|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
6-403 |
0e+00 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 587.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 6 EIPQDGPASMEP--EGVIESTWHEVYDNFDDMNLREELLRGIYGYGFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTAT 83
Cdd:PTZ00424 2 ATSEQKNQSEQVasTGTIESNYDEIVDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 84 FSIAILQQIDTSIRECQALILAPTRELATQIQRVVMALGEYMKVHSHACIGGTNVREDARILESGCHVVVGTPGRVYDMI 163
Cdd:PTZ00424 82 FVIAALQLIDYDLNACQALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 164 NRKVLRTQYIKLFVLDEADEMLSRGFKDQIQDVFKMLPPDVQVILLSATMPPDVLEVSRCFMRDPVSILVKKEELTLEGI 243
Cdd:PTZ00424 162 DKRHLRVDDLKLFILDEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 244 KQFYVNVKQENWKLGTLCDLYDTLSITQSVIFCNTRRKVDQLTQEMSIHNFTVSAMHGDMEQRDREVIMKQFRSGSSRVL 323
Cdd:PTZ00424 242 RQFYVAVEKEEWKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 324 ITTDLLARGIDVQQVSLVINYDLPSNRENYIHRIGRGGRFGRKGVAINFITDDDRRILKDIEQFYHTTIEEMPANIADLI 403
Cdd:PTZ00424 322 ITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEVADYL 401
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
31-396 |
2.90e-147 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 424.17 E-value: 2.90e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 31 NFDDMNLREELLRGIYGYGFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTATFSIAILQQIDTSI-RECQALILAPTRE 109
Cdd:COG0513 3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRpRAPQALILAPTRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 110 LATQIQRVVMALGEYMKVHSHACIGGTNVREDARILESGCHVVVGTPGRVYDMINRKVLRTQYIKLFVLDEADEMLSRGF 189
Cdd:COG0513 83 LALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 190 KDQIQDVFKMLPPDVQVILLSATMPPDVLEVSRCFMRDPVSILVKKEELTLEGIKQFYVNVKQENwKLGTLCDLYDTLSI 269
Cdd:COG0513 163 IEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRD-KLELLRRLLRDEDP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 270 TQSVIFCNTRRKVDQLTQEMSIHNFTVSAMHGDMEQRDREVIMKQFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPSN 349
Cdd:COG0513 242 ERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPED 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 442626267 350 RENYIHrigrggrfgrkgVAINFITDDDRRILKDIEQFYHTTIEEMP 396
Cdd:COG0513 322 PEDYVHrigrtgragaegTAISLVTPDERRLLRAIEKLIGQKIEEEE 368
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
32-232 |
8.25e-145 |
|
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: 409.53 E-value: 8.25e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 32 FDDMNLREELLRGIYGYGFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTATFSIAILQQIDTSIRECQALILAPTRELA 111
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 112 TQIQRVVMALGEYMKVHSHACIGGTNVREDARILESGCHVVVGTPGRVYDMINRKVLRTQYIKLFVLDEADEMLSRGFKD 191
Cdd:cd18046 81 QQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 442626267 192 QIQDVFKMLPPDVQVILLSATMPPDVLEVSRCFMRDPVSIL 232
Cdd:cd18046 161 QIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRIL 201
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
34-232 |
1.47e-125 |
|
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: 360.49 E-value: 1.47e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 34 DMNLREELLRGIYGYGFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTATFSIAILQQIDTSIRECQALILAPTRELATQ 113
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 114 IQRVVMALGEYMKVHSHACIGGTNVREDARILESGCHVVVGTPGRVYDMINRKVLRTQYIKLFVLDEADEMLSRGFKDQI 193
Cdd:cd17939 81 IQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQI 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 442626267 194 QDVFKMLPPDVQVILLSATMPPDVLEVSRCFMRDPVSIL 232
Cdd:cd17939 161 YDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRIL 199
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
32-232 |
1.26e-108 |
|
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: 317.49 E-value: 1.26e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 32 FDDMNLREELLRGIYGYGFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTATFSIAILQQIDTSIRECQALILAPTRELA 111
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 112 TQIQRVVMALGEYMKVHSHACIGGTNVREDARILESGCHVVVGTPGRVYDMINRKVLRTQYIKLFVLDEADEMLSRGFKD 191
Cdd:cd18045 81 VQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 442626267 192 QIQDVFKMLPPDVQVILLSATMPPDVLEVSRCFMRDPVSIL 232
Cdd:cd18045 161 QIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRIL 201
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
32-393 |
3.50e-87 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 272.06 E-value: 3.50e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 32 FDDMNLREELLRGIYGYGFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTATFSIAILQQIDTSIRECQALILAPTRELA 111
Cdd:PRK11776 6 FSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTRELA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 112 TQIQRVVMALGEYM---KVHShACiGGTNVREDARILESGCHVVVGTPGRVYDMINRKVLRTQYIKLFVLDEADEMLSRG 188
Cdd:PRK11776 86 DQVAKEIRRLARFIpniKVLT-LC-GGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 189 FKDQIQDVFKMLPPDVQVILLSATMPPDVLEVSRCFMRDPVSILV--KKEELTLEgiKQFYvNVKQENwKLGTLCDLYDT 266
Cdd:PRK11776 164 FQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVesTHDLPAIE--QRFY-EVSPDE-RLPALQRLLLH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 267 LSITQSVIFCNTRRKVDQLTQEMSIHNFTVSAMHGDMEQRDREVIMKQFRSGSSRVLITTDLLARGIDVQQVSLVINYDL 346
Cdd:PRK11776 240 HQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYEL 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 442626267 347 PSNRENYIHRIGRGGRFGRKGVAINFITDDDRRILKDIEQFYHTTIE 393
Cdd:PRK11776 320 ARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLN 366
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
41-231 |
5.16e-84 |
|
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: 254.67 E-value: 5.16e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 41 LLRGIYGYGFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTATFSIAILQQIDT----SIRECQALILAPTRELATQIQR 116
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPepkkKGRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 117 VVMALGEYMKVHSHACIGGTNVREDARILESGCHVVVGTPGRVYDMINRKVLRTQYIKLFVLDEADEMLSRGFKDQIQDV 196
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 442626267 197 FKMLPPDVQVILLSATMPPDVLEVSRCFMRDPVSI 231
Cdd:cd00268 161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
27-403 |
1.17e-75 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 246.68 E-value: 1.17e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 27 EVYDNFDDMNLREELLRGIYGYGFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTATFSIAILQQIDTSIRECQALILAP 106
Cdd:PRK11634 3 EFETTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 107 TRELATQIQRVVMALGEYMK-VHSHACIGGTNVREDARILESGCHVVVGTPGRVYDMINRKVLRTQYIKLFVLDEADEML 185
Cdd:PRK11634 83 TRELAVQVAEAMTDFSKHMRgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEML 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 186 SRGFKDQIQDVFKMLPPDVQVILLSATMPPDVLEVSRCFMRDPVSILVKKEELTLEGIKQFYVNVkQENWKLGTLCDLYD 265
Cdd:PRK11634 163 RMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTV-WGMRKNEALVRFLE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 266 TLSITQSVIFCNTRRKVDQLTQEMSIHNFTVSAMHGDMEQRDREVIMKQFRSGSSRVLITTDLLARGIDVQQVSLVINYD 345
Cdd:PRK11634 242 AEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYD 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 442626267 346 LPSNRENYIHRIGRGGRFGRKGVAINFITDDDRRILKDIEQFYHTTIEEMPANIADLI 403
Cdd:PRK11634 322 IPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAELL 379
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
32-231 |
9.51e-71 |
|
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: 221.02 E-value: 9.51e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 32 FDDMNLREELLRGIYGYGFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTATFSIAILQQIDTSIRECQALILAPTRELA 111
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 112 TQIQRVVMALGEYMKVHSHACIGGTNVREDARILESGCHVVVGTPGRVYDMINRKVLRTQYIKLFVLDEADEMLSRGFKD 191
Cdd:cd17940 81 LQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 442626267 192 QIQDVFKMLPPDVQVILLSATMPPDVLEVSRCFMRDPVSI 231
Cdd:cd17940 161 IIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
37-231 |
1.04e-68 |
|
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: 215.52 E-value: 1.04e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 37 LREELLRGIYGYGFEKPSAIQQRAIIPCVRG--RDVIAQAQSGTGKTATFSIAILQQIDTSIRECQALILAPTRELATQI 114
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 115 QRVVMALGEYMKVHSHACIGGTNVREDARILEsgcHVVVGTPGRVYDMINRKVLRTQYIKLFVLDEADEML-SRGFKDQI 193
Cdd:cd17963 81 GEVVEKMGKFTGVKVALAVPGNDVPRGKKITA---QIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLdTQGHGDQS 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 442626267 194 QDVFKMLPPDVQVILLSATMPPDVLEVSRCFMRDPVSI 231
Cdd:cd17963 158 IRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
4-396 |
5.63e-68 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 222.87 E-value: 5.63e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 4 RNEIPQDGPASMEPEG-VIEStwHEVYDNFDDMNLREELLRGIYGYGFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTA 82
Cdd:PRK01297 62 RRERKPKPASLWKLEDfVVEP--QEGKTRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 83 TFSIAILQQI-------DTSIRECQALILAPTRELATQIQRVVMALGEYMKVHSHACIGGTNVREDARILESG-CHVVVG 154
Cdd:PRK01297 140 AFLISIINQLlqtpppkERYMGEPRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 155 TPGRVYDMINRKVLRTQYIKLFVLDEADEMLSRGFKDQIQDVFKMLPP--DVQVILLSATMPPDVLEVSRCFMRDPVSIL 232
Cdd:PRK01297 220 TPGRLLDFNQRGEVHLDMVEVMVLDEADRMLDMGFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVE 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 233 VKKEELTLEGIKQ-FYVNVKQENWKLgtLCDLYDTLSITQSVIFCNTRRKVDQLTQEMSIHNFTVSAMHGDMEQRDREVI 311
Cdd:PRK01297 300 IEPENVASDTVEQhVYAVAGSDKYKL--LYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKT 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 312 MKQFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPSNRENYIHRIGRGGRFGRKGVAINFITDDDRRILKDIEQFYHTT 391
Cdd:PRK01297 378 LEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRK 457
|
....*.
gi 442626267 392 IE-EMP 396
Cdd:PRK01297 458 IScEMP 463
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
31-395 |
1.40e-67 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 221.22 E-value: 1.40e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 31 NFDDMNLREELLRGIYGYGFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTATFSIAILQQIDTSI------RECQALIL 104
Cdd:PRK10590 2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQphakgrRPVRALIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 105 APTRELATQIQRVVMALGEYMKVHSHACIGGTNVREDARILESGCHVVVGTPGRVYDMINRKVLRTQYIKLFVLDEADEM 184
Cdd:PRK10590 82 TPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 185 LSRGFKDQIQDVFKMLPPDVQVILLSATMPPDVLEVSRCFMRDPVSILVKKEELTLEGIKQFyVNVKQENWKLGTLCDLY 264
Cdd:PRK10590 162 LDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQH-VHFVDKKRKRELLSQMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 265 DTLSITQSVIFCNTRRKVDQLTQEMSIHNFTVSAMHGDMEQRDREVIMKQFRSGSSRVLITTDLLARGIDVQQVSLVINY 344
Cdd:PRK10590 241 GKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNY 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 442626267 345 DLPSNRENYIHRIGRGGRFGRKGVAINFITDDDRRILKDIEQFYHTTIEEM 395
Cdd:PRK10590 321 ELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRI 371
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
32-233 |
4.79e-63 |
|
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: 201.42 E-value: 4.79e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 32 FDDMNLREELLRGIYGYGFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTATFSIAILQQIDTSIRECQALILAPTRELA 111
Cdd:cd17950 4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRELA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 112 TQIQRVVMALGEYMKVHSHACI-GGTNVREDARILESGC-HVVVGTPGRVYDMINRKVLRTQYIKLFVLDEADEML-SRG 188
Cdd:cd17950 84 FQISNEYERFSKYMPNVKTAVFfGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLeQLD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 442626267 189 FKDQIQDVFKMLPPDVQVILLSATMPPDVLEVSRCFMRDPVSILV 233
Cdd:cd17950 164 MRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
41-384 |
5.52e-62 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 208.86 E-value: 5.52e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 41 LLRGIYGYGFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTATFSI---------AILQQIDTSIrecqALILAPTRELA 111
Cdd:PTZ00110 141 ILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLpaivhinaqPLLRYGDGPI----VLVLAPTRELA 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 112 TQIQRVVMALGEYMKVHSHACIGGTNVREDARILESGCHVVVGTPGRVYDMINRKVLRTQYIKLFVLDEADEMLSRGFKD 191
Cdd:PTZ00110 217 EQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEP 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 192 QIQDVFKMLPPDVQVILLSATMPPDVLEVSRCFMRD-PVSILVKKEELTL-EGIKQfYVNVKQENWKLGTLCDLYDTL-- 267
Cdd:PTZ00110 297 QIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDLTAcHNIKQ-EVFVVEEHEKRGKLKMLLQRImr 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 268 SITQSVIFCNTRRKVDQLTQEMSIHNFTVSAMHGDMEQRDREVIMKQFRSGSSRVLITTDLLARGIDVQQVSLVINYDLP 347
Cdd:PTZ00110 376 DGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFP 455
|
330 340 350
....*....|....*....|....*....|....*..
gi 442626267 348 SNRENYIHRIGRGGRFGRKGVAINFITDDDRRILKDI 384
Cdd:PTZ00110 456 NQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDL 492
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
31-387 |
8.75e-62 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 205.18 E-value: 8.75e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 31 NFDDMNLREELLRGIYGYGFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTATFSIAILQQ-IDTSIRECQA---LILAP 106
Cdd:PRK11192 2 TFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHlLDFPRRKSGPpriLILTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 107 TRELATQIQRVVMALGEYMKVHSHACIGGTNVREDARILESGCHVVVGTPGRVYDMINRKVLRTQYIKLFVLDEADEMLS 186
Cdd:PRK11192 82 TRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 187 RGFKdqiQDVFKMLPPDV---QVILLSATMP-PDVLEVSRCFMRDPVSILVKKEELTLEGIKQFYVNVKQENWKLGTLCD 262
Cdd:PRK11192 162 MGFA---QDIETIAAETRwrkQTLLFSATLEgDAVQDFAERLLNDPVEVEAEPSRRERKKIHQWYYRADDLEHKTALLCH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 263 LYDTLSITQSVIFCNTRRKVDQLTQEMSIHNFTVSAMHGDMEQRDREVIMKQFRSGSSRVLITTDLLARGIDVQQVSLVI 342
Cdd:PRK11192 239 LLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVI 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 442626267 343 NYDLPSNRENYIHRIGRGGRFGRKGVAINFITDDDRRILKDIEQF 387
Cdd:PRK11192 319 NFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERY 363
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
41-231 |
1.56e-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: 194.40 E-value: 1.56e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 41 LLRGIYGYGFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTATFSIAILQQIDTSIRECQALILAPTRELATQIQRVVMA 120
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 121 LGEYMK-VHSHACIGGTNVREDaRILESGCHVVVGTPGRVYDMINRKVLRTQYIKLFVLDEADEMLSRGFKDQIQDVFKM 199
Cdd:cd17943 81 IGKKLEgLKCEVFIGGTPVKED-KKKLKGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSS 159
|
170 180 190
....*....|....*....|....*....|..
gi 442626267 200 LPPDVQVILLSATMPPDVLEVSRCFMRDPVSI 231
Cdd:cd17943 160 LPKNKQVIAFSATYPKNLDNLLARYMRKPVLV 191
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
31-396 |
1.02e-58 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 200.56 E-value: 1.02e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 31 NFDDMNLREELLRGIYGYGFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTATFSIAILQQI-------DTSIRECQALI 103
Cdd:PRK04537 10 TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlsrpalaDRKPEDPRALI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 104 LAPTRELATQIQRVVMALGEYMKVHSHACIGGTNVREDARILESGCHVVVGTPGRVYDMINR-KVLRTQYIKLFVLDEAD 182
Cdd:PRK04537 90 LAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQhKVVSLHACEICVLDEAD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 183 EMLSRGFKDQIQDVFKMLPPDV--QVILLSATMPPDVLEVSRCFMRDPVSILVKKEELTLEGIKQ-FYVNVKQEnwKLGT 259
Cdd:PRK04537 170 RMFDLGFIKDIRFLLRRMPERGtrQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQrIYFPADEE--KQTL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 260 LCDLYDTLSITQSVIFCNTRRKVDQLTQEMSIHNFTVSAMHGDMEQRDREVIMKQFRSGSSRVLITTDLLARGIDVQQVS 339
Cdd:PRK04537 248 LLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVK 327
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 442626267 340 LVINYDLPSNRENYIHRIGRGGRFGRKGVAINFITDDDRRILKDIEQFYHTTIEEMP 396
Cdd:PRK04537 328 YVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKIPVEP 384
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
54-220 |
5.14e-57 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 184.37 E-value: 5.14e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 54 SAIQQRAIIPCVRGRDVIAQAQSGTGKTATFSIAILQQIDTSIRECQALILAPTRELATQIQRVVMALGEYMKVHSHACI 133
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 134 GGTNVREDARILEsGCHVVVGTPGRVYDMINRKVlRTQYIKLFVLDEADEMLSRGFKDQIQDVFKMLPPDVQVILLSATM 213
Cdd:pfam00270 81 GGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATL 158
|
....*..
gi 442626267 214 PPDVLEV 220
Cdd:pfam00270 159 PRNLEDL 165
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
32-386 |
1.43e-56 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 193.85 E-value: 1.43e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 32 FDDMNLREELLRGIYGYGFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTATFSIAILQ-------QIDTSIRECQALIL 104
Cdd:PLN00206 123 FSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISrcctirsGHPSEQRNPLAMVL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 105 APTRELATQIQRVVMALGEYMKVHSHACIGGTNVREDARILESGCHVVVGTPGRVYDMINRKVLRTQYIKLFVLDEADEM 184
Cdd:PLN00206 203 TPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCM 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 185 LSRGFKDQIQDVFKMLPPDvQVILLSATMPPDVLEVSRCFMRDPVSILVKKEELTLEGIKQ--FYVNVKQENWKLgtlcd 262
Cdd:PLN00206 283 LERGFRDQVMQIFQALSQP-QVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQlaIWVETKQKKQKL----- 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 263 lYDTLSITQ-----SVIFCNTRRKVDQLTQEMSI-HNFTVSAMHGDMEQRDREVIMKQFRSGSSRVLITTDLLARGIDVQ 336
Cdd:PLN00206 357 -FDILKSKQhfkppAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLL 435
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 442626267 337 QVSLVINYDLPSNRENYIHRIGRGGRFGRKGVAINFITDDDRRILKDIEQ 386
Cdd:PLN00206 436 RVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVA 485
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
45-246 |
2.09e-53 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 176.14 E-value: 2.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 45 IYGYGFEKPSAIQQRAIIPCVRG-RDVIAQAQSGTGKTATFSIAILQQIDTSiRECQALILAPTRELATQIQRVVMALGE 123
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRG-KGGRVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 124 YMKVHSHACIGGTNVREDARILESGC-HVVVGTPGRVYDMINRKVLRTQYIKLFVLDEADEMLSRGFKDQIQDVFKMLPP 202
Cdd:smart00487 80 SLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 442626267 203 DVQVILLSATMPPDVLEVSRCFMRDPVSILVkkEELTLEGIKQF 246
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFIDV--GFTPLEPIEQF 201
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
32-357 |
2.86e-51 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 177.47 E-value: 2.86e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 32 FDDMNLREELLRGIYGYGFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKT-----ATFSIAILQQIDTSIRECQ--ALIL 104
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTmafltATFHYLLSHPAPEDRKVNQprALIM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 105 APTRELATQIQRVVMALGEYMKVHSHACIGGTNVREDARILESGCHVVVGTPGRVYDMINRKVLRTQYIKLFVLDEADEM 184
Cdd:PRK04837 90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 185 LSRGFKDQIQDVFKMLPPDVQ--VILLSATMPPDVLEVSRCFMRDPVSILVKKEELTLEGIKQ--FYVNvKQENWKLgtL 260
Cdd:PRK04837 170 FDLGFIKDIRWLFRRMPPANQrlNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEelFYPS-NEEKMRL--L 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 261 CDLYDTLSITQSVIFCNTRRKVDQLTQEMSIHNFTVSAMHGDMEQRDREVIMKQFRSGSSRVLITTDLLARGIDVQQVSL 340
Cdd:PRK04837 247 QTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTH 326
|
330
....*....|....*..
gi 442626267 341 VINYDLPSNRENYIHRI 357
Cdd:PRK04837 327 VFNYDLPDDCEDYVHRI 343
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
32-231 |
2.21e-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: 168.26 E-value: 2.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 32 FDDMNLREELLRGIYGYGFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTATFSIAILQQIDTSIRECQALILAPTRELA 111
Cdd:cd17954 2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTRELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 112 TQIQRVVMALGEYMKVHSHACIGGTNVREDARILESGCHVVVGTPGRVYDMI-NRKVLRTQYIKLFVLDEADEMLSRGFK 190
Cdd:cd17954 82 QQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLeNTKGFSLKSLKFLVMDEADRLLNMDFE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 442626267 191 DQIQDVFKMLPPDVQVILLSATMPPDVLEVSRCFMRDPVSI 231
Cdd:cd17954 162 PEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
32-227 |
4.18e-50 |
|
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: 168.43 E-value: 4.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 32 FDDMNLREELLRGIYGYGFEKPSAIQQRAIiPCVR-GRDVIAQAQSGTGKTATFSIAILQQI-------DTSIRECQ--- 100
Cdd:cd17967 2 FEEAGLRELLLENIKRAGYTKPTPVQKYAI-PIILaGRDLMACAQTGSGKTAAFLLPIISKLledgppsVGRGRRKAyps 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 101 ALILAPTRELATQIQRVVMALGEYMKVHSHACIGGTNVREDARILESGCHVVVGTPGRVYDMINRKVLRTQYIKLFVLDE 180
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 442626267 181 ADEMLSRGFKDQIQDVFK---MLPPDV-QVILLSATMPPDVLEVSRCFMRD 227
Cdd:cd17967 161 ADRMLDMGFEPQIRKIVEhpdMPPKGErQTLMFSATFPREIQRLAADFLKN 211
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
32-229 |
3.56e-49 |
|
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: 165.48 E-value: 3.56e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 32 FDDMNLREELLRGIYGYGFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTATFSIAILQQIDTSIRECQALILAPTRELA 111
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 112 TQIQRVVMALGEYMKVHSHACIGGTNVREDARILESGCHVVVGTPGRVYDMIN-----RKVLRtqYIKLFVLDEADEMLS 186
Cdd:cd17955 81 YQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssddtTKVLS--RVKFLVLDEADRLLT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 442626267 187 RGFKDQIQDVFKMLPPDVQVILLSATMPPDVLEVSRCFMRDPV 229
Cdd:cd17955 159 GSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPF 201
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
41-231 |
1.01e-48 |
|
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: 163.96 E-value: 1.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 41 LLRGIYGYGFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTATFSIAILQQI---DTSIRECQALILAPTRELATQIQRV 117
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLlyrPKKKAATRVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 118 VMALGEYMKVHSHACIGGTNVREDARILESGCHVVVGTPGRVYDMI-NRKVLRTQYIKLFVLDEADEMLSRGFKDQIQDV 196
Cdd:cd17947 81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLrNSPSFDLDSIEILVLDEADRMLEEGFADELKEI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 442626267 197 FKMLPPDVQVILLSATMPPDVLEVSRCFMRDPVSI 231
Cdd:cd17947 161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
40-226 |
4.23e-48 |
|
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: 162.75 E-value: 4.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 40 ELLRGIYGYGFEKPSAIQQRAIIPCVR-GRDVIAQAQSGTGKTATFSIAILQ-----QIDTSIRECQALILAPTRELATQ 113
Cdd:cd17964 4 SLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQsllntKPAGRRSGVSALIISPTRELALQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 114 IQRVVMALGEYM-KVHSHACIGGTNVRED-ARILESGCHVVVGTPGRVYDMINRKVLRTQY--IKLFVLDEADEMLSRGF 189
Cdd:cd17964 84 IAAEAKKLLQGLrKLRVQSAVGGTSRRAElNRLRRGRPDILVATPGRLIDHLENPGVAKAFtdLDYLVLDEADRLLDMGF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 442626267 190 KDQIQDVFKMLPP----DVQVILLSATMPPDVLEVSRCFMR 226
Cdd:cd17964 164 RPDLEQILRHLPEknadPRQTLLFSATVPDEVQQIARLTLK 204
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
31-231 |
5.21e-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: 5.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 31 NFDDMNLREELLRGIYGYGFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTATFSIAILQQIDTS-----IRecqALILA 105
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHsptvgAR---ALILS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 106 PTRELATQIQRVVMALGEYMKVHSHACIGGTNVREDARILESGCHVVVGTPGRVYDMINRKVLRTQYIKLFVLDEADEML 185
Cdd:cd17959 79 PTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 442626267 186 SRGFKDQIQDVFKMLPPDVQVILLSATMPPDVLEVSRCFMRDPVSI 231
Cdd:cd17959 159 EMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
37-231 |
1.72e-44 |
|
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: 153.12 E-value: 1.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 37 LREELLRGIYGYGFEKPSAIQQRAIiPC-VRGRDVIAQAQSGTGKTATFSIAILQQI------DTSIRECQALILAPTRE 109
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAI-PLaLEGKDILARARTGSGKTAAYALPIIQKIlkakaeSGEEQGTRALILVPTRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 110 LATQIQRVVMALGEYM--KVHSHACIGGTNVREDARILESGCHVVVGTPGRVYDMINRKVLRTQ-YIKLFVLDEADEMLS 186
Cdd:cd17961 80 LAQQVSKVLEQLTAYCrkDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLLsTLKYLVIDEADLVLS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 442626267 187 RGFKDQIQDVFKMLPPDVQVILLSATMPPDVLEVSRCFMRDPVSI 231
Cdd:cd17961 160 YGYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPAIL 204
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
243-358 |
1.71e-43 |
|
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: 148.04 E-value: 1.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 243 IKQFYVNVKQENWKLGTLCDLYDTLSITQSVIFCNTRRKVDQLTQEMSIHNFTVSAMHGDMEQRDREVIMKQFRSGSSRV 322
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 442626267 323 LITTDLLARGIDVQQVSLVINYDLPSNRENYIHRIG 358
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIG 116
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
41-231 |
4.43e-43 |
|
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: 149.10 E-value: 4.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 41 LLRGIYGYGFEKPSAIQQRAIiPCV-RGRDVIAQAQSGTGKTATFSIAILQQIdTSIRECQ------ALILAPTRELATQ 113
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQAL-PVAlSGRDMIGIAKTGSGKTAAFIWPMLVHI-MDQRELEkgegpiAVIVAPTRELAQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 114 IQRVVMALGEYMKVHSHACIGGTNVREDARILESGCHVVVGTPGRVYDMINRKVLRTQYIKLFVLDEADEMLSRGFKDQI 193
Cdd:cd17952 79 IYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQV 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 442626267 194 QDVFKMLPPDVQVILLSATMPPDVLEVSRCFMRDPVSI 231
Cdd:cd17952 159 RSIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
41-231 |
3.33e-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: 147.47 E-value: 3.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 41 LLRGIYGYGFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTATFSIAILQQIDT----SIRECQ----ALILAPTRELAT 112
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRlpplDEETKDdgpyALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 113 QIQRVVMALGEYMKVHSHACIGGTNVREDARILESGCHVVVGTPGRVYDMINRKVL---RTQYIklfVLDEADEMLSRGF 189
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLvlnQCTYV---VLDEADRMIDMGF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626267 190 KDQIQDVFKMLPPDV--------------------QVILLSATMPPDVLEVSRCFMRDPVSI 231
Cdd:cd17945 158 EPQVTKILDAMPVSNkkpdteeaeklaasgkhryrQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
37-231 |
3.46e-42 |
|
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: 147.52 E-value: 3.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 37 LREELLRGIYGYGFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTATFSIAILQQI---------DTSIrecqALILAPT 107
Cdd:cd17953 19 LSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIkdqrpvkpgEGPI----GLIMAPT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 108 RELATQIQRVVMALGEYMKVHSHACIGGTNVREDARILESGCHVVVGTPGRVYDMI---NRKVLRTQYIKLFVLDEADEM 184
Cdd:cd17953 95 RELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtanNGRVTNLRRVTYVVLDEADRM 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 442626267 185 LSRGFKDQIQDVFKMLPPDVQVILLSATMPPDVLEVSRCFMRDPVSI 231
Cdd:cd17953 175 FDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
31-226 |
3.46e-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: 148.96 E-value: 3.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 31 NFDDMNLREELLRGIYGYGFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTATFSIAILQQIDTS---------IRECQA 101
Cdd:cd18052 44 TFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEgltassfseVQEPQA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 102 LILAPTRELATQIQRVVMALGEYMKVHSHACIGGTNVREDARILESGCHVVVGTPGRVYDMINRKVLRTQYIKLFVLDEA 181
Cdd:cd18052 124 LIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEA 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 442626267 182 DEMLSRGFKDQIQDV---FKMlPP--DVQVILLSATMPPDVLEVSRCFMR 226
Cdd:cd18052 204 DRMLDMGFGPEIRKLvsePGM-PSkeDRQTLMFSATFPEEIQRLAAEFLK 252
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
41-233 |
3.81e-42 |
|
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: 146.58 E-value: 3.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 41 LLRGIYGYGFEKPSAIQQRAIiPC-VRGRDVIAQAQSGTGKTATFSIAILQQI--DTSIRECQALILAPTRELATQIQRV 117
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAI-PIlLHGRDLLACAPTGSGKTLAFLIPILQKLgkPRKKKGLRALILAPTRELASQIYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 118 VMALGEYMKVHSHACIGGTNVR-EDARILESGCHVVVGTPGRVYDMINRKVLRTQYIKLFVLDEADEMLSRGFKDQIQDV 196
Cdd:cd17957 80 LLKLSKGTGLRIVLLSKSLEAKaKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEI 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 442626267 197 FKMLP-PDVQVILLSATMPPDVLEVSRCFMRDPVSILV 233
Cdd:cd17957 160 LAACTnPNLQRSLFSATIPSEVEELARSVMKDPIRIIV 197
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
32-229 |
2.62e-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: 144.77 E-value: 2.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 32 FDDMNLREELLRGIYGYGFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTATFSIAILQQIdtsirecQALILAPTRELA 111
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV-------VALILEPSRELA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 112 TQIQRVVMALGEYM---KVHSHACIGGTNVREDARILESGCHVVVGTPGRVYDMINRKVLRTQYIKLFVLDEADEMLSRG 188
Cdd:cd17938 74 EQTYNCIENFKKYLdnpKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 442626267 189 FKDQIQDVFKMLPP------DVQVILLSATM-PPDVLEVSRCFMRDPV 229
Cdd:cd17938 154 NLETINRIYNRIPKitsdgkRLQVIVCSATLhSFEVKKLADKIMHFPT 201
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
31-239 |
6.43e-41 |
|
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: 144.78 E-value: 6.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 31 NFDDMNLREELLRGIYGYGFEKPSAIQQRAIiPCVRG---RDVIAQAQSGTGKTATFSIAILQQIDTSIRECQALILAPT 107
Cdd:cd18048 19 SFEELHLKEELLRGIYAMGFNRPSKIQENAL-PMMLAdppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLSPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 108 RELATQIQRVVMALGEY-MKVHSHACIGGTNVREDARILEsgcHVVVGTPGRVYDMINR-KVLRTQYIKLFVLDEADEML 185
Cdd:cd18048 98 FELALQTGKVVEEMGKFcVGIQVIYAIRGNRPGKGTDIEA---QIVIGTPGTVLDWCFKlRLIDVTNISVFVLDEADVMI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 442626267 186 S-RGFKDQIQDVFKMLPPDVQVILLSATMPPDVLEVSRCFMRDPVSILVKKEELT 239
Cdd:cd18048 175 NvQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
30-227 |
3.21e-40 |
|
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: 143.26 E-value: 3.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 30 DNFDDMNLREELLRGIYGYGFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTATFSIAILQQIDT-------------SI 96
Cdd:cd18051 21 ETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEqgpgeslpsesgyYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 97 RECQ---ALILAPTRELATQIqrvvmaLGEYMKV----HSHACI--GGTNVREDARILESGCHVVVGTPGRVYDMINRKV 167
Cdd:cd18051 101 RRKQyplALVLAPTRELASQI------YDEARKFayrsRVRPCVvyGGADIGQQMRDLERGCHLLVATPGRLVDMLERGK 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442626267 168 LRTQYIKLFVLDEADEMLSRGFKDQI-----QDVfkmLPP--DVQVILLSATMPPDVLEVSRCFMRD 227
Cdd:cd18051 175 IGLDYCKYLVLDEADRMLDMGFEPQIrriveQDT---MPPtgERQTLMFSATFPKEIQMLARDFLDN 238
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
41-231 |
8.94e-40 |
|
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: 140.38 E-value: 8.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 41 LLRGIYGYGFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTATFSIAILQQIDTSIRECQALILAPTRELATQIQRVVMA 120
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 121 LGE-YMKVHSHACIGGTNVREDARILESGCHVVVGTPGRVYDMINRKVLRTQYIKLFVLDEADEMLSRGFKDQIQDVFKM 199
Cdd:cd17962 81 LMKgLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILEN 160
|
170 180 190
....*....|....*....|....*....|..
gi 442626267 200 LPPDVQVILLSATMPPDVLEVSRCFMRDPVSI 231
Cdd:cd17962 161 ISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
41-231 |
2.38e-39 |
|
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: 139.63 E-value: 2.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 41 LLRGIYGYGFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTATFSIAILQQI-----DTSIRECQALILAPTRELATQIQ 115
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrkaNLKKGQVGALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 116 RVVMALGEYM--KVHSHACIGGTNVRED-ARILESGCHVVVGTPGRVYDMINRK--VLRTQYIKLFVLDEADEMLSRGFK 190
Cdd:cd17960 81 EVLQSFLEHHlpKLKCQLLIGGTNVEEDvKKFKRNGPNILVGTPGRLEELLSRKadKVKVKSLEVLVLDEADRLLDLGFE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 442626267 191 DQIQDVFKMLPPDVQVILLSATMPPDVLEVSRCFMRDPVSI 231
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
41-231 |
1.60e-38 |
|
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts with several spliceosomal proteins and may recognize the bacterial second messengers cyclic di-GMP and cyclic di-AMP, resulting in the induction of genes involved in the innate immune response. Diseases associated with DDX41 include "myeloproliferative/lymphoproliferative neoplasms, familial" and "Ddx41-related susceptibility to familial myeloproliferative/lymphoproliferative neoplasms". DDX41 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350709 [Multi-domain] Cd Length: 206 Bit Score: 137.47 E-value: 1.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 41 LLRGIYGYGFEKPSAIQQRAIiPCV-RGRDVIAQAQSGTGKTATFSIAIL-----QQIDTSIRECQ---ALILAPTRELA 111
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGL-PTIlSGRDMIGIAFTGSGKTLVFTLPLImfaleQEKKLPFIKGEgpyGLIVCPSRELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 112 TQIQRVV------MALGEYMKVHSHACIGGTNVREDARILESGCHVVVGTPGRVYDMINRKVLRTQYIKLFVLDEADEML 185
Cdd:cd17951 80 RQTHEVIeyyckaLQEGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 442626267 186 SRGFKDQIQDVFKMLPPDVQVILLSATMPPDVLEVSRCFMRDPVSI 231
Cdd:cd17951 160 DMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
42-231 |
5.45e-38 |
|
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein and is activated by Myc protein. DDX18 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350700 [Multi-domain] Cd Length: 198 Bit Score: 135.95 E-value: 5.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 42 LRGIYGYGFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTATFSIAILQQIdTSIRECQ-----ALILAPTRELATQIQR 116
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELL-YKLKFKPrngtgVIIISPTRELALQIYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 117 VVMALgeyMKVHSHAC---IGGTNVREDARILESGCHVVVGTPGRVYD-MINRKVLRTQYIKLFVLDEADEMLSRGFKDQ 192
Cdd:cd17942 81 VAKEL---LKYHSQTFgivIGGANRKAEAEKLGKGVNILVATPGRLLDhLQNTKGFLYKNLQCLIIDEADRILEIGFEEE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 442626267 193 IQDVFKMLPPDVQVILLSATMPPDVLEVSR-CFMRDPVSI 231
Cdd:cd17942 158 MRQIIKLLPKRRQTMLFSATQTRKVEDLARiSLKKKPLYV 197
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
41-231 |
1.22e-37 |
|
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: 134.80 E-value: 1.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 41 LLRGIYGYGFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTATFSI---------AILQQIDTSIrecqALILAPTRELA 111
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLpaivhinaqPPLERGDGPI----VLVLAPTRELA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 112 TQIQRVVMALGEYMKVHSHACIGGTNVREDARILESGCHVVVGTPGRVYDMINRKVLRTQYIKLFVLDEADEMLSRGFKD 191
Cdd:cd17966 77 QQIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 442626267 192 QIQDVFKMLPPDVQVILLSATMPPDVLEVSRCFMRDPVSI 231
Cdd:cd17966 157 QIRKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
42-233 |
2.38e-37 |
|
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: 133.95 E-value: 2.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 42 LRGIYGYGFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTATFSIAILQQID----TSIRECQALILAPTRELATQIQRV 117
Cdd:cd17941 2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYrerwTPEDGLGALIISPTRELAMQIFEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 118 VMALGEYmkvHSHAC---IGGTNVREDA-RIleSGCHVVVGTPGRVYDMINRKV-LRTQYIKLFVLDEADEMLSRGFKDQ 192
Cdd:cd17941 82 LRKVGKY---HSFSAgliIGGKDVKEEKeRI--NRMNILVCTPGRLLQHMDETPgFDTSNLQMLVLDEADRILDMGFKET 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 442626267 193 IQDVFKMLPPDVQVILLSATMPPDVLEVSRCFMRDPVSILV 233
Cdd:cd17941 157 LDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
49-231 |
1.71e-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: 132.32 E-value: 1.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 49 GFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTATFSIAILQQI---DTSI-RE--CQALILAPTRELATQIQRVVMALG 122
Cdd:cd17949 10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLlslEPRVdRSdgTLALVLVPTRELALQIYEVLEKLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 123 EYMK-VHSHACIGGTNVR-EDARiLESGCHVVVGTPGRVYDMI-NRKVLRTQYIKLFVLDEADEMLSRGFKDQIQDVFKM 199
Cdd:cd17949 90 KPFHwIVPGYLIGGEKRKsEKAR-LRKGVNILIATPGRLLDHLkNTQSFDVSNLRWLVLDEADRLLDMGFEKDITKILEL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 442626267 200 L-------------PPDVQVILLSATMPPDVLEVSRCFMRDPVSI 231
Cdd:cd17949 169 LddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
41-213 |
7.39e-36 |
|
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: 131.21 E-value: 7.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 41 LLRGIYGYGFEKPSAIQQRAIIPCVR-GRDVIAQAQSGTGKTATFSIAILQQI---------DTSIRECQALILAPTREL 110
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLlsqkssngvGGKQKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 111 ATQIQRVVMALGEYMKVHSHACIGGTNVREDARILESGCHVVVGTPGRVYDMI---NRKVLRTQYIKLFVLDEADEMLSR 187
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIqegNEHLANLKSLRFLVLDEADRMLEK 160
|
170 180 190
....*....|....*....|....*....|...
gi 442626267 188 GFKDQIQDVFKMLP-------PDVQVILLSATM 213
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 ... |
32-228 |
1.22e-35 |
|
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: 129.84 E-value: 1.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 32 FDDMNLREELLRGIYGYGFEKPSAIQQRAIiPCVRG---RDVIAQAQSGTGKTATFSIAILQQIDTSIRECQALILAPTR 108
Cdd:cd18047 3 FEELRLKPQLLQGVYAMGFNRPSKIQENAL-PLMLAeppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 109 ELATQIQRVVMALGE-YMKVHSHACIGGTNVREDARILEsgcHVVVGTPGRVYD-MINRKVLRTQYIKLFVLDEADEML- 185
Cdd:cd18047 82 ELALQTGKVIEQMGKfYPELKLAYAVRGNKLERGQKISE---QIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADVMIa 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 442626267 186 SRGFKDQIQDVFKMLPPDVQVILLSATMPPDVLEVSRCFMRDP 228
Cdd:cd18047 159 TQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
41-231 |
1.41e-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: 1.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 41 LLRGIYGYGFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTATFSIAILQQIDT--SIRECQ----ALILAPTRELATQI 114
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLqpIPREQRngpgVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 115 QrvvmalGEYMKvHSH-----ACI-GGTNVREDARILESGCHVVVGTPGRVYDMINRKVLRTQYIKLFVLDEADEMLSRG 188
Cdd:cd17958 81 E------AECSK-YSYkglksVCVyGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 442626267 189 FKDQIQDVFKMLPPDVQVILLSATMPPDVLEVSRCFMRDPVSI 231
Cdd:cd17958 154 FEPQIRKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
31-231 |
1.29e-31 |
|
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, G17P1, or HUMP68) is involved in pathways that include the alteration of RNA structures, plays a role as a coregulator of transcription, a regulator of splicing, and in the processing of small noncoding RNAs. It synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. Dysregulation of this gene may play a role in cancer development. DDX5 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350807 [Multi-domain] Cd Length: 234 Bit Score: 120.11 E-value: 1.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 31 NFDDMNLREELLRGIYGYGFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTATFSIA---------ILQQIDTSIrecqA 101
Cdd:cd18049 25 NFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPaivhinhqpFLERGDGPI----C 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 102 LILAPTRELATQIQRVVMALGEYMKVHSHACIGGTNVREDARILESGCHVVVGTPGRVYDMI---NRKVLRTQYIklfVL 178
Cdd:cd18049 101 LVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLeagKTNLRRCTYL---VL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 442626267 179 DEADEMLSRGFKDQIQDVFKMLPPDVQVILLSATMPPDVLEVSRCFMRDPVSI 231
Cdd:cd18049 178 DEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHI 230
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
31-231 |
7.81e-31 |
|
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or DEAD Box Protein P82) has a wide variety of functions including regulating the alternative splicing of exons exhibiting specific features such as the inclusion of AC-rich alternative exons in CD44 transcripts, playing a role in innate immunity, and promoting mRNA degradation mediated by the antiviral zinc-finger protein ZC3HAV1 in an ATPase-dependent manner. DDX17 synergizes with DDX5 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. DDX17 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350808 [Multi-domain] Cd Length: 271 Bit Score: 118.96 E-value: 7.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 31 NFDDMNLREELLRGIYGYGFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTATFSIAILQQI---------DTSIrecqA 101
Cdd:cd18050 63 AFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHInhqpylergDGPI----C 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 102 LILAPTRELATQIQRVVMALGEYMKVHSHACIGGTNVREDARILESGCHVVVGTPGRVYDMINRKVLRTQYIKLFVLDEA 181
Cdd:cd18050 139 LVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEA 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 442626267 182 DEMLSRGFKDQIQDVFKMLPPDVQVILLSATMPPDVLEVSRCFMRDPVSI 231
Cdd:cd18050 219 DRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQI 268
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
56-226 |
2.40e-29 |
|
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and nucleolar RNA helicase 2) is an RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II. It promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) and binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs. DDX50 (also called Gu-Beta, Nucleolar Protein Gu2, and malignant cell derived RNA helicase). DDX21 and DDX50 have similar genomic structures and are in tandem orientation on chromosome 10, suggesting that the two genes arose by gene duplication in evolution. Diseases associated with DDX21 include stomach disease and cerebral creatine deficiency syndrome 3. Diseases associated with DDX50 include rectal disease. Both are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. Their name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.
Pssm-ID: 350702 [Multi-domain] Cd Length: 202 Bit Score: 113.02 E-value: 2.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 56 IQQRAIIPCVRGRDVIAQAQSGTGKTATFSIAILQQIDTSI------RECQALILAPTRELATQIQRVVMALGEYMKVhs 129
Cdd:cd17944 16 IQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQqprkrgRAPKVLVLAPTRELANQVTKDFKDITRKLSV-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 130 hACI-GGTNVREDARILESGCHVVVGTPGRVYDMINRKVLRTQYIKLFVLDEADEMLSRGFKDQIQDV----FKMLPPD- 203
Cdd:cd17944 94 -ACFyGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEIlsvsYKKDSEDn 172
|
170 180
....*....|....*....|...
gi 442626267 204 VQVILLSATMPPDVLEVSRCFMR 226
Cdd:cd17944 173 PQTLLFSATCPDWVYNVAKKYMK 195
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
255-358 |
1.35e-27 |
|
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: 105.37 E-value: 1.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 255 WKLGTLCDLYDTLSITQSVIFCNTRRKVDqLTQEMSIHNFTVSAMHGDMEQRDREVIMKQFRSGSSRVLITTDLLARGID 334
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100
....*....|....*....|....
gi 442626267 335 VQQVSLVINYDLPSNRENYIHRIG 358
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIG 103
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
41-220 |
5.83e-26 |
|
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: 104.76 E-value: 5.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 41 LLRGIYGYGFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTATFSIAILQQI-------DTSIRECQALILAPTRELATQ 113
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLlrykllaEGPFNAPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 114 IQRVVMALGEYMKVHSHACIGGTNVREDARILESGCHVVVGTPGRVYDMINRKVLRTQYIKLFVLDEADEMLSRGFKDQI 193
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 442626267 194 QDVFKMLP-------------PDVQVILLSATMPPDVLEV 220
Cdd:cd17948 161 SHFLRRFPlasrrsentdgldPGTQLVLVSATMPSGVGEV 200
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
67-212 |
3.12e-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: 100.17 E-value: 3.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 67 GRDVIAQAQSGTGKTATFSIAILQQIDTsiRECQALILAPTRELATQIQRVVMALGEyMKVHSHACIGGTNVREDARILE 146
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLK--KGKKVLVLVPTKALALQTAERLRELFG-PGIRVAVLVGGSSAEEREKNKL 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442626267 147 SGCHVVVGTPGRVYDMINRKVLRTQY-IKLFVLDEADEMLSRGFKDQI--QDVFKMLPPDVQVILLSAT 212
Cdd:cd00046 78 GDADIIIATPDMLLNLLLREDRLFLKdLKLIIVDEAHALLIDSRGALIldLAVRKAGLKNAQVILLSAT 146
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
283-357 |
4.14e-22 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 89.58 E-value: 4.14e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626267 283 DQLTQEMSIHNFTVSAMHGDMEQRDREVIMKQFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPSNRENYIHRI 357
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRI 75
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
53-217 |
2.19e-19 |
|
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: 86.15 E-value: 2.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 53 PSAIQQRAIIPCVRGRDVIAQAQSGTGKTATFSIAILQQI-DTSIRECQALILAPTRELATQIQRVVMALGEYMKVHSHA 131
Cdd:cd17956 22 PWLLPSSKSTPPYRPGDLCVSAPTGSGKTLAYVLPIVQALsKRVVPRLRALIVVPTKELVQQVYKVFESLCKGTGLKVVS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 132 CIGGTNVREDARILESGCH--------VVVGTPGRVYDMINRKVLRT-QYIKLFVLDEADEMLSRGFKD----------- 191
Cdd:cd17956 102 LSGQKSFKKEQKLLLVDTSgrylsrvdILVATPGRLVDHLNSTPGFTlKHLRFLVIDEADRLLNQSFQDwletvmkalgr 181
|
170 180 190
....*....|....*....|....*....|....*
gi 442626267 192 -QIQDVFKM--------LPPDVQVILLSATMPPDV 217
Cdd:cd17956 182 pTAPDLGSFgdanllerSVRPLQKLLFSATLTRDP 216
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
57-342 |
1.20e-15 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 78.53 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 57 QQRAI-----IPCVRGRDVIAQAQSGTGKTaTFSIAILQQIDTSIRecqALILAPTRELATQIQRvvmalgEYMKVHSHA 131
Cdd:COG1061 85 QQEALeallaALERGGGRGLVVAPTGTGKT-VLALALAAELLRGKR---VLVLVPRRELLEQWAE------ELRRFLGDP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 132 CIGGTNVredarilESGCHVVVGTPGRVYDMINRKVLRtQYIKLFVLDEADEMLSRGFkdqiQDVFKMLPPDVqVILLSA 211
Cdd:COG1061 155 LAGGGKK-------DSDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHHAGAPSY----RRILEAFPAAY-RLGLTA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 212 T--------------------------------MPPDVLEVsrcfmRDPVSILVKKEELTLEGIKQFYVNVKQENWKLgt 259
Cdd:COG1061 222 TpfrsdgreillflfdgivyeyslkeaiedgylAPPEYYGI-----RVDLTDERAEYDALSERLREALAADAERKDKI-- 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 260 LCDLYDTL-SITQSVIFCNTRRKVDQLTQEMSIHNFTVSAMHGDMEQRDREVIMKQFRSGSSRVLITTDLLARGIDVQQV 338
Cdd:COG1061 295 LRELLREHpDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRL 374
|
....
gi 442626267 339 SLVI 342
Cdd:COG1061 375 DVAI 378
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
28-350 |
6.66e-14 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 73.33 E-value: 6.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 28 VYDNFDDmNLREELLRGIYGYGFEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTATFSIAILQQIDTSiRECQALILAPT 107
Cdd:COG1205 33 RYAPWPD-WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLED-PGATALYLYPT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 108 RELAT-QIQRvVMALGEYM--KVHSHACIGGTNVREDARILESGcHVVVGTPgrvyDMINRKVLR--TQYIKLF------ 176
Cdd:COG1205 111 KALARdQLRR-LRELAEALglGVRVATYDGDTPPEERRWIREHP-DIVLTNP----DMLHYGLLPhhTRWARFFrnlryv 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 177 VLDEADE-----------MLSRgfkdqIQDVFKMLPPDVQVILLSATM--PP---------DVLEVSRC----------F 224
Cdd:COG1205 185 VIDEAHTyrgvfgshvanVLRR-----LRRICRHYGSDPQFILASATIgnPAehaerltgrPVTVVDEDgsprgertfvL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 225 MRDPVSILVKKEELTLEGIKQFYVNVKQEnwklgtlcdlydtlsiTQSVIFCNTRRKVDQLTQ------EMSIHNFTVSA 298
Cdd:COG1205 260 WNPPLVDDGIRRSALAEAARLLADLVREG----------------LRTLVFTRSRRGAELLARyarralREPDLADRVAA 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 442626267 299 MHGDMEQRDREVIMKQFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPSNR 350
Cdd:COG1205 324 YRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTR 375
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
32-214 |
1.71e-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: 69.71 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 32 FDDMNL----REELLRGI-YGYGFE----KPSAIQqRAIIPCVRGRDVIAQ-----------------AQSGTGKTATFS 85
Cdd:cd17965 1 FDQLKLlpsvREAIIKEIlKGSNKTdeeiKPSPIQ-TLAIKKLLKTLMRKVtkqtsneepklevfllaAETGSGKTLAYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 86 IAIL-----QQIDTSIRECQ------------ALILAPTRELATQIQRVVMALGEYMK--VHSHACIGGTNVREDARILE 146
Cdd:cd17965 80 APLLdylkrQEQEPFEEAEEeyesakdtgrprSVILVPTHELVEQVYSVLKKLSHTVKlgIKTFSSGFGPSYQRLQLAFK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442626267 147 SGCHVVVGTPGRVYDM--INRKVL-RTQYIklfVLDEADEMLSRGFKDQIQDVFKMLPPDVQVILLSATMP 214
Cdd:cd17965 160 GRIDILVTTPGKLASLakSRPKILsRVTHL---VVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIP 227
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
57-333 |
4.38e-12 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 67.61 E-value: 4.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 57 QQRAIIPCVR-GRDVIAQAQSGTGKTATFSIAILQQIDTSIRecqALILAPTRELATQI------------QRVVMALGE 123
Cdd:COG1204 27 QAEALEAGLLeGKNLVVSAPTASGKTLIAELAILKALLNGGK---ALYIVPLRALASEKyrefkrdfeelgIKVGVSTGD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 124 YmkvhshaciggtnvREDARILESgCHVVVGTPGRV-------YDMINRkvlrtqyIKLFVLDEA----DEmlSRGFkdQ 192
Cdd:COG1204 104 Y--------------DSDDEWLGR-YDILVATPEKLdsllrngPSWLRD-------VDLVVVDEAhlidDE--SRGP--T 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 193 IQDV---FKMLPPDVQVILLSATMP-PDvlEVSRCFMRDPVSIL---VKKEELTLEGIKQFYVNVKQENwkLGTLCDL-Y 264
Cdd:COG1204 158 LEVLlarLRRLNPEAQIVALSATIGnAE--EIAEWLDAELVKSDwrpVPLNEGVLYDGVLRFDDGSRRS--KDPTLALaL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 265 DTLSI-TQSVIFCNTRRKV----DQLTQEMSIH-------------------------NFTVSAM--------HGDMEQR 306
Cdd:COG1204 234 DLLEEgGQVLVFVSSRRDAeslaKKLADELKRRltpeereeleelaeellevseethtNEKLADClekgvafhHAGLPSE 313
|
330 340
....*....|....*....|....*..
gi 442626267 307 DREVIMKQFRSGSSRVLITTDLLARGI 333
Cdd:COG1204 314 LRRLVEDAFREGLIKVLVATPTLAAGV 340
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
259-354 |
5.02e-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: 62.99 E-value: 5.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 259 TLCDLYDTLSITQSVIFCNTRRKVDQLTQEMSIH-----NFTVSAMHG----------DMEQRDREVIMKQFRSGSSRVL 323
Cdd:cd18802 15 ILREYFPKTPDFRGIIFVERRATAVVLSRLLKEHpstlaFIRCGFLIGrgnssqrkrsLMTQRKQKETLDKFRDGELNLL 94
|
90 100 110
....*....|....*....|....*....|.
gi 442626267 324 ITTDLLARGIDVQQVSLVINYDLPSNRENYI 354
Cdd:cd18802 95 IATSVLEEGIDVPACNLVIRFDLPKTLRSYI 125
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
165-353 |
1.30e-11 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 65.93 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 165 RKVLRTQYIKLFVLDEA--------D---EMLsrgfkdQIQDVFKMLPpDVQVILLSATMPPDVLE--VSRCFMRDPVSI 231
Cdd:COG0514 124 LELLRRLKISLFAIDEAhcisqwghDfrpDYR------RLGELRERLP-NVPVLALTATATPRVRAdiAEQLGLEDPRVF 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 232 L--VKKEELTLEgikqfyVNVKQENWKLGTLCDLYDTLSITQSVIFCNTRRKVDQLTQEMSIHNFTVSAMHGDMEQRDRE 309
Cdd:COG0514 197 VgsFDRPNLRLE------VVPKPPDDKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEERE 270
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 442626267 310 VIMKQFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPSNRENY 353
Cdd:COG0514 271 ANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAY 314
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
273-353 |
3.62e-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: 54.52 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 273 VIFCNTRRKVDQLTQEMSIHNFTVSAMHGDMEQRDREVIMKQFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPSNREN 352
Cdd:cd18794 34 IIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMES 113
|
.
gi 442626267 353 Y 353
Cdd:cd18794 114 Y 114
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
272-349 |
4.68e-09 |
|
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: 54.40 E-value: 4.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 272 SVIFCNTRRKVDQLTQEMSIHNFTVSAMHGDMEQRDREVIMKQFRSGSS--RVLITTDLLARGIDVQQVSLVINYDLPSN 349
Cdd:cd18793 30 VLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDirVFLLSTKAGGVGLNLTAANRVILYDPWWN 109
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
66-213 |
1.51e-08 |
|
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: 54.13 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 66 RGRDVIAQAQSGTGKTATFSIAILQQI--DTSIRecqALILAPTRELATQIQRVVMALGEYM--KVHSHACIGGTNVRED 141
Cdd:cd17923 14 AGRSVVVTTGTASGKSLCYQLPILEALlrDPGSR---ALYLYPTKALAQDQLRSLRELLEQLglGIRVATYDGDTPREER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 142 ARILESGCHVVVGTPgrvyDMINRKVLRTQYI--------KLFVLDEAD----------EMLSRgfkdQIQDVFKMLPPD 203
Cdd:cd17923 91 RAIIRNPPRILLTNP----DMLHYALLPHHDRwarflrnlRYVVLDEAHtyrgvfgshvALLLR----RLRRLCRRYGAD 162
|
170
....*....|
gi 442626267 204 VQVILLSATM 213
Cdd:cd17923 163 PQFILTSATI 172
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
58-214 |
4.35e-08 |
|
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: 52.65 E-value: 4.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 58 QRAIIPCV--RGRDVIAQAQSGTGKTATFSIAILQQIDTSirECQALILAPTRELATQI-QRVVMALGEYMKVhshaCIG 134
Cdd:cd17921 6 QREALRALylSGDSVLVSAPTSSGKTLIAELAILRALATS--GGKAVYIAPTRALVNQKeADLRERFGPLGKN----VGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 135 GTNVREDARILESGCHVVVGTPGRVYDMINR-KVLRTQYIKLFVLDEA----DEmlSRGfkDQIQDVFKMLP---PDVQV 206
Cdd:cd17921 80 LTGDPSVNKLLLAEADILVATPEKLDLLLRNgGERLIQDVRLVVVDEAhligDG--ERG--VVLELLLSRLLrinKNARF 155
|
....*...
gi 442626267 207 ILLSATMP 214
Cdd:cd17921 156 VGLSATLP 163
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
273-352 |
7.85e-07 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 51.38 E-value: 7.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 273 VIFCNTRRKVDQLTQEMSIHNFTVSAMHGDMEQRDREVIMKQFRSGSS--RVLITTDLLARGIDVQQVSLVINYDLPSN- 349
Cdd:COG0553 553 LVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEapVFLISLKAGGEGLNLTAADHVIHYDLWWNp 632
|
....
gi 442626267 350 -REN 352
Cdd:COG0553 633 aVEE 636
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
35-353 |
1.69e-06 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 50.10 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 35 MNLREELLRGIYGYGFEKPSaiQQRAIIPCVRGRDVIAQAQSGTGKTATFsiailqQIDTSIRECQALILAPTRELATQI 114
Cdd:PRK11057 10 ESLAKQVLQETFGYQQFRPG--QQEIIDAVLSGRDCLVVMPTGGGKSLCY------QIPALVLDGLTLVVSPLISLMKDQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 115 QRVVMALGEymkvhSHACIGGTNVREDARILESGCH-----VVVGTPGRVY--DMINRkvLRTQYIKLFVLDEAD----- 182
Cdd:PRK11057 82 VDQLLANGV-----AAACLNSTQTREQQLEVMAGCRtgqikLLYIAPERLMmdNFLEH--LAHWNPALLAVDEAHcisqw 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 183 ------EMLSRGfkdQIQDVFkmlpPDVQVILLSATMPP----DVleVSRCFMRDPVS------------ILVKKeeltL 240
Cdd:PRK11057 155 ghdfrpEYAALG---QLRQRF----PTLPFMALTATADDttrqDI--VRLLGLNDPLIqissfdrpniryTLVEK----F 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 241 EGIKQFYVNVKQENWKLGtlcdlydtlsitqsVIFCNTRRKVDQLTQEMSIHNFTVSAMHGDMEQRDREVIMKQFRSGSS 320
Cdd:PRK11057 222 KPLDQLMRYVQEQRGKSG--------------IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDL 287
|
330 340 350
....*....|....*....|....*....|...
gi 442626267 321 RVLITTDLLARGIDVQQVSLVINYDLPSNRENY 353
Cdd:PRK11057 288 QIVVATVAFGMGINKPNVRFVVHFDIPRNIESY 320
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
271-333 |
4.77e-06 |
|
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: 46.01 E-value: 4.77e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442626267 271 QSVIFCNTRRKVDQLTQEMS---IHnftvsamHGDMEQRDREVIMKQFRSGSSRVLITTDLLARGI 333
Cdd:cd18795 45 PVLVFCSSRKECEKTAKDLAgiaFH-------HAGLTREDRELVEELFREGLIKVLVATSTLAAGV 103
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
77-326 |
8.83e-06 |
|
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: 47.77 E-value: 8.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 77 GTGKT-ATFSIAiLQQIDtsIRECQALILA-PTRELATQIQRVVMALGEY--MKVHSHAcigGTNVREDARILESGCH-- 150
Cdd:COG1203 157 GGGKTeAALLFA-LRLAA--KHGGRRIIYAlPFTSIINQTYDRLRDLFGEdvLLHHSLA---DLDLLEEEEEYESEARwl 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 151 ----------VVVGTP--------GRVYDMInRKVLRTQYiKLFVLDEAD----EMLsRGFKDQIQDVFKMlppDVQVIL 208
Cdd:COG1203 231 kllkelwdapVVVTTIdqlfeslfSNRKGQE-RRLHNLAN-SVIILDEVQayppYML-ALLLRLLEWLKNL---GGSVIL 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 209 LSATMPPDVLEvsrcFMRDPVSILVKKEELTLEGIKQFY---VNVKQENWKLGTLCD-LYDTLSITQSVIF-CNTRRKVD 283
Cdd:COG1203 305 MTATLPPLLRE----ELLEAYELIPDEPEELPEYFRAFVrkrVELKEGPLSDEELAElILEALHKGKSVLViVNTVKDAQ 380
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 442626267 284 QLTQEMSIHNFTVSAM--HGDMEQRDREVIMKQ----FRSGSSRVLITT 326
Cdd:COG1203 381 ELYEALKEKLPDEEVYllHSRFCPADRSEIEKEikerLERGKPCILVST 429
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
67-216 |
9.78e-06 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 45.65 E-value: 9.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 67 GRDVIAQAQSGTGKTATFSIAILQQI-DTSIRECQALILAPTRELATQIQRVVMALGEYMKV-----HSHaciGGTNVRE 140
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLaDEPEKGVQVLYISPLKALINDQERRLEEPLDEIDLeipvaVRH---GDTSQSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 141 DARILESGCHVVVGTPGRVYDMINRKVLR-----TQYIklfVLDEADEMLS--RGfkDQIQDVF----KMLPPDVQVILL 209
Cdd:cd17922 78 KAKQLKNPPGILITTPESLELLLVNKKLRelfagLRYV---VVDEIHALLGskRG--VQLELLLerlrKLTGRPLRRIGL 152
|
....*...
gi 442626267 210 SATM-PPD 216
Cdd:cd17922 153 SATLgNLE 160
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
273-348 |
1.10e-05 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 47.42 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 273 VIFCNTRRKVDQLTQEMSIHNFTV------SAMHGD--MEQRDREVIMKQFRSGSSRVLITTDLLARGIDVQQVSLVINY 344
Cdd:COG1111 357 IVFTQYRDTAEMIVEFLSEPGIKAgrfvgqASKEGDkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFY 436
|
....*
gi 442626267 345 DL-PS 348
Cdd:COG1111 437 EPvPS 441
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
39-229 |
2.20e-05 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 44.83 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 39 EELLRGIYGYgfEKPSAIQQRAIIPCVRGRDVIAQAQSGTGKTATFsiailqQIDTSIRECQALILAPTRELatqIQRVV 118
Cdd:cd17920 1 EQILKEVFGY--DEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCY------QLPALLLDGVTLVVSPLISL---MQDQV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 119 MALGEyMKVHShACIGGTNVREDAR-----ILESGCHVVVGTPGRVYDMINRKVLRTQY----IKLFVLDEA-------- 181
Cdd:cd17920 70 DRLQQ-LGIRA-AALNSTLSPEEKRevllrIKNGQYKLLYVTPERLLSPDFLELLQRLPerkrLALIVVDEAhcvsqwgh 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 442626267 182 ---DEMLsrgfkdQIQDVFKMLpPDVQVILLSATMPPDVLE--VSRCFMRDPV 229
Cdd:cd17920 148 dfrPDYL------RLGRLRRAL-PGVPILALTATATPEVREdiLKRLGLRNPV 193
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
69-335 |
8.22e-05 |
|
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
Pssm-ID: 187770 [Multi-domain] Cd Length: 353 Bit Score: 44.34 E-value: 8.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 69 DVIAQAQSGTGKT-ATFSIAiLQQIDTSIREcqALILA-PTRELATQI-QRVVMALGEYMKVHSHACIGGTNVREDARIL 145
Cdd:cd09639 1 LLVIEAPTGYGKTeAALLWA-LHSLKSQKAD--RVIIAlPTRATINAMyRRAKEAFGETGLYHSSILSSRIKEMGDSEEF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 146 ESGCHVVVGTPGRVY---------DMINRKVLRT---QYIKLF-------VLDEADEMLS--RGFkdqIQDVFKMLPP-D 203
Cdd:cd09639 78 EHLFPLYIHSNDTLFldpitvctiDQVLKSVFGEfghYEFTLAsiansllIFDEVHFYDEytLAL---ILAVLEVLKDnD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 204 VQVILLSATMPpdvlEVSRCFMRDpVSILVKKEELTLEGIKQFYVNVKQENW--KLGTLCDLYDTLSITQSV-IFCNTRR 280
Cdd:cd09639 155 VPILLMSATLP----KFLKEYAEK-IGYVEENEPLDLKPNERAPFIKIESDKvgEISSLERLLEFIKKGGSVaIIVNTVD 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442626267 281 KVDQLTQEM--SIHNFTVSAMHGDMEQRDRE----VIMKQFRSGSSRVLITTDLLARGIDV 335
Cdd:cd09639 230 RAQEFYQQLkeKGPEEEIMLIHSRFTEKDRAkkeaELLLEFKKSEKFVIVATQVIEASLDI 290
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
256-345 |
9.46e-05 |
|
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: 42.34 E-value: 9.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 256 KLGTLCDL-------YDTLSITQSVIFCNTRRKVDQLTQEMSIHNFTVSAM----HGD------MEQRDREVIMKQFRSG 318
Cdd:cd18801 10 KLEKLEEIvkehfkkKQEGSDTRVIIFSEFRDSAEEIVNFLSKIRPGIRATrfigQASgksskgMSQKEQKEVIEQFRKG 89
|
90 100
....*....|....*....|....*..
gi 442626267 319 SSRVLITTDLLARGIDVQQVSLVINYD 345
Cdd:cd18801 90 GYNVLVATSIGEEGLDIGEVDLIICYD 116
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
274-342 |
1.73e-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: 40.62 E-value: 1.73e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626267 274 IFCNTRRKVDQLTQEMSIHNFTVSAMHGD--MEQRDREVIMKQF-RSGSSRVLITTDLLARGIDVQQVSLVI 342
Cdd:cd18799 11 IFCVSIEHAEFMAEAFNEAGIDAVALNSDysDRERGDEALILLFfGELKPPILVTVDLLTTGVDIPEVDNVV 82
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
293-345 |
2.13e-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: 2.13e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 442626267 293 NFTVSAMHGDMEQRDREVIMKQFRSGSSRVLITTDLLARGIDVQQVSLVINYD 345
Cdd:cd18811 61 ELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIED 113
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
272-349 |
3.66e-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: 40.71 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 272 SVIFCNTRRKVDQLTQ------EMSIHNFTVSAMHGDMEQRDREVIMKQFRSGSSRVLITTDLLARGIDVQQVSLVINYD 345
Cdd:cd18796 41 TLVFTNTRSQAERLAQrlrelcPDRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIG 120
|
....
gi 442626267 346 LPSN 349
Cdd:cd18796 121 SPKS 124
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
68-181 |
3.85e-04 |
|
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: 41.10 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 68 RDVIAQAQSGTGKTAtfsIAIL-------QQIDTSIRECQALILAPTRELATQiQrvVMALGEYMKVHSHACIGGTNV-- 138
Cdd:cd18034 17 RNTIVVLPTGSGKTL---IAVMlikemgeLNRKEKNPKKRAVFLVPTVPLVAQ-Q--AEAIRSHTDLKVGEYSGEMGVdk 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 442626267 139 --REDARILESGCHVVVGTPGRVYDMINRKVLRTQYIKLFVLDEA 181
Cdd:cd18034 91 wtKERWKEELEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
68-155 |
5.26e-04 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 40.48 E-value: 5.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 68 RDVIAQAQSGTGKTATFSIAILQQIDtsiRECQALILAPTRELATQIQRVVMALgeYMKVHSHACIGGTnvREDArilES 147
Cdd:cd17918 37 MDRLLSGDVGSGKTLVALGAALLAYK---NGKQVAILVPTEILAHQHYEEARKF--LPFINVELVTGGT--KAQI---LS 106
|
....*...
gi 442626267 148 GCHVVVGT 155
Cdd:cd17918 107 GISLLVGT 114
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
278-345 |
9.65e-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: 39.54 E-value: 9.65e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442626267 278 TRRKVDQLTQEMSIHNFTVSAMHGDMEQRDREVIMKQFRSGSSRVLITTDLLARGIDVQQVSLVINYD 345
Cdd:cd18790 36 TKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILD 103
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
269-358 |
1.33e-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: 37.30 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 269 ITQSVIFCNTRRKVDQLTQEMSIhnftvsamhgdmeqrdrevimkqfrsgssrvLITTDLLARGIDVQQVSLVINYDLPS 348
Cdd:cd18785 3 VVKIIVFTNSIEHAEEIASSLEI-------------------------------LVATNVLGEGIDVPSLDTVIFFDPPS 51
|
90
....*....|
gi 442626267 349 NRENYIHRIG 358
Cdd:cd18785 52 SAASYIQRVG 61
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
77-212 |
2.91e-03 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 38.06 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 77 GTGKTATfSIAILQQIdtsiRECQALILAPTRELATQIQRVVMALGEYMKVHshaciggtNVREDARILESGCHVVVGTp 156
Cdd:cd17926 28 GSGKTLT-ALALIAYL----KELRTLIVVPTDALLDQWKERFEDFLGDSSIG--------LIGGGKKKDFDDANVVVAT- 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626267 157 grvYDMINRKVLRTQYIK----LFVLDEADEMLSRGFKDQIQDVFKMLppdvqVILLSAT 212
Cdd:cd17926 94 ---YQSLSNLAEEEKDLFdqfgLLIVDEAHHLPAKTFSEILKELNAKY-----RLGLTAT 145
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
293-345 |
5.74e-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: 37.25 E-value: 5.74e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 442626267 293 NFTVSAMHGDMEQRDREVIMKQFRSGSSRVLITTDLLARGIDVQQVSLVINYD 345
Cdd:cd18792 60 EARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIED 112
|
|
| ComFA |
COG4098 |
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ... |
274-342 |
6.77e-03 |
|
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, recombination and repair];
Pssm-ID: 443274 [Multi-domain] Cd Length: 451 Bit Score: 38.32 E-value: 6.77e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442626267 274 IFCNTRRKVDQLTQEM--SIHNFTVSAMHGDMEQRDREVimKQFRSGSSRVLITTDLLARGIDVQQVSLVI 342
Cdd:COG4098 324 IFVPTIELLEQLVALLqkLFPEERIAGVHAEDPERKEKV--QAFRDGEIPILVTTTILERGVTFPNVDVAV 392
|
|
| |
