|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
14-414 |
0e+00 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 623.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 14 SDKEHSYDGPPGMDpEGIIESNWDEVVDNFDDMNLKEELLRGIYAYGFEKPSAIQQRAIIPCVRGHDVIAQAQSGTGKTA 93
Cdd:PTZ00424 2 ATSEQKNQSEQVAS-TGTIESNYDEIVDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 94 TFSISILQQIDTSARECQALILAPTRELAQQIQKVVIALGDFMGAMCHACIGGTNVREDMRKLEMGVHVLVGTPGRVLDM 173
Cdd:PTZ00424 81 TFVIAALQLIDYDLNACQALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 174 ISRRALKTNTIRIFVLDEADEMLSRGFKDQIHDVFKNLNHEVQVILLSATMPSDVLEVSTCFMRNPIRILVKKEELTLEG 253
Cdd:PTZ00424 161 IDKRHLRVDDLKLFILDEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 254 IKQFFVFVEREEWKLDTLCDLYETLSITQAVIFCNTRRKVDWLTESMHNRDFTVSAMHGDMEQRERDIIMRQFRTGSSRV 333
Cdd:PTZ00424 241 IRQFYVAVEKEEWKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 334 LITTDLLARGIDVQQVSLVINYDLPSNRENYIHRIGRGGRFGRKGVAINFVTEEDKRSLNDIEQFYNTRIEEMPMNVADL 413
Cdd:PTZ00424 321 LITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEVADY 400
|
.
gi 939632536 414 I 414
Cdd:PTZ00424 401 L 401
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
42-408 |
2.52e-149 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 429.95 E-value: 2.52e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 42 NFDDMNLKEELLRGIYAYGFEKPSAIQQRAIIPCVRGHDVIAQAQSGTGKTATFSISILQQIDTS-ARECQALILAPTRE 120
Cdd:COG0513 3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSrPRAPQALILAPTRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 121 LAQQIQKVVIALGDFMGAMCHACIGGTNVREDMRKLEMGVHVLVGTPGRVLDMISRRALKTNTIRIFVLDEADEMLSRGF 200
Cdd:COG0513 83 LALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 201 KDQIHDVFKNLNHEVQVILLSATMPSDVLEVSTCFMRNPIRILVKKEELTLEGIKQFFVFVEREEwKLDTLCDLYETLSI 280
Cdd:COG0513 163 IEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRD-KLELLRRLLRDEDP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 281 TQAVIFCNTRRKVDWLTESMHNRDFTVSAMHGDMEQRERDIIMRQFRTGSSRVLITTDLLARGIDVQQVSLVINYDLPSN 360
Cdd:COG0513 242 ERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPED 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 939632536 361 RENYIHRIgrggrfgrkgVAINFVTEEDKRSLNDIEQFYNTRIEEMPM 408
Cdd:COG0513 322 PEDYVHRIgrtgragaegTAISLVTPDERRLLRAIEKLIGQKIEEEEL 369
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
43-243 |
9.03e-143 |
|
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: 404.91 E-value: 9.03e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 43 FDDMNLKEELLRGIYAYGFEKPSAIQQRAIIPCVRGHDVIAQAQSGTGKTATFSISILQQIDTSARECQALILAPTRELA 122
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 123 QQIQKVVIALGDFMGAMCHACIGGTNVREDMRKLEMGVHVLVGTPGRVLDMISRRALKTNTIRIFVLDEADEMLSRGFKD 202
Cdd:cd18046 81 QQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 939632536 203 QIHDVFKNLNHEVQVILLSATMPSDVLEVSTCFMRNPIRIL 243
Cdd:cd18046 161 QIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRIL 201
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
45-243 |
4.87e-128 |
|
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: 367.42 E-value: 4.87e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 45 DMNLKEELLRGIYAYGFEKPSAIQQRAIIPCVRGHDVIAQAQSGTGKTATFSISILQQIDTSARECQALILAPTRELAQQ 124
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 125 IQKVVIALGDFMGAMCHACIGGTNVREDMRKLEMGVHVLVGTPGRVLDMISRRALKTNTIRIFVLDEADEMLSRGFKDQI 204
Cdd:cd17939 81 IQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQI 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 939632536 205 HDVFKNLNHEVQVILLSATMPSDVLEVSTCFMRNPIRIL 243
Cdd:cd17939 161 YDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRIL 199
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
43-243 |
9.19e-109 |
|
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: 318.26 E-value: 9.19e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 43 FDDMNLKEELLRGIYAYGFEKPSAIQQRAIIPCVRGHDVIAQAQSGTGKTATFSISILQQIDTSARECQALILAPTRELA 122
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 123 QQIQKVVIALGDFMGAMCHACIGGTNVREDMRKLEMGVHVLVGTPGRVLDMISRRALKTNTIRIFVLDEADEMLSRGFKD 202
Cdd:cd18045 81 VQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 939632536 203 QIHDVFKNLNHEVQVILLSATMPSDVLEVSTCFMRNPIRIL 243
Cdd:cd18045 161 QIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRIL 201
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
43-404 |
1.29e-95 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 294.02 E-value: 1.29e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 43 FDDMNLKEELLRGIYAYGFEKPSAIQQRAIIPCVRGHDVIAQAQSGTGKTATFSISILQQIDTSARECQALILAPTRELA 122
Cdd:PRK11776 6 FSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTRELA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 123 QQIQKVVIALGDFMG-----AMChaciGGTNVREDMRKLEMGVHVLVGTPGRVLDMISRRALKTNTIRIFVLDEADEMLS 197
Cdd:PRK11776 86 DQVAKEIRRLARFIPnikvlTLC----GGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 198 RGFKDQIHDVFKNLNHEVQVILLSATMPSDVLEVSTCFMRNPIRILVKKEElTLEGIKQFFVFVEREEwKLDTLCDLYET 277
Cdd:PRK11776 162 MGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTH-DLPAIEQRFYEVSPDE-RLPALQRLLLH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 278 LSITQAVIFCNTRRKVDWLTESMHNRDFTVSAMHGDMEQRERDIIMRQFRTGSSRVLITTDLLARGIDVQQVSLVINYDL 357
Cdd:PRK11776 240 HQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYEL 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 939632536 358 PSNRENYIHRIGRGGRFGRKGVAINFVTEEDKRSLNDIEQFYNTRIE 404
Cdd:PRK11776 320 ARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLN 366
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
52-242 |
6.68e-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: 257.37 E-value: 6.68e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 52 LLRGIYAYGFEKPSAIQQRAIIPCVRGHDVIAQAQSGTGKTATFSISILQQIDT----SARECQALILAPTRELAQQIQK 127
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPepkkKGRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 128 VVIALGDFMGAMCHACIGGTNVREDMRKLEMGVHVLVGTPGRVLDMISRRALKTNTIRIFVLDEADEMLSRGFKDQIHDV 207
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 939632536 208 FKNLNHEVQVILLSATMPSDVLEVSTCFMRNPIRI 242
Cdd:cd00268 161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
43-242 |
6.10e-72 |
|
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: 224.48 E-value: 6.10e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 43 FDDMNLKEELLRGIYAYGFEKPSAIQQRAIIPCVRGHDVIAQAQSGTGKTATFSISILQQIDTSARECQALILAPTRELA 122
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 123 QQIQKVVIALGDFMGAMCHACIGGTNVREDMRKLEMGVHVLVGTPGRVLDMISRRALKTNTIRIFVLDEADEMLSRGFKD 202
Cdd:cd17940 81 LQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 939632536 203 QIHDVFKNLNHEVQVILLSATMPSDVLEVSTCFMRNPIRI 242
Cdd:cd17940 161 IIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
42-406 |
2.23e-70 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 228.92 E-value: 2.23e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 42 NFDDMNLKEELLRGIYAYGFEKPSAIQQRAIIPCVRGHDVIAQAQSGTGKTATFSISILQQIDTSA------RECQALIL 115
Cdd:PRK10590 2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQphakgrRPVRALIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 116 APTRELAQQIQKVVIALGDFMGAMCHACIGGTNVREDMRKLEMGVHVLVGTPGRVLDMISRRALKTNTIRIFVLDEADEM 195
Cdd:PRK10590 82 TPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 196 LSRGFKDQIHDVFKNLNHEVQVILLSATMPSDVLEVSTCFMRNPIRILVKKEELTLEGIKQFFVFVEREEwKLDTLCDLY 275
Cdd:PRK10590 162 LDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKR-KRELLSQMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 276 ETLSITQAVIFCNTRRKVDWLTESMHNRDFTVSAMHGDMEQRERDIIMRQFRTGSSRVLITTDLLARGIDVQQVSLVINY 355
Cdd:PRK10590 241 GKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNY 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 939632536 356 DLPSNRENYIHRIGRGGRFGRKGVAINFVTEEDKRSLNDIEQFYNTRIEEM 406
Cdd:PRK10590 321 ELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRI 371
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
38-414 |
1.79e-69 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 230.89 E-value: 1.79e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 38 EVVDNFDDMNLKEELLRGIYAYGFEKPSAIQQRAIIPCVRGHDVIAQAQSGTGKTATFSISILQQIDTSARECQALILAP 117
Cdd:PRK11634 3 EFETTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 118 TRELAQQIQKvviALGDFMGAM----CHACIGGTNVREDMRKLEMGVHVLVGTPGRVLDMISRRALKTNTIRIFVLDEAD 193
Cdd:PRK11634 83 TRELAVQVAE---AMTDFSKHMrgvnVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 194 EMLSRGFKDQIHDVFKNLNHEVQVILLSATMPSDVLEVSTCFMRNPIRILVKKEELTLEGIKQFF--VFVEReewKLDTL 271
Cdd:PRK11634 160 EMLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYwtVWGMR---KNEAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 272 CDLYETLSITQAVIFCNTRRKVDWLTESMHNRDFTVSAMHGDMEQRERDIIMRQFRTGSSRVLITTDLLARGIDVQQVSL 351
Cdd:PRK11634 237 VRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISL 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939632536 352 VINYDLPSNRENYIHRIGRGGRFGRKGVAINFVTEEDKRSLNDIEQFYNTRIEEMPMNVADLI 414
Cdd:PRK11634 317 VVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAELL 379
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
43-407 |
8.60e-67 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 219.78 E-value: 8.60e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 43 FDDMNLKEELLRGIYAYGFEKPSAIQQRAIIPCVRGHDVIAQAQSGTGKTATFSISILQQIDTSAR-------ECQALIL 115
Cdd:PRK01297 89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPpkerymgEPRALII 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 116 APTRELAQQIQKVVIALGDFMGAMCHACIGGTNVREDMRKLEMG-VHVLVGTPGRVLDMISRRALKTNTIRIFVLDEADE 194
Cdd:PRK01297 169 APTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEADR 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 195 MLSRGFKDQIHDVFKNLNH--EVQVILLSATMPSDVLEVSTCFMRNPIRILVKKEELTLEGIKQ-FFVFVEREEWKLdtL 271
Cdd:PRK01297 249 MLDMGFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQhVYAVAGSDKYKL--L 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 272 CDLYETLSITQAVIFCNTRRKVDWLTESMHNRDFTVSAMHGDMEQRERDIIMRQFRTGSSRVLITTDLLARGIDVQQVSL 351
Cdd:PRK01297 327 YNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISH 406
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 939632536 352 VINYDLPSNRENYIHRIGRGGRFGRKGVAINFVTEEDKRSLNDIEQFYNTRIE-EMP 407
Cdd:PRK01297 407 VINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKIScEMP 463
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
48-242 |
8.78e-66 |
|
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: 208.20 E-value: 8.78e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 48 LKEELLRGIYAYGFEKPSAIQQRAIIPCVRG--HDVIAQAQSGTGKTATFSISILQQIDTSARECQALILAPTRELAQQI 125
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 126 QKVVIALGDFMGAMCHACIGGTNVRedmRKLEMGVHVLVGTPGRVLDMISRRALKTNTIRIFVLDEADEML-SRGFKDQI 204
Cdd:cd17963 81 GEVVEKMGKFTGVKVALAVPGNDVP---RGKKITAQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLdTQGHGDQS 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 939632536 205 HDVFKNLNHEVQVILLSATMPSDVLEVSTCFMRNPIRI 242
Cdd:cd17963 158 IRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
42-405 |
2.35e-60 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 202.09 E-value: 2.35e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 42 NFDDMNLKEELLRGIYAYGFEKPSAIQQRAIIPCVRGHDVIAQAQSGTGKTATFSISILQQ-IDTSARECQA---LILAP 117
Cdd:PRK11192 2 TFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHlLDFPRRKSGPpriLILTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 118 TRELAQQIQKVVIALGDFMGAMCHACIGGTNVREDMRKLEMGVHVLVGTPGRVLDMISRRALKTNTIRIFVLDEADEMLS 197
Cdd:PRK11192 82 TRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 198 RGFKDQIHDVFKNLNHEVQVILLSATMPSD-VLEVSTCFMRNPIRILVKKEELTLEGIKQFFVFVEREEWKLDTLCDLYE 276
Cdd:PRK11192 162 MGFAQDIETIAAETRWRKQTLLFSATLEGDaVQDFAERLLNDPVEVEAEPSRRERKKIHQWYYRADDLEHKTALLCHLLK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 277 TLSITQAVIFCNTRRKVDWLTESMHNRDFTVSAMHGDMEQRERDIIMRQFRTGSSRVLITTDLLARGIDVQQVSLVINYD 356
Cdd:PRK11192 242 QPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFD 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 939632536 357 LPSNRENYIHRIGRGGRFGRKGVAINFVTEEDKRSLNDIEQFYNTRIEE 405
Cdd:PRK11192 322 MPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLKA 370
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
52-242 |
4.44e-60 |
|
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: 193.63 E-value: 4.44e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 52 LLRGIYAYGFEKPSAIQQRAIIPCVRGHDVIAQAQSGTGKTATFSISILQQIDTSARECQALILAPTRELAQQIQKVVIA 131
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 132 LGDFM-GAMCHACIGGTNVREDMRKLEmGVHVLVGTPGRVLDMISRRALKTNTIRIFVLDEADEMLSRGFKDQIHDVFKN 210
Cdd:cd17943 81 IGKKLeGLKCEVFIGGTPVKEDKKKLK-GCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSS 159
|
170 180 190
....*....|....*....|....*....|..
gi 939632536 211 LNHEVQVILLSATMPSDVLEVSTCFMRNPIRI 242
Cdd:cd17943 160 LPKNKQVIAFSATYPKNLDNLLARYMRKPVLV 191
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
43-244 |
1.34e-59 |
|
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: 192.95 E-value: 1.34e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 43 FDDMNLKEELLRGIYAYGFEKPSAIQQRAIIPCVRGHDVIAQAQSGTGKTATFSISILQQIDTSARECQALILAPTRELA 122
Cdd:cd17950 4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRELA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 123 QQIQKVVIALGDFMGAMCHACI-GGTNVREDMRKLEMGV-HVLVGTPGRVLDMISRRALKTNTIRIFVLDEADEML-SRG 199
Cdd:cd17950 84 FQISNEYERFSKYMPNVKTAVFfGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLeQLD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 939632536 200 FKDQIHDVFKNLNHEVQVILLSATMPSDVLEVSTCFMRNPIRILV 244
Cdd:cd17950 164 MRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
42-408 |
8.83e-59 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 201.33 E-value: 8.83e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 42 NFDDMNLKEELLRGIYAYGFEKPSAIQQRAIIPCVRGHDVIAQAQSGTGKTATFSISILQQI-------DTSARECQALI 114
Cdd:PRK04537 10 TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlsrpalaDRKPEDPRALI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 115 LAPTRELAQQIQKVVIALGDFMGAMCHACIGGTNVREDMRKLEMGVHVLVGTPGRVLDMISR-RALKTNTIRIFVLDEAD 193
Cdd:PRK04537 90 LAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQhKVVSLHACEICVLDEAD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 194 EMLSRGFKDQIHDVFKNLNHEV--QVILLSATMPSDVLEVSTCFMRNPIRILVKKEELTLEGIKQFFVFVEREEwKLDTL 271
Cdd:PRK04537 170 RMFDLGFIKDIRFLLRRMPERGtrQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADEE-KQTLL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 272 CDLYETLSITQAVIFCNTRRKVDWLTESMHNRDFTVSAMHGDMEQRERDIIMRQFRTGSSRVLITTDLLARGIDVQQVSL 351
Cdd:PRK04537 249 LGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKY 328
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 939632536 352 VINYDLPSNRENYIHRIGRGGRFGRKGVAINFVTEEDKRSLNDIEQFYNTRIEEMPM 408
Cdd:PRK04537 329 VYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKIPVEPV 385
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
43-397 |
1.37e-58 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 199.63 E-value: 1.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 43 FDDMNLKEELLRGIYAYGFEKPSAIQQRAIIPCVRGHDVIAQAQSGTGKTATFSISILQ-------QIDTSARECQALIL 115
Cdd:PLN00206 123 FSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISrcctirsGHPSEQRNPLAMVL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 116 APTRELAQQIQKVVIALGDFMGAMCHACIGGTNVREDMRKLEMGVHVLVGTPGRVLDMISRRALKTNTIRIFVLDEADEM 195
Cdd:PLN00206 203 TPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCM 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 196 LSRGFKDQIHDVFKNLNHEvQVILLSATMPSDVLEVSTCFMRNPIRILVKKEELTLEGIKQFFVFVEREEWKLDtlcdLY 275
Cdd:PLN00206 283 LERGFRDQVMQIFQALSQP-QVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQK----LF 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 276 ETLSITQ-----AVIFCNTRRKVDWLTESMH-NRDFTVSAMHGDMEQRERDIIMRQFRTGSSRVLITTDLLARGIDVQQV 349
Cdd:PLN00206 358 DILKSKQhfkppAVVFVSSRLGADLLANAITvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRV 437
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 939632536 350 SLVINYDLPSNRENYIHRIGRGGRFGRKGVAINFVTEEDKRSLNDIEQ 397
Cdd:PLN00206 438 RQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVA 485
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
65-231 |
2.19e-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: 185.52 E-value: 2.19e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 65 SAIQQRAIIPCVRGHDVIAQAQSGTGKTATFSISILQQIDTSARECQALILAPTRELAQQIQKVVIALGDFMGAMCHACI 144
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 145 GGTNVREDMRKLEmGVHVLVGTPGRVLDMISRRAlKTNTIRIFVLDEADEMLSRGFKDQIHDVFKNLNHEVQVILLSATM 224
Cdd:pfam00270 81 GGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATL 158
|
....*..
gi 939632536 225 PSDVLEV 231
Cdd:pfam00270 159 PRNLEDL 165
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
40-395 |
2.08e-56 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 194.22 E-value: 2.08e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 40 VDNFDDMNLKEELLRGIYAYGFEKPSAIQQRAIIPCVRGHDVIAQAQSGTGKTATFSISILQQIDTSARECQA-----LI 114
Cdd:PTZ00110 129 VVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGdgpivLV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 115 LAPTRELAQQIQKVVIALGDFMGAMCHACIGGTNVREDMRKLEMGVHVLVGTPGRVLDMISRRAlkTNTIRI--FVLDEA 192
Cdd:PTZ00110 209 LAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNV--TNLRRVtyLVLDEA 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 193 DEMLSRGFKDQIHDVFKNLNHEVQVILLSATMPSDVLEVSTCFMRN-PIRILVKKEELTL-EGIKQFfVFVEREEWKLDT 270
Cdd:PTZ00110 287 DRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDLTAcHNIKQE-VFVVEEHEKRGK 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 271 LCDLYETL--SITQAVIFCNTRRKVDWLTESMHNRDFTVSAMHGDMEQRERDIIMRQFRTGSSRVLITTDLLARGIDVQQ 348
Cdd:PTZ00110 366 LKMLLQRImrDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKD 445
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 939632536 349 VSLVINYDLPSNRENYIHRIGRGGRFGRKGVAINFVTEEDKRSLNDI 395
Cdd:PTZ00110 446 VKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDL 492
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
43-403 |
2.86e-53 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 182.86 E-value: 2.86e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 43 FDDMNLKEELLRGIYAYGFEKPSAIQQRAIIPCVRGHDVIAQAQSGTGKT-----ATFSISILQQIDTSARECQ--ALIL 115
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTmafltATFHYLLSHPAPEDRKVNQprALIM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 116 APTRELAQQIQKVVIALGDFMGAMCHACIGGTNVREDMRKLEMGVHVLVGTPGRVLDMISRRALKTNTIRIFVLDEADEM 195
Cdd:PRK04837 90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 196 LSRGFKDQIHDVF-------KNLNhevqvILLSATMPSDVLEVSTCFMRNPIRILVKKEELTLEGIKQFFVFVEREEwKL 268
Cdd:PRK04837 170 FDLGFIKDIRWLFrrmppanQRLN-----MLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYPSNEE-KM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 269 DTLCDLYETLSITQAVIFCNTRRKV----DWLTESMHNrdftVSAMHGDMEQRERDIIMRQFRTGSSRVLITTDLLARGI 344
Cdd:PRK04837 244 RLLQTLIEEEWPDRAIIFANTKHRCeeiwGHLAADGHR----VGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGL 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 939632536 345 DVQQVSLVINYDLPSNRENYIHRIGRGGRFGRKGVAINFVTEEDKRSLNDIEQFYNTRI 403
Cdd:PRK04837 320 HIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIGHSI 378
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
56-257 |
5.63e-53 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 175.37 E-value: 5.63e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 56 IYAYGFEKPSAIQQRAIIPCVRG-HDVIAQAQSGTGKTATFSISILQQIDTSaRECQALILAPTRELAQQIQKVVIALGD 134
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRG-KGGRVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 135 FMGAMCHACIGGTNVREDMRKLEMGV-HVLVGTPGRVLDMISRRALKTNTIRIFVLDEADEMLSRGFKDQIHDVFKNLNH 213
Cdd:smart00487 80 SLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 939632536 214 EVQVILLSATMPSDVLEVSTCFMRNPIRILVkkEELTLEGIKQF 257
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFIDV--GFTPLEPIEQF 201
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
43-242 |
1.92e-50 |
|
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: 169.03 E-value: 1.92e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 43 FDDMNLKEELLRGIYAYGFEKPSAIQQRAIIPCVRGHDVIAQAQSGTGKTATFSISILQQIDTSARECQALILAPTRELA 122
Cdd:cd17954 2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTRELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 123 QQIQKVVIALGDFMGAMCHACIGGTNVREDMRKLEMGVHVLVGTPGRVLDMISR-RALKTNTIRIFVLDEADEMLSRGFK 201
Cdd:cd17954 82 QQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENtKGFSLKSLKFLVMDEADRLLNMDFE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 939632536 202 DQIHDVFKNLNHEVQVILLSATMPSDVLEVSTCFMRNPIRI 242
Cdd:cd17954 162 PEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
52-242 |
2.12e-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: 168.59 E-value: 2.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 52 LLRGIYAYGFEKPSAIQQRAIIPCVRGHDVIAQAQSGTGKTATFSISILQQIDTSARE---CQALILAPTRELAQQIQKV 128
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKkaaTRVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 129 VIALGDFMGAMCHACIGGTNVREDMRKLEMGVHVLVGTPGRVLDMI-SRRALKTNTIRIFVLDEADEMLSRGFKDQIHDV 207
Cdd:cd17947 81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLrNSPSFDLDSIEILVLDEADRMLEEGFADELKEI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 939632536 208 FKNLNHEVQVILLSATMPSDVLEVSTCFMRNPIRI 242
Cdd:cd17947 161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
48-231 |
1.01e-46 |
|
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: 159.29 E-value: 1.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 48 LKEELLRGIYAYGFEKPSAIQQRAIIPCVR-GHDVIAQAQSGTGKTATFSISILQ-----QIDTSARECQALILAPTREL 121
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQsllntKPAGRRSGVSALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 122 AQQIQKVVIALGDFMGAM-CHACIGGTNVREDMRKLE-MGVHVLVGTPGRVLDMIS--RRALKTNTIRIFVLDEADEMLS 197
Cdd:cd17964 81 ALQIAAEAKKLLQGLRKLrVQSAVGGTSRRAELNRLRrGRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRLLD 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 939632536 198 RGFKDQIHDVFKNLNH----EVQVILLSATMPSDVLEV 231
Cdd:cd17964 161 MGFRPDLEQILRHLPEknadPRQTLLFSATVPDEVQQI 198
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
43-238 |
1.58e-46 |
|
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: 159.19 E-value: 1.58e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 43 FDDMNLKEELLRGIYAYGFEKPSAIQQRAIiPCVR-GHDVIAQAQSGTGKTATFSISILQQI----------DTSARECQ 111
Cdd:cd17967 2 FEEAGLRELLLENIKRAGYTKPTPVQKYAI-PIILaGRDLMACAQTGSGKTAAFLLPIISKLledgppsvgrGRRKAYPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 112 ALILAPTRELAQQIQKVVIALGDFMGAMCHACIGGTNVREDMRKLEMGVHVLVGTPGRVLDMISRRALKTNTIRIFVLDE 191
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 939632536 192 ADEMLSRGFKDQIHDVfknLNH-------EVQVILLSATMPSDVLEVSTCFMRN 238
Cdd:cd17967 161 ADRMLDMGFEPQIRKI---VEHpdmppkgERQTLMFSATFPREIQRLAADFLKN 211
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
52-244 |
3.43e-46 |
|
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: 157.75 E-value: 3.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 52 LLRGIYAYGFEKPSAIQQRAIiPC-VRGHDVIAQAQSGTGKTATFSISILQQI--DTSARECQALILAPTRELAQQIQKV 128
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAI-PIlLHGRDLLACAPTGSGKTLAFLIPILQKLgkPRKKKGLRALILAPTRELASQIYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 129 VIALGDFMGAMCHACIGGTNVR-EDMRKLEMGVHVLVGTPGRVLDMISRRALKTNTIRIFVLDEADEMLSRGFKDQIHDV 207
Cdd:cd17957 80 LLKLSKGTGLRIVLLSKSLEAKaKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEI 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 939632536 208 FKNL-NHEVQVILLSATMPSDVLEVSTCFMRNPIRILV 244
Cdd:cd17957 160 LAACtNPNLQRSLFSATIPSEVEELARSVMKDPIRIIV 197
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
254-369 |
3.35e-45 |
|
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: 152.66 E-value: 3.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 254 IKQFFVFVEREEWKLDTLCDLYETLSITQAVIFCNTRRKVDWLTESMHNRDFTVSAMHGDMEQRERDIIMRQFRTGSSRV 333
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 939632536 334 LITTDLLARGIDVQQVSLVINYDLPSNRENYIHRIG 369
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIG 116
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
52-242 |
5.35e-45 |
|
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: 154.24 E-value: 5.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 52 LLRGIYAYGFEKPSAIQQRAIIPCVRGHDVIAQAQSGTGKTATFSISILQQIDTSARECQALILAPTRELAQQIQKVVIA 131
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 132 LGDFMGAMCHA-CIGGTNVREDMRKLEMGVHVLVGTPGRVLDMISRRALKTNTIRIFVLDEADEMLSRGFKDQIHDVFKN 210
Cdd:cd17962 81 LMKGLPPMKTAlLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILEN 160
|
170 180 190
....*....|....*....|....*....|..
gi 939632536 211 LNHEVQVILLSATMPSDVLEVSTCFMRNPIRI 242
Cdd:cd17962 161 ISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
43-239 |
5.95e-45 |
|
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: 154.69 E-value: 5.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 43 FDDMNLKEELLRGIYAYGFEKPSAIQQRAIIPCVRGHDVIAQAQSGTGKTATFSISILQQIDTSARECQALILAPTRELA 122
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 123 QQIQKVVIALGDFMGAMCHACIGGTNVREDMRKLEMGVHVLVGTPGRVLDMISRRALKTNT---IRIFVLDEADEMLSRG 199
Cdd:cd17955 81 YQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDTTKVlsrVKFLVLDEADRLLTGS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 939632536 200 FKDQIHDVFKNLNHEVQVILLSATMPSDVLEVSTCFMRNP 239
Cdd:cd17955 161 FEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
42-242 |
7.97e-45 |
|
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: 154.38 E-value: 7.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 42 NFDDMNLKEELLRGIYAYGFEKPSAIQQRAIIPCVRGHDVIAQAQSGTGKTATFSISILQQI-DTSARE-CQALILAPTR 119
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLkAHSPTVgARALILSPTR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 120 ELAQQIQKVVIALGDFMGAMCHACIGGTNVREDMRKLEMGVHVLVGTPGRVLDMISRRALKTNTIRIFVLDEADEMLSRG 199
Cdd:cd17959 82 ELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 939632536 200 FKDQIHDVFKNLNHEVQVILLSATMPSDVLEVSTCFMRNPIRI 242
Cdd:cd17959 162 FAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
40-250 |
3.88e-42 |
|
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: 148.25 E-value: 3.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 40 VDNFDDMNLKEELLRGIYAYGFEKPSAIQQRAIiPCVRGH---DVIAQAQSGTGKTATFSISILQQIDTSARECQALILA 116
Cdd:cd18048 17 VKSFEELHLKEELLRGIYAMGFNRPSKIQENAL-PMMLADppqNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 117 PTRELAQQIQKVVIALGDF-MGAMCHACIGGTNVRedmRKLEMGVHVLVGTPGRVLDMISR-RALKTNTIRIFVLDEADE 194
Cdd:cd18048 96 PTFELALQTGKVVEEMGKFcVGIQVIYAIRGNRPG---KGTDIEAQIVIGTPGTVLDWCFKlRLIDVTNISVFVLDEADV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 939632536 195 MLS-RGFKDQIHDVFKNLNHEVQVILLSATMPSDVLEVSTCFMRNPIRILVKKEELT 250
Cdd:cd18048 173 MINvQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
52-242 |
4.04e-42 |
|
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: 147.85 E-value: 4.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 52 LLRGIYAYGFEKPSAIQQRAIIPCVRGHDVIAQAQSGTGKTATFSISILQQIDTSAREC--------QALILAPTRELAQ 123
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDeetkddgpYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 124 QIQKVVIALGDFMGAMCHACIGGTNVREDMRKLEMGVHVLVGTPGRVLDMISRRALKTNTIRIFVLDEADEMLSRGFKDQ 203
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 939632536 204 IHDVFKNL--------------------NHEVQVILLSATMPSDVLEVSTCFMRNPIRI 242
Cdd:cd17945 161 VTKILDAMpvsnkkpdteeaeklaasgkHRYRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
42-237 |
7.73e-42 |
|
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: 148.19 E-value: 7.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 42 NFDDMNLKEELLRGIYAYGFEKPSAIQQRAIIPCVRGHDVIAQAQSGTGKTATFSISILQQI------DTSARECQ---A 112
Cdd:cd18052 44 TFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMmkegltASSFSEVQepqA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 113 LILAPTRELAQQIQKVVIALGDfmGAMCHACI--GGTNVREDMRKLEMGVHVLVGTPGRVLDMISRRALKTNTIRIFVLD 190
Cdd:cd18052 124 LIVAPTRELANQIFLEARKFSY--GTCIRPVVvyGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILD 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 939632536 191 EADEMLSRGFKDQIHDVFKNLN----HEVQVILLSATMPSDVLEVSTCFMR 237
Cdd:cd18052 202 EADRMLDMGFGPEIRKLVSEPGmpskEDRQTLMFSATFPEEIQRLAAEFLK 252
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
48-240 |
1.37e-41 |
|
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: 145.80 E-value: 1.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 48 LKEELLRGIYAYGFEKPSAIQQRAIiPC-VRGHDVIAQAQSGTGKTATFSISILQQI------DTSARECQALILAPTRE 120
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAI-PLaLEGKDILARARTGSGKTAAYALPIIQKIlkakaeSGEEQGTRALILVPTRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 121 LAQQIQKVVIALgdfmgamCHAC--------IGGTNVREDMRKLEMGV-HVLVGTPGRVLDMISRRALK-TNTIRIFVLD 190
Cdd:cd17961 80 LAQQVSKVLEQL-------TAYCrkdvrvvnLSASSSDSVQRALLAEKpDIVVSTPARLLSHLESGSLLlLSTLKYLVID 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 939632536 191 EADEMLSRGFKDQIHDVFKNLNHEVQVILLSATMPSDVLEVSTCFMRNPI 240
Cdd:cd17961 153 EADLVLSYGYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
43-239 |
1.58e-41 |
|
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: 145.54 E-value: 1.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 43 FDDMNLKEELLRGIYAYGFEKPSAIQQRAIIPCVRGHDVIAQAQSGTGKTATFSISILQQIdtsarecQALILAPTRELA 122
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV-------VALILEPSRELA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 123 QQIQKVVIALGDFMGA---MCHACIGGTNVREDMRKLEMGVHVLVGTPGRVLDMISRRALKTNTIRIFVLDEADEMLSRG 199
Cdd:cd17938 74 EQTYNCIENFKKYLDNpklRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 939632536 200 FKDQIHDVFKNL------NHEVQVILLSATMPS-DVLEVSTCFMRNP 239
Cdd:cd17938 154 NLETINRIYNRIpkitsdGKRLQVIVCSATLHSfEVKKLADKIMHFP 200
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
52-242 |
3.95e-41 |
|
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: 144.64 E-value: 3.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 52 LLRGIYAYGFEKPSAIQqRAIIPCVRGH-DVIAQAQSGTGKTATFSISILQQIdtSARECQ-------ALILAPTRELAQ 123
Cdd:cd17960 1 ILDVVAELGFTSMTPVQ-AATIPLFLSNkDVVVEAVTGSGKTLAFLIPVLEIL--LKRKANlkkgqvgALIISPTRELAT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 124 QIQKVVIALGDFMGAMCHA--CIGGTNVREDMRKLEM-GVHVLVGTPGRVLDMISRRALKTN--TIRIFVLDEADEMLSR 198
Cdd:cd17960 78 QIYEVLQSFLEHHLPKLKCqlLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLSRKADKVKvkSLEVLVLDEADRLLDL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 939632536 199 GFKDQIHDVFKNLNHEVQVILLSATMPSDVLEVSTCFMRNPIRI 242
Cdd:cd17960 158 GFEADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
52-242 |
3.58e-40 |
|
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: 141.78 E-value: 3.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 52 LLRGIYAYGFEKPSAIQQRAIiPCV-RGHDVIAQAQSGTGKTATFS----ISILQQIDTSARECQ-ALILAPTRELAQQI 125
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQAL-PVAlSGRDMIGIAKTGSGKTAAFIwpmlVHIMDQRELEKGEGPiAVIVAPTRELAQQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 126 QKVVIALGDFMGAMCHACIGGTNVREDMRKLEMGVHVLVGTPGRVLDMISRRALKTNTIRIFVLDEADEMLSRGFKDQIH 205
Cdd:cd17952 80 YLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 939632536 206 DVFKNLNHEVQVILLSATMPSDVLEVSTCFMRNPIRI 242
Cdd:cd17952 160 SIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
52-242 |
2.72e-39 |
|
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: 139.43 E-value: 2.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 52 LLRGIYAYGFEKPSAIQQRAIIPCVRGHDVIAQAQSGTGKTATFSISILQQIDTSARECQ-----ALILAPTRELAQQIQ 126
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERgdgpiVLVLAPTRELAQQIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 127 KVVIALGDFMGAMCHACIGGTNVREDMRKLEMGVHVLVGTPGRVLDMISrrALKTNTIRI--FVLDEADEMLSRGFKDQI 204
Cdd:cd17966 81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLD--QGKTNLRRVtyLVLDEADRMLDMGFEPQI 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 939632536 205 HDVFKNLNHEVQVILLSATMPSDVLEVSTCFMRNPIRI 242
Cdd:cd17966 159 RKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
48-242 |
1.05e-38 |
|
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: 138.66 E-value: 1.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 48 LKEELLRGIYAYGFEKPSAIQQRAIiPCV-RGHDVIAQAQSGTGKTATFSISILQQI-DTSARECQ----ALILAPTREL 121
Cdd:cd17953 19 LSEKVLDLIKKLGYEKPTPIQAQAL-PAImSGRDVIGIAKTGSGKTLAFLLPMFRHIkDQRPVKPGegpiGLIMAPTREL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 122 AQQIQKVVIALGDFMGAMCHACIGGTNVREDMRKLEMGVHVLVGTPGRVLDMISRRALK-TNTIRI--FVLDEADEMLSR 198
Cdd:cd17953 98 ALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNGRvTNLRRVtyVVLDEADRMFDM 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 939632536 199 GFKDQIHDVFKNLNHEVQVILLSATMPSDVLEVSTCFMRNPIRI 242
Cdd:cd17953 178 GFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
34-240 |
9.79e-38 |
|
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: 137.09 E-value: 9.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 34 SNWDEVVDNFDDMNLKEELLRGIYAYGFEKPSAIQQRAIIPCVRGHDVIAQAQSGTGKTATFSISILQQIDT-------- 105
Cdd:cd18051 14 ENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEqgpgeslp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 106 -----SARECQ---ALILAPTRELAQQI----QKVVIAlgdfmgAMCHACI--GGTNVREDMRKLEMGVHVLVGTPGRVL 171
Cdd:cd18051 94 sesgyYGRRKQyplALVLAPTRELASQIydeaRKFAYR------SRVRPCVvyGGADIGQQMRDLERGCHLLVATPGRLV 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939632536 172 DMISRRALKTNTIRIFVLDEADEMLSRGFKDQIHDVFKNLNH----EVQVILLSATMPSDVLEVSTCFMRNPI 240
Cdd:cd18051 168 DMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMpptgERQTLMFSATFPKEIQMLARDFLDNYI 240
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
53-244 |
1.37e-36 |
|
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: 132.41 E-value: 1.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 53 LRGIYAYGFEKPSAIQQRAIIPCVRGHDVIAQAQSGTGKTATFSISILQQID----TSARECQALILAPTRELAQQIQKV 128
Cdd:cd17941 2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYrerwTPEDGLGALIISPTRELAMQIFEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 129 VIALGDFMGAMCHACIGGTNVREDMRKLEmGVHVLVGTPGRVLD-MISRRALKTNTIRIFVLDEADEMLSRGFKDQIHDV 207
Cdd:cd17941 82 LRKVGKYHSFSAGLIIGGKDVKEEKERIN-RMNILVCTPGRLLQhMDETPGFDTSNLQMLVLDEADRILDMGFKETLDAI 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 939632536 208 FKNLNHEVQVILLSATMPSDVLEVSTCFMRNPIRILV 244
Cdd:cd17941 161 VENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
60-242 |
2.85e-36 |
|
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: 131.94 E-value: 2.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 60 GFEKPSAIQQRAIIPCVRGHDVIAQAQSGTGKTATFSISILQQIDTSA----RE--CQALILAPTRELAQQIQKVVIALG 133
Cdd:cd17949 10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEprvdRSdgTLALVLVPTRELALQIYEVLEKLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 134 DFmgamCHAC-----IGGTNVREDMRKLEMGVHVLVGTPGRVLDMI-SRRALKTNTIRIFVLDEADEMLSRGFKDQIHDV 207
Cdd:cd17949 90 KP----FHWIvpgylIGGEKRKSEKARLRKGVNILIATPGRLLDHLkNTQSFDVSNLRWLVLDEADRLLDMGFEKDITKI 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 939632536 208 FKNLN-------------HEVQVILLSATMPSDVLEVSTCFMRNPIRI 242
Cdd:cd17949 166 LELLDdkrskaggekskpSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
52-225 |
3.64e-35 |
|
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: 129.00 E-value: 3.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 52 LLRGIYAYGFEKPSAIQQRAIiPCV-RGHDVIAQAQSGTGKTATFSISILQQI---DTSARECQ-----ALILAPTRELA 122
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGL-PTIlSGRDMIGIAFTGSGKTLVFTLPLIMFAleqEKKLPFIKgegpyGLIVCPSRELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 123 QQIQKVV------IALGDFMGAMCHACIGGTNVREDMRKLEMGVHVLVGTPGRVLDMISRRALKTNTIRIFVLDEADEML 196
Cdd:cd17951 80 RQTHEVIeyyckaLQEGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMI 159
|
170 180
....*....|....*....|....*....
gi 939632536 197 SRGFKDQIHDVFKNLNHEVQVILLSATMP 225
Cdd:cd17951 160 DMGFEEDIRTIFSYFKGQRQTLLFSATMP 188
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
53-223 |
4.80e-35 |
|
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: 128.25 E-value: 4.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 53 LRGIYAYGFEKPSAIQQRAIIPCVRGHDVIAQAQSGTGKTATFSISILQQIDTSA----RECQALILAPTRELAQQIQKV 128
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKfkprNGTGVIIISPTRELALQIYGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 129 VIALGDFMGAMCHACIGGTNVREDMRKLEMGVHVLVGTPGRVLD-MISRRALKTNTIRIFVLDEADEMLSRGFKDQIHDV 207
Cdd:cd17942 82 AKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDhLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQI 161
|
170
....*....|....*.
gi 939632536 208 FKNLNHEVQVILLSAT 223
Cdd:cd17942 162 IKLLPKRRQTMLFSAT 177
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
52-242 |
1.70e-33 |
|
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: 124.11 E-value: 1.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 52 LLRGIYAYGFEKPSAIQQRAIIPCVRGHDVIAQAQSGTGKTATFSISILQQIDT--SARECQ----ALILAPTRELAQQI 125
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLqpIPREQRngpgVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 126 Q-KVVIALGDFMGAMChaCIGGTNVREDMRKLEMGVHVLVGTPGRVLDMISRRALKTNTIRIFVLDEADEMLSRGFKDQI 204
Cdd:cd17958 81 EaECSKYSYKGLKSVC--VYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQI 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 939632536 205 HDVFKNLNHEVQVILLSATMPSDVLEVSTCFMRNPIRI 242
Cdd:cd17958 159 RKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
52-224 |
5.92e-32 |
|
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: 121.19 E-value: 5.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 52 LLRGIYAYGFEKPSAIQQRAIIPCVR-GHDVIAQAQSGTGKTATFSISILQQI---------DTSARECQALILAPTREL 121
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLlsqkssngvGGKQKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 122 AQQIQKVVIALGDFMGAMCHACIGGTNVREDMRKLEMGVHVLVGTPGRVLDMISRRALKTN---TIRIFVLDEADEMLSR 198
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLAnlkSLRFLVLDEADRMLEK 160
|
170 180 190
....*....|....*....|....*....|...
gi 939632536 199 GFKDQIHDVFKNLN-------HEVQVILLSATM 224
Cdd:cd17946 161 GHFAELEKILELLNkdragkkRKRQTFVFSATL 193
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
43-239 |
6.01e-32 |
|
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: 120.21 E-value: 6.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 43 FDDMNLKEELLRGIYAYGFEKPSAIQQRAIiPCVRG---HDVIAQAQSGTGKTATFSISILQQIDTSARECQALILAPTR 119
Cdd:cd18047 3 FEELRLKPQLLQGVYAMGFNRPSKIQENAL-PLMLAeppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 120 ELAQQIQKVVIALGDFMG--AMCHACIGgtnvredmRKLEMGV----HVLVGTPGRVLD-MISRRALKTNTIRIFVLDEA 192
Cdd:cd18047 82 ELALQTGKVIEQMGKFYPelKLAYAVRG--------NKLERGQkiseQIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 939632536 193 DEML-SRGFKDQIHDVFKNLNHEVQVILLSATMPSDVLEVSTCFMRNP 239
Cdd:cd18047 154 DVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
67-237 |
6.42e-31 |
|
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: 117.26 E-value: 6.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 67 IQQRAIIPCVRGHDVIAQAQSGTGKTATFSISIL------QQIDTSARECQALILAPTRELAQQIQKvviALGDFMGAMC 140
Cdd:cd17944 16 IQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIeklqedQQPRKRGRAPKVLVLAPTRELANQVTK---DFKDITRKLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 141 HACI-GGTNVREDMRKLEMGVHVLVGTPGRVLDMISRRALKTNTIRIFVLDEADEMLSRGFKDQIHDVF-----KNLNHE 214
Cdd:cd17944 93 VACFyGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILsvsykKDSEDN 172
|
170 180
....*....|....*....|...
gi 939632536 215 VQVILLSATMPSDVLEVSTCFMR 237
Cdd:cd17944 173 PQTLLFSATCPDWVYNVAKKYMK 195
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
40-242 |
7.77e-30 |
|
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: 115.49 E-value: 7.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 40 VDNFDDMNLKEELLRGIYAYGFEKPSAIQQRAIIPCVRGHDVIAQAQSGTGKTATFSISILQQIDTSARECQA-----LI 114
Cdd:cd18049 23 VLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGdgpicLV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 115 LAPTRELAQQIQKVVIALGDfMGAMCHACI-GGTNVREDMRKLEMGVHVLVGTPGRVLDMIsrRALKTNTIRI--FVLDE 191
Cdd:cd18049 103 LAPTRELAQQVQQVAAEYGR-ACRLKSTCIyGGAPKGPQIRDLERGVEICIATPGRLIDFL--EAGKTNLRRCtyLVLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 939632536 192 ADEMLSRGFKDQIHDVFKNLNHEVQVILLSATMPSDVLEVSTCFMRNPIRI 242
Cdd:cd18049 180 ADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHI 230
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
266-369 |
9.97e-30 |
|
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: 111.15 E-value: 9.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 266 WKLDTLCDLYETLSITQAVIFCNTRRKVDwLTESMHNRDFTVSAMHGDMEQRERDIIMRQFRTGSSRVLITTDLLARGID 345
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100
....*....|....*....|....
gi 939632536 346 VQQVSLVINYDLPSNRENYIHRIG 369
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIG 103
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
40-242 |
6.82e-29 |
|
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: 113.95 E-value: 6.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 40 VDNFDDMNLKEELLRGIYAYGFEKPSAIQQRAIIPCVRGHDVIAQAQSGTGKTATFSISILQQIDTSARECQA-----LI 114
Cdd:cd18050 61 VFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGdgpicLV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 115 LAPTRELAQQIQKVVIALGDfMGAMCHACI-GGTNVREDMRKLEMGVHVLVGTPGRVLDMIsrRALKTNTIRI--FVLDE 191
Cdd:cd18050 141 LAPTRELAQQVQQVADDYGK-SSRLKSTCIyGGAPKGPQIRDLERGVEICIATPGRLIDFL--EAGKTNLRRCtyLVLDE 217
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 939632536 192 ADEMLSRGFKDQIHDVFKNLNHEVQVILLSATMPSDVLEVSTCFMRNPIRI 242
Cdd:cd18050 218 ADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQI 268
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
52-231 |
7.86e-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: 109.76 E-value: 7.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 52 LLRGIYAYGFEKPSAIQQRAIIPCVRGHDVIAQAQSGTGKTATFSISILQQIDTSARECQ-------ALILAPTRELAQQ 124
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEgpfnaprGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 125 IQKVVIALGDFMGAMCHaCIGGTNVREDMRKLEMG-VHVLVGTPGRVLDMISRRALKTNTIRIFVLDEADEMLSRGFKDQ 203
Cdd:cd17948 81 IGSVAQSLTEGLGLKVK-VITGGRTKRQIRNPHFEeVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 939632536 204 IHDVFKN-------------LNHEVQVILLSATMPSDVLEV 231
Cdd:cd17948 160 LSHFLRRfplasrrsentdgLDPGTQLVLVSATMPSGVGEV 200
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
78-223 |
7.66e-25 |
|
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: 99.01 E-value: 7.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 78 GHDVIAQAQSGTGKTATFSISILQQIDTsaRECQALILAPTRELAQQIQKVVIALGDfMGAMCHACIGGTNVREDMRKLE 157
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLK--KGKKVLVLVPTKALALQTAERLRELFG-PGIRVAVLVGGSSAEEREKNKL 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 939632536 158 MGVHVLVGTPGRVLDMISR-RALKTNTIRIFVLDEADEMLSRGFKDQIHD--VFKNLNHEVQVILLSAT 223
Cdd:cd00046 78 GDADIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLIDSRGALILDlaVRKAGLKNAQVILLSAT 146
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
294-368 |
2.66e-22 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 89.96 E-value: 2.66e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 939632536 294 DWLTESMHNRDFTVSAMHGDMEQRERDIIMRQFRTGSSRVLITTDLLARGIDVQQVSLVINYDLPSNRENYIHRI 368
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRI 75
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
64-239 |
1.02e-20 |
|
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: 90.00 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 64 PSAIQQRAIIPCVRGHDVIAQAQSGTGKTATFSISILQQI-DTSARECQALILAPTRELAQQIQKVVIALGDFMGAMCHA 142
Cdd:cd17956 22 PWLLPSSKSTPPYRPGDLCVSAPTGSGKTLAYVLPIVQALsKRVVPRLRALIVVPTKELVQQVYKVFESLCKGTGLKVVS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 143 CIGGTNVREDMRKLEMGVH--------VLVGTPGRVLDMI-SRRALKTNTIRIFVLDEADEMLSRGFKDQIHDVFKNLNH 213
Cdd:cd17956 102 LSGQKSFKKEQKLLLVDTSgrylsrvdILVATPGRLVDHLnSTPGFTLKHLRFLVIDEADRLLNQSFQDWLETVMKALGR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 939632536 214 E--------------------VQVILLSATMPSDVLEVSTCFMRNP 239
Cdd:cd17956 182 PtapdlgsfgdanllersvrpLQKLLFSATLTRDPEKLSSLKLHRP 227
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
63-225 |
1.51e-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: 70.10 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 63 KPSAIQqRAIIPCVRGHDVIAQ-----------------AQSGTGKTATFSISIL-----QQIDTSARECQ--------- 111
Cdd:cd17965 30 KPSPIQ-TLAIKKLLKTLMRKVtkqtsneepklevfllaAETGSGKTLAYLAPLLdylkrQEQEPFEEAEEeyesakdtg 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 112 ---ALILAPTRELAQQIQKVVIALGDF--MGAMCHACIGGTNVREDMRKLEMGVHVLVGTPGRVLDMISRRALKTNTIRI 186
Cdd:cd17965 109 rprSVILVPTHELVEQVYSVLKKLSHTvkLGIKTFSSGFGPSYQRLQLAFKGRIDILVTTPGKLASLAKSRPKILSRVTH 188
|
170 180 190
....*....|....*....|....*....|....*....
gi 939632536 187 FVLDEADEMLSRGFKDQIHDVFKNLNHEVQVILLSATMP 225
Cdd:cd17965 189 LVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIP 227
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
47-361 |
7.41e-13 |
|
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: 70.25 E-value: 7.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 47 NLKEELLRGIYAYGFEKPSAIQQRAIIPCVRGHDVIAQAQSGTGKTATFSISILQQIdTSARECQALILAPTRELAQ-QI 125
Cdd:COG1205 40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEAL-LEDPGATALYLYPTKALARdQL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 126 QKVViALGDFMGAMCHACI--GGT--NVREDMRKlemGVHVLVGTPgrvlDMISRRALKTNT--------IRIFVLDEAD 193
Cdd:COG1205 119 RRLR-ELAEALGLGVRVATydGDTppEERRWIRE---HPDIVLTNP----DMLHYGLLPHHTrwarffrnLRYVVIDEAH 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 194 EMlsRG-FKDQIHDVFKNLNH-------EVQVILLSATM--PS---------DVLEVSTC----------FMRNPIRILV 244
Cdd:COG1205 191 TY--RGvFGSHVANVLRRLRRicrhygsDPQFILASATIgnPAehaerltgrPVTVVDEDgsprgertfvLWNPPLVDDG 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 245 KKEELTLEGIKQFFVFVEREewkLDTLCdlyetlsitqaviFCNTRRKV----DWLTESMHNRDFT--VSAMHGDMEQRE 318
Cdd:COG1205 269 IRRSALAEAARLLADLVREG---LRTLV-------------FTRSRRGAellaRYARRALREPDLAdrVAAYRAGYLPEE 332
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 939632536 319 RDIIMRQFRTGSSRVLITTDLLARGIDVQQVSLVINYDLPSNR 361
Cdd:COG1205 333 RREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTR 375
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
35-353 |
2.79e-12 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 68.13 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 35 NWDEVVDNFDDMNLKEELLRGIYAYGFE-KPSAIQQRAI-----IPCVRGHDVIAQAQSGTGKTaTFSISILQQIDTSAR 108
Cdd:COG1061 51 RRLPEEDTERELAEAEALEAGDEASGTSfELRPYQQEALeallaALERGGGRGLVVAPTGTGKT-VLALALAAELLRGKR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 109 ecqALILAPTRELAQQIQKvviALGDFMGAmchaCIGGTNVREDMRklemgvHVLVGTpgrvLDMISRRALKTNTIRIF- 187
Cdd:COG1061 130 ---VLVLVPRRELLEQWAE---ELRRFLGD----PLAGGGKKDSDA------PITVAT----YQSLARRAHLDELGDRFg 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 188 --VLDEADEMLSRGFKDqihdVFKNLNHeVQVILLSATmP--SDVLEVSTCFMRN-----------------PIRILVKK 246
Cdd:COG1061 190 lvIIDEAHHAGAPSYRR----ILEAFPA-AYRLGLTAT-PfrSDGREILLFLFDGivyeyslkeaiedgylaPPEYYGIR 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 247 EELTLEgIKQFFVFVEREEWKLDTLCD---------LYETLSITQAVIFCNTRRKVDWLTESMHNRDFTVSAMHGDMEQR 317
Cdd:COG1061 264 VDLTDE-RAEYDALSERLREALAADAErkdkilrelLREHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKK 342
|
330 340 350
....*....|....*....|....*....|....*.
gi 939632536 318 ERDIIMRQFRTGSSRVLITTDLLARGIDVQQVSLVI 353
Cdd:COG1061 343 EREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI 378
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
268-365 |
3.16e-12 |
|
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: 63.76 E-value: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 268 LDTLCDLYETLSITQAVIFCNTRRKV----DWLTESMHNRD-FTVSAMHG----------DMEQRERDIIMRQFRTGSSR 332
Cdd:cd18802 13 IEILREYFPKTPDFRGIIFVERRATAvvlsRLLKEHPSTLAfIRCGFLIGrgnssqrkrsLMTQRKQKETLDKFRDGELN 92
|
90 100 110
....*....|....*....|....*....|...
gi 939632536 333 VLITTDLLARGIDVQQVSLVINYDLPSNRENYI 365
Cdd:cd18802 93 LLIATSVLEEGIDVPACNLVIRFDLPKTLRSYI 125
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
68-344 |
2.38e-10 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 62.22 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 68 QQRAIIPCVR-GHDVIAQAQSGTGKTATFSISILQQIDTSARecqALILAPTRELAQQI------------QKVVIALGD 134
Cdd:COG1204 27 QAEALEAGLLeGKNLVVSAPTASGKTLIAELAILKALLNGGK---ALYIVPLRALASEKyrefkrdfeelgIKVGVSTGD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 135 FmgamchaciggtnvREDMRKLEmGVHVLVGTPGRVLDMISRRALKTNTIRIFVLDEA----DEmlSRGFK-DQIHDVFK 209
Cdd:COG1204 104 Y--------------DSDDEWLG-RYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAhlidDE--SRGPTlEVLLARLR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 210 NLNHEVQVILLSATMPS--DVLE------VSTCFMRNPIRILVKKEELtlegikqfFVFVEREEWKLDTLCDL-YETLSI 280
Cdd:COG1204 167 RLNPEAQIVALSATIGNaeEIAEwldaelVKSDWRPVPLNEGVLYDGV--------LRFDDGSRRSKDPTLALaLDLLEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 281 -TQAVIFCNTRRKV--------DWLT----------------------ESMHNRDFTVSAM-------HGDMEQRERDII 322
Cdd:COG1204 239 gGQVLVFVSSRRDAeslakklaDELKrrltpeereeleelaeellevsEETHTNEKLADCLekgvafhHAGLPSELRRLV 318
|
330 340
....*....|....*....|..
gi 939632536 323 MRQFRTGSSRVLITTDLLARGI 344
Cdd:COG1204 319 EDAFREGLIKVLVATPTLAAGV 340
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
267-360 |
5.45e-10 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 57.10 E-value: 5.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 267 KLDTLCDLYETLSITQ--AVIFCNTRRKVDWLTESMHNRDFTVSAMHGDMEQRERDIIMRQFRTGSS--RVLITTDLLAR 342
Cdd:cd18793 12 KLEALLELLEELREPGekVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDirVFLLSTKAGGV 91
|
90
....*....|....*...
gi 939632536 343 GIDVQQVSLVINYDLPSN 360
Cdd:cd18793 92 GLNLTAANRVILYDPWWN 109
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
284-364 |
2.44e-09 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 59.00 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 284 VIFCNTRRKVDWLTESMHNRDFTVSAMHGDMEQRERDIIMRQFRTGSSRVLITTDLLARGIDVQQVSLVINYDLPSNREN 363
Cdd:COG0514 234 IVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEA 313
|
.
gi 939632536 364 Y 364
Cdd:COG0514 314 Y 314
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
283-364 |
4.96e-09 |
|
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: 54.14 E-value: 4.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 283 AVIFCNTRRKVDWLTESMHNRDFTVSAMHGDMEQRERDIIMRQFRTGSSRVLITTDLLARGIDVQQVSLVINYDLPSNRE 362
Cdd:cd18794 33 GIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSME 112
|
..
gi 939632536 363 NY 364
Cdd:cd18794 113 SY 114
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
284-364 |
5.86e-08 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 54.72 E-value: 5.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 284 VIFCNTRRKVDWLTESMHNRDFTVSAMHGDMEQRERDIIMRQFRTGSSRVLITTDLLARGIDVQQVSLVINYDLPSNREN 363
Cdd:PRK11057 240 IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIES 319
|
.
gi 939632536 364 Y 364
Cdd:PRK11057 320 Y 320
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
283-363 |
3.90e-07 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 52.15 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 283 AVIFCNTRRKVDWLTESMHNRDFTVSAMHGDMEQRERDIIMRQFRTGSS--RVLITTDLLARGIDVQQVSLVINYDLPSN 360
Cdd:COG0553 552 VLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEapVFLISLKAGGEGLNLTAADHVIHYDLWWN 631
|
....*
gi 939632536 361 --REN 363
Cdd:COG0553 632 paVEE 636
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
79-192 |
1.79e-06 |
|
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: 48.42 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 79 HDVIAQAQSGTGKTAtfsISIL-------QQIDTSARECQALILAPTRELAQQIQKVVIALGDFMGAMCHaciGGTNV-- 149
Cdd:cd18034 17 RNTIVVLPTGSGKTL---IAVMlikemgeLNRKEKNPKKRAVFLVPTVPLVAQQAEAIRSHTDLKVGEYS---GEMGVdk 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 939632536 150 -REDMRKLEM-GVHVLVGTPGRVLDMISRRALKTNTIRIFVLDEA 192
Cdd:cd18034 91 wTKERWKEELeKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
69-225 |
6.23e-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: 46.49 E-value: 6.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 69 QRAIIPCVRGHD--VIAQAQSGTGKTATFSISILQQIDTSarECQALILAPTRELAQQI--------QKVVIALGDFMGa 138
Cdd:cd17921 6 QREALRALYLSGdsVLVSAPTSSGKTLIAELAILRALATS--GGKAVYIAPTRALVNQKeadlrerfGPLGKNVGLLTG- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 139 mchaciggtNVREDMRKLEmGVHVLVGTPGRvLDMISRRA--LKTNTIRIFVLDEA----DEmlSRGFK-DQIHDVFKNL 211
Cdd:cd17921 83 ---------DPSVNKLLLA-EADILVATPEK-LDLLLRNGgeRLIQDVRLVVVDEAhligDG--ERGVVlELLLSRLLRI 149
|
170
....*....|....
gi 939632536 212 NHEVQVILLSATMP 225
Cdd:cd17921 150 NKNARFVGLSATLP 163
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
162-337 |
8.97e-05 |
|
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: 44.69 E-value: 8.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 162 VLVGTPGRVLDMI----SRRALKTNTIR--IFVLDEAD----EMLSrgfkdQIHDVFKNLNH-EVQVILLSATMPSDVLE 230
Cdd:COG1203 241 VVVTTIDQLFESLfsnrKGQERRLHNLAnsVIILDEVQayppYMLA-----LLLRLLEWLKNlGGSVILMTATLPPLLRE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 231 vstcFMRNPIRILVKKEELTLEGIKQFF---VFVEREEWKLDTLCDLYETL--SITQAVIFCNTRRKVDWLTESMHNRDF 305
Cdd:COG1203 316 ----ELLEAYELIPDEPEELPEYFRAFVrkrVELKEGPLSDEELAELILEAlhKGKSVLVIVNTVKDAQELYEALKEKLP 391
|
170 180 190
....*....|....*....|....*....|....*....
gi 939632536 306 TVSAM--HGDM-----EQRERDIIMRqFRTGSSRVLITT 337
Cdd:COG1203 392 DEEVYllHSRFcpadrSEIEKEIKER-LERGKPCILVST 429
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
77-224 |
1.19e-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: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 77 RGHDVIAQAQSGTGKTATFSISILQQI--DTSARecqALILAPTRELAQQIQKVVIALGDFMGA--MCHACIGGT--NVR 150
Cdd:cd17923 14 AGRSVVVTTGTASGKSLCYQLPILEALlrDPGSR---ALYLYPTKALAQDQLRSLRELLEQLGLgiRVATYDGDTprEER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 151 EDMRKLEmgVHVLVGTPgrvlDMI--------SRRALKTNTIRIFVLDEAdEMLSRGFKDQIHDVFKNL-------NHEV 215
Cdd:cd17923 91 RAIIRNP--PRILLTNP----DMLhyallphhDRWARFLRNLRYVVLDEA-HTYRGVFGSHVALLLRRLrrlcrryGADP 163
|
....*....
gi 939632536 216 QVILLSATM 224
Cdd:cd17923 164 QFILTSATI 172
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
289-356 |
1.51e-04 |
|
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: 42.23 E-value: 1.51e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 939632536 289 TRRKVDWLTESMHNRDFTVSAMHGDMEQRERDIIMRQFRTGSSRVLITTDLLARGIDVQQVSLVINYD 356
Cdd:cd18790 36 TKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILD 103
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
283-353 |
1.66e-04 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350186 [Multi-domain] Cd Length: 116 Bit Score: 41.01 E-value: 1.66e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 939632536 283 AVIFCNTRRKVDWLTESMHNRDFTVSAMHGD--MEQRERDIIMRQF-RTGSSRVLITTDLLARGIDVQQVSLVI 353
Cdd:cd18799 9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDysDRERGDEALILLFfGELKPPILVTVDLLTTGVDIPEVDNVV 82
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
304-356 |
1.75e-04 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 41.56 E-value: 1.75e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 939632536 304 DFTVSAMHGDMEQRERDIIMRQFRTGSSRVLITTDLLARGIDVQQVSLVINYD 356
Cdd:cd18811 61 ELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIED 113
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
282-359 |
1.84e-04 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 43.57 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 282 QAVIFCNTRRKVDWLTESMHNRDFTV------SAMHGD--MEQRERDIIMRQFRTGSSRVLITTDLLARGIDVQQVSLVI 353
Cdd:COG1111 355 RIIVFTQYRDTAEMIVEFLSEPGIKAgrfvgqASKEGDkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVI 434
|
....*..
gi 939632536 354 NYDL-PS 359
Cdd:COG1111 435 FYEPvPS 441
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
285-360 |
2.85e-04 |
|
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: 41.10 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 285 IFCNTRRKVDWLTESMHNR------DFTVSAMHGDMEQRERDIIMRQFRTGSSRVLITTDLLARGIDVQQVSLVINYDLP 358
Cdd:cd18796 43 VFTNTRSQAERLAQRLRELcpdrvpPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSP 122
|
..
gi 939632536 359 SN 360
Cdd:cd18796 123 KS 124
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
50-240 |
4.14e-04 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 41.37 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 50 EELLRGIYayGFEKPSAIQQRAIIPCVRGHDVIAQAQSGTGKTATFsisilqQIDTSARECQALILAPTRELaQQIQkvV 129
Cdd:cd17920 1 EQILKEVF--GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCY------QLPALLLDGVTLVVSPLISL-MQDQ--V 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 130 IALGDfMGAMChACIGGT----NVREDMRKLEMGV--HVLVgTPGRVLDMISRRALK----TNTIRIFVLDEA------- 192
Cdd:cd17920 70 DRLQQ-LGIRA-AALNSTlspeEKREVLLRIKNGQykLLYV-TPERLLSPDFLELLQrlpeRKRLALIVVDEAhcvsqwg 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 939632536 193 ----DEMLsrgfkdQIHDVFKNLNHeVQVILLSATMPSDVLE--VSTCFMRNPI 240
Cdd:cd17920 147 hdfrPDYL------RLGRLRRALPG-VPILALTATATPEVREdiLKRLGLRNPV 193
|
|
| PRK05298 |
PRK05298 |
excinuclease ABC subunit UvrB; |
296-352 |
1.12e-03 |
|
excinuclease ABC subunit UvrB;
Pssm-ID: 235395 [Multi-domain] Cd Length: 652 Bit Score: 41.19 E-value: 1.12e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 939632536 296 LTESMHNRDFTVSAMHGDMEQRERDIIMRQFRTGSSRVLITTDLLARGIDVQQVSLV 352
Cdd:PRK05298 462 LTDYLKELGIKVRYLHSDIDTLERVEIIRDLRLGEFDVLVGINLLREGLDIPEVSLV 518
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
282-344 |
1.18e-03 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350182 [Multi-domain] Cd Length: 154 Bit Score: 39.07 E-value: 1.18e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939632536 282 QAVIFCNTRRKVDWLTESMhnrdFTVSAMHGDMEQRERDIIMRQFRTGSSRVLITTDLLARGI 344
Cdd:cd18795 45 PVLVFCSSRKECEKTAKDL----AGIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGV 103
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
267-356 |
1.47e-03 |
|
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: 38.88 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 267 KLDTLCDL-------YETLSITQAVIFCNTRRKVDWLTESMHNRDFTVSAM----HGD------MEQRERDIIMRQFRTG 329
Cdd:cd18801 10 KLEKLEEIvkehfkkKQEGSDTRVIIFSEFRDSAEEIVNFLSKIRPGIRATrfigQASgksskgMSQKEQKEVIEQFRKG 89
|
90 100
....*....|....*....|....*..
gi 939632536 330 SSRVLITTDLLARGIDVQQVSLVINYD 356
Cdd:cd18801 90 GYNVLVATSIGEEGLDIGEVDLIICYD 116
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
215-346 |
3.34e-03 |
|
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
Pssm-ID: 187770 [Multi-domain] Cd Length: 353 Bit Score: 39.34 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 215 VQVILLSATMPSDVLEvstcFMRNpIRILVKKEELTLEGIKQFFVFVEREEWKLD--TLCDLYETL-SITQAVIFCNTRR 291
Cdd:cd09639 155 VPILLMSATLPKFLKE----YAEK-IGYVEENEPLDLKPNERAPFIKIESDKVGEisSLERLLEFIkKGGSVAIIVNTVD 229
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939632536 292 KV----DWLTESMHnrDFTVSAMHGDMEQRER----DIIMRQFRTGSSRVLITTDLLARGIDV 346
Cdd:cd09639 230 RAqefyQQLKEKGP--EEEIMLIHSRFTEKDRakkeAELLLEFKKSEKFVIVATQVIEASLDI 290
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
304-356 |
4.69e-03 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350179 [Multi-domain] Cd Length: 160 Bit Score: 37.63 E-value: 4.69e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 939632536 304 DFTVSAMHGDMEQRERDIIMRQFRTGSSRVLITTDLLARGIDVQQVSLVINYD 356
Cdd:cd18792 60 EARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIED 112
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
280-369 |
8.76e-03 |
|
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: 34.99 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939632536 280 ITQAVIFCNTRRKVDWLTESMhnrdftvsamhgdmeqrerdiimrqfrtgssRVLITTDLLARGIDVQQVSLVINYDLPS 359
Cdd:cd18785 3 VVKIIVFTNSIEHAEEIASSL-------------------------------EILVATNVLGEGIDVPSLDTVIFFDPPS 51
|
90
....*....|
gi 939632536 360 NRENYIHRIG 369
Cdd:cd18785 52 SAASYIQRVG 61
|
|
| |
