|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
2-400 |
0e+00 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 601.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 2 SEDRKKKNDDMATVEFESSEEvSIIPTFDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATF 81
Cdd:PTZ00424 4 SEQKNQSEQVASTGTIESNYD-EIVDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 82 SISVLQSLDTQVRETQALILSPTRELAVQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIR 161
Cdd:PTZ00424 83 VIAALQLIDYDLNACQALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMID 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 162 RRNLRTRAIKLLVLDEADEMLNKGFKEQLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRILVKRDELTLEGIK 241
Cdd:PTZ00424 163 KRHLRVDDLKLFILDEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 242 QFFVAVDKEEWKFDTLIDLYDTLTITQAVLFCNTRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGNTRVLI 321
Cdd:PTZ00424 243 QFYVAVEKEEWKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLI 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 268563240 322 STDVWARGLDVPQVSLVINYDLPNNRELYIHRIGRSGRFGRKGVAINFVKQDDVRILRDIEQYYSTQIDEMPMNIADII 400
Cdd:PTZ00424 323 TTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEVADYL 401
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
26-394 |
3.62e-161 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 459.23 E-value: 3.62e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 26 IPTFDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQV-RETQALILSPT 104
Cdd:COG0513 1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRpRAPQALILAPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 105 RELAVQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNK 184
Cdd:COG0513 81 RELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 185 GFKEQLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRILVKRDELTLEGIKQFFVAVDKEEwKFDTLIDLYDTL 264
Cdd:COG0513 161 GFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRD-KLELLRRLLRDE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 265 TITQAVLFCNTRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGNTRVLISTDVWARGLDVPQVSLVINYDLP 344
Cdd:COG0513 240 DPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLP 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 268563240 345 NNRELYIHRIGRSGRFGRKGVAINFVKQDDVRILRDIEQYYSTQIDEMPM 394
Cdd:COG0513 320 EDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEEL 369
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
29-229 |
1.39e-134 |
|
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: 383.36 E-value: 1.39e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 29 FDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRETQALILSPTRELA 108
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 109 VQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKGFKE 188
Cdd:cd18045 81 VQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 268563240 189 QLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRIL 229
Cdd:cd18045 161 QIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRIL 201
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
32-229 |
6.65e-124 |
|
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: 356.25 E-value: 6.65e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 32 MGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRETQALILSPTRELAVQI 111
Cdd:cd17939 2 MGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 112 QKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKGFKEQLY 191
Cdd:cd17939 82 QKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQIY 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 268563240 192 DIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRIL 229
Cdd:cd17939 162 DIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRIL 199
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
29-229 |
5.29e-122 |
|
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: 351.36 E-value: 5.29e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 29 FDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRETQALILSPTRELA 108
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 109 VQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKGFKE 188
Cdd:cd18046 81 QQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 268563240 189 QLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRIL 229
Cdd:cd18046 161 QIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRIL 201
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
29-390 |
6.82e-110 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 330.22 E-value: 6.82e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 29 FDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRETQALILSPTRELA 108
Cdd:PRK11776 6 FSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTRELA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 109 VQIQKVVLALGDYM-NVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKGFK 187
Cdd:PRK11776 86 DQVAKEIRRLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMGFQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 188 EQLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRILV--KRDELTlegIKQFFVAVDKEEwKFDTLIDLYDTLT 265
Cdd:PRK11776 166 DAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVesTHDLPA---IEQRFYEVSPDE-RLPALQRLLLHHQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 266 ITQAVLFCNTRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGNTRVLISTDVWARGLDVPQVSLVINYDLPN 345
Cdd:PRK11776 242 PESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELAR 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 268563240 346 NRELYIHRIGRSGRFGRKGVAINFVKQDDVRILRDIEQYYSTQID 390
Cdd:PRK11776 322 DPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLN 366
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
28-400 |
2.30e-86 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 274.80 E-value: 2.30e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 28 TFDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRETQALILSPTREL 107
Cdd:PRK11634 7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 108 AVQIQKVVLALGDYMN-VQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKGF 186
Cdd:PRK11634 87 AVQVAEAMTDFSKHMRgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 187 KEQLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRILVKRDELTLEGIKQFFVAVDKEEwKFDTLIDLYDTLTI 266
Cdd:PRK11634 167 IEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMR-KNEALVRFLEAEDF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 267 TQAVLFCNTRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGNTRVLISTDVWARGLDVPQVSLVINYDLPNN 346
Cdd:PRK11634 246 DAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMD 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 268563240 347 RELYIHRIGRSGRFGRKGVAINFVKQDDVRILRDIEQYYSTQIDEMPMNIADII 400
Cdd:PRK11634 326 SESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAELL 379
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
27-384 |
1.29e-85 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 267.19 E-value: 1.29e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 27 PTFDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRE----TQALILS 102
Cdd:PRK11192 1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRksgpPRILILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 103 PTRELAVQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEML 182
Cdd:PRK11192 81 PTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 183 NKGFKEQLYDI-----YRylppgAQVVLLSATLPHE-ILEMTSKFMTDPIRILVKRDELTLEGIKQFFVAVDKEEWKFDT 256
Cdd:PRK11192 161 DMGFAQDIETIaaetrWR-----KQTLLFSATLEGDaVQDFAERLLNDPVEVEAEPSRRERKKIHQWYYRADDLEHKTAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 257 LIDLYDTLTITQAVLFCNTRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGNTRVLISTDVWARGLDVPQVS 336
Cdd:PRK11192 236 LCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVS 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 268563240 337 LVINYDLPNNRELYIHRIGRSGRFGRKGVAINFVKQDDVRILRDIEQY 384
Cdd:PRK11192 316 HVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERY 363
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
38-228 |
7.34e-85 |
|
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: 256.60 E-value: 7.34e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 38 LLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQ----VRETQALILSPTRELAVQIQK 113
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEpkkkGRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 114 VVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKGFKEQLYDI 193
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 268563240 194 YRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRI 228
Cdd:cd00268 161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
28-392 |
3.29e-83 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 261.67 E-value: 3.29e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 28 TFDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQV------RETQALIL 101
Cdd:PRK10590 2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQphakgrRPVRALIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 102 SPTRELAVQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEM 181
Cdd:PRK10590 82 TPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 182 LNKGFkeqLYDIYRY---LPPGAQVVLLSATLPHEILEMTSKFMTDPIRILVKRDELTLEGIKQFFVAVDKEEwKFDTLI 258
Cdd:PRK10590 162 LDMGF---IHDIRRVlakLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKR-KRELLS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 259 DLYDTLTITQAVLFCNTRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGNTRVLISTDVWARGLDVPQVSLV 338
Cdd:PRK10590 238 QMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHV 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 268563240 339 INYDLPNNRELYIHRIGRSGRFGRKGVAINFVKQDDVRILRDIEQYYSTQIDEM 392
Cdd:PRK10590 318 VNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRI 371
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
29-393 |
7.89e-75 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 240.58 E-value: 7.89e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 29 FDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVL-QSLDTQVR------ETQALIL 101
Cdd:PRK01297 89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIInQLLQTPPPkerymgEPRALII 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 102 SPTRELAVQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDyGQH--VVSGTPGRVFDMIRRRNLRTRAIKLLVLDEAD 179
Cdd:PRK01297 169 APTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLE-ARFcdILVATPGRLLDFNQRGEVHLDMVEVMVLDEAD 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 180 EMLNKGFKEQLYDIYRYLPPGA--QVVLLSATLPHEILEMTSKFMTDPIRILVKRDELTLEGIKQFFVAVDKEEwKFDTL 257
Cdd:PRK01297 248 RMLDMGFIPQVRQIIRQTPRKEerQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSD-KYKLL 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 258 IDLYDTLTITQAVLFCNTRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGNTRVLISTDVWARGLDVPQVSL 337
Cdd:PRK01297 327 YNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISH 406
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 268563240 338 VINYDLPNNRELYIHRIGRSGRFGRKGVAINFVKQDDVRILRDIEQYYSTQID-EMP 393
Cdd:PRK01297 407 VINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKIScEMP 463
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
34-228 |
1.79e-71 |
|
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: 222.45 E-value: 1.79e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 34 LREDLLRGIYAYGFEKPSAIQQRAIPAILKA--RDVIAQAQSGTGKTATFSISVLQSLDTQVRETQALILSPTRELAVQI 111
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 112 QKVVLALGDYMNVQCHACIGGTNL--GEDIRkldygQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLN-KGFKE 188
Cdd:cd17963 81 GEVVEKMGKFTGVKVALAVPGNDVprGKKIT-----AQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDtQGHGD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 268563240 189 QLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRI 228
Cdd:cd17963 156 QSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
28-394 |
1.65e-70 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 231.76 E-value: 1.65e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 28 TFDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSL-------DTQVRETQALI 100
Cdd:PRK04537 10 TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlsrpalaDRKPEDPRALI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 101 LSPTRELAVQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRT-RAIKLLVLDEAD 179
Cdd:PRK04537 90 LAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVVSlHACEICVLDEAD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 180 EMLNKGFKEQLYDIYRYLPPGA--QVVLLSATLPHEILEMTSKFMTDPIRILVKRDELTLEGIKQ--FFVAvdkEEWKFD 255
Cdd:PRK04537 170 RMFDLGFIKDIRFLLRRMPERGtrQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQriYFPA---DEEKQT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 256 TLIDLYDTLTITQAVLFCNTRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGNTRVLISTDVWARGLDVPQV 335
Cdd:PRK04537 247 LLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGV 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 268563240 336 SLVINYDLPNNRELYIHRIGRSGRFGRKGVAINFVKQDDVRILRDIEQYYSTQIDEMPM 394
Cdd:PRK04537 327 KYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKIPVEPV 385
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
29-228 |
6.27e-69 |
|
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or p54) participates in mRNA regulation mediated by miRNA-mediated silencing. It also plays a role in global and transcript-specific messenger RNA (mRNA) storage, translational repression, and decay. It is a member of the DEAD-box helicase family, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350698 [Multi-domain] Cd Length: 201 Bit Score: 216.01 E-value: 6.27e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 29 FDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRETQALILSPTRELA 108
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 109 VQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKGFKE 188
Cdd:cd17940 81 LQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 268563240 189 QLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRI 228
Cdd:cd17940 161 IIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
29-389 |
4.50e-67 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 218.69 E-value: 4.50e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 29 FDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSL-------DTQVRETQALIL 101
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLlshpapeDRKVNQPRALIM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 102 SPTRELAVQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEM 181
Cdd:PRK04837 90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 182 LNKGFKEQLYDIYRYLPPGAQ--VVLLSATLPHEILEMTSKFMTDPIRILVKRDELTLEGIKQFFVAVDKEEwKFDTLID 259
Cdd:PRK04837 170 FDLGFIKDIRWLFRRMPPANQrlNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYPSNEE-KMRLLQT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 260 LYDTLTITQAVLFCNTRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGNTRVLISTDVWARGLDVPQVSLVI 339
Cdd:PRK04837 249 LIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVF 328
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 268563240 340 NYDLPNNRELYIHRIGRSGRFGRKGVAINFVKQDDVRILRDIEQYYSTQI 389
Cdd:PRK04837 329 NYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIGHSI 378
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
26-383 |
9.16e-67 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 221.19 E-value: 9.16e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 26 IPTFDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRETQA-----LI 100
Cdd:PTZ00110 129 VVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGdgpivLV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 101 LSPTRELAVQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADE 180
Cdd:PTZ00110 209 LAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADR 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 181 MLNKGFKEQLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTD-PIRILVKRDELTL-EGIKQFFVAVDKEEwKFDTLI 258
Cdd:PTZ00110 289 MLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDLTAcHNIKQEVFVVEEHE-KRGKLK 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 259 DLYDTLTI--TQAVLFCNTRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGNTRVLISTDVWARGLDVPQVS 336
Cdd:PTZ00110 368 MLLQRIMRdgDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVK 447
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 268563240 337 LVINYDLPNNRELYIHRIGRSGRFGRKGVAINFVKQDD-------VRILRDIEQ 383
Cdd:PTZ00110 448 YVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKyrlardlVKVLREAKQ 501
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
26-383 |
1.44e-66 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 220.04 E-value: 1.44e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 26 IPTFDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVL--------QSLDTQvRETQ 97
Cdd:PLN00206 120 ILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIIsrcctirsGHPSEQ-RNPL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 98 ALILSPTRELAVQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDE 177
Cdd:PLN00206 199 AMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDE 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 178 ADEMLNKGFKEQLYDIYRYLPPgAQVVLLSATLPHEILEMTSKFMTDPIRILVKRDELTLEGIKQFFVAVDKEEWKfdtl 257
Cdd:PLN00206 279 VDCMLERGFRDQVMQIFQALSQ-PQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKK---- 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 258 IDLYDTLTITQ-----AVLFCNTRRKVDWLTDKMKEAN-FTVSSMHGDMEQKDRDEVMKEFRAGNTRVLISTDVWARGLD 331
Cdd:PLN00206 354 QKLFDILKSKQhfkppAVVFVSSRLGADLLANAITVVTgLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVD 433
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 268563240 332 VPQVSLVINYDLPNNRELYIHRIGRSGRFGRKGVAINFVKQDDVRILRDIEQ 383
Cdd:PLN00206 434 LLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVA 485
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
38-228 |
2.60e-62 |
|
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: 198.64 E-value: 2.60e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 38 LLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRETQALILSPTRELAVQIQKVVLA 117
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 118 LGDYM-NVQCHACIGGTNLGEDIRKLDyGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKGFKEQLYDIYRY 196
Cdd:cd17943 81 IGKKLeGLKCEVFIGGTPVKEDKKKLK-GCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSS 159
|
170 180 190
....*....|....*....|....*....|..
gi 268563240 197 LPPGAQVVLLSATLPHEILEMTSKFMTDPIRI 228
Cdd:cd17943 160 LPKNKQVIAFSATYPKNLDNLLARYMRKPVLV 191
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
240-370 |
2.21e-61 |
|
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350174 [Multi-domain] Cd Length: 131 Bit Score: 194.26 E-value: 2.21e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 240 IKQFFVAVDKEEWKFDTLIDLYDTLTITQAVLFCNTRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGNTRV 319
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 268563240 320 LISTDVWARGLDVPQVSLVINYDLPNNRELYIHRIGRSGRFGRKGVAINFV 370
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
51-216 |
5.07e-57 |
|
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: 184.37 E-value: 5.07e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 51 SAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRETQALILSPTRELAVQIQKVVLALGDYMNVQCHACI 130
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 131 GGTNLGEDIRKLDyGQHVVSGTPGRVFDMIRRRNlRTRAIKLLVLDEADEMLNKGFKEQLYDIYRYLPPGAQVVLLSATL 210
Cdd:pfam00270 81 GGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATL 158
|
....*.
gi 268563240 211 PHEILE 216
Cdd:pfam00270 159 PRNLED 164
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
42-243 |
9.28e-55 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 179.61 E-value: 9.28e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 42 IYAYGFEKPSAIQQRAIPAILK-ARDVIAQAQSGTGKTATFSISVLQSLDTQvRETQALILSPTRELAVQIQKVVLALGD 120
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSgLRDVILAAPTGSGKTLAALLPALEALKRG-KGGRVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 121 YMNVQCHACIGGTNLGEDIRKLDYGQ-HVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKGFKEQLYDIYRYLPP 199
Cdd:smart00487 80 SLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 268563240 200 GAQVVLLSATLPHEILEMTSKFMTDPIRILVKRdeLTLEGIKQF 243
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
28-228 |
1.39e-53 |
|
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: 176.73 E-value: 1.39e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 28 TFDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLdtQVRETQ----ALILSP 103
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKL--KAHSPTvgarALILSP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 104 TRELAVQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLN 183
Cdd:cd17959 80 TRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 268563240 184 KGFKEQLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRI 228
Cdd:cd17959 160 MGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
29-230 |
8.44e-53 |
|
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and is required for the export of mRNA out of the nucleus. DDX39B is an essential splicing factor required for association of U2 small nuclear ribonucleoprotein with pre-mRNA, and it also plays an important role in mRNA export from the nucleus to the cytoplasm. Diseases associated with DDX39A (also called UAP56-Related Helicase, 49 kDa) include gastrointestinal stromal tumor and inflammatory bowel disease 6, while diseases associated with DDX39B (also called 56 kDa U2AF65-Associated Protein) include Plasmodium vivax malaria. DDX39 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350708 [Multi-domain] Cd Length: 208 Bit Score: 174.84 E-value: 8.44e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 29 FDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRETQALILSPTRELA 108
Cdd:cd17950 4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRELA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 109 VQIQKVVLALGDYM-NVQCHACIGGTNLGEDIRKL-DYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNK-G 185
Cdd:cd17950 84 FQISNEYERFSKYMpNVKTAVFFGGVPIKKDIEVLkNKCPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLEQlD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 268563240 186 FKEQLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRILV 230
Cdd:cd17950 164 MRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
29-225 |
3.19e-52 |
|
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: 173.18 E-value: 3.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 29 FDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRETQALILSPTRELA 108
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 109 VQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRT---RAIKLLVLDEADEMLNKG 185
Cdd:cd17955 81 YQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDTTkvlSRVKFLVLDEADRLLTGS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 268563240 186 FKEQLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDP 225
Cdd:cd17955 161 FEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
38-228 |
1.03e-50 |
|
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: 168.97 E-value: 1.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 38 LLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSL---DTQVRETQALILSPTRELAVQIQKV 114
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLlyrPKKKAATRVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 115 VLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRR-RNLRTRAIKLLVLDEADEMLNKGFKEQLYDI 193
Cdd:cd17947 81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNsPSFDLDSIEILVLDEADRMLEEGFADELKEI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 268563240 194 YRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRI 228
Cdd:cd17947 161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
28-228 |
1.01e-49 |
|
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: 166.72 E-value: 1.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 28 TFDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRETQALILSPTREL 107
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 108 AVQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRN-LRTRAIKLLVLDEADEMLNKGF 186
Cdd:cd17954 81 AQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLKFLVMDEADRLLNMDF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 268563240 187 KEQLYDIYRYLPPGAQVVLLSATlpheileMTSKF-------MTDPIRI 228
Cdd:cd17954 161 EPEIDKILKVIPRERTTYLFSAT-------MTTKVaklqrasLKNPVKI 202
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
28-232 |
7.62e-48 |
|
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: 162.27 E-value: 7.62e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 28 TFDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSL----------DTQVRETQ 97
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLledgppsvgrGRRKAYPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 98 ALILSPTRELAVQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDE 177
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 268563240 178 ADEMLNKGFKEQLYDIYRY--LPPGA--QVVLLSATLPHEILEMTSKFMTDPIRILVKR 232
Cdd:cd17967 161 ADRMLDMGFEPQIRKIVEHpdMPPKGerQTLMFSATFPREIQRLAADFLKNYIFLTVGR 219
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
8-222 |
2.55e-46 |
|
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: 159.75 E-value: 2.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 8 KNDDMAtVEFESSEEVSIIPTFDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQ 87
Cdd:cd18052 25 KYDEIP-VEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 88 SLDTQ---------VRETQALILSPTRELAVQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFD 158
Cdd:cd18052 104 GMMKEgltassfseVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLD 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 268563240 159 MIRRRNLRTRAIKLLVLDEADEMLNKGFKEQLYDIYRYL--PPGA--QVVLLSATLPHEILEMTSKFM 222
Cdd:cd18052 184 FIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPgmPSKEdrQTLMFSATFPEEIQRLAAEFL 251
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
38-222 |
8.68e-45 |
|
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: 153.89 E-value: 8.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 38 LLRGIYAYGFEKPSAIQQRAIPAILKAR-DVIAQAQSGTGKTATFSISVLQSL-----DTQVRETQALILSPTRELAVQI 111
Cdd:cd17964 5 LLKALTRMGFETMTPVQQKTLKPILSTGdDVLARAKTGTGKTLAFLLPAIQSLlntkpAGRRSGVSALIISPTRELALQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 112 QKVVLALGDYM-NVQCHACIGGTNLGEDIRKL-DYGQHVVSGTPGRVFDMIRRRNLRTRA--IKLLVLDEADEMLNKGFK 187
Cdd:cd17964 85 AAEAKKLLQGLrKLRVQSAVGGTSRRAELNRLrRGRPDILVATPGRLIDHLENPGVAKAFtdLDYLVLDEADRLLDMGFR 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 268563240 188 EQLYDIYRYLPPGA----QVVLLSATLPHEILEMTSKFM 222
Cdd:cd17964 165 PDLEQILRHLPEKNadprQTLLFSATVPDEVQQIARLTL 203
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
26-236 |
2.85e-44 |
|
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: 153.25 E-value: 2.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 26 IPTFDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILK--ARDVIAQAQSGTGKTATFSISVLQSLDTQVRETQALILSP 103
Cdd:cd18048 17 VKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLAdpPQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLSP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 104 TRELAVQIQKVVLALGDYMN-VQCHACIGGTNLGediRKLDYGQHVVSGTPGRVFD-MIRRRNLRTRAIKLLVLDEADEM 181
Cdd:cd18048 97 TFELALQTGKVVEEMGKFCVgIQVIYAIRGNRPG---KGTDIEAQIVIGTPGTVLDwCFKLRLIDVTNISVFVLDEADVM 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 268563240 182 LN-KGFKEQLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRILVKRDELT 236
Cdd:cd18048 174 INvQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
26-228 |
1.91e-43 |
|
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: 150.99 E-value: 1.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 26 IPTFDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQ--VRETQ---ALI 100
Cdd:cd17953 11 IQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQrpVKPGEgpiGLI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 101 LSPTRELAVQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMI---RRRNLRTRAIKLLVLDE 177
Cdd:cd17953 91 MAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtanNGRVTNLRRVTYVVLDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 268563240 178 ADEMLNKGFKEQLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRI 228
Cdd:cd17953 171 ADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
38-228 |
2.42e-43 |
|
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: 149.62 E-value: 2.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 38 LLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRETQALILSPTRELAVQIQKVVLA 117
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 118 LGD-YMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKGFKEQLYDIYRY 196
Cdd:cd17962 81 LMKgLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILEN 160
|
170 180 190
....*....|....*....|....*....|..
gi 268563240 197 LPPGAQVVLLSATLPHEILEMTSKFMTDPIRI 228
Cdd:cd17962 161 ISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
38-230 |
2.94e-43 |
|
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: 149.66 E-value: 2.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 38 LLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRET--QALILSPTRELAVQIQKVV 115
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKKglRALILAPTRELASQIYREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 116 LALGDYMNVQCHACIGGTNLG-----EDIRKLDygqhVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKGFKEQL 190
Cdd:cd17957 81 LKLSKGTGLRIVLLSKSLEAKakdgpKSITKYD----ILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQT 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 268563240 191 YDIYRYLP-PGAQVVLLSATLPHEILEMTSKFMTDPIRILV 230
Cdd:cd17957 157 DEILAACTnPNLQRSLFSATIPSEVEELARSVMKDPIRIIV 197
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
29-225 |
3.83e-43 |
|
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: 149.39 E-value: 3.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 29 FDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSldtqvreTQALILSPTRELA 108
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQI-------VVALILEPSRELA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 109 VQIQKVVLALGDYMN---VQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKG 185
Cdd:cd17938 74 EQTYNCIENFKKYLDnpkLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 268563240 186 FKEQLYDIYRYLPPGA------QVVLLSATLpH--EILEMTSKFMTDP 225
Cdd:cd17938 154 NLETINRIYNRIPKITsdgkrlQVIVCSATL-HsfEVKKLADKIMHFP 200
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
38-228 |
1.17e-42 |
|
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: 147.95 E-value: 1.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 38 LLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQvRETQ------ALILSPTRELAVQI 111
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQ-RELEkgegpiAVIVAPTRELAQQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 112 QKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKGFKEQLY 191
Cdd:cd17952 80 YLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 268563240 192 DIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRI 228
Cdd:cd17952 160 SIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
38-226 |
1.40e-42 |
|
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: 148.12 E-value: 1.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 38 LLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSL------DTQVRETQALILSPTRELAVQI 111
Cdd:cd17961 5 LLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlkakaeSGEEQGTRALILVPTRELAQQV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 112 QKVVLALGDYMN--VQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRA-IKLLVLDEADEMLNKGFKE 188
Cdd:cd17961 85 SKVLEQLTAYCRkdVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLLStLKYLVIDEADLVLSYGYEE 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 268563240 189 QLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPI 226
Cdd:cd17961 165 DLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
38-228 |
4.24e-42 |
|
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: 146.75 E-value: 4.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 38 LLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRETQ-----ALILSPTRELAVQIQ 112
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERgdgpiVLVLAPTRELAQQIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 113 KVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKGFKEQLYD 192
Cdd:cd17966 81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 268563240 193 IYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRI 228
Cdd:cd17966 161 IVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
38-228 |
3.26e-40 |
|
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: 141.56 E-value: 3.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 38 LLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSL---DTQVRETQ--ALILSPTRELAVQIQ 112
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrKANLKKGQvgALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 113 KVVLALGDYM--NVQCHACIGGTNLGEDIRKLD-YGQHVVSGTPGRVFDMIRRRN--LRTRAIKLLVLDEADEMLNKGFK 187
Cdd:cd17960 81 EVLQSFLEHHlpKLKCQLLIGGTNVEEDVKKFKrNGPNILVGTPGRLEELLSRKAdkVKVKSLEVLVLDEADRLLDLGFE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 268563240 188 EQLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRI 228
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
38-228 |
7.88e-40 |
|
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: 141.30 E-value: 7.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 38 LLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRET--------QALILSPTRELAV 109
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDeetkddgpYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 110 QIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKGFKEQ 189
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 268563240 190 LYDIYRYLPPGA--------------------QVVLLSATLPHEILEMTSKFMTDPIRI 228
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 ... |
39-230 |
4.02e-39 |
|
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin gene, NUP98, by inversion 11 (p15q22) chromosome translocation is found in the patients with de novo or therapy-related myeloid malignancies. Diseases associated with DDX10 (also known as DDX10-NUP98 Fusion Protein Type 2) include myelodysplastic syndrome and leukemia, acute myeloid. DDX10 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350699 [Multi-domain] Cd Length: 198 Bit Score: 138.58 E-value: 4.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 39 LRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLdtqVRE-------TQALILSPTRELAVQI 111
Cdd:cd17941 2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKL---YRErwtpedgLGALIISPTRELAMQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 112 QKVVLALGDYMNVQCHACIGGTNLGEDIRKLDyGQHVVSGTPGRVFD-MIRRRNLRTRAIKLLVLDEADEMLNKGFKEQL 190
Cdd:cd17941 79 FEVLRKVGKYHSFSAGLIIGGKDVKEEKERIN-RMNILVCTPGRLLQhMDETPGFDTSNLQMLVLDEADRILDMGFKETL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 268563240 191 YDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRILV 230
Cdd:cd17941 158 DAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
26-232 |
8.89e-39 |
|
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: 139.40 E-value: 8.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 26 IPTFDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQ------------- 92
Cdd:cd18051 20 IETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQgpgeslpsesgyy 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 93 VRETQ---ALILSPTRELAVQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRA 169
Cdd:cd18051 100 GRRKQyplALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDY 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 268563240 170 IKLLVLDEADEMLNKGFKEQLYDIYRY--LPPGA--QVVLLSATLPHEILEMTSKFMTDPIRILVKR 232
Cdd:cd18051 180 CKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPTGerQTLMFSATFPKEIQMLARDFLDNYIFLAVGR 246
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
39-209 |
2.94e-38 |
|
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: 136.34 E-value: 2.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 39 LRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATF---SISVLQSLDTQVRE-TQALILSPTRELAVQIQKV 114
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFlipAIELLYKLKFKPRNgTGVIIISPTRELALQIYGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 115 VLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIR-RRNLRTRAIKLLVLDEADEMLNKGFKEQLYDI 193
Cdd:cd17942 82 AKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQnTKGFLYKNLQCLIIDEADRILEIGFEEEMRQI 161
|
170
....*....|....*.
gi 268563240 194 YRYLPPGAQVVLLSAT 209
Cdd:cd17942 162 IKLLPKRRQTMLFSAT 177
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
28-225 |
3.00e-38 |
|
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: 136.77 E-value: 3.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 28 TFDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILK--ARDVIAQAQSGTGKTATFSISVLQSLDTQVRETQALILSPTR 105
Cdd:cd18047 2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAepPQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 106 ELAVQIQKVVLALGD-YMNVQCHACIGGTNLGEDIRKLDygqHVVSGTPGRVFD-MIRRRNLRTRAIKLLVLDEADEML- 182
Cdd:cd18047 82 ELALQTGKVIEQMGKfYPELKLAYAVRGNKLERGQKISE---QIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADVMIa 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 268563240 183 NKGFKEQLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDP 225
Cdd:cd18047 159 TQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
38-228 |
3.21e-37 |
|
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: 134.00 E-value: 3.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 38 LLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSIS-VLQSLDTQVR-------ETQALILSPTRELAV 109
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPlIMFALEQEKKlpfikgeGPYGLIVCPSRELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 110 QIQKVV------LALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLN 183
Cdd:cd17951 81 QTHEVIeyyckaLQEGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 268563240 184 KGFKEQLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRI 228
Cdd:cd17951 161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
252-361 |
5.87e-37 |
|
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: 130.02 E-value: 5.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 252 WKFDTLIDLYDTLTITQAVLFCNTRRKVDwlTDKMKEA-NFTVSSMHGDMEQKDRDEVMKEFRAGNTRVLISTDVWARGL 330
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLE--AELLLEKeGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
|
90 100 110
....*....|....*....|....*....|.
gi 268563240 331 DVPQVSLVINYDLPNNRELYIHRIGRSGRFG 361
Cdd:pfam00271 79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
38-228 |
5.30e-36 |
|
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: 130.66 E-value: 5.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 38 LLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQV--RETQ----ALILSPTRELAVQI 111
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPipREQRngpgVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 112 QKVVLALgDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKGFKEQLY 191
Cdd:cd17958 81 EAECSKY-SYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 268563240 192 DIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRI 228
Cdd:cd17958 160 KILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
46-228 |
1.34e-34 |
|
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: 127.32 E-value: 1.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 46 GFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFS---ISVLQSLDTQVRETQ---ALILSPTRELAVQIQKVVLALG 119
Cdd:cd17949 10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLlpiIQRLLSLEPRVDRSDgtlALVLVPTRELALQIYEVLEKLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 120 DYM-NVQCHACIGGTNLGED---IRKldyGQHVVSGTPGRVFDMIRR-RNLRTRAIKLLVLDEADEMLNKGFKEQLYDIY 194
Cdd:cd17949 90 KPFhWIVPGYLIGGEKRKSEkarLRK---GVNILIATPGRLLDHLKNtQSFDVSNLRWLVLDEADRLLDMGFEKDITKIL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 268563240 195 RYL-------------PPGAQVVLLSATLPHEILEMTSKFMTDPIRI 228
Cdd:cd17949 167 ELLddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
38-210 |
4.72e-34 |
|
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: 126.58 E-value: 4.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 38 LLRGIYAYGFEKPSAIQQRAIPAILKAR-DVIAQAQSGTGKTATFSISVLQSLDTQVRET---------QALILSPTREL 107
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRDGkDVIGAAETGSGKTLAFGIPILERLLSQKSSNgvggkqkplRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 108 AVQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNL---RTRAIKLLVLDEADEMLNK 184
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEhlaNLKSLRFLVLDEADRMLEK 160
|
170 180 190
....*....|....*....|....*....|...
gi 268563240 185 G-FKE--QLYDIYRYLPPGA----QVVLLSATL 210
Cdd:cd17946 161 GhFAEleKILELLNKDRAGKkrkrQTFVFSATL 193
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
47-228 |
2.02e-31 |
|
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: 120.50 E-value: 2.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 47 FEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRETQA-----LILSPTRELAVQIQKVVLALGDY 121
Cdd:cd18050 82 FKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGdgpicLVLAPTRELAQQVQQVADDYGKS 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 122 MNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKGFKEQLYDIYRYLPPGA 201
Cdd:cd18050 162 SRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDR 241
|
170 180
....*....|....*....|....*..
gi 268563240 202 QVVLLSATLPHEILEMTSKFMTDPIRI 228
Cdd:cd18050 242 QTLMWSATWPKEVRQLAEDFLRDYVQI 268
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
16-228 |
2.75e-31 |
|
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: 118.96 E-value: 2.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 16 EFESSEEVSI--------IPTFDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQ 87
Cdd:cd18049 5 QYRRSKEITVrghncpkpVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 88 SLDTQVRETQA-----LILSPTRELAVQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRR 162
Cdd:cd18049 85 HINHQPFLERGdgpicLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 268563240 163 RNLRTRAIKLLVLDEADEMLNKGFKEQLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRI 228
Cdd:cd18049 165 GKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHI 230
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
280-361 |
6.16e-31 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 113.08 E-value: 6.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 280 DWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGNTRVLISTDVWARGLDVPQVSLVINYDLPNNRELYIHRIGRSGR 359
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 268563240 360 FG 361
Cdd:smart00490 81 AG 82
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
53-222 |
3.87e-29 |
|
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: 112.25 E-value: 3.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 53 IQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQV------RETQALILSPTRELAVQIQKVVLALGDYMNVQC 126
Cdd:cd17944 16 IQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQqprkrgRAPKVLVLAPTRELANQVTKDFKDITRKLSVAC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 127 HacIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKGFKEQLYDI----YRYLPP-GA 201
Cdd:cd17944 96 F--YGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEIlsvsYKKDSEdNP 173
|
170 180
....*....|....*....|.
gi 268563240 202 QVVLLSATLPHEILEMTSKFM 222
Cdd:cd17944 174 QTLLFSATCPDWVYNVAKKYM 194
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
38-220 |
1.35e-28 |
|
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: 111.69 E-value: 1.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 38 LLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSL-------DTQVRETQALILSPTRELAVQ 110
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLlrykllaEGPFNAPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 111 IQKVVLALGDYMNVQCHaCIGGTNLGEDIRKLDYGQ-HVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKGFKEQ 189
Cdd:cd17948 81 IGSVAQSLTEGLGLKVK-VITGGRTKRQIRNPHFEEvDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 268563240 190 LYDIYRYLP-------------PGAQVVLLSATLPHEILEMTSK 220
Cdd:cd17948 160 LSHFLRRFPlasrrsentdgldPGTQLVLVSATMPSGVGEVLSK 203
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
66-209 |
9.86e-22 |
|
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: 90.54 E-value: 9.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 66 DVIAQAQSGTGKTATFSISVLQSLDTQvrETQALILSPTRELAVQIQKVVLALGDyMNVQCHACIGGTNLGEDIRKLDYG 145
Cdd:cd00046 3 NVLITAPTGSGKTLAALLAALLLLLKK--GKKVLVLVPTKALALQTAERLRELFG-PGIRVAVLVGGSSAEEREKNKLGD 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 268563240 146 QHVVSGTPGRVFDMIRR-RNLRTRAIKLLVLDEADEMLNKGFKEQLYD--IYRYLPPGAQVVLLSAT 209
Cdd:cd00046 80 ADIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLIDSRGALILDlaVRKAGLKNAQVILLSAT 146
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
38-210 |
2.00e-21 |
|
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: 91.92 E-value: 2.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 38 LLRGIYAYGFEKPSAIQQRAIPAILKA---------RDVIAQAQSGTGKTATFSISVLQSL-DTQVRETQALILSPTREL 107
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALsKRVVPRLRALIVVPTKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 108 AVQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQH---------VVSgTPGRVFDMIRR------RNLRtraikL 172
Cdd:cd17956 81 VQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTSgrylsrvdiLVA-TPGRLVDHLNStpgftlKHLR-----F 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 268563240 173 LVLDEADEMLNKGFKEQLYDIYRYL--------------------PPGAQVVLLSATL 210
Cdd:cd17956 155 LVIDEADRLLNQSFQDWLETVMKALgrptapdlgsfgdanllersVRPLQKLLFSATL 212
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
268-367 |
1.36e-14 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 75.54 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 268 QAVLFCNTRRKVDWLTDKMKEANFTV------SSMHGD--MEQKDRDEVMKEFRAGNTRVLISTDVWARGLDVPQVSLVI 339
Cdd:COG1111 355 RIIVFTQYRDTAEMIVEFLSEPGIKAgrfvgqASKEGDkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVI 434
|
90 100 110
....*....|....*....|....*....|
gi 268563240 340 NYDL-PNnrEL-YIHRIGRSGRFGRKGVAI 367
Cdd:COG1111 435 FYEPvPS--EIrSIQRKGRTGRKREGRVVV 462
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
254-356 |
1.59e-14 |
|
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: 70.31 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 254 FDTLIDLYDTLTITQAVLFCNTRRKVDWLTDKMKE-----ANFTVSSMHG----------DMEQKDRDEVMKEFRAGNTR 318
Cdd:cd18802 13 IEILREYFPKTPDFRGIIFVERRATAVVLSRLLKEhpstlAFIRCGFLIGrgnssqrkrsLMTQRKQKETLDKFRDGELN 92
|
90 100 110
....*....|....*....|....*....|....*...
gi 268563240 319 VLISTDVWARGLDVPQVSLVINYDLPNNRELYIHRIGR 356
Cdd:cd18802 93 LLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR 130
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
33-385 |
2.47e-14 |
|
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: 74.87 E-value: 2.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 33 GLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLdTQVRETQALILSPTRELAV-QI 111
Cdd:COG1205 40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEAL-LEDPGATALYLYPTKALARdQL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 112 QKVV-LALGDYMNVQCHACIGGTNLGE--DIRklDYGQHVVSgTPgrvfDMI-----------RR--RNLRtraikLLVL 175
Cdd:COG1205 119 RRLReLAEALGLGVRVATYDGDTPPEErrWIR--EHPDIVLT-NP----DMLhygllphhtrwARffRNLR-----YVVI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 176 DEAdemlnkgfkeQLYD----------------IYRYLPPGAQVVLLSATL--PHEILE-MTSK---------------- 220
Cdd:COG1205 187 DEA----------HTYRgvfgshvanvlrrlrrICRHYGSDPQFILASATIgnPAEHAErLTGRpvtvvdedgsprgert 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 221 --FMTDPIRILVKRDELTLEGIKQFFVAVDKEewkfdtlidlydtltiTQAVLFCNTRRKV----DWLTDKMKEANFT-- 292
Cdd:COG1205 257 fvLWNPPLVDDGIRRSALAEAARLLADLVREG----------------LRTLVFTRSRRGAellaRYARRALREPDLAdr 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 293 VSSMHGDMEQKDRDEVMKEFRAGNTRVLISTDVWARGLDVPQVSLVINYDLPNNRELYIHRIGRSGRFGRKGVAInFVKQ 372
Cdd:COG1205 321 VAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV-LVAG 399
|
410
....*....|...
gi 268563240 373 DDVrilrdIEQYY 385
Cdd:COG1205 400 DDP-----LDQYY 407
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
54-356 |
2.97e-13 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 71.21 E-value: 2.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 54 QQRAIPAILKA-----RDVIAQAQSGTGKTaTFSISVLQSLDTQVRetqALILSPTRELAVQIQKVVLALgdymnvqcha 128
Cdd:COG1061 85 QQEALEALLAAlerggGRGLVVAPTGTGKT-VLALALAAELLRGKR---VLVLVPRRELLEQWAEELRRF---------- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 129 cIGGTNLGEDIRKLDYgqHVVSGTPGRVFDMIRRRNLRtRAIKLLVLDEADEMLNKGFKEqlydIYRYLPPgAQVVLLSA 208
Cdd:COG1061 151 -LGDPLAGGGKKDSDA--PITVATYQSLARRAHLDELG-DRFGLVIIDEAHHAGAPSYRR----ILEAFPA-AYRLGLTA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 209 T-------------LPHEILEMTSKFMTD-----PIRILVKRDELTLEG-----IKQFFVA--VDKEEWKFDTLIDLYDT 263
Cdd:COG1061 222 TpfrsdgreillflFDGIVYEYSLKEAIEdgylaPPEYYGIRVDLTDERaeydaLSERLREalAADAERKDKILRELLRE 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 264 LTITQAVL-FCNTRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGNTRVLISTDVWARGLDVPQVSLVINYD 342
Cdd:COG1061 302 HPDDRKTLvFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLR 381
|
330
....*....|....
gi 268563240 343 LPNNRELYIHRIGR 356
Cdd:COG1061 382 PTGSPREFIQRLGR 395
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
49-228 |
3.26e-13 |
|
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: 68.94 E-value: 3.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 49 KPSAIQQRAIPAILKARD-----------------VIAqAQSGTGKTATFSISVLQSLDTQVRET--------------- 96
Cdd:cd17965 30 KPSPIQTLAIKKLLKTLMrkvtkqtsneepklevfLLA-AETGSGKTLAYLAPLLDYLKRQEQEPfeeaeeeyesakdtg 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 97 --QALILSPTRELAVQIQKVVLALGDYMNVQCH---ACIGGTNlgedIRKLDYGQH---VVSGTPGRVFDMIRRRNLRTR 168
Cdd:cd17965 109 rpRSVILVPTHELVEQVYSVLKKLSHTVKLGIKtfsSGFGPSY----QRLQLAFKGridILVTTPGKLASLAKSRPKILS 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 169 AIKLLVLDEADEMLNKGFKEQLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRI 228
Cdd:cd17965 185 RVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLRKLFPDVVRI 244
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
273-379 |
1.01e-12 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 69.40 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 273 CNTRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGNTRVLISTDVWARGLDVPQVSLVINYDLPNNRELYIH 352
Cdd:COG0514 237 CLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQ 316
|
90 100
....*....|....*....|....*..
gi 268563240 353 RIGRSGRFGRKGVAINFVKQDDVRILR 379
Cdd:COG0514 317 EIGRAGRDGLPAEALLLYGPEDVAIQR 343
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
272-369 |
1.17e-12 |
|
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: 64.54 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 272 FCNTRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGNTRVLISTDVWARGLDVPQVSLVINYDLPNNRELYI 351
Cdd:cd18794 36 YCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYY 115
|
90
....*....|....*...
gi 268563240 352 HRIGRSGRFGRKGVAINF 369
Cdd:cd18794 116 QESGRAGRDGLPSECILF 133
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
253-355 |
2.82e-11 |
|
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: 60.57 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 253 KFDTLIDLYDTLTITQ--AVLFCNTRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGNT--RVLISTDVWAR 328
Cdd:cd18793 12 KLEALLELLEELREPGekVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDirVFLLSTKAGGV 91
|
90 100 110
....*....|....*....|....*....|....*.
gi 268563240 329 GLDVPQVSLVINYDLPNN---------RelyIHRIG 355
Cdd:cd18793 92 GLNLTAANRVILYDPWWNpaveeqaidR---AHRIG 124
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
270-379 |
4.14e-11 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 64.73 E-value: 4.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 270 VLFCNTRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGNTRVLISTDVWARGLDVPQVSLVINYDLPNNREL 349
Cdd:PRK11057 240 IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIES 319
|
90 100 110
....*....|....*....|....*....|
gi 268563240 350 YIHRIGRSGRFGRKGVAINFVKQDDVRILR 379
Cdd:PRK11057 320 YYQETGRAGRDGLPAEAMLFYDPADMAWLR 349
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
171-323 |
1.09e-10 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 63.18 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 171 KLLVLDEAD----EMLnKGFKEQLYDIYRYlppGAQVVLLSATLPHEILEmtskFMTDPIRILVKRDELTLEGIKQFF-- 244
Cdd:COG1203 270 SVIILDEVQayppYML-ALLLRLLEWLKNL---GGSVILMTATLPPLLRE----ELLEAYELIPDEPEELPEYFRAFVrk 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 245 -VAVDKEEWKFDTLID-LYDTLTITQAVLF-CNTRRKVDWLTDKMKEANFTVSSM--HGDMEQKDR----DEVMKEFRAG 315
Cdd:COG1203 342 rVELKEGPLSDEELAElILEALHKGKSVLViVNTVKDAQELYEALKEKLPDEEVYllHSRFCPADRseieKEIKERLERG 421
|
....*...
gi 268563240 316 NTRVLIST 323
Cdd:COG1203 422 KPCILVST 429
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
300-364 |
1.62e-10 |
|
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: 58.91 E-value: 1.62e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 268563240 300 MEQKDRDEVMKEFRAGNTRVLISTDVWARGLDVPQVSLVINYDlPNNREL-YIHRIGRSGRfGRKG 364
Cdd:cd18801 74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYD-ASPSPIrMIQRMGRTGR-KRQG 137
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
54-391 |
1.66e-10 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 62.61 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 54 QQRAIPA-ILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRetqALILSPTRELAVQI------------QKVVLALGD 120
Cdd:COG1204 27 QAEALEAgLLEGKNLVVSAPTASGKTLIAELAILKALLNGGK---ALYIVPLRALASEKyrefkrdfeelgIKVGVSTGD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 121 YMnvqchaciggtnlgEDIRKLDYGQHVVSgTPGRVFDMIRRRNLRTRAIKLLVLDEA----DEmlNKGFK-EQLYDIYR 195
Cdd:COG1204 104 YD--------------SDDEWLGRYDILVA-TPEKLDSLLRNGPSWLRDVDLVVVDEAhlidDE--SRGPTlEVLLARLR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 196 YLPPGAQVVLLSATL--PHEILE-MTSKFMTDPIRIlVKRDELTL-EGIKQFfvaVDKEEWKFDTLIDL-YDTLTI-TQA 269
Cdd:COG1204 167 RLNPEAQIVALSATIgnAEEIAEwLDAELVKSDWRP-VPLNEGVLyDGVLRF---DDGSRRSKDPTLALaLDLLEEgGQV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 270 VLFCNTRRKV----DWLTDKMK-------------------------EANFTVSSM--------HGDMEQKDRDEVMKEF 312
Cdd:COG1204 243 LVFVSSRRDAeslaKKLADELKrrltpeereeleelaeellevseetHTNEKLADClekgvafhHAGLPSELRRLVEDAF 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 313 RAGNTRVLISTDVWARGLDVPqVSLVInydLPNNRELYIHRI---------GRSGRFGR--KGVAInFVKQDDVRILRDI 381
Cdd:COG1204 323 REGLIKVLVATPTLAAGVNLP-ARRVI---IRDTKRGGMVPIpvlefkqmaGRAGRPGYdpYGEAI-LVAKSSDEADELF 397
|
410
....*....|
gi 268563240 382 EQYYSTQIDE 391
Cdd:COG1204 398 ERYILGEPEP 407
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
221-366 |
3.19e-10 |
|
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: 58.51 E-value: 3.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 221 FMTDPIRILVKRDELTLEGIKQFFVAvdkeewkfdTLIDLYDTLTITQAVLFCNtrrkvdWLTDKMKeANFTVSSMHGDM 300
Cdd:cd18811 8 FHTRLDKVYEFVREEIAKGRQAYVIY---------PLIEESEKLDLKAAVAMYE------YLKERFR-PELNVGLLHGRL 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 268563240 301 EQKDRDEVMKEFRAGNTRVLISTDVWARGLDVPQVSLVINYDlpnnrelyIHRIGRS------GRFGRKGVA 366
Cdd:cd18811 72 KSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIED--------AERFGLSqlhqlrGRVGRGDHQ 135
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
253-394 |
3.59e-10 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 61.81 E-value: 3.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 253 KFDTLIDLY-DTLTI---TQAVLFCNTRRKVDWLTDKMKEANFTV------SSMHGD--MEQKDRDEVMKEFRAGNTRVL 320
Cdd:PRK13766 348 KLEKLREIVkEQLGKnpdSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDkgMSQKEQIEILDKFRAGEFNVL 427
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 268563240 321 ISTDVWARGLDVPQVSLVINYDlPNNREL-YIHRIGRSGRfGRKGVAINFVKQDDvrilRDIEQYYSTQIDEMPM 394
Cdd:PRK13766 428 VSTSVAEEGLDIPSVDLVIFYE-PVPSEIrSIQRKGRTGR-QEEGRVVVLIAKGT----RDEAYYWSSRRKEKKM 496
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
253-379 |
9.73e-10 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 60.24 E-value: 9.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 253 KFDTLIDLYDTLTITQ--AVLFCNTRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGN--TRVLISTDVWAR 328
Cdd:COG0553 534 KLEALLELLEELLAEGekVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGGE 613
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 268563240 329 GLDVPQVSLVINYDLPNNRELYIHRIGRSGRFG-RKGV-AINFVKQD--DVRILR 379
Cdd:COG0553 614 GLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGqTRDVqVYKLVAEGtiEEKILE 668
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
172-363 |
2.32e-08 |
|
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: 55.51 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 172 LLVLDEAD--EMLNKGFKEQLYDIYRYLppGAQVVLLSATLPHEILEMTSKfmtdpIRILVKRDELTLEGIKQFFVAVDK 249
Cdd:cd09639 126 LLIFDEVHfyDEYTLALILAVLEVLKDN--DVPILLMSATLPKFLKEYAEK-----IGYVEENEPLDLKPNERAPFIKIE 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 250 EEWKFD-----TLIDLYDTLTitQAVLFCNTRRKVDWLTDKMKEANFTVSSM--HGDMEQKDR----DEVMKEFRAGNTR 318
Cdd:cd09639 199 SDKVGEissleRLLEFIKKGG--SVAIIVNTVDRAQEFYQQLKEKGPEEEIMliHSRFTEKDRakkeAELLLEFKKSEKF 276
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 268563240 319 VLISTDVWARGLDVpQVSLVINYDLPNNRelYIHRIGRSGRFGRK 363
Cdd:cd09639 277 VIVATQVIEASLDI-SVDVMITELAPIDS--LIQRLGRLHRYGEK 318
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
264-370 |
1.17e-07 |
|
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: 48.85 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 264 LTITQAVLFCNTRRKVDWLTDKMKeanftvssmhgdmeqkdrdevmkefragntrVLISTDVWARGLDVPQVSLVINYDL 343
Cdd:cd18785 1 VMVVKIIVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDP 49
|
90 100
....*....|....*....|....*...
gi 268563240 344 PNNRELYIHRIGRSGRFG-RKGVAINFV 370
Cdd:cd18785 50 PSSAASYIQRVGRAGRGGkDEGEVILFV 77
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
54-370 |
1.94e-07 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 52.96 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 54 QQRAIPAILKARDVIAQAQSGTGKTAtfsISVLQSLDTQVRETQALILSPTRELAVQIQKVVLALGDyMNVQCHACIGGT 133
Cdd:PRK01172 27 QRMAIEQLRKGENVIVSVPTAAGKTL---IAYSAIYETFLAGLKSIYIVPLRSLAMEKYEELSRLRS-LGMRVKISIGDY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 134 NLGED-IRKLDygqhVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEAdEMLNKGFK----EQLYDIYRYLPPGAQVVLLSA 208
Cdd:PRK01172 103 DDPPDfIKRYD----VVILTSEKADSLIHHDPYIINDVGLIVADEI-HIIGDEDRgptlETVLSSARYVNPDARILALSA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 209 TLPH--EILE------MTSKFMTDPIRI-LVKRDELTLEGikqffvavdKEEWKFDTLIDLYDTLTIT-QAVLFCNTRRK 278
Cdd:PRK01172 178 TVSNanELAQwlnaslIKSNFRPVPLKLgILYRKRLILDG---------YERSQVDINSLIKETVNDGgQVLVFVSSRKN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 279 VDWLTDKMKE-----ANFTVSSM--------------------HGDMEQKDRDEVMKEFRAGNTRVLISTDVWARGLDVP 333
Cdd:PRK01172 249 AEDYAEMLIQhfpefNDFKVSSEnnnvyddslnemlphgvafhHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLP 328
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 268563240 334 qVSLVINYDLPNNRELYI---------HRIGRSGRFGRKGVAINFV 370
Cdd:PRK01172 329 -ARLVIVRDITRYGNGGIrylsnmeikQMIGRAGRPGYDQYGIGYI 373
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
285-367 |
2.05e-07 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350179 [Multi-domain] Cd Length: 160 Bit Score: 50.34 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 285 KMKEANFTVSSMHGDMEQKDRDEVMKEFRAGNTRVLISTDVWARGLDVPQVSLVINYDlPNN---RELYIHRiGRSGRFG 361
Cdd:cd18792 55 KELVPEARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIED-ADRfglSQLHQLR-GRVGRGK 132
|
....*.
gi 268563240 362 RKGVAI 367
Cdd:cd18792 133 HQSYCY 138
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
275-359 |
6.89e-07 |
|
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350177 [Multi-domain] Cd Length: 171 Bit Score: 48.78 E-value: 6.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 275 TRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGNTRVLISTDVWARGLDVPQVSLVINYD------LPNNRE 348
Cdd:cd18790 36 TKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDadkegfLRSETS 115
|
90
....*....|.
gi 268563240 349 LyIHRIGRSGR 359
Cdd:cd18790 116 L-IQTIGRAAR 125
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
270-394 |
7.24e-07 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 51.44 E-value: 7.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 270 VLFCNTRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGNTRVLISTDVWARGLDVPQVSLVINYDLPNNREL 349
Cdd:PLN03137 684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEG 763
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 268563240 350 YIHRIGRSGRFG-RKGVAINFVKQDDVRILRDIEQyysTQIDEMPM 394
Cdd:PLN03137 764 YHQECGRAGRDGqRSSCVLYYSYSDYIRVKHMISQ---GGVEQSPM 806
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
271-359 |
1.13e-06 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 48.03 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 271 LFCNTRRKVDWLTDKMKEA------NFTVSSMHGDMEQKDRDEVMKEFRAGNTRVLISTDVWARGLDVPQVSLVINYDLP 344
Cdd:cd18796 43 VFTNTRSQAERLAQRLRELcpdrvpPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSP 122
|
90
....*....|....*
gi 268563240 345 NNRELYIHRIGRSGR 359
Cdd:cd18796 123 KSVARLLQRLGRSGH 137
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
296-339 |
3.40e-06 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 48.99 E-value: 3.40e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 268563240 296 MHGDMEQKDRDEVMKEFRAGNTRVLISTDVWARGLDVPQVSL-VI 339
Cdd:PRK10917 511 LHGRMKPAEKDAVMAAFKAGEIDILVATTVIEVGVDVPNATVmVI 555
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
53-211 |
7.53e-06 |
|
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: 46.10 E-value: 7.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 53 IQQRAIPAILKARD-VIAQAQSGTGKTATFSISVLQSLDTQvrETQALILSPTRELAVQI------------QKVVLALG 119
Cdd:cd17921 5 IQREALRALYLSGDsVLVSAPTSSGKTLIAELAILRALATS--GGKAVYIAPTRALVNQKeadlrerfgplgKNVGLLTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 120 DYmnvqchaciggTNLGEDIRKLDygqhVVSGTPGRVFDMIRR-RNLRTRAIKLLVLDEAdEMLNKGFK----EQLYDIY 194
Cdd:cd17921 83 DP-----------SVNKLLLAEAD----ILVATPEKLDLLLRNgGERLIQDVRLVVVDEA-HLIGDGERgvvlELLLSRL 146
|
170
....*....|....*..
gi 268563240 195 RYLPPGAQVVLLSATLP 211
Cdd:cd17921 147 LRINKNARFVGLSATLP 163
|
|
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
289-339 |
9.86e-06 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 47.74 E-value: 9.86e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 268563240 289 ANFTVSSMHGDMEQKDRDEVMKEFRAGNTRVLISTDVWARGLDVPQVSL-VI 339
Cdd:COG1200 502 PGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTVIEVGVDVPNATVmVI 553
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
268-367 |
3.93e-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: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 268 QAVLFCNTRRKVDWLTDKMKEANFtvssMHGDMEQKDRDEVMKEFRAGNTRVLISTDVWARGLDVPQVSLVIN----YDL 343
Cdd:cd18795 45 PVLVFCSSRKECEKTAKDLAGIAF----HHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKgtqrYDG 120
|
90 100 110
....*....|....*....|....*....|
gi 268563240 344 PNNREL----YIHRIGRSGR--FGRKGVAI 367
Cdd:cd18795 121 KGYRELspleYLQMIGRAGRpgFDTRGEAI 150
|
|
| SF2_C_priA |
cd18804 |
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ... |
302-367 |
4.45e-05 |
|
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350191 [Multi-domain] Cd Length: 238 Bit Score: 44.54 E-value: 4.45e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 268563240 302 QKDRDEVMKEFRAGNTRVLISTDVWARGLDVPQVSLV--INYD----LPNNR------ELYIHRIGRSGRFGRKGVAI 367
Cdd:cd18804 130 KGALEKLLDQFERGEIDILIGTQMIAKGLDFPNVTLVgiLNADsglnSPDFRaserafQLLTQVSGRAGRGDKPGKVI 207
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
297-366 |
6.72e-05 |
|
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF 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: 350197 [Multi-domain] Cd Length: 151 Bit Score: 42.72 E-value: 6.72e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 268563240 297 HGDMEQKDRDEVMKEFRAGNTRVLISTDVWARGLDVPQVSLVI--NYDLPNNRELYIHRiGRSGRFGRKGVA 366
Cdd:cd18810 58 HGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIieRADKFGLAQLYQLR-GRVGRSKERAYA 128
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
36-217 |
9.55e-05 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 42.91 E-value: 9.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 36 EDLLRGIYayGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLqsldtqVRETQALILSPTRELavqIQKVV 115
Cdd:cd17920 1 EQILKEVF--GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPAL------LLDGVTLVVSPLISL---MQDQV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 116 LALGDyMNVQChACIGGTNLGEDIR----KLDYGQ-HVVSGTP-----GRVFDMIRRRNLRTRaIKLLVLDEA------- 178
Cdd:cd17920 70 DRLQQ-LGIRA-AALNSTLSPEEKRevllRIKNGQyKLLYVTPerllsPDFLELLQRLPERKR-LALIVVDEAhcvsqwg 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 268563240 179 ----DEMLNKG-FKEQLYDIyrylppgaQVVLLSATLP----HEILEM 217
Cdd:cd17920 147 hdfrPDYLRLGrLRRALPGV--------PILALTATATpevrEDILKR 186
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
268-367 |
1.13e-04 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 41.86 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 268 QAVLFCNTRRKVD----WLTDKMKEANF---TVSSMHGDMEQKDRDEVMKEFRAGNTRVLISTDVWARGLDVPQVSLVIN 340
Cdd:cd18797 37 KTIVFCRSRKLAElllrYLKARLVEEGPlasKVASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVL 116
|
90 100
....*....|....*....|....*..
gi 268563240 341 YDLPNNRELYIHRIGRSGRFGRKGVAI 367
Cdd:cd18797 117 AGYPGSLASLWQQAGRAGRRGKDSLVI 143
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
54-210 |
1.21e-04 |
|
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: 42.57 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 54 QQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLdTQVRETQALILSPTRELAvQIQKVVL-ALGDYM--NVQCHACI 130
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEAL-LRDPGSRALYLYPTKALA-QDQLRSLrELLEQLglGIRVATYD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 131 GGTNLGEDIRKLDYGQHVVSGTPgrvfDMI----------RRRNLRTraIKLLVLDEAdEMLNKGFK-------EQLYDI 193
Cdd:cd17923 83 GDTPREERRAIIRNPPRILLTNP----DMLhyallphhdrWARFLRN--LRYVVLDEA-HTYRGVFGshvalllRRLRRL 155
|
170
....*....|....*..
gi 268563240 194 YRYLPPGAQVVLLSATL 210
Cdd:cd17923 156 CRRYGADPQFILTSATI 172
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
49-125 |
6.34e-04 |
|
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: 40.48 E-value: 6.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 49 KPSAIQQRAIPAILK------ARDVIAQAQSGTGKTATFSISVLQSLDtqvRETQALILSPTRELAVQIQKVVLALGDYM 122
Cdd:cd17918 15 SLTKDQAQAIKDIEKdlhspePMDRLLSGDVGSGKTLVALGAALLAYK---NGKQVAILVPTEILAHQHYEEARKFLPFI 91
|
...
gi 268563240 123 NVQ 125
Cdd:cd17918 92 NVE 94
|
|
| PRK05298 |
PRK05298 |
excinuclease ABC subunit UvrB; |
282-359 |
1.41e-03 |
|
excinuclease ABC subunit UvrB;
Pssm-ID: 235395 [Multi-domain] Cd Length: 652 Bit Score: 40.80 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 282 LTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGNTRVLISTDVWARGLDVPQVSLVINYD------LPNNRELyIHRIG 355
Cdd:PRK05298 462 LTDYLKELGIKVRYLHSDIDTLERVEIIRDLRLGEFDVLVGINLLREGLDIPEVSLVAILDadkegfLRSERSL-IQTIG 540
|
....
gi 268563240 356 RSGR 359
Cdd:PRK05298 541 RAAR 544
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
63-178 |
1.42e-03 |
|
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: 39.56 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 63 KARDVIAQAQSGTGKTAtfsISVL-------QSLDTQVRETQALILSPTRELAVQIQKvvlALGDYMNVQCHACIGGTNL 135
Cdd:cd18034 15 LKRNTIVVLPTGSGKTL---IAVMlikemgeLNRKEKNPKKRAVFLVPTVPLVAQQAE---AIRSHTDLKVGEYSGEMGV 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 268563240 136 G--------EDIRKLDygqhVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEA 178
Cdd:cd18034 89 DkwtkerwkEELEKYD----VLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
291-358 |
4.42e-03 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 39.52 E-value: 4.42e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 268563240 291 FTVSSMHGDMEQKDRDEVMKEFRAGNTRVLISTDVWARGLDVPQVSLVINYDLPNNRELYIHRIGRSG 358
Cdd:PRK09751 302 FIARSHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
|
|
| PRK05580 |
PRK05580 |
primosome assembly protein PriA; Validated |
304-367 |
9.92e-03 |
|
primosome assembly protein PriA; Validated
Pssm-ID: 235514 [Multi-domain] Cd Length: 679 Bit Score: 38.21 E-value: 9.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268563240 304 DRDEVM---------KEFRAGNTRVLISTDVWARGLDVPQVSLV--INYDL----PNNR------ELYIHRIGRSGRFGR 362
Cdd:PRK05580 459 DRDTTRrkgaleqllAQFARGEADILIGTQMLAKGHDFPNVTLVgvLDADLglfsPDFRasertfQLLTQVAGRAGRAEK 538
|
....*
gi 268563240 363 KGVAI 367
Cdd:PRK05580 539 PGEVL 543
|
|
| |
