|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
1-429 |
0e+00 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 576.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 1 MLFQDLNLDPSIIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLtkdsmNYEEYNQIKALV 80
Cdd:COG0513 2 MSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRL-----DPSRPRAPQALI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 81 LAPTRELAIQIGESFNTYGQHLDIETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEADR 160
Cdd:COG0513 77 LAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 161 MLDLGMIRDVKNIISKLPKVRQNLLFSATMPQEVSKLVHSILRNPVKIEVKSKPSNKLQIKQQVYYVDEPDKTSLLLHLL 240
Cdd:COG0513 157 MLDMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 241 KDKAFESVLVFARTKKKADIVSKAINIENIRSKAIHGDKNQSERQKALERFKNKEIRVLVATDVAARGIDIEKLSHVVNM 320
Cdd:COG0513 237 RDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 321 DIPNVPETYIHRIGRTGRAGMGGTAISFCSNQEIAFLKDVEKLQGKKIEVVQNHPYVLmniaIKQNREKYsEKPELKGNK 400
Cdd:COG0513 317 DLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEP----VEEKRLER-LKPKIKEKL 391
|
410 420
....*....|....*....|....*....
gi 1308681313 401 KTSSEKPNHKKDNDRKSNSKNNNFTKRKE 429
Cdd:COG0513 392 KGKKAGRGGRPGPKGERKARRGKRRRRKR 420
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
1-368 |
7.70e-140 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 408.04 E-value: 7.70e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 1 MLFQDLNLDPSIIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLTKDSMNYEEYNQIKALV 80
Cdd:PRK10590 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVRALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 81 LAPTRELAIQIGESFNTYGQHLDIETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEADR 160
Cdd:PRK10590 81 LTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 161 MLDLGMIRDVKNIISKLPKVRQNLLFSATMPQEVSKLVHSILRNPVKIEVKSKPSNKLQIKQQVYYVDEPDKTSLLLHLL 240
Cdd:PRK10590 161 MLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 241 KDKAFESVLVFARTKKKADIVSKAINIENIRSKAIHGDKNQSERQKALERFKNKEIRVLVATDVAARGIDIEKLSHVVNM 320
Cdd:PRK10590 241 GKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNY 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1308681313 321 DIPNVPETYIHRIGRTGRAGMGGTAISFCSNQEIAFLKDVEKLQGKKI 368
Cdd:PRK10590 321 ELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEI 368
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
3-369 |
4.22e-117 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 349.87 E-value: 4.22e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 3 FQDLNLDPSIIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLtkDSMNYeeynQIKALVLA 82
Cdd:PRK11776 6 FSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL--DVKRF----RVQALVLC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 83 PTRELAIQIGESFNTYGQHLD-IETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEADRM 161
Cdd:PRK11776 80 PTRELADQVAKEIRRLARFIPnIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 162 LDLGMIRDVKNIISKLPKVRQNLLFSATMPQEVSKLVHSILRNPVKIEVKSKPSNkLQIKQQVYYVDEPDKTSLLLHLLK 241
Cdd:PRK11776 160 LDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDL-PAIEQRFYEVSPDERLPALQRLLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 242 DKAFESVLVFARTKKKADIVSKAINIENIRSKAIHGDKNQSERQKALERFKNKEIRVLVATDVAARGIDIEKLSHVVNMD 321
Cdd:PRK11776 239 HHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYE 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1308681313 322 IPNVPETYIHRIGRTGRAGMGGTAISFCSNQEIAFLKDVEKLQGKKIE 369
Cdd:PRK11776 319 LARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLN 366
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
1-436 |
2.05e-112 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 336.91 E-value: 2.05e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 1 MLFQDLNLDPSIIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLT----KDSmnyeeyNQI 76
Cdd:PRK11192 1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLdfprRKS------GPP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 77 KALVLAPTRELAIQIGESFNTYGQHLDIETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLEQGYVDLNNIEVFVLD 156
Cdd:PRK11192 75 RILILTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 157 EADRMLDLGMIRDVKNIISKLPKVRQNLLFSATMPQE-VSKLVHSILRNPVKIEVKSKPSNKLQIKQQVYYVDEPD-KTS 234
Cdd:PRK11192 155 EADRMLDMGFAQDIETIAAETRWRKQTLLFSATLEGDaVQDFAERLLNDPVEVEAEPSRRERKKIHQWYYRADDLEhKTA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 235 LLLHLLKDKAFESVLVFARTKKKADIVSKAINIENIRSKAIHGDKNQSERQKALERFKNKEIRVLVATDVAARGIDIEKL 314
Cdd:PRK11192 235 LLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 315 SHVVNMDIPNVPETYIHRIGRTGRAGMGGTAISFCSNQEIAFLKDVEKLQGKKIEvvqnhPYVlmniaIKQNREKYSEKP 394
Cdd:PRK11192 315 SHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLK-----ARV-----IDELRPKTKAPS 384
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1308681313 395 ElkGNKKTSSEKPNHKKDNDRKSNSKNNNFTKRKEKVTNKKK 436
Cdd:PRK11192 385 E--KKTGKPSKKVLAKRAEKKEKEKEKPKVKKRHRDTKNIGK 424
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
3-362 |
6.40e-106 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 326.81 E-value: 6.40e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 3 FQDLNLDPSIIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLTKDsmnyeeynqIKA---L 79
Cdd:PRK11634 8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPE---------LKApqiL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 80 VLAPTRELAIQIGESFNTYGQHL-DIETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEA 158
Cdd:PRK11634 79 VLAPTRELAVQVAEAMTDFSKHMrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 159 DRMLDLGMIRDVKNIISKLPKVRQNLLFSATMPQEVSKLVHSILRNPVKIEVKSKPSNKLQIKQQVYYVDEPDKTSLLLH 238
Cdd:PRK11634 159 DEMLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 239 LLKDKAFESVLVFARTKKKADIVSKAINIENIRSKAIHGDKNQSERQKALERFKNKEIRVLVATDVAARGIDIEKLSHVV 318
Cdd:PRK11634 239 FLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVV 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1308681313 319 NMDIPNVPETYIHRIGRTGRAGMGGTAISFCSNQEIAFLKDVEK 362
Cdd:PRK11634 319 NYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIER 362
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
3-369 |
2.63e-102 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 312.62 E-value: 2.63e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 3 FQDLNLDPSIIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLTKDSMNYEEY-NQIKALVL 81
Cdd:PRK01297 89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKERYmGEPRALII 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 82 APTRELAIQIGESFNTYGQHLDIETGVIFGGITPKRHIKVLK-RDPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEADR 160
Cdd:PRK01297 169 APTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEADR 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 161 MLDLGMIRDVKNIISKLPKV--RQNLLFSATMPQEVSKLVHSILRNPVKIEVKSKPSNKLQIKQQVYYVDEPDKTSLLLH 238
Cdd:PRK01297 249 MLDMGFIPQVRQIIRQTPRKeeRQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDKYKLLYN 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 239 LLKDKAFESVLVFARTKKKADIVSKAINIENIRSKAIHGDKNQSERQKALERFKNKEIRVLVATDVAARGIDIEKLSHVV 318
Cdd:PRK01297 329 LVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVI 408
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1308681313 319 NMDIPNVPETYIHRIGRTGRAGMGGTAISFCSNQEIAFLKDVEKLQGKKIE 369
Cdd:PRK01297 409 NFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKIS 459
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
3-348 |
6.44e-102 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 309.98 E-value: 6.44e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 3 FQDLNLDPSIIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKL-TKDSMNYEEYNQIKALVL 81
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLlSHPAPEDRKVNQPRALIM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 82 APTRELAIQIGESFNTYGQHLDIETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEADRM 161
Cdd:PRK04837 90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 162 LDLGMIRDVKNIISKLP--KVRQNLLFSATMPQEVSKLVHSILRNPVKIEVKSKPSNKLQIKQQVYYVDEPDKTSLLLHL 239
Cdd:PRK04837 170 FDLGFIKDIRWLFRRMPpaNQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYPSNEEKMRLLQTL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 240 LKDKAFESVLVFARTKKKADIVSKAINIENIRSKAIHGDKNQSERQKALERFKNKEIRVLVATDVAARGIDIEKLSHVVN 319
Cdd:PRK04837 250 IEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFN 329
|
330 340
....*....|....*....|....*....
gi 1308681313 320 MDIPNVPETYIHRIGRTGRAGMGGTAISF 348
Cdd:PRK04837 330 YDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
12-209 |
3.31e-99 |
|
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350669 [Multi-domain] Cd Length: 196 Bit Score: 294.73 E-value: 3.31e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 12 IIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLTKDSMNyeEYNQIKALVLAPTRELAIQI 91
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKK--KGRGPQALVLAPTRELAMQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 92 GESFNTYGQHLDIETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEADRMLDLGMIRDVK 171
Cdd:cd00268 79 AEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVE 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 1308681313 172 NIISKLPKVRQNLLFSATMPQEVSKLVHSILRNPVKIE 209
Cdd:cd00268 159 KILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
12-348 |
8.82e-95 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 295.53 E-value: 8.82e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 12 IIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIP-ILQKLTKDSMNYEEyNQIkALVLAPTRELAIQ 90
Cdd:PTZ00110 141 ILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPaIVHINAQPLLRYGD-GPI-VLVLAPTRELAEQ 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 91 IGESFNTYGQHLDIETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEADRMLDLGMIRDV 170
Cdd:PTZ00110 219 IREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQI 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 171 KNIISKLPKVRQNLLFSATMPQEVSKLVHSILRN-PVKIEVKSKPSNKLQ-IKQQVYYVDEPDKTSLLLHLLKdKAFES- 247
Cdd:PTZ00110 299 RKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDLTACHnIKQEVFVVEEHEKRGKLKMLLQ-RIMRDg 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 248 --VLVFARTKKKADIVSKAINIENIRSKAIHGDKNQSERQKALERFKNKEIRVLVATDVAARGIDIEKLSHVVNMDIPNV 325
Cdd:PTZ00110 378 dkILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQ 457
|
330 340
....*....|....*....|...
gi 1308681313 326 PETYIHRIGRTGRAGMGGTAISF 348
Cdd:PTZ00110 458 IEDYVHRIGRTGRAGAKGASYTF 480
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
3-370 |
1.06e-86 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 275.29 E-value: 1.06e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 3 FQDLNLDPSIIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKL-TKDSMNYEEYNQIKALVL 81
Cdd:PRK04537 11 FSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlSRPALADRKPEDPRALIL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 82 APTRELAIQIGESFNTYGQHLDIETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLEQ-GYVDLNNIEVFVLDEADR 160
Cdd:PRK04537 91 APTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQhKVVSLHACEICVLDEADR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 161 MLDLGMIRDVKNIISKLPK--VRQNLLFSATMPQEVSKLVHSILRNPVKIEVKSKPSNKLQIKQQVYYVDEPDKTSLLLH 238
Cdd:PRK04537 171 MFDLGFIKDIRFLLRRMPErgTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADEEKQTLLLG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 239 LLKDKAFESVLVFARTKKKADIVSKAINIENIRSKAIHGDKNQSERQKALERFKNKEIRVLVATDVAARGIDIEKLSHVV 318
Cdd:PRK04537 251 LLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVY 330
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1308681313 319 NMDIPNVPETYIHRIGRTGRAGMGGTAISFCSNQEIAFLKDVEKLQGKKIEV 370
Cdd:PRK04537 331 NYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKIPV 382
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
3-369 |
1.19e-84 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 264.77 E-value: 1.19e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 3 FQDLNLDPSIIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLTKDsmnyeeYNQIKALVLA 82
Cdd:PTZ00424 30 FDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYD------LNACQALILA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 83 PTRELAIQIGESFNTYGQHLDIETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEADRML 162
Cdd:PTZ00424 104 PTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEML 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 163 DLGMIRDVKNIISKLPKVRQNLLFSATMPQEVSKLVHSILRNPVKIEVKSKPSNKLQIKQQVYYVDEPD-KTSLLLHLLK 241
Cdd:PTZ00424 184 SRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEwKFDTLCDLYE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 242 DKAFESVLVFARTKKKADIVSKAINIENIRSKAIHGDKNQSERQKALERFKNKEIRVLVATDVAARGIDIEKLSHVVNMD 321
Cdd:PTZ00424 264 TLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYD 343
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1308681313 322 IPNVPETYIHRIGRTGRAGMGGTAISFCSNQEIAFLKDVEKLQGKKIE 369
Cdd:PTZ00424 344 LPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIE 391
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
1-359 |
8.82e-75 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 242.77 E-value: 8.82e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 1 MLFQDLNLDPSIIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLTK-DSMNYEEYNQIKAL 79
Cdd:PLN00206 121 LSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTiRSGHPSEQRNPLAM 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 80 VLAPTRELAIQIGESFNTYGQHLDIETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEAD 159
Cdd:PLN00206 201 VLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVD 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 160 RMLDLGMIRDVKNIISKLPKvRQNLLFSATMPQEVSKLVHSILRNPVKIEVKSKPSNKLQIKQQVYYVDEPDKTSLLLHL 239
Cdd:PLN00206 281 CMLERGFRDQVMQIFQALSQ-PQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQKLFDI 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 240 LKDKAF--ESVLVFARTKKKADIVSKAINI-ENIRSKAIHGDKNQSERQKALERFKNKEIRVLVATDVAARGIDIEKLSH 316
Cdd:PLN00206 360 LKSKQHfkPPAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQ 439
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1308681313 317 VVNMDIPNVPETYIHRIGRTGRAGMGGTAISFCSNQEIAFLKD 359
Cdd:PLN00206 440 VIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPE 482
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
3-209 |
9.05e-75 |
|
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: 232.50 E-value: 9.05e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 3 FQDLNLDPSIIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLTKDSMNyeeynqIKALVLA 82
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYG------IFALVLT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 83 PTRELAIQIGESFNTYGQHLDIETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLE---QGYVDLNNIEVFVLDEAD 159
Cdd:cd17955 75 PTRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEAD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1308681313 160 RMLDLGMIRDVKNIISKLPKVRQNLLFSATMPQEVSKLVHSILRNPVKIE 209
Cdd:cd17955 155 RLLTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFFWE 204
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
3-204 |
3.51e-74 |
|
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: 231.61 E-value: 3.51e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 3 FQDLNLDPSIIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLTKD----SMNYEEYNQIKA 78
Cdd:cd17967 2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDgppsVGRGRRKAYPSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 79 LVLAPTRELAIQIGE-----SFNTYgqhldIETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLEQGYVDLNNIEVF 153
Cdd:cd17967 82 LILAPTRELAIQIYEearkfSYRSG-----VRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1308681313 154 VLDEADRMLDLGMIRDVKNII--SKLPKV--RQNLLFSATMPQEVSKLVHSILRN 204
Cdd:cd17967 157 VLDEADRMLDMGFEPQIRKIVehPDMPPKgeRQTLMFSATFPREIQRLAADFLKN 211
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
3-209 |
7.26e-74 |
|
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: 229.90 E-value: 7.26e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 3 FQDLNLDPSIIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLTKDSMNYeeynqiKALVLA 82
Cdd:cd17954 2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRF------FALVLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 83 PTRELAIQIGESFNTYGQHLDIETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLEQ--GYvDLNNIEVFVLDEADR 160
Cdd:cd17954 76 PTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENtkGF-SLKSLKFLVMDEADR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1308681313 161 MLDLGMIRDVKNIISKLPKVRQNLLFSATMPQEVSKLVHSILRNPVKIE 209
Cdd:cd17954 155 LLNMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKIE 203
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
12-208 |
2.92e-72 |
|
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: 225.60 E-value: 2.92e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 12 IIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKL-TKDSMnyeeYNQIKALVLAPTRELAIQ 90
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLlYRPKK----KAATRVLVLVPTRELAMQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 91 IGESFNTYGQHLDIETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLEQGY-VDLNNIEVFVLDEADRMLDLGMIRD 169
Cdd:cd17947 77 CFSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGFADE 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 1308681313 170 VKNIISKLPKVRQNLLFSATMPQEVSKLVHSILRNPVKI 208
Cdd:cd17947 157 LKEILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
1-203 |
1.43e-67 |
|
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: 215.99 E-value: 1.43e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 1 MLFQDLNLDPSIIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLTKDSMNYEEYNQIK--- 77
Cdd:cd18052 43 LTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEGLTASSFSEVQepq 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 78 ALVLAPTRELAIQIGESFNTYGQHLDIETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLEQGYVDLNNIEVFVLDE 157
Cdd:cd18052 123 ALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1308681313 158 ADRMLDLGMIRDVKNIISKL---PK-VRQNLLFSATMPQEVSKLVHSILR 203
Cdd:cd18052 203 ADRMLDMGFGPEIRKLVSEPgmpSKeDRQTLMFSATFPEEIQRLAAEFLK 252
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
3-208 |
2.51e-65 |
|
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: 208.31 E-value: 2.51e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 3 FQDLNLDPSIIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLTKDSMNyeeyNQIKALVLA 82
Cdd:cd17959 3 FQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPT----VGARALILS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 83 PTRELAIQIGESFNTYGQHLDIETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEADRML 162
Cdd:cd17959 79 PTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1308681313 163 DLGMIRDVKNIISKLPKVRQNLLFSATMPQEVSKLVHSILRNPVKI 208
Cdd:cd17959 159 EMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
8-203 |
2.25e-63 |
|
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350722 [Multi-domain] Cd Length: 211 Bit Score: 203.20 E-value: 2.25e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 8 LDPSIIRAIEDQKYKNPTPIQEKAIPSILR-GKDLLGCAQTGTGKTAAFAIPILQKLTKDSMNYEEyNQIKALVLAPTRE 86
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRR-SGVSALIISPTRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 87 LAIQIGESFNTYGQHL-DIETGVIFGGITPKRHIKVLKRD-PNILVATPGRLLDLLEQGYV--DLNNIEVFVLDEADRML 162
Cdd:cd17964 80 LALQIAAEAKKLLQGLrKLRVQSAVGGTSRRAELNRLRRGrPDILVATPGRLIDHLENPGVakAFTDLDYLVLDEADRLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1308681313 163 DLGMIRDVKNIISKLPKV----RQNLLFSATMPQEVSKLVHSILR 203
Cdd:cd17964 160 DMGFRPDLEQILRHLPEKnadpRQTLLFSATVPDEVQQIARLTLK 204
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
12-208 |
3.60e-62 |
|
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: 199.72 E-value: 3.60e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 12 IIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLTKDSMNYEEyNQIKALVLAPTRELAIQI 91
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKK-GQVGALIISPTRELATQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 92 GE---SFNTYgQHLDIETGVIFGGITPKRHIKVLKRD-PNILVATPGRLLDLLE--QGYVDLNNIEVFVLDEADRMLDLG 165
Cdd:cd17960 80 YEvlqSFLEH-HLPKLKCQLLIGGTNVEEDVKKFKRNgPNILVGTPGRLEELLSrkADKVKVKSLEVLVLDEADRLLDLG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1308681313 166 MIRDVKNIISKLPKVRQNLLFSATMPQEVSKLVHSILRNPVKI 208
Cdd:cd17960 159 FEADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
12-210 |
3.73e-62 |
|
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: 199.74 E-value: 3.73e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 12 IIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLTKDSMNYEeynqIKALVLAPTRELAIQI 91
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKKG----LRALILAPTRELASQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 92 GESFNTYGQHLDIETGVIFGGITPK-RHIKVLKRDPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEADRMLDLGMIRDV 170
Cdd:cd17957 77 YRELLKLSKGTGLRIVLLSKSLEAKaKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQT 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1308681313 171 KNIISKL--PKVRQnLLFSATMPQEVSKLVHSILRNPVKIEV 210
Cdd:cd17957 157 DEILAACtnPNLQR-SLFSATIPSEVEELARSVMKDPIRIIV 197
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
25-197 |
5.33e-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: 198.24 E-value: 5.33e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 25 TPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLTKdsmnyeEYNQIKALVLAPTRELAIQIGESFNTYGQHLDI 104
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDK------LDNGPQALVLAPTRELAEQIYEELKKLGKGLGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 105 ETGVIFGGITPKRHIKVLKRdPNILVATPGRLLDLLEQgYVDLNNIEVFVLDEADRMLDLGMIRDVKNIISKLPKVRQNL 184
Cdd:pfam00270 75 KVASLLGGDSRKEQLEKLKG-PDILVGTPGRLLDLLQE-RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQIL 152
|
170
....*....|...
gi 1308681313 185 LFSATMPQEVSKL 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 |
2.37e-61 |
|
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and PRP28 homolog) is involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation. Diseases associated with DDX23 include distal hereditary motor neuropathy, type II. DDX23 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350703 [Multi-domain] Cd Length: 220 Bit Score: 198.31 E-value: 2.37e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 12 IIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLTK-DSMNYEEYNQI-KALVLAPTRELAI 89
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRlPPLDEETKDDGpYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 90 QIGESFNTYGQHLDIETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEADRMLDLGMIRD 169
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1308681313 170 VKNIISKLP--------------------KVRQNLLFSATMPQEVSKLVHSILRNPVKI 208
Cdd:cd17945 161 VTKILDAMPvsnkkpdteeaeklaasgkhRYRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
14-210 |
4.14e-61 |
|
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: 197.13 E-value: 4.14e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 14 RAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLTKDsmNYEEYNQIKALVLAPTRELAIQIGE 93
Cdd:cd17941 3 KGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRE--RWTPEDGLGALIISPTRELAMQIFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 94 SFNTYGQHLDIETGVIFGGITPKRHIKVLKRdPNILVATPGRLLDLLEQG-YVDLNNIEVFVLDEADRMLDLGMIRDVKN 172
Cdd:cd17941 81 VLRKVGKYHSFSAGLIIGGKDVKEEKERINR-MNILVCTPGRLLQHMDETpGFDTSNLQMLVLDEADRILDMGFKETLDA 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1308681313 173 IISKLPKVRQNLLFSATMPQEVSKLVHSILRNPVKIEV 210
Cdd:cd17941 160 IVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
3-208 |
2.19e-60 |
|
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: 195.21 E-value: 2.19e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 3 FQDLNLDPSIIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLtkdsmnYEEYNQIKALVLA 82
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKI------DPKKDVIQALILV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 83 PTRELAIQIGESFNTYGQHLDIETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEADRML 162
Cdd:cd17940 75 PTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1308681313 163 DLGMIRDVKNIISKLPKVRQNLLFSATMPQEVSKLVHSILRNPVKI 208
Cdd:cd17940 155 SQDFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
5-208 |
1.08e-58 |
|
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: 190.61 E-value: 1.08e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 5 DLNLDPSIIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLTKDsmnyeeYNQIKALVLAPT 84
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTT------VRETQALVLAPT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 85 RELAIQIGESFNTYGQHLDIETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEADRMLDL 164
Cdd:cd17939 75 RELAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1308681313 165 GMIRDVKNIISKLPKVRQNLLFSATMPQEVSKLVHSILRNPVKI 208
Cdd:cd17939 155 GFKDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
8-206 |
1.90e-58 |
|
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: 190.49 E-value: 1.90e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 8 LDPSIIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLTKDSMNYEEYNQIKALVLAPTREL 87
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGEEQGTRALILVPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 88 AIQIGESFNTYGQHL--DIETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLEQGY-VDLNNIEVFVLDEADRMLDL 164
Cdd:cd17961 81 AQQVSKVLEQLTAYCrkDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSlLLLSTLKYLVIDEADLVLSY 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1308681313 165 GMIRDVKNIISKLPKVRQNLLFSATMPQEVSKLVHSILRNPV 206
Cdd:cd17961 161 GYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
3-204 |
2.63e-58 |
|
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: 191.41 E-value: 2.63e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 3 FQDLNLDPSIIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLTKD------SMNYEEYNQI 76
Cdd:cd18051 23 FSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQgpgeslPSESGYYGRR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 77 K----ALVLAPTRELAIQIGESFNTYGQHLDIETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLEQGYVDLNNIEV 152
Cdd:cd18051 103 KqyplALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYCKY 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1308681313 153 FVLDEADRMLDLGMIRDVKNIISK--LPK--VRQNLLFSATMPQEVSKLVHSILRN 204
Cdd:cd18051 183 LVLDEADRMLDMGFEPQIRRIVEQdtMPPtgERQTLMFSATFPKEIQMLARDFLDN 238
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
220-349 |
6.57e-58 |
|
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: 186.17 E-value: 6.57e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 220 IKQQVYYVDEPDKTSLLL-HLLKDKAFESVLVFARTKKKADIVSKAINIENIRSKAIHGDKNQSERQKALERFKNKEIRV 298
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLlLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1308681313 299 LVATDVAARGIDIEKLSHVVNMDIPNVPETYIHRIGRTGRAGMGGTAISFC 349
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
3-210 |
2.07e-57 |
|
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: 187.94 E-value: 2.07e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 3 FQDLNLDPSIIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLTKDSmnyeeyNQIKALVLA 82
Cdd:cd17950 4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVD------GQVSVLVIC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 83 PTRELAIQIGESFNTYGQHL-DIETGVIFGGITPKRHIKVLKRD-PNILVATPGRLLDLLEQGYVDLNNIEVFVLDEADR 160
Cdd:cd17950 78 HTRELAFQISNEYERFSKYMpNVKTAVFFGGVPIKKDIEVLKNKcPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1308681313 161 ML-DLGMIRDVKNIISKLPKVRQNLLFSATMPQEVSKLVHSILRNPVKIEV 210
Cdd:cd17950 158 MLeQLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
12-208 |
6.51e-57 |
|
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: 186.04 E-value: 6.51e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 12 IIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLTKDSMNYEEYNQIkALVLAPTRELAIQI 91
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGDGPI-VLVLAPTRELAQQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 92 GESFNTYGQHLDIETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEADRMLDLGMIRDVK 171
Cdd:cd17966 80 QQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 1308681313 172 NIISKLPKVRQNLLFSATMPQEVSKLVHSILRNPVKI 208
Cdd:cd17966 160 KIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
3-208 |
9.78e-56 |
|
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: 183.42 E-value: 9.78e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 3 FQDLNLDPSIIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLTKdsmnyeEYNQIKALVLA 82
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDT------SLKATQALVLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 83 PTRELAIQIGESFNTYGQHLDIETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEADRML 162
Cdd:cd18046 75 PTRELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEML 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1308681313 163 DLGMIRDVKNIISKLPKVRQNLLFSATMPQEVSKLVHSILRNPVKI 208
Cdd:cd18046 155 SRGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
3-206 |
6.52e-55 |
|
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: 180.98 E-value: 6.52e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 3 FQDLNLDPSIIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQkltkdsmnyeeynQIKALVLA 82
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQ-------------IVVALILE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 83 PTRELAIQIGESFNTYGQHLD---IETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEAD 159
Cdd:cd17938 68 PSRELAEQTYNCIENFKKYLDnpkLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEAD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1308681313 160 RMLDLGMIRDVKNIISKLPKVR------QNLLFSATMPQ-EVSKLVHSILRNPV 206
Cdd:cd17938 148 RLLSQGNLETINRIYNRIPKITsdgkrlQVIVCSATLHSfEVKKLADKIMHFPT 201
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
16-221 |
1.71e-54 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 180.00 E-value: 1.71e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 16 IEDQKYKNPTPIQEKAIPSILRG-KDLLGCAQTGTGKTAAFAIPILQKLTKDsmnyeeyNQIKALVLAPTRELAIQIGES 94
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRG-------KGGRVLVLVPTRELAEQWAEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 95 FNTYGQHLDIETGVIFGGITPKRHIKVLKR-DPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEADRMLDLGMIRDVKNI 173
Cdd:smart00487 74 LKKLGPSLGLKVVGLYGGDSKREQLRKLESgKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1308681313 174 ISKLPKVRQNLLFSATMPQEVSKLVHSILRNPVKIEVKSKPSNKLQIK 221
Cdd:smart00487 154 LKLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFTPLEPIEQF 201
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
12-222 |
5.16e-54 |
|
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box protein, which shows little similarity to any of the other known human DEAD box proteins, but shows a high similarity to mouse Ddx24 at the amino acid level. MDM2 mediates nonproteolytic polyubiquitylation of the DEAD-Box RNA helicase DDX24. DDX24 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.
Pssm-ID: 350704 [Multi-domain] Cd Length: 235 Bit Score: 179.74 E-value: 5.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 12 IIRAIEDQKYKNPTPIQEKAIPSILR-GKDLLGCAQTGTGKTAAFAIPILQKL---TKDSMNYEEYNQIKALVLAPTREL 87
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLlsqKSSNGVGGKQKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 88 AIQIGESFNTYGQHLDIETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLEQGYVDLNN---IEVFVLDEADRMLDL 164
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLANlksLRFLVLDEADRMLEK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1308681313 165 GMIRDVKNIISKLPKV-------RQNLLFSATMpqevsKLVHSiLRNPVKIEVKSKPSNKLQIKQ 222
Cdd:cd17946 161 GHFAELEKILELLNKDragkkrkRQTFVFSATL-----TLDHQ-LPLKLNSKKKKKKKEKKQKLE 219
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
12-208 |
1.38e-52 |
|
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: 174.91 E-value: 1.38e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 12 IIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLTkDSMNYEEYNQIKALVLAPTRELAIQI 91
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIM-DQRELEKGEGPIAVIVAPTRELAQQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 92 GESFNTYGQHLDIETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEADRMLDLGMIRDVK 171
Cdd:cd17952 80 YLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 1308681313 172 NIISKLPKVRQNLLFSATMPQEVSKLVHSILRNPVKI 208
Cdd:cd17952 160 SIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
8-208 |
4.13e-49 |
|
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: 166.78 E-value: 4.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 8 LDPSIIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLtKDSMNYEEYNQIKALVLAPTREL 87
Cdd:cd17953 19 LSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHI-KDQRPVKPGEGPIGLIMAPTREL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 88 AIQIGESFNTYGQHLDIETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLL--EQGYV-DLNNIEVFVLDEADRMLDL 164
Cdd:cd17953 98 ALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtaNNGRVtNLRRVTYVVLDEADRMFDM 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1308681313 165 GMIRDVKNIISKLPKVRQNLLFSATMPQEVSKLVHSILRNPVKI 208
Cdd:cd17953 178 GFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
12-209 |
6.88e-49 |
|
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: 165.13 E-value: 6.88e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 12 IIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLTKdsmnyeEYNQIKALVLAPTRELAIQI 91
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDL------ERRHPQVLILAPTREIAVQI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 92 GESFNTYGQHL-DIETGVIFGGITPKRHIKVLKRdPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEADRMLDLGMIRDV 170
Cdd:cd17943 75 HDVFKKIGKKLeGLKCEVFIGGTPVKEDKKKLKG-CHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDV 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 1308681313 171 KNIISKLPKVRQNLLFSATMPQEVSKLVHSILRNPVKIE 209
Cdd:cd17943 154 NWIFSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
12-214 |
7.54e-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: 162.53 E-value: 7.54e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 12 IIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLTKdsMNYEEYNQIKALVLAPTRELAIQI 91
Cdd:cd17942 1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYK--LKFKPRNGTGVIIISPTRELALQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 92 gesfntYGQHLDIET------GVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLE--QGYVdLNNIEVFVLDEADRMLD 163
Cdd:cd17942 79 ------YGVAKELLKyhsqtfGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQntKGFL-YKNLQCLIIDEADRILE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1308681313 164 LGMIRDVKNIISKLPKVRQNLLFSATMPQEVSKLvhsilrnpVKIEVKSKP 214
Cdd:cd17942 152 IGFEEEMRQIIKLLPKRRQTMLFSATQTRKVEDL--------ARISLKKKP 194
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
8-208 |
1.90e-47 |
|
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: 161.20 E-value: 1.90e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 8 LDPSIIRAIEDQKYKNPTPIQEKAIPSILRG--KDLLGCAQTGTGKTAAFAIPILQKLTkdsmnyEEYNQIKALVLAPTR 85
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVD------PTLKSPQALCLAPTR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 86 ELAIQIGESFNTYGQHLDIETGVIFGGITPKRHIKVlkrDPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEADRMLDL- 164
Cdd:cd17963 75 ELARQIGEVVEKMGKFTGVKVALAVPGNDVPRGKKI---TAQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTq 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1308681313 165 GMIRDVKNIISKLPKVRQNLLFSATMPQEVSKLVHSILRNPVKI 208
Cdd:cd17963 152 GHGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
12-208 |
4.19e-47 |
|
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: 160.97 E-value: 4.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 12 IIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIP-ILQKLTKD-SMNYEEYNQIKALVLAPTRELAI 89
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPlIMFALEQEkKLPFIKGEGPYGLIVCPSRELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 90 QIGESFNTYGQHLD------IETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEADRMLD 163
Cdd:cd17951 81 QTHEVIEYYCKALQeggypqLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1308681313 164 LGMIRDVKNIISKLPKVRQNLLFSATMPQEVSKLVHSILRNPVKI 208
Cdd:cd17951 161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
3-210 |
1.41e-46 |
|
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: 160.56 E-value: 1.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 3 FQDLNLDPSIIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLTKDSMnYEEYNQIKALVLA 82
Cdd:cd18049 26 FYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPF-LERGDGPICLVLA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 83 PTRELAIQIGESFNTYGQHLDIETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEADRML 162
Cdd:cd18049 105 PTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRML 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1308681313 163 DLGMIRDVKNIISKLPKVRQNLLFSATMPQEVSKLVHSILRNPVKIEV 210
Cdd:cd18049 185 DMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINI 232
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
20-208 |
3.72e-46 |
|
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: 158.52 E-value: 3.72e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 20 KYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLTKDSMNYEEYNQIKALVLAPTRELAIQIGESFNTYG 99
Cdd:cd17949 10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDRSDGTLALVLVPTRELALQIYEVLEKLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 100 Q-HLDIETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLEQGYV-DLNNIEVFVLDEADRMLDLGMIRDVKNIISKL 177
Cdd:cd17949 90 KpFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQSfDVSNLRWLVLDEADRLLDMGFEKDITKILELL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1308681313 178 -------------PKVRQNLLFSATMPQEVSKLVHSILRNPVKI 208
Cdd:cd17949 170 ddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
16-208 |
7.62e-46 |
|
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: 157.33 E-value: 7.62e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 16 IEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLTkdsmnyEEYNQIKALVLAPTRELAIQIGESF 95
Cdd:cd17962 5 LKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCL------TEHRNPSALILTPTRELAVQIEDQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 96 NTYGQHL-DIETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEADRMLDLGMIRDVKNII 174
Cdd:cd17962 79 KELMKGLpPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDIL 158
|
170 180 190
....*....|....*....|....*....|....
gi 1308681313 175 SKLPKVRQNLLFSATMPQEVSKLVHSILRNPVKI 208
Cdd:cd17962 159 ENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
12-208 |
9.11e-46 |
|
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: 157.24 E-value: 9.11e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 12 IIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLTKDSMNYEEYNQIKALVLAPTRELAIQI 91
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPREQRNGPGVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 92 GESFNTYgQHLDIETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEADRMLDLGMIRDVK 171
Cdd:cd17958 81 EAECSKY-SYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 1308681313 172 NIISKLPKVRQNLLFSATMPQEVSKLVHSILRNPVKI 208
Cdd:cd17958 160 KILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
3-210 |
9.91e-46 |
|
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: 159.41 E-value: 9.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 3 FQDLNLDPSIIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLtkdsmNYEEY----NQIKA 78
Cdd:cd18050 64 FHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHI-----NHQPYlergDGPIC 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 79 LVLAPTRELAIQIGESFNTYGQHLDIETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEA 158
Cdd:cd18050 139 LVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEA 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1308681313 159 DRMLDLGMIRDVKNIISKLPKVRQNLLFSATMPQEVSKLVHSILRNPVKIEV 210
Cdd:cd18050 219 DRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINI 270
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
3-208 |
1.16e-39 |
|
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: 141.07 E-value: 1.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 3 FQDLNLDPSIIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLtkdSMNYEEynqIKALVLA 82
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCL---DIQVRE---TQALILS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 83 PTRELAIQIGESFNTYGQHLDIETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEADRML 162
Cdd:cd18045 75 PTRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEML 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1308681313 163 DLGMIRDVKNIISKLPKVRQNLLFSATMPQEVSKLVHSILRNPVKI 208
Cdd:cd18045 155 NKGFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
12-201 |
2.84e-38 |
|
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: 138.27 E-value: 2.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 12 IIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLTKDSMNYE-EYNQIKALVLAPTRELAIQ 90
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEgPFNAPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 91 IGESFNTYGQHLDIETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEADRMLD---LGMI 167
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDdsfNEKL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1308681313 168 RDV----------KNIISKLPKVRQNLLFSATMPQEVSKLVHSI 201
Cdd:cd17948 161 SHFlrrfplasrrSENTDGLDPGTQLVLVSATMPSGVGEVLSKV 204
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
26-203 |
2.73e-36 |
|
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: 132.28 E-value: 2.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 26 PIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLTKDSMNYEEYNQIKALVLAPTRELAIQIGESFNTYGQHLDIe 105
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRGRAPKVLVLAPTRELANQVTKDFKDITRKLSV- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 106 tGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEADRMLDLGMIRDVKNIISKLPKVR---- 181
Cdd:cd17944 94 -ACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSVSYKKDsedn 172
|
170 180
....*....|....*....|...
gi 1308681313 182 -QNLLFSATMPQEVSKLVHSILR 203
Cdd:cd17944 173 pQTLLFSATCPDWVYNVAKKYMK 195
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
12-205 |
5.06e-36 |
|
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: 132.37 E-value: 5.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 12 IIRAIEDQKYKNPTPIQEKAIPSIL---------RGKDLLGCAQTGTGKTAAFAIPILQKLTKDSMnyeeyNQIKALVLA 82
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLpsskstppyRPGDLCVSAPTGSGKTLAYVLPIVQALSKRVV-----PRLRALIVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 83 PTRELAIQIGESFNTYGQHLDIETGVIFG---------GITPKRHIKVLKRdPNILVATPGRLLDLLEQG-YVDLNNIEV 152
Cdd:cd17956 76 PTKELVQQVYKVFESLCKGTGLKVVSLSGqksfkkeqkLLLVDTSGRYLSR-VDILVATPGRLVDHLNSTpGFTLKHLRF 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1308681313 153 FVLDEADRMLD---------------------LGMIRDVKNIISKLPKVrQNLLFSATMPQEVSKLVHSILRNP 205
Cdd:cd17956 155 LVIDEADRLLNqsfqdwletvmkalgrptapdLGSFGDANLLERSVRPL-QKLLFSATLTRDPEKLSSLKLHRP 227
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
231-340 |
2.28e-35 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 126.56 E-value: 2.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 231 DKTSLLLHLLKDKAFESVLVFARTKKKADIvSKAINIENIRSKAIHGDKNQSERQKALERFKNKEIRVLVATDVAARGID 310
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 1308681313 311 IEKLSHVVNMDIPNVPETYIHRIGRTGRAG 340
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
259-340 |
3.78e-28 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 106.14 E-value: 3.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 259 DIVSKAINIENIRSKAIHGDKNQSERQKALERFKNKEIRVLVATDVAARGIDIEKLSHVVNMDIPNVPETYIHRIGRTGR 338
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 1308681313 339 AG 340
Cdd:smart00490 81 AG 82
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
3-213 |
1.96e-27 |
|
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH) is a testis-specific protein essential for completion of spermatogenesis. DDX25 is also a novel negative regulator of IFN pathway and facilitates RNA virus infection. Diseases associated with DDX25 include hydrolethalus syndrome, an autosomal recessive lethal malformation syndrome characterized by multiple developmental defects of fetus.. DDX25 (also called gonadotropin-regulated testicular RNA helicase) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350806 [Multi-domain] Cd Length: 229 Bit Score: 108.96 E-value: 1.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 3 FQDLNLDPSIIRAIEDQKYKNPTPIQEKAIPSILRG--KDLLGCAQTGTGKTAAFAIPILQKLTKDsmnyEEYNQikALV 80
Cdd:cd18048 20 FEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDAL----KLYPQ--CLC 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 81 LAPTRELAIQIGESFNTYGQH-LDIETGVIFGGITPKRHIKVLKRdpnILVATPGRLLD-LLEQGYVDLNNIEVFVLDEA 158
Cdd:cd18048 94 LSPTFELALQTGKVVEEMGKFcVGIQVIYAIRGNRPGKGTDIEAQ---IVIGTPGTVLDwCFKLRLIDVTNISVFVLDEA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1308681313 159 DRMLDLGMIRDVKNIISK-LPKVRQNLLFSATMPQEVSKLVHSILRNPVKIEVKSK 213
Cdd:cd18048 171 DVMINVQGHSDHSVRVKRsMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKE 226
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
3-196 |
8.68e-24 |
|
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 (MRH4) plays an essential role during the late stages of mitochondrial ribosome or mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions. MRH4 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350723 [Multi-domain] Cd Length: 251 Bit Score: 99.37 E-value: 8.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 3 FQDLNLDPSIIRAIEDQKYK---------NPTPIQEKAIPSIL----------------RGKDLLGCAQTGTGKTAAFAI 57
Cdd:cd17965 1 FDQLKLLPSVREAIIKEILKgsnktdeeiKPSPIQTLAIKKLLktlmrkvtkqtsneepKLEVFLLAAETGSGKTLAYLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 58 PILQKLTKDSMNYEE-----------YNQIKALVLAPTRELAIQIGESFNTYGQHLDIETGVIFGGITPkRHIKVLKRDP 126
Cdd:cd17965 81 PLLDYLKRQEQEPFEeaeeeyesakdTGRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGP-SYQRLQLAFK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1308681313 127 N---ILVATPGRLLDLLEQGYVDLNNIEVFVLDEADRMLDLGMIRDVKNIISKLPKVRQNLLFSATMPQEVSK 196
Cdd:cd17965 160 GridILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDK 232
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
3-205 |
2.46e-22 |
|
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: 94.40 E-value: 2.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 3 FQDLNLDPSIIRAIEDQKYKNPTPIQEKAIPSILR--GKDLLGCAQTGTGKTAAFAIPILQKLTKDSmnyeEYNQikALV 80
Cdd:cd18047 3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAepPQNLIAQSQSGTGKTAAFVLAMLSQVEPAN----KYPQ--CLC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 81 LAPTRELAIQIGESFNTYGQ-HLDIETGVIFGGITPKRHIKVLKRdpnILVATPGRLLD-LLEQGYVDLNNIEVFVLDEA 158
Cdd:cd18047 77 LSPTYELALQTGKVIEQMGKfYPELKLAYAVRGNKLERGQKISEQ---IVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1308681313 159 DRMLDLGMIRDVKNIISK-LPKVRQNLLFSATMPQEVSKLVHSILRNP 205
Cdd:cd18047 154 DVMIATQGHQDQSIRIQRmLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
3-344 |
1.49e-20 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 93.94 E-value: 1.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 3 FQDLNLDPSIIRAIEDQKYKNPTPI-----QEKAIPSILR-----GKDLLGCAQTGTGKT--AAFAIpilqkltkdsmnY 70
Cdd:COG1061 55 EEDTERELAEAEALEAGDEASGTSFelrpyQQEALEALLAalergGGRGLVVAPTGTGKTvlALALA------------A 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 71 EEYNQIKALVLAPTRELAIQIGESF-------NTYGQHLDIETGVIFGGI---TPKRHIKVLKRDPNILV---------- 130
Cdd:COG1061 123 ELLRGKRVLVLVPRRELLEQWAEELrrflgdpLAGGGKKDSDAPITVATYqslARRAHLDELGDRFGLVIideahhagap 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 131 ------------------ATPGRLlDLLEQGYVDLNNIeVFVLDEADrMLDLGMIR--DVKNIISKLPKVRQNllfsatm 190
Cdd:COG1061 203 syrrileafpaayrlgltATPFRS-DGREILLFLFDGI-VYEYSLKE-AIEDGYLAppEYYGIRVDLTDERAE------- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 191 pqevsklvHSILRNPVKIEVKSKPSNKLQIKQQVyyvdepdktslllhLLKDKAFESVLVFARTKKKADIVSKAINIENI 270
Cdd:COG1061 273 --------YDALSERLREALAADAERKDKILREL--------------LREHPDDRKTLVFCSSVDHAEALAELLNEAGI 330
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1308681313 271 RSKAIHGDKNQSERQKALERFKNKEIRVLVATDVAARGIDIEKLSHVVNMDIPNVPETYIHRIGRTGRAGMGGT 344
Cdd:COG1061 331 RAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPGKE 404
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
28-364 |
2.85e-19 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 89.81 E-value: 2.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 28 QEKAIPSILRGKDLLGCAQTGTGKTAAFAIP--ILQKLT----------KDsmnyeeynQIKALVlaptrelaiQIGE-- 93
Cdd:COG0514 22 QEEIIEAVLAGRDALVVMPTGGGKSLCYQLPalLLPGLTlvvsplialmKD--------QVDALR---------AAGIra 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 94 ----SFNTYGQHLDIETGVIFGgitpkrHIKVLkrdpniLVAtPGRL-----LDLLEQGYVDLnnievFVLDEA------ 158
Cdd:COG0514 85 aflnSSLSAEERREVLRALRAG------ELKLL------YVA-PERLlnprfLELLRRLKISL-----FAIDEAhcisqw 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 159 --D-----RMLdlgmirdvKNIISKLPKVrQNLLFSATMPQEVSK-------------LVHSILRNPVKIEVKSKPSNkl 218
Cdd:COG0514 147 ghDfrpdyRRL--------GELRERLPNV-PVLALTATATPRVRAdiaeqlgledprvFVGSFDRPNLRLEVVPKPPD-- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 219 qikqqvyyvdepDKTSLLLHLLKDKAFESVLVFARTKKKADIVSKAINIENIRSKAIHGDKNQSERQKALERFKNKEIRV 298
Cdd:COG0514 216 ------------DKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDV 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1308681313 299 LVATdVA-ARGIDIEKLSHVVNMDIPNVPETYIHRIGRTGRAGMGGTAISFCSnqeiafLKDVEKLQ 364
Cdd:COG0514 284 IVAT-IAfGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYG------PEDVAIQR 343
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1-346 |
4.55e-19 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 89.18 E-value: 4.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 1 MLFQDLNLdPSIIRAIEDQKYKNPTPIQEKAIPS-ILRGKDLLGCAQTGTGKTAAFAIPILQKLTKDSmnyeeynqiKAL 79
Cdd:COG1204 1 MKVAELPL-EKVIEFLKERGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTLIAELAILKALLNGG---------KAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 80 VLAPTRELAIQIGESFNTYGQHLDIETGVIFGGITPKRhikVLKRDPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEA- 158
Cdd:COG1204 71 YIVPLRALASEKYREFKRDFEELGIKVGVSTGDYDSDD---EWLGRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAh 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 159 -----DRMLDLGMirdvknIISKLPKVRQNLLF---SATM--PQEVS-----KLVHSILRnPVKIEVKSKPSNKLQIKqQ 223
Cdd:COG1204 148 liddeSRGPTLEV------LLARLRRLNPEAQIvalSATIgnAEEIAewldaELVKSDWR-PVPLNEGVLYDGVLRFD-D 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 224 VYYVDEPDKTSLLLHLLKDKafESVLVFARTKKK----ADIVSKAIN----------IENIRSKAI-------------- 275
Cdd:COG1204 220 GSRRSKDPTLALALDLLEEG--GQVLVFVSSRRDaeslAKKLADELKrrltpeereeLEELAEELLevseethtneklad 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 276 ---------HGDKNQSERqKALER-FKNKEIRVLVATD-------VAARGIDIEKLSHVVNMDIPnvPETYIHRIGRTGR 338
Cdd:COG1204 298 clekgvafhHAGLPSELR-RLVEDaFREGLIKVLVATPtlaagvnLPARRVIIRDTKRGGMVPIP--VLEFKQMAGRAGR 374
|
410
....*....|
gi 1308681313 339 AGMG--GTAI 346
Cdd:COG1204 375 PGYDpyGEAI 384
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
7-346 |
3.00e-18 |
|
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: 87.20 E-value: 3.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 7 NLDPSIIRAIEDQKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLTKDSmnyeeynQIKALVLAPTRE 86
Cdd:COG1205 40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDP-------GATALYLYPTKA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 87 LAI-QIgESFNTYGQHL--DIETGVIFGGiTPKRHIKVLKRDPNILVATPgrllDLLEQGYVD--------LNNIEVFVL 155
Cdd:COG1205 113 LARdQL-RRLRELAEALglGVRVATYDGD-TPPEERRWIREHPDIVLTNP----DMLHYGLLPhhtrwarfFRNLRYVVI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 156 DEA---------------DRMLdlgmiRDVKNIISKlPKVrqnLLFSATM--PQE-VSKLV-----------------HS 200
Cdd:COG1205 187 DEAhtyrgvfgshvanvlRRLR-----RICRHYGSD-PQF---ILASATIgnPAEhAERLTgrpvtvvdedgsprgerTF 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 201 ILRNPVKIEVKSKPSNKLQIKQqvyyvdepdktsLLLHLLKDKAfeSVLVFARTKKKADIVskAINIENIRSKAIHGDKN 280
Cdd:COG1205 258 VLWNPPLVDDGIRRSALAEAAR------------LLADLVREGL--RTLVFTRSRRGAELL--ARYARRALREPDLADRV 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1308681313 281 QS-------ERQKALER-FKNKEIRVLVATDVAARGIDIEKLSHVVNMDIPNVPETYIHRIGRTGRAGMGGTAI 346
Cdd:COG1205 322 AAyragylpEERREIERgLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV 395
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
38-189 |
1.60e-17 |
|
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: 78.98 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 38 GKDLLGCAQTGTGKTAAFAIPILQKLTKdsmnyeeyNQIKALVLAPTRELAIQIGESFNTYGQHlDIETGVIFGGITPKR 117
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLK--------KGKKVLVLVPTKALALQTAERLRELFGP-GIRVAVLVGGSSAEE 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1308681313 118 HIKVLKRDPNILVATPGRLLDLLEQ-GYVDLNNIEVFVLDEADRMLD-----LGMIRDVKNIISKLPKVrqnLLFSAT 189
Cdd:cd00046 72 REKNKLGDADIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLIdsrgaLILDLAVRKAGLKNAQV---ILLSAT 146
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
19-311 |
2.39e-13 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 72.06 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 19 QKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKT-AAFaIPILQKLTKDSMNYEEYNQIKALVLAPTRELA--IQ----- 90
Cdd:COG1201 20 ARFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPRPGELPDGLRVLYISPLKALAndIErnlra 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 91 ----IGEsfnTYGQHLD-IETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLeqGYVD----LNNIEVFVLDE---- 157
Cdd:COG1201 99 pleeIGE---AAGLPLPeIRVGVRTGDTPASERQRQRRRPPHILITTPESLALLL--TSPDarelLRGVRTVIVDEihal 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 158 AD--R----MLDLGMIRDvkniISKLPKVRQNLlfSATM--PQEVSK-LVHSILRNPVKIeVKSKPSNKLQIKQQVYYVD 228
Cdd:COG1201 174 AGskRgvhlALSLERLRA----LAPRPLQRIGL--SATVgpLEEVARfLVGYEDPRPVTI-VDAGAGKKPDLEVLVPVED 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 229 ----EPDKTSLLLHLLKD-----KAFESVLVFARTKKKADIVSKAIN------IENIRskAIHG--DKNQseRQKALERF 291
Cdd:COG1201 247 lierFPWAGHLWPHLYPRvldliEAHRTTLVFTNTRSQAERLFQRLNelnpedALPIA--AHHGslSREQ--RLEVEEAL 322
|
330 340
....*....|....*....|...
gi 1308681313 292 KNKEIRVLVAT---DVaarGIDI 311
Cdd:COG1201 323 KAGELRAVVATsslEL---GIDI 342
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
15-342 |
3.56e-13 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 71.68 E-value: 3.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 15 AIEDQKYknptpiQEKAIPSILRgKDLLGCAQTGTGKTAAFAIPILQKLTKDsmnyeeynQIKALVLAPTRELAIQIGES 94
Cdd:COG1111 1 TIERRLY------QLNLAASALR-KNTLVVLPTGLGKTAVALLVIAERLHKK--------GGKVLFLAPTKPLVEQHAEF 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 95 FNTYGQHLDIETGVIFGGITP-KRhiKVLKRDPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEADR------------- 160
Cdd:COG1111 66 FKEALNIPEDEIVVFTGEVSPeKR--KELWEKARIIVATPQVIENDLIAGRIDLDDVSLLIFDEAHRavgnyayvyiaer 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 161 -------MLDLGM-------------------IRDV------------------------------KNIISKLPKV---- 180
Cdd:COG1111 144 yhedakdPLILGMtaspgsdeekieevcenlgIENVevrteedpdvapyvhdtevewirvelpeelKEIRDLLNEVlddr 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 181 -----------------------------------RQNLLFSATMPQ-EVSKLVHSI-----------------LRNPVK 207
Cdd:COG1111 224 lkklkelgvivstspdlskkdllalqkklqrrireDDSEGYRAISILaEALKLRHALelletqgveallrylerLEEEAR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 208 IEVKSKPSNKL----QIKQQVY----YVDEPDKTSLLLHLLKD----KAFESVLVFARTKKKADIVSKAINIENIRSK-- 273
Cdd:COG1111 304 SSGGSKASKRLvsdpRFRKAMRlaeeADIEHPKLSKLREILKEqlgtNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGrf 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1308681313 274 ----AIHGDK--NQSERQKALERFKNKEIRVLVATDVAARGIDIEKLSHVVNMDipNVPET--YIHRIGRTGRAGMG 342
Cdd:COG1111 384 vgqaSKEGDKglTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYE--PVPSEirSIQRKGRTGRKREG 458
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
232-334 |
8.68e-13 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 65.19 E-value: 8.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 232 KTSLLLHLLKDKAFES--VLVFARTKKKADIVSKAINIENIRSKAIHGDKNQSERQKALERFKN--KEIRVLVATDVAAR 307
Cdd:cd18793 12 KLEALLELLEELREPGekVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEdpDIRVFLLSTKAGGV 91
|
90 100 110
....*....|....*....|....*....|...
gi 1308681313 308 GIDIEKLSHVVNMDI---PNVPETYI---HRIG 334
Cdd:cd18793 92 GLNLTAANRVILYDPwwnPAVEEQAIdraHRIG 124
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
28-158 |
1.24e-11 |
|
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: 62.99 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 28 QEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLTKDSmnyeeynQIKALVLAPTRELAIQIGESFNTYGQHLDIETG 107
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDP-------GSRALYLYPTKALAQDQLRSLRELLEQLGLGIR 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1308681313 108 V-IFGGITPKR-HIKVLKRDPNILVATPgrllDLLEQG--------YVDLNNIEVFVLDEA 158
Cdd:cd17923 78 VaTYDGDTPREeRRAIIRNPPRILLTNP----DMLHYAllphhdrwARFLRNLRYVVLDEA 134
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
219-348 |
2.74e-11 |
|
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: 60.69 E-value: 2.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 219 QIKQQVYYVDEPDKTSLLLHLLKDKAF-ESVLVFARTKKKADIVSKAINIENIRSKAIHGDKNQSERQKALERFKNKEIR 297
Cdd:cd18794 3 NLFYSVRPKDKKDEKLDLLKRIKVEHLgGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQ 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1308681313 298 VLVATDVAARGIDIEKLSHVVNMDIPNVPETYIHRIGRTGRAGMGGTAISF 348
Cdd:cd18794 83 VIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILF 133
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
25-158 |
1.02e-10 |
|
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: 60.35 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 25 TPIQEKAIPSI-LRGKDLLGCAQTGTGKTAAFAIPILQKLTKdsmnyeeyNQIKALVLAPTRELAIQIGESFNTYGQHLD 103
Cdd:cd17921 3 NPIQREALRALyLSGDSVLVSAPTSSGKTLIAELAILRALAT--------SGGKAVYIAPTRALVNQKEADLRERFGPLG 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1308681313 104 IETGVIFGGITPKrhiKVLKRDPNILVATPGRLLDLL---EQGYVDlnNIEVFVLDEA 158
Cdd:cd17921 75 KNVGLLTGDPSVN---KLLLAEADILVATPEKLDLLLrngGERLIQ--DVRLVVVDEA 127
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
19-337 |
5.94e-10 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 61.44 E-value: 5.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 19 QKYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKT-AAFaIPILQKLTKDSMNYEEYNQIKALVLAPTRELA--IQ----- 90
Cdd:PRK13767 28 EKFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAF-LAIIDELFRLGREGELEDKVYCLYVSPLRALNndIHrnlee 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 91 ----IGESFNTYGQHL-DIETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLL------EQgyvdLNNIEVFVLDEAD 159
Cdd:PRK13767 107 plteIREIAKERGEELpEIRVAIRTGDTSSYEKQKMLKKPPHILITTPESLAILLnspkfrEK----LRTVKWVIVDEIH 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 160 RM--------LDLGMIRdVKNIISKlPKVRQNLlfSATM--PQEVSK---------------LVHSILRNPVKIEVKS-- 212
Cdd:PRK13767 183 SLaenkrgvhLSLSLER-LEELAGG-EFVRIGL--SATIepLEEVAKflvgyeddgeprdceIVDARFVKPFDIKVISpv 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 213 -----KPSNKLQIKqqVYyvdepdktSLLLHLLKDKafESVLVFARTKKKADIVS--------KAINIENIrsKAIHGDK 279
Cdd:PRK13767 259 ddlihTPAEEISEA--LY--------ETLHELIKEH--RTTLIFTNTRSGAERVLynlrkrfpEEYDEDNI--GAHHSSL 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1308681313 280 NQSERQKALERFKNKEIRVLVATDVAARGIDIEKLSHVVNMDIPNVPETYIHRIGRTG 337
Cdd:PRK13767 325 SREVRLEVEEKLKRGELKVVVSSTSLELGIDIGYIDLVVLLGSPKSVSRLLQRIGRAG 382
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
21-369 |
1.20e-09 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 60.11 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 21 YKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQK------------LTKDSMNYEEYNQIKALVLAPT--RE 86
Cdd:PRK11057 23 YQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLdgltlvvsplisLMKDQVDQLLANGVAAACLNSTqtRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 87 laiqigesfntygQHLDIETGVIFGGItpkrhikvlkrdpNILVATPGRLL--DLLEQgyVDLNNIEVFVLDEADRMLDL 164
Cdd:PRK11057 103 -------------QQLEVMAGCRTGQI-------------KLLYIAPERLMmdNFLEH--LAHWNPALLAVDEAHCISQW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 165 GmiRDVKNIISKLPKVRQ---NLLFSA-------TMPQEVSKLVHsiLRNPVkIEVKS--KPSnklqIKqqvYYVDEPDK 232
Cdd:PRK11057 155 G--HDFRPEYAALGQLRQrfpTLPFMAltataddTTRQDIVRLLG--LNDPL-IQISSfdRPN----IR---YTLVEKFK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 233 -TSLLLHLLKDKAFESVLVFARTKKKADIVSKAINIENIRSKAIHGDKNQSERQKALERFKNKEIRVLVATDVAARGIDI 311
Cdd:PRK11057 223 pLDQLMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINK 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1308681313 312 EKLSHVVNMDIPNVPETYIHRIGRTGRAGMGGTAISFCSNQEIAFLKDV--EKLQG--KKIE 369
Cdd:PRK11057 303 PNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPADMAWLRRCleEKPAGqqQDIE 364
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
282-340 |
2.68e-09 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 53.48 E-value: 2.68e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1308681313 282 SERQKALERFKNkEIRVLVATDVAARGIDIEKLSHVVNMDIPNVPETYIHRIGRTGRAG 340
Cdd:cd18785 10 TNSIEHAEEIAS-SLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGG 67
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
218-336 |
3.00e-09 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 59.08 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 218 LQIKQQVYYVDEPDKTSLLLHLLKDKAF--ESVLVFARTKKKADIVSKAINIENIRSKAIHGDKNQSERQKALERFKNKE 295
Cdd:COG0553 520 LLLEEGAELSGRSAKLEALLELLEELLAegEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGP 599
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1308681313 296 --IRVLVATDVAARGIDIEKLSHVVNMDIP-NvPETY------IHRIGRT 336
Cdd:COG0553 600 eaPVFLISLKAGGEGLNLTAADHVIHYDLWwN-PAVEeqaidrAHRIGQT 648
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
240-342 |
4.23e-09 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 58.73 E-value: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 240 LKDKAFESVLVFARTKKKADIVSKAINIENIRSKAI------HGDK--NQSERQKALERFKNKEIRVLVATDVAARGIDI 311
Cdd:PRK13766 360 LGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFvgqaskDGDKgmSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDI 439
|
90 100 110
....*....|....*....|....*....|....*.
gi 1308681313 312 EKlshvVNMDI---PnVPET--YIHRIGRTGRAGMG 342
Cdd:PRK13766 440 PS----VDLVIfyeP-VPSEirSIQRKGRTGRQEEG 470
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
47-158 |
2.49e-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: 53.81 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 47 TGTGKT--AAFAIPILQKLtkdsmNYEEYNQIK-ALVLAPTRELAIQIGESfntYGQHLDIETGVIFGGITP----KRHI 119
Cdd:cd18034 25 TGSGKTliAVMLIKEMGEL-----NRKEKNPKKrAVFLVPTVPLVAQQAEA---IRSHTDLKVGEYSGEMGVdkwtKERW 96
|
90 100 110
....*....|....*....|....*....|....*....
gi 1308681313 120 KVLKRDPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEA 158
Cdd:cd18034 97 KEELEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
225-339 |
3.68e-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: 52.21 E-value: 3.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 225 YYVDEPdKTSLLLHLLkDKAFESV-----LVFARTKKKADIVSK-----AINIENIRSKAI--HGDKNQSER-------Q 285
Cdd:cd18802 2 EIVVIP-KLQKLIEIL-REYFPKTpdfrgIIFVERRATAVVLSRllkehPSTLAFIRCGFLigRGNSSQRKRslmtqrkQ 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1308681313 286 K-ALERFKNKEIRVLVATDVAARGIDIEKLSHVVNMDIPNvpeTYIHRIGRTGRA 339
Cdd:cd18802 80 KeTLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPK---TLRSYIQSRGRA 131
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
256-343 |
1.01e-07 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350188 [Multi-domain] Cd Length: 143 Bit Score: 50.82 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 256 KKADIVSKAINIENIRSKAIHGdKNQSERQKALERFKNKEIRVLVATDVAARGIDIEKLSHVVNMDIPNVPETYIHRIGR 335
Cdd:cd18801 52 KIRPGIRATRFIGQASGKSSKG-MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGR 130
|
....*...
gi 1308681313 336 TGRaGMGG 343
Cdd:cd18801 131 TGR-KRQG 137
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
221-311 |
2.97e-07 |
|
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350176 [Multi-domain] Cd Length: 153 Bit Score: 49.94 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 221 KQQVYYVDEPDKTSLLLHLLK-DKAFESVLVFARTKKKADIVSKAINIEnirskAIHGDKNQSERQKALERFKNKEIRVL 299
Cdd:cd18789 24 KRRLLAAMNPNKLRALEELLKrHEQGDKIIVFTDNVEALYRYAKRLLKP-----FITGETPQSEREEILQNFREGEYNTL 98
|
90
....*....|..
gi 1308681313 300 VATDVAARGIDI 311
Cdd:cd18789 99 VVSKVGDEGIDL 110
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
245-318 |
4.95e-07 |
|
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: 48.32 E-value: 4.95e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1308681313 245 FESVLVFARTKKKADIVSKAINIENIRSKAIHGDKNQSER-QKALERFKNKEI--RVLVATDVAARGIDIEKLSHVV 318
Cdd:cd18799 6 EIKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERgDEALILLFFGELkpPILVTVDLLTTGVDIPEVDNVV 82
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
38-157 |
9.08e-07 |
|
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: 48.73 E-value: 9.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 38 GKDLLGCAQTGTGKTAAFAIPILQKLTKdsmnyEEYNQIKALVLAPTRELAIQIGESFNTYGQH--LDIETGVIFGGITP 115
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLAD-----EPEKGVQVLYISPLKALINDQERRLEEPLDEidLEIPVAVRHGDTSQ 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1308681313 116 KRHIKVLKRDPNILVATPGRLLDLL--EQGYVDLNNIEVFVLDE 157
Cdd:cd17922 76 SEKAKQLKNPPGILITTPESLELLLvnKKLRELFAGLRYVVVDE 119
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
26-158 |
1.10e-06 |
|
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: 48.07 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 26 PIQEKAIPSIL---RGKDLLGCAQTGTGKTA-AFAIPilqkltkdsmnyEEYNQIKALVLAPTRELAIQIGESFNTYGQH 101
Cdd:cd17926 3 PYQEEALEAWLahkNNRRGILVLPTGSGKTLtALALI------------AYLKELRTLIVVPTDALLDQWKERFEDFLGD 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1308681313 102 LDIetGVIFGGitpkrhIKVLKRDPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEA 158
Cdd:cd17926 71 SSI--GLIGGG------KKKDFDDANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEA 119
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
226-338 |
2.66e-06 |
|
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: 47.30 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 226 YVDEPDKTSLLLHLLKdKAFESVLVFART---KKKADIVSKAINIENIRSKAIHgdknqSERQKALERFKNKEIRVLVAT 302
Cdd:cd18798 6 YIEDSDSLEKLLELVK-KLGDGGLIFVSIdygKEYAEELKEFLERHGIKAELAL-----SSTEKNLEKFEEGEIDVLIGV 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1308681313 303 ----DVAARGIDI-EKLSHVVNMDIPnvPETYIHRIGRTGR 338
Cdd:cd18798 80 asyyGVLVRGIDLpERIKYAIFYGVP--VTTYIQASGRTSR 118
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
27-160 |
3.56e-06 |
|
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: 47.12 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 27 IQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLTKDSMnyeeynqiKALVLAPTRELAIQIGESFNtygQHLDIET 106
Cdd:cd18035 5 LYQVLIAAVALNGNTLIVLPTGLGKTIIAILVAADRLTKKGG--------KVLILAPSRPLVEQHAENLK---RVLNIPD 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1308681313 107 GV--IFGGITPKRHIKVLKRDpNILVATPGRLLDLLEQGYVDLNNIEVFVLDEADR 160
Cdd:cd18035 74 KItsLTGEVKPEERAERWDAS-KIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
20-212 |
4.88e-06 |
|
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: 47.14 E-value: 4.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 20 KYKNPTPIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIP--ILQKLTkdsmnyeeynqikaLVLAP--------TRELai 89
Cdd:cd17920 9 GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPalLLDGVT--------------LVVSPlislmqdqVDRL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 90 qigesfntygQHLDIETGVIFGGITPKRHIKVLKR----DPNILVATPGRL-----LDLLEQGYVdLNNIEVFVLDEA-- 158
Cdd:cd17920 73 ----------QQLGIRAAALNSTLSPEEKREVLLRikngQYKLLYVTPERLlspdfLELLQRLPE-RKRLALIVVDEAhc 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1308681313 159 ------D-R--MLDLGMIRDvkniisKLPKVrQNLLFSATMPQEVSKLVHSILR-NPVKIEVKS 212
Cdd:cd17920 142 vsqwghDfRpdYLRLGRLRR------ALPGV-PILALTATATPEVREDILKRLGlRNPVIFRAS 198
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
249-346 |
5.23e-06 |
|
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: 46.10 E-value: 5.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 249 LVFARTKKKADIVSKAINiENIRSKAIHGDK--------NQSERQKALERFKNKEIRVLVATDVAARGIDIEKLSHVVNM 320
Cdd:cd18797 39 IVFCRSRKLAELLLRYLK-ARLVEEGPLASKvasyragyLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLA 117
|
90 100
....*....|....*....|....*.
gi 1308681313 321 DIPNVPETYIHRIGRTGRAGMGGTAI 346
Cdd:cd18797 118 GYPGSLASLWQQAGRAGRRGKDSLVI 143
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
22-189 |
7.27e-06 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 45.74 E-value: 7.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 22 KNPTPIQEKAIPSILRG---KDLLGCAQ--TGTGKT--AAFAIPILqkltkdsmnYEEYNQIKALVLAPTRELAIQIGES 94
Cdd:pfam04851 2 LELRPYQIEAIENLLESiknGQKRGLIVmaTGSGKTltAAKLIARL---------FKKGPIKKVLFLVPRKDLLEQALEE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 95 FNTYGqhldiETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLEQGYVDL--NNIEVFVLDEADRMLDLGMirdvKN 172
Cdd:pfam04851 73 FKKFL-----PNYVEIGEIISGDKKDESVDDNKIVVTTIQSLYKALELASLELlpDFFDVIIIDEAHRSGASSY----RN 143
|
170
....*....|....*..
gi 1308681313 173 IISKLPKVRQnLLFSAT 189
Cdd:pfam04851 144 ILEYFKPAFL-LGLTAT 159
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
246-338 |
1.33e-05 |
|
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: 44.95 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 246 ESVLVFARTKKKADIVSK------AINIENIRSKAIHGDKNQSERQKALERFKNKEIRVLVATDVAARGIDIEKLSHVVN 319
Cdd:cd18796 39 KSTLVFTNTRSQAERLAQrlrelcPDRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQ 118
|
90
....*....|....*....
gi 1308681313 320 MDIPNVPETYIHRIGRTGR 338
Cdd:cd18796 119 IGSPKSVARLLQRLGRSGH 137
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
24-161 |
1.47e-05 |
|
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: 45.48 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 24 PTPIQEKAIPSIL----RGK--DLLGCAQTGTGKTAAFAIPILqkltkdsMNYEEYNQikALVLAPTRELAIQIGESFNT 97
Cdd:cd17918 16 LTKDQAQAIKDIEkdlhSPEpmDRLLSGDVGSGKTLVALGAAL-------LAYKNGKQ--VAILVPTEILAHQHYEEARK 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1308681313 98 YGQHLDIEtgVIFGGITPKrhikvLKRDPNILVATPGrLLDLLEQGYvdlnNIEVFVLDEADRM 161
Cdd:cd17918 87 FLPFINVE--LVTGGTKAQ-----ILSGISLLVGTHA-LLHLDVKFK----NLDLVIVDEQHRF 138
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
24-160 |
2.15e-05 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 45.12 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 24 PTPIQEKAIPSILRGKDLLGCAQTGTGKTAAfAIPILQKLTKdsmNYEEYNQIKALVLAPTRELAIQIGESFNTYGQHLD 103
Cdd:cd17927 3 PRNYQLELAQPALKGKNTIICLPTGSGKTFV-AVLICEHHLK---KFPAGRKGKVVFLANKVPLVEQQKEVFRKHFERPG 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1308681313 104 IETGVIFGGITPKRHIKVLKRDPNILVATPGRLLDLLEQG-YVDLNNIEVFVLDEADR 160
Cdd:cd17927 79 YKVTGLSGDTSENVSVEQIVESSDVIIVTPQILVNDLKSGtIVSLSDFSLLVFDECHN 136
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
26-191 |
2.57e-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: 44.63 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 26 PIQEKAIPS-ILRGKDLLGCAQTGTGKTAAFAIPILQKLTKDSmnyeeynqiKALVLAPTRELAIQIGESFNTYgQHLDI 104
Cdd:cd18028 4 PPQAEAVRAgLLKGENLLISIPTASGKTLIAEMAMVNTLLEGG---------KALYLVPLRALASEKYEEFKKL-EEIGL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 105 ETGVIFGGI-TPKRHIKvlkrDPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEadrmldLGMIRD------VKNIISKL 177
Cdd:cd18028 74 KVGISTGDYdEDDEWLG----DYDIIVATYEKFDSLLRHSPSWLRDVGVVVVDE------IHLISDeergptLESIVARL 143
|
170
....*....|....*..
gi 1308681313 178 PKVRQNLLF---SATMP 191
Cdd:cd18028 144 RRLNPNTQIiglSATIG 160
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
27-157 |
4.28e-05 |
|
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: 44.27 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 27 IQEKAIPSILRG-KDLLGCAQTGTGKTAAFAIPILQKLTKDSMNYEeyNQIKALVLAPTRELAiqiGESFNTYGQHLDiE 105
Cdd:cd18023 5 IQSEVFPDLLYSdKNFVVSAPTGSGKTVLFELAILRLLKERNPLPW--GNRKVVYIAPIKALC---SEKYDDWKEKFG-P 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1308681313 106 TGVIFGGITPKRHIKVLK--RDPNILVATPGRlLDLLEQGYVDLNN----IEVFVLDE 157
Cdd:cd18023 79 LGLSCAELTGDTEMDDTFeiQDADIILTTPEK-WDSMTRRWRDNGNlvqlVALVLIDE 135
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
205-349 |
5.45e-05 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350182 [Multi-domain] Cd Length: 154 Bit Score: 43.31 E-value: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 205 PVKIEVKSKPSNKLQIK--QQVYYVDEPDKTSLLLHLLKdKAFESVLVFARTKKKADIVSKAI-NIenirsKAIHGDKNQ 281
Cdd:cd18795 2 PVPLEEYVLGFNGLGIKlrVDVMNKFDSDIIVLLKIETV-SEGKPVLVFCSSRKECEKTAKDLaGI-----AFHHAGLTR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 282 SERQKALERFKNKEIRVLVATdvaargidiEKLSHVVNM-------------------DIPnvPETYIHRIGRTGRAGMG 342
Cdd:cd18795 76 EDRELVEELFREGLIKVLVAT---------STLAAGVNLpartviikgtqrydgkgyrELS--PLEYLQMIGRAGRPGFD 144
|
....*....
gi 1308681313 343 --GTAISFC 349
Cdd:cd18795 145 trGEAIIMT 153
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
151-340 |
5.93e-05 |
|
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
Pssm-ID: 187770 [Multi-domain] Cd Length: 353 Bit Score: 45.11 E-value: 5.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 151 EVFVLDEADRMLDLGMIRDVKNIISKLpkvrqnLLFSATMPQEVSKLVHSILrNPVKIEVKSKPSNKLQIKQQVYYVDEP 230
Cdd:cd09639 131 EVHFYDEYTLALILAVLEVLKDNDVPI------LLMSATLPKFLKEYAEKIG-YVEENEPLDLKPNERAPFIKIESDKVG 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 231 DKTSLLLHLLKDKAFESVLVFARTKKKADIVSKAINIENIRSKAI--HGDKNQSERQKA----LERFKNKEIRVLVATDV 304
Cdd:cd09639 204 EISSLERLLEFIKKGGSVAIIVNTVDRAQEFYQQLKEKGPEEEIMliHSRFTEKDRAKKeaelLLEFKKSEKFVIVATQV 283
|
170 180 190
....*....|....*....|....*....|....*...
gi 1308681313 305 AARGIDIEklshvVNMDI--PNVPETYIHRIGRTGRAG 340
Cdd:cd09639 284 IEASLDIS-----VDVMIteLAPIDSLIQRLGRLHRYG 316
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
39-160 |
2.71e-04 |
|
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350791 [Multi-domain] Cd Length: 182 Bit Score: 41.54 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 39 KDLLGCAQTGTGKT--AAFAIpilqkltkdsMNYEE-YNQIKALVLAPTREL-AIQIGESFNTYGQHLDIEtgVIFGGIT 114
Cdd:cd18033 17 QNTLVALPTGLGKTfiAAVVM----------LNYYRwFPKGKIVFMAPTKPLvSQQIEACYKITGIPSSQT--AELTGSV 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1308681313 115 PKRHIKVLKRDPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEADR 160
Cdd:cd18033 85 PPTKRAELWASKRVFFLTPQTLENDLKEGDCDPKSIVCLVIDEAHR 130
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
24-194 |
2.96e-04 |
|
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: 41.48 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 24 PTPIQEKAIPSILRGKDLLGCAQTGTGKT--AAFAIPILQKltkdsmnyeeyNQIKALVLAPTRELAIQIGESF-NTYGq 100
Cdd:cd18027 9 LDVFQKQAILHLEAGDSVFVAAHTSAGKTvvAEYAIALAQK-----------HMTRTIYTSPIKALSNQKFRDFkNTFG- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 101 hldiETGVIFGGITpkrhikvLKRDPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEADRMLDLGmiRDV--KNIISKLP 178
Cdd:cd18027 77 ----DVGLITGDVQ-------LNPEASCLIMTTEILRSMLYNGSDVIRDLEWVIFDEVHYINDAE--RGVvwEEVLIMLP 143
|
170
....*....|....*.
gi 1308681313 179 KVRQNLLFSATMPQEV 194
Cdd:cd18027 144 DHVSIILLSATVPNTV 159
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
39-133 |
1.16e-03 |
|
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350778 [Multi-domain] Cd Length: 199 Bit Score: 40.11 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 39 KDLLGCAQTGTGKTAAFAIPILQKLTK--DSMNYEEYNQIKALVLAPTRELAIQIGESFNTYGQHLDIETGVIFGGIT-P 115
Cdd:cd18020 18 ENMLICAPTGAGKTNIAMLTILHEIRQhvNQGGVIKKDDFKIVYIAPMKALAAEMVEKFSKRLAPLGIKVKELTGDMQlT 97
|
90
....*....|....*...
gi 1308681313 116 KRHIKvlkrDPNILVATP 133
Cdd:cd18020 98 KKEIA----ETQIIVTTP 111
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
24-160 |
1.49e-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: 39.08 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 24 PTPIQEKAI----PSILRGKD--LLGCAqTGTGKT--AAFAIPILQKLTKDSmnyeeynqiKALVLAPTRELAIQIGESF 95
Cdd:cd18032 1 PRYYQQEAIealeEAREKGQRraLLVMA-TGTGKTytAAFLIKRLLEANRKK---------RILFLAHREELLEQAERSF 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1308681313 96 NTygqhldietgviFGGITPKRHIKVLKRDP---NILVATPGRL-----LDLLEQGYVDLnnIevfVLDEADR 160
Cdd:cd18032 71 KE------------VLPDGSFGNLKGGKKKPddaRVVFATVQTLnkrkrLEKFPPDYFDL--I---IIDEAHH 126
|
|
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
275-324 |
2.20e-03 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 40.42 E-value: 2.20e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1308681313 275 IHGDKNQSERQKALERFKNKEIRVLVATDVaargidIEklshvVNMDIPN 324
Cdd:COG1200 509 LHGRMKPAEKDAVMAAFKAGEIDVLVATTV------IE-----VGVDVPN 547
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
22-189 |
2.34e-03 |
|
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: 38.85 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 22 KNPTPIQEKAIPSILRGKDLLGCAQTGTGKT---AAFAIPILQKltkdsmnyeeynQIKALVLAPTRELAIQIGESFNTY 98
Cdd:cd17924 16 FPPWGAQRTWAKRLLRGKSFAIIAPTGVGKTtfgLATSLYLASK------------GKRSYLIFPTKSLVKQAYERLSKY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 99 GQHLDIETGVIF--GGITPKRHIKVLKR----DPNILVATPGRL---LDLLEQGYVDLnnieVFVlDEADRMLdlgmiRD 169
Cdd:cd17924 84 AEKAGVEVKILVyhSRLKKKEKEELLEKiekgDFDILVTTNQFLsknFDLLSNKKFDF----VFV-DDVDAVL-----KS 153
|
170 180
....*....|....*....|..
gi 1308681313 170 VKNI--ISKLPKVRQNLLFSAT 189
Cdd:cd17924 154 SKNIdrLLKLLGFGQLVVSSAT 175
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
26-208 |
3.14e-03 |
|
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or SKIV2L2) is a type II DEAD box helicase that plays a role in the processing of structured RNAs, including the maturation of 5.8S ribosomal RNA (rRNA)and is part of the TRAMP complex that is involved in exosome-mediated degradation of aberrant RNAs. Mtr4 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: 350782 [Multi-domain] Cd Length: 205 Bit Score: 38.58 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 26 PIQEKAIPSILRGKDLLGCAQTGTGKTAAFAIPILQKLtKDSMNYEEYNQIKALVLAPTRELaiqiGESFNtygqhldiE 105
Cdd:cd18024 35 PFQKTAIACIERNESVLVSAHTSAGKTVVAEYAIAQSL-RDKQRVIYTSPIKALSNQKYREL----QEEFG--------D 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308681313 106 TGVIFGGITpkrhikvLKRDPNILVATPGRLLDLLEQGYVDLNNIEVFVLDEADRMLDlgMIRDV---KNIISKLPKVRQ 182
Cdd:cd18024 102 VGLMTGDVT-------INPNASCLVMTTEILRSMLYRGSEIMREVAWVIFDEIHYMRD--KERGVvweETIILLPDKVRY 172
|
170 180
....*....|....*....|....*...
gi 1308681313 183 NLLfSATMP--QEVSKLVHSILRNPVKI 208
Cdd:cd18024 173 VFL-SATIPnaRQFAEWICKIHKQPCHV 199
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
275-324 |
3.72e-03 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 39.75 E-value: 3.72e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1308681313 275 IHGDKNQSERQKALERFKNKEIRVLVATDVaargidIEklshvVNMDIPN 324
Cdd:PRK10917 511 LHGRMKPAEKDAVMAAFKAGEIDILVATTV------IE-----VGVDVPN 549
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
275-349 |
4.07e-03 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 37.71 E-value: 4.07e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1308681313 275 IHGDKNQSERQKALERFKNKEIRVLVATDVAARGIDIEKLSHVVNMDIPNVPETYIHRI-GRTGRagmgGTAISFC 349
Cdd:cd18811 67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLHQLrGRVGR----GDHQSYC 138
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
26-57 |
5.52e-03 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 39.15 E-value: 5.52e-03
10 20 30
....*....|....*....|....*....|....
gi 1308681313 26 PIQEKAIPSILRGKDLLGCAQTGTGKT--AAFAI 57
Cdd:COG4581 28 PFQEEAILALEAGRSVLVAAPTGSGKTlvAEFAI 61
|
|
| |
