|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
1-454 |
0e+00 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 915.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVRALI 80
Cdd:PRK10590 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVRALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 81 LTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADR 160
Cdd:PRK10590 81 LTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 161 MLDMGFIHDIRRVLTKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASDQVTQHVHFVDKKRKRELLSHMI 240
Cdd:PRK10590 161 MLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 241 GKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNY 320
Cdd:PRK10590 241 GKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 321 ELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRIAIPGYEPDPSIKAEPIQNGRQQRGGGGRG 400
Cdd:PRK10590 321 ELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRIAIPGYEPDPSIKAEPIQNGRQQRGGGGRG 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128765 401 QGGGRGQQQ--PRRGEGGAKSASAKPAEKPSRRLGDAKPAGEQQRRRRPRKPAAAQ 454
Cdd:PRK10590 401 QGGGRGQQQgqPRRGEGGAKSASAKPAEKPSRRLGDAKPAGEQQRRRRPRKPAAAQ 456
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
1-388 |
0e+00 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 646.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPhakgrRPVRALI 80
Cdd:COG0513 2 MSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP-----RAPQALI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 81 LTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADR 160
Cdd:COG0513 77 LAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 161 MLDMGFIHDIRRVLTKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASDQVTQHVHFVDKKRKRELLSHMI 240
Cdd:COG0513 157 MLDMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 241 GKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNY 320
Cdd:COG0513 237 RDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINY 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128765 321 ELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRIAIPGYEPDPSIKAEPIQ 388
Cdd:COG0513 317 DLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLK 384
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
1-374 |
2.88e-122 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 363.74 E-value: 2.88e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRqphakgRRPVRALI 80
Cdd:PRK11776 4 TAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVK------RFRVQALV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 81 LTPTRELAAQIGENVRDYSKYL-NIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEAD 159
Cdd:PRK11776 78 LCPTRELADQVAKEIRRLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEAD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 160 RMLDMGFIHDIRRVLTKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASdQVTQHVHFVDKKRKRELLSHM 239
Cdd:PRK11776 158 RMLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLP-AIEQRFYEVSPDERLPALQRL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 240 IGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVN 319
Cdd:PRK11776 237 LLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVIN 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 16128765 320 YELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRIAIP 374
Cdd:PRK11776 317 YELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLP 371
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
1-378 |
2.87e-119 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 355.40 E-value: 2.87e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLIT---RQPHakgrrPVR 77
Cdd:PRK11192 1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDfprRKSG-----PPR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 78 ALILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDE 157
Cdd:PRK11192 76 ILILTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 158 ADRMLDMGFIHDIRRVLTKLPAKRQNLLFSATF-SDDIKALAEKLLHNPLEIEVA--RRNTAsdQVTQHVHFVD-KKRKR 233
Cdd:PRK11192 156 ADRMLDMGFAQDIETIAAETRWRKQTLLFSATLeGDAVQDFAERLLNDPVEVEAEpsRRERK--KIHQWYYRADdLEHKT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 234 ELLSHMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEE 313
Cdd:PRK11192 234 ALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDD 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128765 314 LPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRIAIPGYEP 378
Cdd:PRK11192 314 VSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLKARVIDELRP 378
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
3-368 |
8.56e-111 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 334.96 E-value: 8.56e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 3 FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLI-TRQPHAKGRRPVRALIL 81
Cdd:PRK01297 89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLqTPPPKERYMGEPRALII 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 82 TPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGG-VDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADR 160
Cdd:PRK01297 169 APTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEADR 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 161 MLDMGFIHDIRRVLTKLPAK--RQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASDQVTQHVHFVDKKRKRELLSH 238
Cdd:PRK01297 249 MLDMGFIPQVRQIIRQTPRKeeRQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDKYKLLYN 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 239 MIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVV 318
Cdd:PRK01297 329 LVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVI 408
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 16128765 319 NYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEI 368
Cdd:PRK01297 409 NFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKI 458
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
2-369 |
5.88e-107 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 327.50 E-value: 5.88e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHlITRQPHAK-GRRPVrALI 80
Cdd:PTZ00110 131 SFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVH-INAQPLLRyGDGPI-VLV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 81 LTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADR 160
Cdd:PTZ00110 209 LAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADR 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 161 MLDMGFIHDIRRVLTKLPAKRQNLLFSATFSDDIKALAEKLL-HNPLEIEVARRN-TASDQVTQHVHFVDKKRKRELLSH 238
Cdd:PTZ00110 289 MLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCkEEPVHVNVGSLDlTACHNIKQEVFVVEEHEKRGKLKM 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 239 MIGK--GNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPH 316
Cdd:PTZ00110 369 LLQRimRDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKY 448
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128765 317 VVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLL---KKEIP 369
Cdd:PTZ00110 449 VINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLreaKQPVP 504
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
12-209 |
8.45e-104 |
|
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: 307.06 E-value: 8.45e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 12 ILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQphAKGRRPVRALILTPTRELAAQI 91
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEP--KKKGRGPQALVLAPTRELAMQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 92 GENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFIHDIR 171
Cdd:cd00268 79 AEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVE 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 16128765 172 RVLTKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIE 209
Cdd:cd00268 159 KILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
3-369 |
7.45e-100 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 305.36 E-value: 7.45e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 3 FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITrQPHAKGRRPV--RALI 80
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLS-HPAPEDRKVNqpRALI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 81 LTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADR 160
Cdd:PRK04837 89 MAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 161 MLDMGFIHDIRRVLTKLPA--KRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASDQVTQHVHFVDKKRKRELLSH 238
Cdd:PRK04837 169 MFDLGFIKDIRWLFRRMPPanQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYPSNEEKMRLLQT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 239 MIgKGNW-QQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHV 317
Cdd:PRK04837 249 LI-EEEWpDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHV 327
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 16128765 318 VNYELPNVPEDYVHRIGRTGRAAATGEALSLVCvDEHKL-LRDIEKLLKKEIP 369
Cdd:PRK04837 328 FNYDLPDDCEDYVHRIGRTGRAGASGHSISLAC-EEYALnLPAIETYIGHSIP 379
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
1-377 |
6.50e-98 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 306.77 E-value: 6.50e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLitrqpHAKGRRPvRALI 80
Cdd:PRK11634 6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNL-----DPELKAP-QILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 81 LTPTRELAAQIGENVRDYSKYLN-IRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEAD 159
Cdd:PRK11634 80 LAPTRELAVQVAEAMTDFSKHMRgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 160 RMLDMGFIHDIRRVLTKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASDQVTQHVHFVDKKRKRELLSHM 239
Cdd:PRK11634 160 EMLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVRF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 240 IGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVN 319
Cdd:PRK11634 240 LEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVN 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 16128765 320 YELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRIAIPGYE 377
Cdd:PRK11634 320 YDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAE 377
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
1-369 |
8.05e-89 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 281.45 E-value: 8.05e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRqPHAKGRRP--VRA 78
Cdd:PRK04537 9 LTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSR-PALADRKPedPRA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 79 LILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLD-LEHQNAVKLDQVEILVLDE 157
Cdd:PRK04537 88 LILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDyVKQHKVVSLHACEICVLDE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 158 ADRMLDMGFIHDIRRVLTKLPAK--RQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASDQVTQHVHFVDKKRKREL 235
Cdd:PRK04537 168 ADRMFDLGFIKDIRFLLRRMPERgtRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADEEKQTL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 236 LSHMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELP 315
Cdd:PRK04537 248 LLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVK 327
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 16128765 316 HVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIP 369
Cdd:PRK04537 328 YVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKIP 381
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
2-212 |
9.54e-84 |
|
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: 256.65 E-value: 9.54e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAK--GRRPV--R 77
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVgrGRRKAypS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 78 ALILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDE 157
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16128765 158 ADRMLDMGFIHDIRRVLTK--LPAK--RQNLLFSATFSDDIKALAEKLLHNPLEIEVAR 212
Cdd:cd17967 161 ADRMLDMGFEPQIRKIVEHpdMPPKgeRQTLMFSATFPREIQRLAADFLKNYIFLTVGR 219
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
2-368 |
1.37e-78 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 249.74 E-value: 1.37e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQhLITRQPHAkgrrpVRALIL 81
Cdd:PTZ00424 29 SFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQ-LIDYDLNA-----CQALIL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 82 TPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRM 161
Cdd:PTZ00424 103 APTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEM 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 162 LDMGFIHDIRRVLTKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASDQVTQHVHFVDKKR-KRELLSHMI 240
Cdd:PTZ00424 183 LSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEwKFDTLCDLY 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 241 GKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNY 320
Cdd:PTZ00424 263 ETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINY 342
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 16128765 321 ELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEI 368
Cdd:PTZ00424 343 DLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQI 390
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
1-370 |
1.30e-76 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 248.16 E-value: 1.30e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLIT-RQPHAKGRRPVRAL 79
Cdd:PLN00206 121 LSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTiRSGHPSEQRNPLAM 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 80 ILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEAD 159
Cdd:PLN00206 201 VLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVD 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 160 RMLDMGFIHDIRRVLTKLPaKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASDQVTQHVHFVD-KKRKRELLSH 238
Cdd:PLN00206 281 CMLERGFRDQVMQIFQALS-QPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVEtKQKKQKLFDI 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 239 MIGKGNWQ-QVLVFTRTKHGANHLAEQLNK-DGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPH 316
Cdd:PLN00206 360 LKSKQHFKpPAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQ 439
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 16128765 317 VVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKE---IPR 370
Cdd:PLN00206 440 VIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKSSgaaIPR 496
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
1-203 |
2.11e-74 |
|
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: 234.09 E-value: 2.11e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQ---PHAKGRRPVR 77
Cdd:cd18052 43 LTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEGltaSSFSEVQEPQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 78 ALILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDE 157
Cdd:cd18052 123 ALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16128765 158 ADRMLDMGFIHDIRRVLTKL--PAK--RQNLLFSATFSDDIKALAEKLLH 203
Cdd:cd18052 203 ADRMLDMGFGPEIRKLVSEPgmPSKedRQTLMFSATFPEEIQRLAAEFLK 252
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
12-208 |
7.71e-74 |
|
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: 230.22 E-value: 7.71e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 12 ILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRqphAKGRRPVRALILTPTRELAAQI 91
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYR---PKKKAATRVLVLVPTRELAMQC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 92 GENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQN-AVKLDQVEILVLDEADRMLDMGFIHDI 170
Cdd:cd17947 78 FSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSpSFDLDSIEILVLDEADRMLEEGFADEL 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 16128765 171 RRVLTKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEI 208
Cdd:cd17947 158 KEILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
3-209 |
1.74e-69 |
|
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: 219.40 E-value: 1.74e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 3 FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLiTRQPHAkgrrpVRALILT 82
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRL-SEDPYG-----IFALVLT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 83 PTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLD-LEHQNAVK--LDQVEILVLDEAD 159
Cdd:cd17955 75 PTRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADhLRSSDDTTkvLSRVKFLVLDEAD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16128765 160 RMLDMGFIHDIRRVLTKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIE 209
Cdd:cd17955 155 RLLTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFFWE 204
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
3-208 |
2.89e-69 |
|
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: 218.71 E-value: 2.89e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 3 FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHakgrrpVRALILT 82
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDV------IQALILV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 83 PTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRML 162
Cdd:cd17940 75 PTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16128765 163 DMGFIHDIRRVLTKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEI 208
Cdd:cd17940 155 SQDFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
6-208 |
2.65e-68 |
|
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: 216.86 E-value: 2.65e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 6 LGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVrALILTPTR 85
Cdd:cd17953 17 CGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVKPGEGPI-GLIMAPTR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 86 ELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVK---LDQVEILVLDEADRML 162
Cdd:cd17953 96 ELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNGRvtnLRRVTYVVLDEADRMF 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16128765 163 DMGFIHDIRRVLTKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEI 208
Cdd:cd17953 176 DMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
2-209 |
9.30e-68 |
|
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: 214.87 E-value: 9.30e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQphakgrRPVRALIL 81
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENP------QRFFALVL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 82 TPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLD-LEHQNAVKLDQVEILVLDEADR 160
Cdd:cd17954 75 APTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDhLENTKGFSLKSLKFLVMDEADR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16128765 161 MLDMGFIHDIRRVLTKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIE 209
Cdd:cd17954 155 LLNMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKIE 203
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
2-205 |
1.94e-66 |
|
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: 211.39 E-value: 1.94e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPhakgRRPVRALIL 81
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSP----TVGARALIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 82 TPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRM 161
Cdd:cd17959 78 SPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16128765 162 LDMGFIHDIRRVLTKLPAKRQNLLFSATFSDDIKALAEKLLHNP 205
Cdd:cd17959 158 FEMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEP 201
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
12-208 |
1.52e-65 |
|
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: 209.15 E-value: 1.52e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 12 ILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHlITRQPH-AKGRRPVrALILTPTRELAAQ 90
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVH-INAQPPlERGDGPI-VLVLAPTRELAQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 91 IGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFIHDI 170
Cdd:cd17966 79 IQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQI 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 16128765 171 RRVLTKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEI 208
Cdd:cd17966 159 RKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
2-212 |
1.63e-65 |
|
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: 210.67 E-value: 1.63e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAK--------GR 73
Cdd:cd18051 22 TFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQGPGESlpsesgyyGR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 74 R---PVrALILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQV 150
Cdd:cd18051 102 RkqyPL-ALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYC 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128765 151 EILVLDEADRMLDMGFIHDIRRVLTK--LPAK--RQNLLFSATFSDDIKALAEKLLHNPLEIEVAR 212
Cdd:cd18051 181 KYLVLDEADRMLDMGFEPQIRRIVEQdtMPPTgeRQTLMFSATFPKEIQMLARDFLDNYIFLAVGR 246
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
12-208 |
3.37e-63 |
|
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: 203.03 E-value: 3.37e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 12 ILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVrALILTPTRELAAQI 91
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGEGPI-AVIVAPTRELAQQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 92 GENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFIHDIR 171
Cdd:cd17952 80 YLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 16128765 172 RVLTKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEI 208
Cdd:cd17952 160 SIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
25-197 |
1.16e-62 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 200.16 E-value: 1.16e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 25 TPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHakgrrpVRALILTPTRELAAQIGENVRDYSKYLNI 104
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNG------PQALVLAPTRELAEQIYEELKKLGKGLGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 105 RSLVVFGGVSINPQMMKLRGgVDVLVATPGRLLDLEhQNAVKLDQVEILVLDEADRMLDMGFIHDIRRVLTKLPAKRQNL 184
Cdd:pfam00270 75 KVASLLGGDSRKEQLEKLKG-PDILVGTPGRLLDLL-QERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQIL 152
|
170
....*....|...
gi 16128765 185 LFSATFSDDIKAL 197
Cdd:pfam00270 153 LLSATLPRNLEDL 165
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
12-208 |
5.37e-62 |
|
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: 200.62 E-value: 5.37e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 12 ILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLIT--RQPHAKGRRPVRALILTPTRELAA 89
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRlpPLDEETKDDGPYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 90 QIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLD-LEHQNAVkLDQVEILVLDEADRMLDMGFIH 168
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDcLERRLLV-LNQCTYVVLDEADRMIDMGFEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 169 DIRRVLTKLP--------------------AKRQNLLFSATFSDDIKALAEKLLHNPLEI 208
Cdd:cd17945 160 QVTKILDAMPvsnkkpdteeaeklaasgkhRYRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
8-198 |
5.99e-62 |
|
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: 200.12 E-value: 5.99e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 8 LSPDILRAVAEQGYREPTPIQQQAIPAVLE-GRDLMASAQTGTGKTAGFTLPLLQHLITRQPhAKGRRPVRALILTPTRE 86
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKP-AGRRSGVSALIISPTRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 87 LAAQIGENVRDYSKYL-NIRSLVVFGGVSINPQMMKL-RGGVDVLVATPGRLLDL--EHQNAVKLDQVEILVLDEADRML 162
Cdd:cd17964 80 LALQIAAEAKKLLQGLrKLRVQSAVGGTSRRAELNRLrRGRPDILVATPGRLIDHleNPGVAKAFTDLDYLVLDEADRLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16128765 163 DMGFIHDIRRVLTKLPAK----RQNLLFSATFSDDIKALA 198
Cdd:cd17964 160 DMGFRPDLEQILRHLPEKnadpRQTLLFSATVPDEVQQIA 199
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
3-205 |
1.54e-60 |
|
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: 196.39 E-value: 1.54e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 3 FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQhlitrqphakgrrPVRALILT 82
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQ-------------IVVALILE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 83 PTRELAAQIGENVRDYSKYLN---IRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEAD 159
Cdd:cd17938 68 PSRELAEQTYNCIENFKKYLDnpkLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEAD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16128765 160 RMLDMGFIHDIRRVLTKLP-----AKR-QNLLFSATF-SDDIKALAEKLLHNP 205
Cdd:cd17938 148 RLLSQGNLETINRIYNRIPkitsdGKRlQVIVCSATLhSFEVKKLADKIMHFP 200
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
220-349 |
8.06e-59 |
|
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: 189.26 E-value: 8.06e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 220 VTQHVHFVDKKRKRE-LLSHMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRV 298
Cdd:cd18787 1 IKQLYVVVEEEEKKLlLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 16128765 299 LVATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLV 349
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
12-208 |
1.09e-58 |
|
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: 191.14 E-value: 1.09e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 12 ILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITrQPHAKGRRP-VRALILTPTRELAAQ 90
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDL-QPIPREQRNgPGVLVLTPTRELALQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 91 IGENVRDYSkYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFIHDI 170
Cdd:cd17958 80 IEAECSKYS-YKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQI 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 16128765 171 RRVLTKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEI 208
Cdd:cd17958 159 RKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
12-210 |
2.40e-58 |
|
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: 190.49 E-value: 2.40e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 12 ILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLItRQPHAKGrrpVRALILTPTRELAAQI 91
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLG-KPRKKKG---LRALILAPTRELASQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 92 GENVRDYSKYLNIRSLVVFGG-VSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFIHDI 170
Cdd:cd17957 77 YRELLKLSKGTGLRIVLLSKSlEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQT 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16128765 171 RRVLTKLPAKR-QNLLFSATFSDDIKALAEKLLHNPLEIEV 210
Cdd:cd17957 157 DEILAACTNPNlQRSLFSATIPSEVEELARSVMKDPIRIIV 197
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
8-205 |
2.56e-57 |
|
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: 187.79 E-value: 2.56e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 8 LSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVRALILTPTREL 87
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGEEQGTRALILVPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 88 AAQIGENVRDYSKYLN--IRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLD-LEHQNAVKLDQVEILVLDEADRMLDM 164
Cdd:cd17961 81 AQQVSKVLEQLTAYCRkdVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLShLESGSLLLLSTLKYLVIDEADLVLSY 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16128765 165 GFIHDIRRVLTKLPAKRQNLLFSATFSDDIKALAEKLLHNP 205
Cdd:cd17961 161 GYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNP 201
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
12-208 |
3.20e-56 |
|
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: 185.09 E-value: 3.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 12 ILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKgRRPVRALILTPTRELAAQI 91
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLK-KGQVGALIISPTRELATQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 92 GENVRDYSKY--LNIRSLVVFGGVSINPQMMKL-RGGVDVLVATPGRLLD-LEHQN-AVKLDQVEILVLDEADRMLDMGF 166
Cdd:cd17960 80 YEVLQSFLEHhlPKLKCQLLIGGTNVEEDVKKFkRNGPNILVGTPGRLEElLSRKAdKVKVKSLEVLVLDEADRLLDLGF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16128765 167 IHDIRRVLTKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEI 208
Cdd:cd17960 160 EADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
12-208 |
1.30e-55 |
|
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: 183.69 E-value: 1.30e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 12 ILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLI---TRQPHAKGRRPVrALILTPTRELA 88
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALeqeKKLPFIKGEGPY-GLIVCPSRELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 89 AQIGENVRDYSKYLN------IRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRML 162
Cdd:cd17951 80 RQTHEVIEYYCKALQeggypqLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16128765 163 DMGFIHDIRRVLTKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEI 208
Cdd:cd17951 160 DMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
6-208 |
9.91e-55 |
|
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: 180.98 E-value: 9.91e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 6 LGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKgrrpvrALILTPTR 85
Cdd:cd17939 2 MGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQ------ALVLAPTR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 86 ELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMG 165
Cdd:cd17939 76 ELAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRG 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16128765 166 FIHDIRRVLTKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEI 208
Cdd:cd17939 156 FKDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
20-208 |
6.70e-54 |
|
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: 179.32 E-value: 6.70e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 20 GYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVRALILTPTRELAAQIGENVRDY- 98
Cdd:cd17949 10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDRSDGTLALVLVPTRELALQIYEVLEKLl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 99 SKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLD-LEHQNAVKLDQVEILVLDEADRMLDMGFIHDIRRVL--- 174
Cdd:cd17949 90 KPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDhLKNTQSFDVSNLRWLVLDEADRLLDMGFEKDITKILell 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16128765 175 ----------TKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEI 208
Cdd:cd17949 170 ddkrskaggeKSKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
16-223 |
6.79e-54 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 178.84 E-value: 6.79e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 16 VAEQGYREPTPIQQQAIPAVLEG-RDLMASAQTGTGKTAGFTLPLLQHLitrqphaKGRRPVRALILTPTRELAAQIGEN 94
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAL-------KRGKGGRVLVLVPTRELAEQWAEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 95 VRDYSKYLNIRSLVVFGGVSINPQMMKLRGGV-DVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFIHDIRRV 173
Cdd:smart00487 74 LKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16128765 174 LTKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVarRNTASDQVTQH 223
Cdd:smart00487 154 LKLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDV--GFTPLEPIEQF 201
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
12-210 |
5.65e-53 |
|
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: 176.33 E-value: 5.65e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 12 ILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQ-PHAKGrrpVRALILTPTRELAAQ 90
Cdd:cd17941 1 TLKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERwTPEDG---LGALIISPTRELAMQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 91 IGENVRDYSKYLNIRSLVVFGGVSINPQMMKLrGGVDVLVATPGRLLD-LEHQNAVKLDQVEILVLDEADRMLDMGFIHD 169
Cdd:cd17941 78 IFEVLRKVGKYHSFSAGLIIGGKDVKEEKERI-NRMNILVCTPGRLLQhMDETPGFDTSNLQMLVLDEADRILDMGFKET 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16128765 170 IRRVLTKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEV 210
Cdd:cd17941 157 LDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
2-210 |
3.31e-52 |
|
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: 174.84 E-value: 3.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHakgrrpVRALIL 81
Cdd:cd17950 3 GFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQ------VSVLVI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 82 TPTRELAAQIGENVRDYSKYL-NIRSLVVFGGVSINPQMMKLRGGV-DVLVATPGRLLDLEHQNAVKLDQVEILVLDEAD 159
Cdd:cd17950 77 CHTRELAFQISNEYERFSKYMpNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16128765 160 RM---LDMGfiHDIRRVLTKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEV 210
Cdd:cd17950 157 KMleqLDMR--RDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
12-193 |
7.70e-52 |
|
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: 174.73 E-value: 7.70e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 12 ILRAVAEQGYREPTPIQQQAIP-AVLEGRDLMASAQTGTGKTAGFTLPLLQHLIT---RQPHAKGRRPVRALILTPTREL 87
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERLLSqksSNGVGGKQKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 88 AAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDL---EHQNAVKLDQVEILVLDEADRMLDM 164
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELiqeGNEHLANLKSLRFLVLDEADRMLEK 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 16128765 165 GFIHDIRRVLTKLPA-------KRQNLLFSATFSDD 193
Cdd:cd17946 161 GHFAELEKILELLNKdragkkrKRQTFVFSATLTLD 196
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
20-208 |
7.92e-52 |
|
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: 173.12 E-value: 7.92e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 20 GYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITrqphaKGRRPVrALILTPTRELAAQIGENVRDYS 99
Cdd:cd17962 9 GYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLT-----EHRNPS-ALILTPTRELAVQIEDQAKELM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 100 K-YLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFIHDIRRVLTKLP 178
Cdd:cd17962 83 KgLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILENIS 162
|
170 180 190
....*....|....*....|....*....|
gi 16128765 179 AKRQNLLFSATFSDDIKALAEKLLHNPLEI 208
Cdd:cd17962 163 HDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
1-211 |
4.19e-51 |
|
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: 172.89 E-value: 4.19e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHlITRQPH-AKGRRPVrAL 79
Cdd:cd18049 24 LNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVH-INHQPFlERGDGPI-CL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 80 ILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEAD 159
Cdd:cd18049 102 VLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEAD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16128765 160 RMLDMGFIHDIRRVLTKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVA 211
Cdd:cd18049 182 RMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIG 233
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
3-208 |
1.64e-50 |
|
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: 169.93 E-value: 1.64e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 3 FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHakgrrpVRALILT 82
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKA------TQALVLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 83 PTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRML 162
Cdd:cd18046 75 PTRELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEML 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16128765 163 DMGFIHDIRRVLTKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEI 208
Cdd:cd18046 155 SRGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
12-211 |
4.51e-50 |
|
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: 171.35 E-value: 4.51e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 12 ILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHlITRQPH-AKGRRPVrALILTPTRELAAQ 90
Cdd:cd18050 73 VMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVH-INHQPYlERGDGPI-CLVLAPTRELAQQ 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 91 IGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFIHDI 170
Cdd:cd18050 151 VQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQI 230
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16128765 171 RRVLTKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVA 211
Cdd:cd18050 231 RKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINIG 271
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
12-198 |
1.47e-48 |
|
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: 164.84 E-value: 1.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 12 ILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQphAKGRRPVRALILTPTRELAAQI 91
Cdd:cd17942 1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLK--FKPRNGTGVIIISPTRELALQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 92 GENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLD-LEHQNAVKLDQVEILVLDEADRMLDMGFIHDI 170
Cdd:cd17942 79 YGVAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDhLQNTKGFLYKNLQCLIIDEADRILEIGFEEEM 158
|
170 180
....*....|....*....|....*...
gi 16128765 171 RRVLTKLPAKRQNLLFSATFSDDIKALA 198
Cdd:cd17942 159 RQIIKLLPKRRQTMLFSATQTRKVEDLA 186
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
3-208 |
3.04e-47 |
|
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: 161.48 E-value: 3.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 3 FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQphakgrRPVRALILT 82
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQV------RETQALILS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 83 PTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRML 162
Cdd:cd18045 75 PTRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEML 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16128765 163 DMGF---IHDIRRVltkLPAKRQNLLFSATFSDDIKALAEKLLHNPLEI 208
Cdd:cd18045 155 NKGFkeqIYDVYRY---LPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
8-208 |
1.97e-43 |
|
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: 151.19 E-value: 1.97e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 8 LSPDILRAVAEQGYREPTPIQQQAIPAVLEG--RDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKgrrpvrALILTPTR 85
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQ------ALCLAPTR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 86 ELAAQIGENVRDYSKYLNIRSLVVFGGVSINPqmmklRGGVD--VLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLD 163
Cdd:cd17963 75 ELARQIGEVVEKMGKFTGVKVALAVPGNDVPR-----GKKITaqIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLD 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16128765 164 M-GFIHDIRRVLTKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEI 208
Cdd:cd17963 150 TqGHGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
12-205 |
7.11e-42 |
|
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: 147.03 E-value: 7.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 12 ILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLItrqphaKGRRPVRALILTPTRELAAQI 91
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLD------LERRHPQVLILAPTREIAVQI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 92 GENVRDYSKYL-NIRSLVVFGGVSINPQMMKLRGgVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFIHDI 170
Cdd:cd17943 75 HDVFKKIGKKLeGLKCEVFIGGTPVKEDKKKLKG-CHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDV 153
|
170 180 190
....*....|....*....|....*....|....*
gi 16128765 171 RRVLTKLPAKRQNLLFSATFSDDIKALAEKLLHNP 205
Cdd:cd17943 154 NWIFSSLPKNKQVIAFSATYPKNLDNLLARYMRKP 188
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
26-207 |
2.94e-41 |
|
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: 145.76 E-value: 2.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 26 PIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLIT-RQPHAKGRRPvRALILTPTRELAAQIGENVRDYSKYLNI 104
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEdQQPRKRGRAP-KVLVLAPTRELANQVTKDFKDITRKLSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 105 RSLvvFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGF---IHDIRRVLTKLPAKR 181
Cdd:cd17944 94 ACF--YGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFaeqVEEILSVSYKKDSED 171
|
170 180
....*....|....*....|....*...
gi 16128765 182 --QNLLFSATFSDDIKALAEKLLHNPLE 207
Cdd:cd17944 172 npQTLLFSATCPDWVYNVAKKYMKSQYE 199
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
12-225 |
9.86e-37 |
|
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: 134.80 E-value: 9.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 12 ILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLItRQPHAKGR--RPVRALILTPTRELAA 89
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLL-RYKLLAEGpfNAPRGLVITPSRELAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 90 QIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFIHD 169
Cdd:cd17948 80 QIGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128765 170 IRRVL-------------TKLPAKRQNLLFSATFSDDikalAEKLLHnpleiEVARRNTASDQVTQHVH 225
Cdd:cd17948 160 LSHFLrrfplasrrsentDGLDPGTQLVLVSATMPSG----VGEVLS-----KVIDVDSIETVTSDKLH 219
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
12-205 |
2.65e-35 |
|
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: 130.83 E-value: 2.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 12 ILRAVAEQGYREPTPIQQQAIPAVLEG---------RDLMASAQTGTGKTAGFTLPLLQHLITRQphakgRRPVRALILT 82
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKRV-----VPRLRALIVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 83 PTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGG--------VDVLVATPGRLLDleHQNAVK---LDQVE 151
Cdd:cd17956 76 PTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRLVD--HLNSTPgftLKHLR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128765 152 ILVLDEADRMLDMGF--------------------IHDIRRVLTKLPAKRQNLLFSATFSDDIKALAEKLLHNP 205
Cdd:cd17956 154 FLVIDEADRLLNQSFqdwletvmkalgrptapdlgSFGDANLLERSVRPLQKLLFSATLTRDPEKLSSLKLHRP 227
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
232-339 |
3.28e-32 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 118.47 E-value: 3.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 232 KRELLSHMIGKGNWQQVLVFTRTKhgaNHLAEQ--LNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGL 309
Cdd:pfam00271 2 KLEALLELLKKERGGKVLIFSQTK---KTLEAEllLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
|
90 100 110
....*....|....*....|....*....|
gi 16128765 310 DIEELPHVVNYELPNVPEDYVHRIGRTGRA 339
Cdd:pfam00271 79 DLPDVDLVINYDLPWNPASYIQRIGRAGRA 108
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
2-205 |
9.38e-30 |
|
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: 115.89 E-value: 9.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEG--RDLMASAQTGTGKTAGFTLPLLQHLitrqpHAKGRRPvRAL 79
Cdd:cd18048 19 SFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRV-----DALKLYP-QCL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 80 ILTPTRELAAQIGENVRDYSKYLNirslvvfgGVSInpqMMKLRG-----GVD----VLVATPGRLLDLEHQ-NAVKLDQ 149
Cdd:cd18048 93 CLSPTFELALQTGKVVEEMGKFCV--------GIQV---IYAIRGnrpgkGTDieaqIVIGTPGTVLDWCFKlRLIDVTN 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16128765 150 VEILVLDEADRMLDM-GFIHDIRRVLTKLPAKRQNLLFSATFSDDIKALAEKLLHNP 205
Cdd:cd18048 162 ISVFVLDEADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDP 218
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
3-189 |
1.06e-27 |
|
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: 110.54 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 3 FDSLGLSPDILRAVAEQ---------GYREPTPIQQQAIPAVLEGR----------------DLMASAQTGTGKTAGFTL 57
Cdd:cd17965 1 FDQLKLLPSVREAIIKEilkgsnktdEEIKPSPIQTLAIKKLLKTLmrkvtkqtsneepkleVFLLAAETGSGKTLAYLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 58 PLLQHL------------ITRQPHAKGRRPvRALILTPTRELAAQIGENVRDYSKY--LNIRSLVVFGGVSINPQMMKLR 123
Cdd:cd17965 81 PLLDYLkrqeqepfeeaeEEYESAKDTGRP-RSVILVPTHELVEQVYSVLKKLSHTvkLGIKTFSSGFGPSYQRLQLAFK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128765 124 GGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFIHDIRRVLTKLPAKRQNLLFSAT 189
Cdd:cd17965 160 GRIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSAT 225
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
261-339 |
1.60e-26 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 101.90 E-value: 1.60e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128765 261 LAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGRA 339
Cdd:smart00490 3 LAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRA 81
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
2-205 |
3.22e-25 |
|
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: 102.49 E-value: 3.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEG--RDLMASAQTGTGKTAGFTLPLLQHLitrQPHAKGRrpvRAL 79
Cdd:cd18047 2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV---EPANKYP---QCL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 80 ILTPTRELAAQIGENVRDYSKY-------LNIRSLVVFGGVSINPQmmklrggvdVLVATPGRLLDLehqnAVKL----- 147
Cdd:cd18047 76 CLSPTYELALQTGKVIEQMGKFypelklaYAVRGNKLERGQKISEQ---------IVIGTPGTVLDW----CSKLkfidp 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16128765 148 DQVEILVLDEADRML-DMGFIHDIRRVLTKLPAKRQNLLFSATFSDDIKALAEKLLHNP 205
Cdd:cd18047 143 KKIKVFVLDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
23-386 |
2.21e-23 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 102.80 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 23 EPTPIQQQAIPAVL-----EGRDLMASAQTGTGKTAgftlpLLQHLItrqphAKGRRPVRALILTPTRELAAQigeNVRD 97
Cdd:COG1061 80 ELRPYQQEALEALLaalerGGGRGLVVAPTGTGKTV-----LALALA-----AELLRGKRVLVLVPRRELLEQ---WAEE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 98 YSKYLNIRSlvvFGGVSINPqmmklrgGVDVLVATPGRLLDLEHQNAVKlDQVEILVLDEADRMLDMGFihdiRRVLTKL 177
Cdd:COG1061 147 LRRFLGDPL---AGGGKKDS-------DAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHHAGAPSY----RRILEAF 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 178 PAKRQnLLFSAT------------------FSDDIK-ALAEKLL--------HNPLEIEVARRNTASDQVTQHVhFVDKK 230
Cdd:COG1061 212 PAAYR-LGLTATpfrsdgreillflfdgivYEYSLKeAIEDGYLappeyygiRVDLTDERAEYDALSERLREAL-AADAE 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 231 RKRELLSHMIGK-GNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGL 309
Cdd:COG1061 290 RKDKILRELLREhPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGV 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 310 DIEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALS---LVCVDEHKLLRDIEKLLKKEIPRIAIPGYEPDPSIKAEP 386
Cdd:COG1061 370 DVPRLDVAILLRPTGSPREFIQRLGRGLRPAPGKEDALvydFVGNDVPVLEELAKDLRDLAGYRVEFLDEEESEELALLI 449
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1-371 |
5.61e-19 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 89.18 E-value: 5.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 1 MSFDSLgLSPDILRAVAEQGYREPTPIQQQAIPA-VLEGRDLMASAQTGTGKTAGFTLPLLQHLitrqphAKGRRpvrAL 79
Cdd:COG1204 1 MKVAEL-PLEKVIEFLKERGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTLIAELAILKAL------LNGGK---AL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 80 ILTPTRELAAQI-GENVRDYSKyLNIRSLVVFGGVSINPQmmkLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEA 158
Cdd:COG1204 71 YIVPLRALASEKyREFKRDFEE-LGIKVGVSTGDYDSDDE---WLGRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 159 DrmldmgFIHDIRR------VLTKLpaKRQN-----LLFSATFS--DDIKA-LAEKLLH-----NPLEIEVARRNTasdq 219
Cdd:COG1204 147 H------LIDDESRgptlevLLARL--RRLNpeaqiVALSATIGnaEEIAEwLDAELVKsdwrpVPLNEGVLYDGV---- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 220 vtqhVHFVDKKRKRE-----LLSHMIGKGnwQQVLVFTRTKHGANHLAEQL-----------NKDGIRSAAI-------- 275
Cdd:COG1204 215 ----LRFDDGSRRSKdptlaLALDLLEEG--GQVLVFVSSRRDAESLAKKLadelkrrltpeEREELEELAEellevsee 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 276 ------------------HGNKSQGARTRALADFKSGDIRVLVATDIAARGLDieeLP--HVV--------NYELPnvPE 327
Cdd:COG1204 289 thtnekladclekgvafhHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVN---LParRVIirdtkrggMVPIP--VL 363
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 16128765 328 DYVHRIGRTGRAAA--TGEALsLVCVDEHKLLRDIEKLLKKEIPRI 371
Cdd:COG1204 364 EFKQMAGRAGRPGYdpYGEAI-LVAKSSDEADELFERYILGEPEPI 408
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
7-343 |
5.98e-17 |
|
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: 83.35 E-value: 5.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 7 GLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLitrqphAKGRRPvRALILTPTRE 86
Cdd:COG1205 40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEAL------LEDPGA-TALYLYPTKA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 87 LAA-QIgENVRDYSKYL--NIRSLVVFGGVSINpQMMKLRGGVDVLVATPgrllD------LEHQNAVK--LDQVEILVL 155
Cdd:COG1205 113 LARdQL-RRLRELAEALglGVRVATYDGDTPPE-ERRWIREHPDIVLTNP----DmlhyglLPHHTRWArfFRNLRYVVI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 156 DEA---------------DRMldmgfihdiRRVLTKLPAKRQNLLFSATfSDDIKALAEKL------------------- 201
Cdd:COG1205 187 DEAhtyrgvfgshvanvlRRL---------RRICRHYGSDPQFILASAT-IGNPAEHAERLtgrpvtvvdedgsprgert 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 202 --LHNPLEIEVARRNTASDQVtqhvhfvdkkrkRELLSHMIGKGnwQQVLVFTRTKHGANHLAEQLNK------DGIRSA 273
Cdd:COG1205 257 fvLWNPPLVDDGIRRSALAEA------------ARLLADLVREG--LRTLVFTRSRRGAELLARYARRalrepdLADRVA 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128765 274 AIHGNKSQGARtRAL-ADFKSGDIRVLVAT-------DIAarGLDIeelphVVNYELPNVPEDYVHRIGRTGRAAATG 343
Cdd:COG1205 323 AYRAGYLPEER-REIeRGLRSGELLGVVSTnalelgiDIG--GLDA-----VVLAGYPGTRASFWQQAGRAGRRGQDS 392
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
233-341 |
2.28e-16 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 81.70 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 233 RELLSHMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRS------AAIHGNK--SQGARTRALADFKSGDIRVLVATDI 304
Cdd:COG1111 341 REILKEQLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAgrfvgqASKEGDKglTQKEQIEILERFRAGEFNVLVATSV 420
|
90 100 110
....*....|....*....|....*....|....*....
gi 16128765 305 AARGLDIEELPHVVNYElpNVPED--YVHRIGRTGRAAA 341
Cdd:COG1111 421 AEEGLDIPEVDLVIFYE--PVPSEirSIQRKGRTGRKRE 457
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
38-189 |
7.23e-16 |
|
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: 74.36 E-value: 7.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 38 GRDLMASAQTGTGKTAGFTLPLLQHLITRQPhakgrrpvRALILTPTRELAAQIGENVRDYSKyLNIRSLVVFGGVSINP 117
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLKKGK--------KVLVLVPTKALALQTAERLRELFG-PGIRVAVLVGGSSAEE 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128765 118 QMMKLRGGVDVLVATPGRLL-DLEHQNAVKLDQVEILVLDEADRMLDMGFIHDI--RRVLTKLPAKRQNLLFSAT 189
Cdd:cd00046 72 REKNKLGDADIIIATPDMLLnLLLREDRLFLKDLKLIIVDEAHALLIDSRGALIldLAVRKAGLKNAQVILLSAT 146
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
11-348 |
2.59e-13 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 71.71 E-value: 2.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 11 DILRAVAeqGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTA----------GFTL---PLL-----Qhlitrqphakg 72
Cdd:COG0514 7 EVLKRVF--GYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLcyqlpalllpGLTLvvsPLIalmkdQ----------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 73 rrpVRALiltptrelaAQIGENVRdyskYLNirSlvvfggvSINPQ-----MMKLRGG-VDVLVATPGRLLDLEHQNAvk 146
Cdd:COG0514 74 ---VDAL---------RAAGIRAA----FLN--S-------SLSAEerrevLRALRAGeLKLLYVAPERLLNPRFLEL-- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 147 LDQVEI--LVLDEADRMLDMGfiHD-------IRRVLTKLPaKRQNLLFSATFS----DDIkalAEKL-LHNPLEIE--V 210
Cdd:COG0514 127 LRRLKIslFAIDEAHCISQWG--HDfrpdyrrLGELRERLP-NVPVLALTATATprvrADI---AEQLgLEDPRVFVgsF 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 211 ARRNTAsdqvTQHVHFVDKKRKRELLSHmIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALAD 290
Cdd:COG0514 201 DRPNLR----LEVVPKPPDDKLAQLLDF-LKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDR 275
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 16128765 291 FKSGDIRVLVATdIA-ARGLDIEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSL 348
Cdd:COG0514 276 FLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLL 333
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
25-192 |
1.33e-11 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 63.05 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 25 TPIQQQAI-PAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPhakgrrpvRALILTPTRELAAQIGENVRDYSKYLN 103
Cdd:cd17921 3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRALATSGG--------KAVYIAPTRALVNQKEADLRERFGPLG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 104 IRSLVVFGGVSINPQMMKLRggvDVLVATP----GRLLDLEHQNavkLDQVEILVLDEADrmldmgFIHDIRR------V 173
Cdd:cd17921 75 KNVGLLTGDPSVNKLLLAEA---DILVATPekldLLLRNGGERL---IQDVRLVVVDEAH------LIGDGERgvvlelL 142
|
170 180
....*....|....*....|..
gi 16128765 174 LTKLPA---KRQNLLFSATFSD 192
Cdd:cd17921 143 LSRLLRinkNARFVGLSATLPN 164
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
21-96 |
3.78e-11 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 65.51 E-value: 3.78e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128765 21 YREPTPIQQQAIPAVLEGRDLMASAQTGTGKT-AGFtLPLLQHLITRQPHAKGRRPVRALILTPTRELAAQIGENVR 96
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPRPGELPDGLRVLYISPLKALANDIERNLR 97
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
224-338 |
1.22e-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: 59.14 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 224 VHFVDKKRKRELLSHMI-GKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVAT 302
Cdd:cd18794 8 VRPKDKKDEKLDLLKRIkVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVAT 87
|
90 100 110
....*....|....*....|....*....|....*.
gi 16128765 303 DIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGR 338
Cdd:cd18794 88 VAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGR 123
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
233-349 |
5.11e-10 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 61.81 E-value: 5.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 233 RELLSHMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHG--NK------SQGARTRALADFKSGDIRVLVATDI 304
Cdd:PRK13766 353 REIVKEQLGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGqaSKdgdkgmSQKEQIEILDKFRAGEFNVLVSTSV 432
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 16128765 305 AARGLDIEELPHVVNYElPnVPED--YVHRIGRTGRAAAtGEALSLV 349
Cdd:PRK13766 433 AEEGLDIPSVDLVIFYE-P-VPSEirSIQRKGRTGRQEE-GRVVVLI 476
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
233-334 |
6.92e-10 |
|
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: 57.10 E-value: 6.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 233 RELLSHMIGKGnwQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFK--SGDIRVLVATDIAARGLD 310
Cdd:cd18793 17 LELLEELREPG--EKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNedPDIRVFLLSTKAGGVGLN 94
|
90 100 110
....*....|....*....|....*....|
gi 16128765 311 IEELPHVVNYEL---PNVPE---DYVHRIG 334
Cdd:cd18793 95 LTAANRVILYDPwwnPAVEEqaiDRAHRIG 124
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
26-190 |
7.47e-09 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 54.23 E-value: 7.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 26 PIQQQAIPAVLE---GRDLMASAQTGTGKTA-GFTLPLLqhlitrqphakgRRPVRALILTPTRELAAQIgenVRDYSKY 101
Cdd:cd17926 3 PYQEEALEAWLAhknNRRGILVLPTGSGKTLtALALIAY------------LKELRTLIVVPTDALLDQW---KERFEDF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 102 LNIRSLVVFGGVSInpqmmKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFihdiRRVLTKLPAKR 181
Cdd:cd17926 68 LGDSSIGLIGGGKK-----KDFDDANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHHLPAKTF----SEILKELNAKY 138
|
....*....
gi 16128765 182 QnLLFSATF 190
Cdd:cd17926 139 R-LGLTATP 146
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
1-310 |
1.00e-08 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 57.59 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 1 MSFDSLGLSPDiLRAVAEQGYREPTPIQQQAIPA-VLEGRDLMASAQTGTGKT-----AGftlpllqhlITRQPHAKGrr 74
Cdd:COG1202 188 VPVDDLDLPPE-LKDLLEGRGEELLPVQSLAVENgLLEGKDQLVVSATATGKTligelAG---------IKNALEGKG-- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 75 pvRALILTPTRELAAQIGENVRD-YSKYLNIRSLVvfgGVSinpqMMKLRGG-----VDVLVAT---------PGRllDL 139
Cdd:COG1202 256 --KMLFLVPLVALANQKYEDFKDrYGDGLDVSIRV---GAS----RIRDDGTrfdpnADIIVGTyegidhalrTGR--DL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 140 EHQNAVKLDqvEILVLDEADR--MLDmGFihdIRRvLTKLPAKRQNLLFSATFSDDiKALAEKLLHNPLEIEvaRRNTAs 217
Cdd:COG1202 325 GDIGTVVID--EVHMLEDPERghRLD-GL---IAR-LKYYCPGAQWIYLSATVGNP-EELAKKLGAKLVEYE--ERPVP- 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 218 dqVTQHVHFVDKKRKRELLSHMI--------GKGNWQQVLVFTRTKHGANHLAEQLnkdGIRSAAIHGNKSQGARTRALA 289
Cdd:COG1202 394 --LERHLTFADGREKIRIINKLVkrefdtksSKGYRGQTIIFTNSRRRCHEIARAL---GYKAAPYHAGLDYGERKKVER 468
|
330 340
....*....|....*....|.
gi 16128765 290 DFKSGDIRVLVATDIAARGLD 310
Cdd:COG1202 469 RFADQELAAVVTTAALAAGVD 489
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
233-336 |
1.19e-08 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 57.16 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 233 RELLSHMIGKGnwQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGD--IRVLVATDIAARGLD 310
Cdd:COG0553 539 LELLEELLAEG--EKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGGEGLN 616
|
90 100 110
....*....|....*....|....*....|..
gi 16128765 311 IEELPHVVNYEL---PNVPE---DYVHRIGRT 336
Cdd:COG0553 617 LTAADHVIHYDLwwnPAVEEqaiDRAHRIGQT 648
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
249-340 |
1.29e-08 |
|
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: 53.36 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 249 LVFTRTKHGA---NHLAEQLNK--DGIRSAAI--HGNKSQGAR--------TRALADFKSGDIRVLVATDIAARGLDIEE 313
Cdd:cd18802 29 IIFVERRATAvvlSRLLKEHPStlAFIRCGFLigRGNSSQRKRslmtqrkqKETLDKFRDGELNLLIATSVLEEGIDVPA 108
|
90 100
....*....|....*....|....*..
gi 16128765 314 LPHVVNYELPNVPEDYVHRIGRtGRAA 340
Cdd:cd18802 109 CNLVIRFDLPKTLRSYIQSRGR-ARAP 134
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
246-338 |
3.59e-08 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350188 [Multi-domain] Cd Length: 143 Bit Score: 52.36 E-value: 3.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 246 QQVLVFTRTKHGANHLAEQLNK--DGIRSAAI--HGNK------SQGARTRALADFKSGDIRVLVATDIAARGLDIEELP 315
Cdd:cd18801 31 TRVIIFSEFRDSAEEIVNFLSKirPGIRATRFigQASGksskgmSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVD 110
|
90 100
....*....|....*....|...
gi 16128765 316 HVVNYELPNVPEDYVHRIGRTGR 338
Cdd:cd18801 111 LIICYDASPSPIRMIQRMGRTGR 133
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
47-158 |
4.37e-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: 53.04 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 47 TGTGKTAgFTLPLLQHLItRQPHAKGRRPVRALILTPTRELAAQIGENVRDYSKYLNIrslVVFG--GVSINPQMMKLR- 123
Cdd:cd18034 25 TGSGKTL-IAVMLIKEMG-ELNRKEKNPKKRAVFLVPTVPLVAQQAEAIRSHTDLKVG---EYSGemGVDKWTKERWKEe 99
|
90 100 110
....*....|....*....|....*....|....*.
gi 16128765 124 -GGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEA 158
Cdd:cd18034 100 lEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
223-366 |
6.48e-08 |
|
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350185 [Multi-domain] Cd Length: 174 Bit Score: 52.31 E-value: 6.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 223 HVHFVDKKRKRELLSHM--IGKGnwqqVLVFTRTKHG---ANHLAEQLNKDGIRSAAIHGNksqgaRTRALADFKSGDIR 297
Cdd:cd18798 4 DVYIEDSDSLEKLLELVkkLGDG----GLIFVSIDYGkeyAEELKEFLERHGIKAELALSS-----TEKNLEKFEEGEID 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128765 298 VLVAT----DIAARGLDieeLPHVVNYEL-PNVP-EDYVHRIGRTGRAAATG--EALSLVCVDEHKLLRDIEKLLKK 366
Cdd:cd18798 75 VLIGVasyyGVLVRGID---LPERIKYAIfYGVPvTTYIQASGRTSRLYAGGltKGLSVVLVDDPELFEALKKRLKL 148
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
8-362 |
7.33e-08 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 54.72 E-value: 7.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 8 LSPDILRAVAeqGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLL---------QHLIT------RQPHAKG 72
Cdd:PRK11057 12 LAKQVLQETF--GYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALvldgltlvvSPLISlmkdqvDQLLANG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 73 rrpVRALILTPTRELAAQigenvrdyskylnirsLVVFGGVSinpqmmklRGGVDVLVATPGRLL------DLEHQNAVk 146
Cdd:PRK11057 90 ---VAAACLNSTQTREQQ----------------LEVMAGCR--------TGQIKLLYIAPERLMmdnfleHLAHWNPA- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 147 ldqveILVLDEADRMLDMGfiHDIR---RVLTKLPAKRQNLLF---SATFSD----DIKALAEklLHNPLeIEVA---RR 213
Cdd:PRK11057 142 -----LLAVDEAHCISQWG--HDFRpeyAALGQLRQRFPTLPFmalTATADDttrqDIVRLLG--LNDPL-IQISsfdRP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 214 NTASDQVTQHvhfvdkKRKRELLSHMIG-KGNWQQVLVFTRTKhgANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFK 292
Cdd:PRK11057 212 NIRYTLVEKF------KPLDQLMRYVQEqRGKSGIIYCNSRAK--VEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQ 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 293 SGDIRVLVATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLV----------CVDEHKL--LRDI 360
Cdd:PRK11057 284 RDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYdpadmawlrrCLEEKPAgqQQDI 363
|
..
gi 16128765 361 EK 362
Cdd:PRK11057 364 ER 365
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
248-338 |
2.49e-07 |
|
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: 49.96 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 248 VLVFTRTKHGANHLAEQLNK------DGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYE 321
Cdd:cd18796 41 TLVFTNTRSQAERLAQRLRElcpdrvPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIG 120
|
90
....*....|....*..
gi 16128765 322 LPNVPEDYVHRIGRTGR 338
Cdd:cd18796 121 SPKSVARLLQRLGRSGH 137
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
23-161 |
2.63e-07 |
|
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: 50.49 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 23 EPTPIQQQAIPAVL------EGRDLMASAQTGTGKTAGFTLPLLQHLitrqphakgRRPVRALILTPTRELAAQIGENVR 96
Cdd:cd17918 15 SLTKDQAQAIKDIEkdlhspEPMDRLLSGDVGSGKTLVALGAALLAY---------KNGKQVAILVPTEILAHQHYEEAR 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128765 97 DYskYLNIRSLVVFGGVSinpqmMKLRGGVDVLVATPGRLldlehQNAVKLDQVEILVLDEADRM 161
Cdd:cd17918 86 KF--LPFINVELVTGGTK-----AQILSGISLLVGTHALL-----HLDVKFKNLDLVIVDEQHRF 138
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
28-96 |
3.74e-07 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 50.28 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 28 QQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLItRQPHAkgrrpvRALILTPT-----------RELAAQIGENVR 96
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALL-RDPGS------RALYLYPTkalaqdqlrslRELLEQLGLGIR 77
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
1-359 |
7.17e-07 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 51.74 E-value: 7.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPA-VLEGRDLMASAQTGTGKTAGFTLPLLQHLItrqphakgRRPVRAL 79
Cdd:PRK00254 1 MKVDELRVDERIKRVLKERGIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIVMVNKLL--------REGGKAV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 80 ILTPTRELAAQIGENVRDYSKyLNIRSLVVFGGVSINPQMMklrGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEA- 158
Cdd:PRK00254 73 YLVPLKALAEEKYREFKDWEK-LGLRVAMTTGDYDSTDEWL---GKYDIIIATAEKFDSLLRHGSSWIKDVKLVVADEIh 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 159 -----DRMLDMGFIhdirrvLTKLPAKRQNLLFSATFSDDiKALAEKLlhNPLEIEVARRNTASDQVTQHVHFV---DKK 230
Cdd:PRK00254 149 ligsyDRGATLEMI------LTHMLGRAQILGLSATVGNA-EELAEWL--NAELVVSDWRPVKLRKGVFYQGFLfweDGK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 231 RKR------ELLSHMIGKGnwQQVLVFTRTKHGA-----------------------NHLAEQLN--------KDGIRS- 272
Cdd:PRK00254 220 IERfpnsweSLVYDAVKKG--KGALVFVNTRRSAekealelakkikrfltkpelralKELADSLEenptneklKKALRGg 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 273 -AAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLD-------IEELPHVVNYELPNVPEDYVHR-IGRTGRAA--A 341
Cdd:PRK00254 298 vAFHHAGLGRTERVLIEDAFREGLIKVITATPTLSAGINlpafrviIRDTKRYSNFGWEDIPVLEIQQmMGRAGRPKydE 377
|
410
....*....|....*...
gi 16128765 342 TGEALSLVCVDEHKLLRD 359
Cdd:PRK00254 378 VGEAIIVATTEEPSKLME 395
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
245-343 |
1.37e-06 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 45.77 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 245 WQQVLVFTRTKHGANHLAEQLNkdgirsaaihgnksqgartraladfksgdirVLVATDIAARGLDIEELPHVVNYELPN 324
Cdd:cd18785 3 VVKIIVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDPPS 51
|
90
....*....|....*....
gi 16128765 325 VPEDYVHRIGRTGRAAATG 343
Cdd:cd18785 52 SAASYIQRVGRAGRGGKDE 70
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
231-313 |
1.59e-06 |
|
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: 47.63 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 231 RKRELLSHMIGK-GNWQQVLVFTRTKHGANHLAEQLNKdgirsAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGL 309
Cdd:cd18789 34 NKLRALEELLKRhEQGDKIIVFTDNVEALYRYAKRLLK-----PFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGI 108
|
....
gi 16128765 310 DIEE 313
Cdd:cd18789 109 DLPE 112
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
27-157 |
5.54e-06 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350781 [Multi-domain] Cd Length: 206 Bit Score: 46.97 E-value: 5.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 27 IQQQAIPAVLEG-RDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRpvRALILTPTRELAAQIGENVRDYSKYLNIR 105
Cdd:cd18023 5 IQSEVFPDLLYSdKNFVVSAPTGSGKTVLFELAILRLLKERNPLPWGNR--KVVYIAPIKALCSEKYDDWKEKFGPLGLS 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 16128765 106 SLVVFGgvsiNPQMMKLRG--GVDVLVATPGRL-----LDLEHQNAVKLdqVEILVLDE 157
Cdd:cd18023 83 CAELTG----DTEMDDTFEiqDADIILTTPEKWdsmtrRWRDNGNLVQL--VALVLIDE 135
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
23-190 |
2.84e-05 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 44.20 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 23 EPTPIQQQAIPAVLEGRD-----LMASAQTGTGKTagFTLPLLQHLITRQPHAKgrrpvRALILTPTRELAAQIGENVRD 97
Cdd:pfam04851 3 ELRPYQIEAIENLLESIKngqkrGLIVMATGSGKT--LTAAKLIARLFKKGPIK-----KVLFLVPRKDLLEQALEEFKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 98 YSKylnirSLVVFGGVSINPQMMKLRGGVDVLVATP---GRLLDLEHQNAVKlDQVEILVLDEADRMLDMGFihdiRRVL 174
Cdd:pfam04851 76 FLP-----NYVEIGEIISGDKKDESVDDNKIVVTTIqslYKALELASLELLP-DFFDVIIIDEAHRSGASSY----RNIL 145
|
170
....*....|....*.
gi 16128765 175 TKLPAKRQnLLFSATF 190
Cdd:pfam04851 146 EYFKPAFL-LGLTATP 160
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
26-201 |
4.94e-05 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 43.86 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 26 PIQQQAIPA-VLEGRDLMASAQTGTGKTAGFTLPLLQHLItrqphaKGRrpvRALILTPTRELAaqiGENVRDYSKYLNI 104
Cdd:cd18028 4 PPQAEAVRAgLLKGENLLISIPTASGKTLIAEMAMVNTLL------EGG---KALYLVPLRALA---SEKYEEFKKLEEI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 105 RSLVvfgGVSI--NPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEadrmldMGFIHDIRR------VLTK 176
Cdd:cd18028 72 GLKV---GISTgdYDEDDEWLGDYDIIVATYEKFDSLLRHSPSWLRDVGVVVVDE------IHLISDEERgptlesIVAR 142
|
170 180
....*....|....*....|....*...
gi 16128765 177 LPA---KRQNLLFSATFSdDIKALAEKL 201
Cdd:cd18028 143 LRRlnpNTQIIGLSATIG-NPDELAEWL 169
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
11-60 |
1.22e-04 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 42.91 E-value: 1.22e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 16128765 11 DILRAVAeqGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLL 60
Cdd:cd17920 2 QILKEVF--GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPAL 49
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
3-192 |
2.17e-04 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 43.77 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 3 FDSLGLSPDILRAVAEQGYrEPTPIQQQAIPAVLEGRDLMASAQTGTGKTagftlpllqhLITRQPH----AKGRR---- 74
Cdd:COG4581 6 ARADARLEALADFAEERGF-ELDPFQEEAILALEAGRSVLVAAPTGSGKT----------LVAEFAIflalARGRRsfyt 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 75 -PVRALILTPTRELAAQIG-ENVrdyskylnirSLVVfGGVSINPQmmklrggVDVLVATPGRLLDLEHQNAVKLDQVEI 152
Cdd:COG4581 75 aPIKALSNQKFFDLVERFGaENV----------GLLT-GDASVNPD-------APIVVMTTEILRNMLYREGADLEDVGV 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16128765 153 LVLDEADrmldmgFIHDIRR------VLTKLPAKRQNLLFSATFSD 192
Cdd:COG4581 137 VVMDEFH------YLADPDRgwvweePIIHLPARVQLVLLSATVGN 176
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
11-94 |
2.52e-04 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 43.72 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 11 DILR-AVAE---QGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKT-AGFtLPLLQHLITRQPHAKGRRPVRALILTPTR 85
Cdd:PRK13767 16 DLLRpYVREwfkEKFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAF-LAIIDELFRLGREGELEDKVYCLYVSPLR 94
|
....*....
gi 16128765 86 ELAAQIGEN 94
Cdd:PRK13767 95 ALNNDIHRN 103
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
23-162 |
6.24e-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: 40.77 E-value: 6.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 23 EPTPIQQQAIPAVLEGRDLMASAQTGTGKTagfTLPLLQHLITRqphAKGRrpvRALILTPTRELAAQIGENVRDYSKYL 102
Cdd:cd17924 17 PPWGAQRTWAKRLLRGKSFAIIAPTGVGKT---TFGLATSLYLA---SKGK---RSYLIFPTKSLVKQAYERLSKYAEKA 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128765 103 N--IRSLVVFGGVSINPQ---MMKLR-GGVDVLVATPGRLldleHQNAVKLDQVE--ILVLDEADRML 162
Cdd:cd17924 88 GveVKILVYHSRLKKKEKeelLEKIEkGDFDILVTTNQFL----SKNFDLLSNKKfdFVFVDDVDAVL 151
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
249-319 |
6.80e-04 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350186 [Multi-domain] Cd Length: 116 Bit Score: 39.08 E-value: 6.80e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128765 249 LVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTR-ALADFKSGDI--RVLVATDIAARGLDIeelPHVVN 319
Cdd:cd18799 10 LIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDeALILLFFGELkpPILVTVDLLTTGVDI---PEVDN 80
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
201-349 |
7.74e-04 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 39.93 E-value: 7.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 201 LLHNPLEIEVARRNTASDQVTQhvhfvdkkrkRELLSHMIGKGnwQQVLVFTRTKHGA----NHLAEQLNKDGIRSAAIH 276
Cdd:cd18797 3 VLWNPPLLDRKDGERGSARREA----------ARLFADLVRAG--VKTIVFCRSRKLAelllRYLKARLVEEGPLASKVA 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128765 277 GNKS---QGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGRAAatGEALSLV 349
Cdd:cd18797 71 SYRAgylAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRG--KDSLVIL 144
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
23-160 |
1.00e-03 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 40.11 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 23 EPTPIQQQAIPAVLEGRDLMASAQTGTGKTAgFTLPLLQHLITRQPhakGRRPVRALILTPTRELAAQIGENVRDYSKYL 102
Cdd:cd17927 2 KPRNYQLELAQPALKGKNTIICLPTGSGKTF-VAVLICEHHLKKFP---AGRKGKVVFLANKVPLVEQQKEVFRKHFERP 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 16128765 103 NIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLL-DLEHQNAVKLDQVEILVLDEADR 160
Cdd:cd17927 78 GYKVTGLSGDTSENVSVEQIVESSDVIIVTPQILVnDLKSGTIVSLSDFSLLVFDECHN 136
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
246-313 |
1.07e-03 |
|
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350177 [Multi-domain] Cd Length: 171 Bit Score: 39.92 E-value: 1.07e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128765 246 QQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEE 313
Cdd:cd18790 28 ERVLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPE 95
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
24-160 |
1.20e-03 |
|
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350790 [Multi-domain] Cd Length: 163 Bit Score: 39.47 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 24 PTPIQQQAIPAVLEGRD------LMASAqTGTGKT--AGFtlpllqhLITRqpHAKGRRPVRALILTPTRELAAQIgenV 95
Cdd:cd18032 1 PRYYQQEAIEALEEAREkgqrraLLVMA-TGTGKTytAAF-------LIKR--LLEANRKKRILFLAHREELLEQA---E 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128765 96 RDYSKYLNIRSLVVFGGVSINPqmmklrGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADR 160
Cdd:cd18032 68 RSFKEVLPDGSFGNLKGGKKKP------DDARVVFATVQTLNKRKRLEKFPPDYFDLIIIDEAHH 126
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
1-189 |
1.34e-03 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 41.10 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPA-VLEGRDLMASAQTGTGKTAGFTLPLLQHLitrqphAKGRrpvRAL 79
Cdd:PRK02362 1 MKIAELPLPEGVIEFYEAEGIEELYPPQAEAVEAgLLDGKNLLAAIPTASGKTLIAELAMLKAI------ARGG---KAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 80 ILTPTRELAaqiGENVRDYSKYlniRSLVVFGGVSI-NPQMMKLRGGV-DVLVATPGRLLDLEHQNAVKLDQVEILVLDE 157
Cdd:PRK02362 72 YIVPLRALA---SEKFEEFERF---EELGVRVGISTgDYDSRDEWLGDnDIIVATSEKVDSLLRNGAPWLDDITCVVVDE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16128765 158 ------ADR--MLDMgfihdirrVLTKLpaKRQN-----LLFSAT 189
Cdd:PRK02362 146 vhlidsANRgpTLEV--------TLAKL--RRLNpdlqvVALSAT 180
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
27-160 |
2.08e-03 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 39.03 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 27 IQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPhakgrrpvRALILTPTRELAAQIGENVRdysKYLNIRS 106
Cdd:cd18035 5 LYQVLIAAVALNGNTLIVLPTGLGKTIIAILVAADRLTKKGG--------KVLILAPSRPLVEQHAENLK---RVLNIPD 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 16128765 107 LVVFGGVSINP-QMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADR 160
Cdd:cd18035 74 KITSLTGEVKPeERAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
26-133 |
2.11e-03 |
|
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350779 [Multi-domain] Cd Length: 191 Bit Score: 39.16 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 26 PIQQQAIPAVLEGRD-LMASAQTGTGKTAGFTLPLLQHLITRQPHakgrrpvRALILTPTRELAAQIGENVRD-YSKYLN 103
Cdd:cd18021 6 PIQTQVFNSLYNTDDnVFVGAPTGSGKTVCAELALLRHWRQNPKG-------RAVYIAPMQELVDARYKDWRAkFGPLLG 78
|
90 100 110
....*....|....*....|....*....|
gi 16128765 104 IRSLVVFGGVSINpqmMKLRGGVDVLVATP 133
Cdd:cd18021 79 KKVVKLTGETSTD---LKLLAKSDVILATP 105
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
23-200 |
2.41e-03 |
|
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also called SKI2 or DHX13) plays a role in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. SKIV2L 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: 350785 [Multi-domain] Cd Length: 179 Bit Score: 38.78 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 23 EPTPIQQQAIPAVLEGRDLMASAQTGTGKT--AGFTLPLLQHLITrqphakgrrpvRALILTPTRELAAQigeNVRDYSK 100
Cdd:cd18027 8 ELDVFQKQAILHLEAGDSVFVAAHTSAGKTvvAEYAIALAQKHMT-----------RTIYTSPIKALSNQ---KFRDFKN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 101 YLNIRSLVVfGGVSINPqmmklrgGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADrmldmgFIHDIRR------VL 174
Cdd:cd18027 74 TFGDVGLIT-GDVQLNP-------EASCLIMTTEILRSMLYNGSDVIRDLEWVIFDEVH------YINDAERgvvweeVL 139
|
170 180 190
....*....|....*....|....*....|..
gi 16128765 175 TKLPAKRQNLLFSAT------FSDDIKALAEK 200
Cdd:cd18027 140 IMLPDHVSIILLSATvpntveFADWIGRIKKK 171
|
|
| Cas1 |
COG1518 |
CRISPR-Cas system-associated integrase Cas1 [Defense mechanisms]; CRISPR-Cas system-associated ... |
103-201 |
5.97e-03 |
|
CRISPR-Cas system-associated integrase Cas1 [Defense mechanisms]; CRISPR-Cas system-associated integrase Cas1 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 441127 Cd Length: 329 Bit Score: 38.64 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128765 103 NIRSLVVFGGVSINPQMMK--LRGGVDVLVATP-----GRLLDLEHQNAVKLD--QVEILvLDEADRM-----LDMGFIH 168
Cdd:COG1518 34 DIEQIVLFGEVSLSTALLRflAENGIPVHFLDYygrylGRLLPRESGGNVLLRraQYQAY-LDEEKRLalarsIVRGKIR 112
|
90 100 110
....*....|....*....|....*....|...
gi 16128765 169 DIRRVLTKLPAKRQNLLFSAtfSDDIKALAEKL 201
Cdd:COG1518 113 NQRAVLRRYGRRRKEDLEEA--IERLEELLKRL 143
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
38-103 |
6.33e-03 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 37.56 E-value: 6.33e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128765 38 GRDLMASAQTGTGKTAGFTLPLLQHLITRQPhakgrRPVRALILTPTRELAAQIGENVRDYSKYLN 103
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPE-----KGVQVLYISPLKALINDQERRLEEPLDEID 61
|
|
| ASKHA_NBD_LGK |
cd24051 |
nucleotide-binding domain (NBD) of levoglucosan kinase (LGK) and similar proteins; LGK (EC 2.7. ... |
51-120 |
9.58e-03 |
|
nucleotide-binding domain (NBD) of levoglucosan kinase (LGK) and similar proteins; LGK (EC 2.7.1.232) catalyzes the transfer of a phosphate group from ATP to levoglucosan (1,6-anhydro-beta-D-glucopyranose, LG) to yield glucose 6-phosphate in the presence of magnesium ion and ATP. In addition to the canonical kinase phosphotransfer reaction, the conversion requires cleavage of the 1,6-anhydro ring to allow ATP-dependent phosphorylation of the sugar O-6 atom.
Pssm-ID: 466901 Cd Length: 409 Bit Score: 38.30 E-value: 9.58e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128765 51 KTAG---FTLPLLQHLItRQPHAKGRRPvRALILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMM 120
Cdd:cd24051 252 KTTGrevFRDTLAHDLI-RRAEAKGLSP-DDIVATTTRITAQSIVDHYRRYAPSQEIDEIFMCGGGAFNPNIV 322
|
|
| |
