AIQVVVLDEA------DRMYDLgfikdiRWLFR 184
Cdd:cd17921 74 GKNVGLLTGDPSVNKL---LLAEADILVATPEKLDLLLRNGGERLIqDVRLVVVDEAhligdgERGVVL------ELLLS 144
|
170
....*....|....*....
gi 445969644 185 RMPPANQRLNMLF-SATLS 202
Cdd:cd17921 145 RLLRINKNARFVGlSATLP 163
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
260-361 |
5.60e-06 |
|
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: 46.10 E-value: 5.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 260 IIFANTKHRCEeIWGHL-------AADGHRVGLLTGDVAQKKRLRILDEFTRGDLDILVATDVAARGLHIPAVTHVFNYD 332
Cdd:cd18796 42 LVFTNTRSQAE-RLAQRlrelcpdRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIG 120
|
90 100
....*....|....*....|....*....
gi 445969644 333 LPDDCEDYVHRIGRTGRagaSGHSISLAC 361
Cdd:cd18796 121 SPKSVARLLQRLGRSGH---RPGAASKGR 146
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
260-351 |
3.01e-05 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 46.43 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 260 IIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILDEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCED 339
Cdd:PLN03137 684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEG 763
|
90
....*....|..
gi 445969644 340 YVHRIGRTGRAG 351
Cdd:PLN03137 764 YHQECGRAGRDG 775
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
44-210 |
6.39e-04 |
|
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase 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: 350682 [Multi-domain] Cd Length: 189 Bit Score: 40.39 E-value: 6.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 44 LAGRDVAGQAQTGTGKTmAFLTSTFHYLlshpAIADRKVnqpraLIMAPTRELAVQIHADAEPLAEATGLKLGLAYGGDG 123
Cdd:cd17924 30 LRGKSFAIIAPTGVGKT-TFGLATSLYL----ASKGKRS-----YLIFPTKSLVKQAYERLSKYAEKAGVEVKILVYHSR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 124 YDKQ-----LKVLESG-VDILIGTTGRLIDYAKQnhinLGAIQvvvldeadrmYDLGFIKDIRWLFRRMPPANQRLNML- 196
Cdd:cd17924 100 LKKKekeelLEKIEKGdFDILVTTNQFLSKNFDL----LSNKK----------FDFVFVDDVDAVLKSSKNIDRLLKLLg 165
|
170 180
....*....|....*....|.
gi 445969644 197 F------SATLSYR-VRELAF 210
Cdd:cd17924 166 FgqlvvsSATGRPRgIRPLLF 186
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
269-326 |
9.74e-04 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 39.63 E-value: 9.74e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 445969644 269 CEEIWGHLAADgHRVGLLTGDVAQKKRLRILDEFTRGDLDILVATDVAARGLHIPAVT 326
Cdd:cd18811 51 YEYLKERFRPE-LNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNAT 107
|
|
| PRK05580 |
PRK05580 |
primosome assembly protein PriA; Validated |
293-326 |
4.21e-03 |
|
primosome assembly protein PriA; Validated
Pssm-ID: 235514 [Multi-domain] Cd Length: 679 Bit Score: 39.37 E-value: 4.21e-03
10 20 30
....*....|....*....|....*....|....*
gi 445969644 293 KKRLR-ILDEFTRGDLDILVATDVAARGLHIPAVT 326
Cdd:PRK05580 466 KGALEqLLAQFARGEADILIGTQMLAKGHDFPNVT 500
|
|
| PriA |
COG1198 |
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, ... |
280-326 |
5.09e-03 |
|
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440811 [Multi-domain] Cd Length: 728 Bit Score: 39.33 E-value: 5.09e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 445969644 280 GHRVGLLTGDVAQKKR--LRILDEFTRGDLDILVATDVAARGLHIPAVT 326
Cdd:COG1198 503 DARVLRMDRDTTRRKGalEKLLEAFARGEADILVGTQMLAKGHDFPNVT 551
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
52-170 |
5.12e-03 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 37.78 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 52 QAQTGTGKTMAFLTSTFHYLLSHpaiadrkvnqPRALIMAPTRELAVQIHADAE------PLAEATGlklglayggdgyD 125
Cdd:cd17918 42 SGDVGSGKTLVALGAALLAYKNG----------KQVAILVPTEILAHQHYEEARkflpfiNVELVTG------------G 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 445969644 126 KQLKVLeSGVDILIGTTGRLIDYAKQNHINLgaiqvVVLDEADRM 170
Cdd:cd17918 100 TKAQIL-SGISLLVGTHALLHLDVKFKNLDL-----VIVDEQHRF 138
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
217-357 |
5.44e-03 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350182 [Multi-domain] Cd Length: 154 Bit Score: 37.15 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 217 EYIEVEPEQKTGHRIKEELFYPSNEEKMRLLQTLIEEEwPdrAIIFANTKHRCEEIWGHLAADG-HRVGLLTGDvaqkKR 295
Cdd:cd18795 7 EYVLGFNGLGIKLRVDVMNKFDSDIIVLLKIETVSEGK-P--VLVFCSSRKECEKTAKDLAGIAfHHAGLTRED----RE 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445969644 296 LrILDEFTRGDLDILVATDVAARGLHIPAVTHVFN----YDLPDDCE----DYVHRIGRTGRAG--ASGHSI 357
Cdd:cd18795 80 L-VEELFREGLIKVLVATSTLAAGVNLPARTVIIKgtqrYDGKGYRElsplEYLQMIGRAGRPGfdTRGEAI 150
|
|
| SF2_C_priA |
cd18804 |
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ... |
292-357 |
7.83e-03 |
|
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350191 [Multi-domain] Cd Length: 238 Bit Score: 37.61 E-value: 7.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445969644 292 QKKRLRILDEFTRGDLDILVATDVAARGLHIPAVTHV--FNYD----LPDdcedyvHR------------IGRTGRAGAS 353
Cdd:cd18804 130 KGALEKLLDQFERGEIDILIGTQMIAKGLDFPNVTLVgiLNADsglnSPD------FRaserafqlltqvSGRAGRGDKP 203
|
....
gi 445969644 354 GHSI 357
Cdd:cd18804 204 GKVI 207
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
282-326 |
7.97e-03 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350179 [Multi-domain] Cd Length: 160 Bit Score: 36.86 E-value: 7.97e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 445969644 282 RVGLLTGDVAQKKRLRILDEFTRGDLDILVATDVAARGLHIPAVT 326
Cdd:cd18792 62 RVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNAN 106
|
|
| |
