|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
157-582 |
1.84e-166 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 481.18 E-value: 1.84e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 157 TFAEIDLGEALNQNIQRCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIISGIMREQyAQRPRvartaypl 236
Cdd:COG0513 3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSR-PRAPQ-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 237 ALILSPTRELSCQIHDEAKKFSYQTGVKVVVAYGGAPINQQLRELERGVDILVATPGRLVDLLERARVSLQMIRYLALDE 316
Cdd:COG0513 74 ALILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 317 ADRMLDMGFEPQIRKIVEQMdmppPGMRQTLLFSATFPKEIQALASDFLSNYVFLAVGRVGSSTDLIAQRVEYVLESDKR 396
Cdd:COG0513 154 ADRMLDMGFIEDIERILKLL----PKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 397 SHLMDLLHAQREtgvngkqGLTLVFVETKKGADALEHCLCVNGFPAASIHGDRTQQERELALRSFKTGNTPILVATDVAA 476
Cdd:COG0513 230 ELLRRLLRDEDP-------ERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 477 RGLDIPRVAHVVNFDLPNDIDDYVHRIGRTGRAGKMGLATAFFNEGNLNLAKSLADLMQE--ANQEVPAWLSRYAARAIY 554
Cdd:COG0513 303 RGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQkiEEEELPGFEPVEEKRLER 382
|
410 420
....*....|....*....|....*...
gi 356530675 555 SGGNRNRKSGGSRFGGRDFRKEGSFNKA 582
Cdd:COG0513 383 LKPKIKEKLKGKKAGRGGRPGPKGERKA 410
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
157-377 |
1.42e-161 |
|
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: 460.80 E-value: 1.42e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 157 TFAEIDLGEALNQNIQRCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIISGIMREQYAQRPRVARTAYPL 236
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGRRKAYPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 237 ALILSPTRELSCQIHDEAKKFSYQTGVKVVVAYGGAPINQQLRELERGVDILVATPGRLVDLLERARVSLQMIRYLALDE 316
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 356530675 317 ADRMLDMGFEPQIRKIVEQMDMPPPGMRQTLLFSATFPKEIQALASDFLSNYVFLAVGRVG 377
Cdd:cd17967 161 ADRMLDMGFEPQIRKIVEHPDMPPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVGRVG 221
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
136-378 |
8.34e-146 |
|
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: 421.76 E-value: 8.34e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 136 FDAYDDIPVETSGENVPPPVNTFAEIDLGEALNQNIQRCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPII 215
Cdd:cd18051 1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 216 SGIMRE------QYAQRPRVARTAYPLALILSPTRELSCQIHDEAKKFSYQTGVKVVVAYGGAPINQQLRELERGVDILV 289
Cdd:cd18051 81 SQIYEQgpgeslPSESGYYGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 290 ATPGRLVDLLERARVSLQMIRYLALDEADRMLDMGFEPQIRKIVEQMDMPPPGMRQTLLFSATFPKEIQALASDFLSNYV 369
Cdd:cd18051 161 ATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFLDNYI 240
|
....*....
gi 356530675 370 FLAVGRVGS 378
Cdd:cd18051 241 FLAVGRVGS 249
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
120-377 |
5.22e-141 |
|
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: 410.13 E-value: 5.22e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 120 EAEDQSFSELEnTGINFDAYDDIPVETSGENVPPPVNTFAEIDLGEALNQNIQRCKYVKPTPVQRYAIPISLAGRDLMAC 199
Cdd:cd18052 8 EDEDEIFATIQ-TGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMAC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 200 AQTGSGKTAAFCFPIISGIMREQYAQrPRVARTAYPLALILSPTRELSCQIHDEAKKFSYQTGVKVVVAYGGAPINQQLR 279
Cdd:cd18052 87 AQTGSGKTAAFLLPVLTGMMKEGLTA-SSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 280 ELERGVDILVATPGRLVDLLERARVSLQMIRYLALDEADRMLDMGFEPQIRKIVEQMDMPPPGMRQTLLFSATFPKEIQA 359
Cdd:cd18052 166 QIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQTLMFSATFPEEIQR 245
|
250
....*....|....*....
gi 356530675 360 LASDFL-SNYVFLAVGRVG 377
Cdd:cd18052 246 LAAEFLkEDYLFLTVGRVG 264
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
148-570 |
1.90e-137 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 411.47 E-value: 1.90e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 148 GENVPPPVNTFAEIDLGEALNQNIQRCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIISGIMreqyAQrP 227
Cdd:PTZ00110 122 GENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHIN----AQ-P 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 228 RVARTAYPLALILSPTRELSCQIHDEAKKFSYQTGVKVVVAYGGAPINQQLRELERGVDILVATPGRLVDLLERARVSLQ 307
Cdd:PTZ00110 197 LLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLR 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 308 MIRYLALDEADRMLDMGFEPQIRKIVEQMdMPPpgmRQTLLFSATFPKEIQALASDFLSNY-VFLAVGrvgsSTDL---- 382
Cdd:PTZ00110 277 RVTYLVLDEADRMLDMGFEPQIRKIVSQI-RPD---RQTLMWSATWPKEVQSLARDLCKEEpVHVNVG----SLDLtach 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 383 -IAQRVEYVLESDKRSHLMDLLhaQRETGVNGKqglTLVFVETKKGADALEHCLCVNGFPAASIHGDRTQQERELALRSF 461
Cdd:PTZ00110 349 nIKQEVFVVEEHEKRGKLKMLL--QRIMRDGDK---ILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEF 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 462 KTGNTPILVATDVAARGLDIPRVAHVVNFDLPNDIDDYVHRIGRTGRAGKMGLATAFFNEGNLNLAKSLADLMQEANQEV 541
Cdd:PTZ00110 424 KTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQPV 503
|
410 420
....*....|....*....|....*....
gi 356530675 542 PAWLSRYAARAiySGGNRNRKSGGSRFGG 570
Cdd:PTZ00110 504 PPELEKLSNER--SNGTERRRWGGYGRFS 530
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
156-535 |
3.91e-103 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 320.21 E-value: 3.91e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 156 NTFAEIDLGEALNQNIQRCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIISGIMreqyAQRPRVArtayp 235
Cdd:PRK11776 4 TAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLD----VKRFRVQ----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 236 lALILSPTRELSCQIHDEAKKFSYQT-GVKVVVAYGGAPINQQLRELERGVDILVATPGRLVDLLERARVSLQMIRYLAL 314
Cdd:PRK11776 75 -ALVLCPTRELADQVAKEIRRLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 315 DEADRMLDMGFEPQIRKIVEQMdmppPGMRQTLLFSATFPKEIQALASDFLSNYVFLAVGRVGSSTDlIAQRVeYVLESD 394
Cdd:PRK11776 154 DEADRMLDMGFQDAIDAIIRQA----PARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPA-IEQRF-YEVSPD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 395 KRSHLMD--LLHAQRETgvngkqglTLVFVETKKGADALEHCLCVNGFPAASIHGDRTQQERELALRSFKTGNTPILVAT 472
Cdd:PRK11776 228 ERLPALQrlLLHHQPES--------CVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVAT 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 356530675 473 DVAARGLDIPRVAHVVNFDLPNDIDDYVHRIGRTGRAGKMGLATAFFNEGNLNLAKSLADLMQ 535
Cdd:PRK11776 300 DVAARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLG 362
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
176-571 |
2.69e-100 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 312.90 E-value: 2.69e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 176 YVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIISG-IMREQYAQRPRVARtayplALILSPTRELSCQIHDEA 254
Cdd:PRK10590 21 YREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHlITRQPHAKGRRPVR-----ALILTPTRELAAQIGENV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 255 KKFSYQTGVKVVVAYGGAPINQQLRELERGVDILVATPGRLVDLLERARVSLQMIRYLALDEADRMLDMGFEPQIRKIVE 334
Cdd:PRK10590 96 RDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFIHDIRRVLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 335 QMdmppPGMRQTLLFSATFPKEIQALASDFLSNYVFLAVGRVGSSTDLIAQRVEYVLESDKRSHLMDLLHAQretgvNGK 414
Cdd:PRK10590 176 KL----PAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQMIGKG-----NWQ 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 415 QglTLVFVETKKGADALEHCLCVNGFPAASIHGDRTQQERELALRSFKTGNTPILVATDVAARGLDIPRVAHVVNFDLPN 494
Cdd:PRK10590 247 Q--VLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPN 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 495 DIDDYVHRIGRTGRAGKMGLATAFFNEGNLNLAKSLADLMQeanQEVPawlsRYA-----------ARAIYSGGNRNRKS 563
Cdd:PRK10590 325 VPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLK---KEIP----RIAipgyepdpsikAEPIQNGRQQRGGG 397
|
....*...
gi 356530675 564 GGSRFGGR 571
Cdd:PRK10590 398 GRGQGGGR 405
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
142-563 |
2.26e-98 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 309.80 E-value: 2.26e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 142 IPVETSGENVPPPVNTFAEIDLGEALNQNIQRCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIIS--GIM 219
Cdd:PLN00206 107 LEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISrcCTI 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 220 REQYAQRPRvartaYPLALILSPTRELSCQIHDEAKKFSYQTGVKVVVAYGGAPINQQLRELERGVDILVATPGRLVDLL 299
Cdd:PLN00206 187 RSGHPSEQR-----NPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLL 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 300 ERARVSLQMIRYLALDEADRMLDMGFEPQIRKIVEQMDMPppgmrQTLLFSATFPKEIQALASDFLSNYVFLAVGRVGSS 379
Cdd:PLN00206 262 SKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQALSQP-----QVLLFSATVSPEVEKFASSLAKDIILISIGNPNRP 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 380 TDLIAQRVEYVLESDKRSHLMDLLHAQRETgvngkQGLTLVFVETKKGADALEHCLCV-NGFPAASIHGDRTQQERELAL 458
Cdd:PLN00206 337 NKAVKQLAIWVETKQKKQKLFDILKSKQHF-----KPPAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERREVM 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 459 RSFKTGNTPILVATDVAARGLDIPRVAHVVNFDLPNDIDDYVHRIGRTGRAGKMGLATAFFNEGNLNLAKSLADLMQEAN 538
Cdd:PLN00206 412 KSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKSSG 491
|
410 420
....*....|....*....|....*
gi 356530675 539 QEVPAWLSRyaARAIYSGGNRNRKS 563
Cdd:PLN00206 492 AAIPRELAN--SRYLGSGRKRKKKR 514
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
167-371 |
3.10e-96 |
|
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: 292.81 E-value: 3.10e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 167 LNQNIQRCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIISGIMREQYAQRPRvartayPLALILSPTREL 246
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRG------PQALVLAPTREL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 247 SCQIHDEAKKFSYQTGVKVVVAYGGAPINQQLRELERGVDILVATPGRLVDLLERARVSLQMIRYLALDEADRMLDMGFE 326
Cdd:cd00268 75 AMQIAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 356530675 327 PQIRKIVEQMdmppPGMRQTLLFSATFPKEIQALASDFLSNYVFL 371
Cdd:cd00268 155 EDVEKILSAL----PKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
158-521 |
2.11e-90 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 287.58 E-value: 2.11e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 158 FAEIDLGEALNQNIQRCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIISGIM-----REQYAQRPRvart 232
Cdd:PRK01297 89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLqtpppKERYMGEPR---- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 233 ayplALILSPTRELSCQIHDEAKKFSYQTGVKVVVAYGGAPINQQLRELE-RGVDILVATPGRLVDLLERARVSLQMIRY 311
Cdd:PRK01297 165 ----ALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMVEV 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 312 LALDEADRMLDMGFEPQIRKIVEQMdmPPPGMRQTLLFSATFPKEIQALASDFLSNYVFLAVGRVGSSTDLIAQRVEYVL 391
Cdd:PRK01297 241 MVLDEADRMLDMGFIPQVRQIIRQT--PRKEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVA 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 392 ESDKRSHLMDLLHAQRETGVngkqgltLVFVETKKGADALEHCLCVNGFPAASIHGDRTQQERELALRSFKTGNTPILVA 471
Cdd:PRK01297 319 GSDKYKLLYNLVTQNPWERV-------MVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVA 391
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 356530675 472 TDVAARGLDIPRVAHVVNFDLPNDIDDYVHRIGRTGRAGKMGLATAFFNE 521
Cdd:PRK01297 392 TDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGE 441
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
157-518 |
6.49e-89 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 282.22 E-value: 6.49e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 157 TFAEIDLGEALNQNIQRCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIISGIM--REQYAQRPRVartay 234
Cdd:PRK11192 2 TFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLdfPRRKSGPPRI----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 235 plaLILSPTRELSCQIHDEAKKFSYQTGVKVVVAYGGAPINQQLRELERGVDILVATPGRLVDLLERARVSLQMIRYLAL 314
Cdd:PRK11192 77 ---LILTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 315 DEADRMLDMGFEPQIRKIVEQMDmpppGMRQTLLFSATFPKE-IQALASDFLSNYVFLAVGRVGSSTDLIAQrveYVLES 393
Cdd:PRK11192 154 DEADRMLDMGFAQDIETIAAETR----WRKQTLLFSATLEGDaVQDFAERLLNDPVEVEAEPSRRERKKIHQ---WYYRA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 394 DKRSHLMDLL-HAQRETGVngkqGLTLVFVETKKGADALEHCLCVNGFPAASIHGDRTQQERELALRSFKTGNTPILVAT 472
Cdd:PRK11192 227 DDLEHKTALLcHLLKQPEV----TRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVAT 302
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 356530675 473 DVAARGLDIPRVAHVVNFDLPNDIDDYVHRIGRTGRAGKMGLATAF 518
Cdd:PRK11192 303 DVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
165-575 |
1.84e-83 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 267.99 E-value: 1.84e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 165 EALN-QNIQRCkyvkpTPVQRYAIPISLAGRDLMACAQTGSGKTAAF---CF------PIISGIMREQyaqrPRvartay 234
Cdd:PRK04837 21 EALEkKGFHNC-----TPIQALALPLTLAGRDVAGQAQTGTGKTMAFltaTFhyllshPAPEDRKVNQ----PR------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 235 plALILSPTRELSCQIHDEAKKFSYQTGVKVVVAYGGAPINQQLRELERGVDILVATPGRLVDLLERARVSLQMIRYLAL 314
Cdd:PRK04837 86 --ALIMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 315 DEADRMLDMGFEPQIRKIVEQmdMPPPGMRQTLLFSATFPKEIQALASDFLSNYVFLAVGRVGSSTDLIAQRVEYVLESD 394
Cdd:PRK04837 164 DEADRMFDLGFIKDIRWLFRR--MPPANQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYPSNEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 395 KrshlMDLLhaqretgvngkqgLTL----------VFVETKKGadalehCLCVNGFPAASIH------GDRTQQERELAL 458
Cdd:PRK04837 242 K----MRLL-------------QTLieeewpdraiIFANTKHR------CEEIWGHLAADGHrvglltGDVAQKKRLRIL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 459 RSFKTGNTPILVATDVAARGLDIPRVAHVVNFDLPNDIDDYVHRIGRTGRAGKMGLATAFFNEgnlNLAKSLADLMQEAN 538
Cdd:PRK04837 299 EEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACE---EYALNLPAIETYIG 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 356530675 539 QEVPawLSRYAARAI------------YSGGNRNRKSGGSRFGGRDFRK 575
Cdd:PRK04837 376 HSIP--VSKYDSDALltdlpkplrltrPRTGNGPRRSGAPRNRRRRKRS 422
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
157-542 |
8.25e-83 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 270.67 E-value: 8.25e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 157 TFAEIDLGEALNQNIQRCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIISGIMreqyaQRPRVA--RTAY 234
Cdd:PRK04537 10 TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLL-----SRPALAdrKPED 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 235 PLALILSPTRELSCQIHDEAKKFSYQTGVKVVVAYGGAPINQQLRELERGVDILVATPGRLVDLLERARV-SLQMIRYLA 313
Cdd:PRK04537 85 PRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVvSLHACEICV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 314 LDEADRMLDMGFEPQIRKIVEQMdmPPPGMRQTLLFSATFPKEIQALASDFLSNYVFLAVGRVGSSTDLIAQRVEYVLES 393
Cdd:PRK04537 165 LDEADRMFDLGFIKDIRFLLRRM--PERGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 394 DKRSHLMDLLhaQRETGVNgkqglTLVFVETKKGADALEHCLCVNGFPAASIHGDRTQQERELALRSFKTGNTPILVATD 473
Cdd:PRK04537 243 EKQTLLLGLL--SRSEGAR-----TMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATD 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 356530675 474 VAARGLDIPRVAHVVNFDLPNDIDDYVHRIGRTGRAGKMGLATAFFNEgnlNLAKSLADLMQEANQEVP 542
Cdd:PRK04537 316 VAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACE---RYAMSLPDIEAYIEQKIP 381
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
171-371 |
1.29e-78 |
|
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: 247.28 E-value: 1.29e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 171 IQRCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIISGImreqyAQRPRVARTAYPLALILSPTRELSCQI 250
Cdd:cd17966 5 LKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHI-----NAQPPLERGDGPIVLVLAPTRELAQQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 251 HDEAKKFSYQTGVKVVVAYGGAPINQQLRELERGVDILVATPGRLVDLLERARVSLQMIRYLALDEADRMLDMGFEPQIR 330
Cdd:cd17966 80 QQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 356530675 331 KIVEQMDmppPGmRQTLLFSATFPKEIQALASDFLSNYVFL 371
Cdd:cd17966 160 KIVDQIR---PD-RQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
147-367 |
9.08e-77 |
|
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: 243.44 E-value: 9.08e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 147 SGENVPPPVNTFAEIDLGEALNQNIQRCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIISGIMreqyAQR 226
Cdd:cd17953 3 RGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIK----DQR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 227 PrVARTAYPLALILSPTRELSCQIHDEAKKFSYQTGVKVVVAYGGAPINQQLRELERGVDILVATPGRLVDLL--ERARV 304
Cdd:cd17953 79 P-VKPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtaNNGRV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 356530675 305 -SLQMIRYLALDEADRMLDMGFEPQIRKIVEQM--DmpppgmRQTLLFSATFPKEIQALASDFLSN 367
Cdd:cd17953 158 tNLRRVTYVVLDEADRMFDMGFEPQIMKIVNNIrpD------RQTVLFSATFPRKVEALARKVLHK 217
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
157-518 |
6.73e-75 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 251.31 E-value: 6.73e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 157 TFAEIDLGEALNQNIQRCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIISGIMREQYAqrprvartayPL 236
Cdd:PRK11634 7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKA----------PQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 237 ALILSPTRELSCQIHDEAKKFS-YQTGVKVVVAYGGAPINQQLRELERGVDILVATPGRLVDLLERARVSLQMIRYLALD 315
Cdd:PRK11634 77 ILVLAPTRELAVQVAEAMTDFSkHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 316 EADRMLDMGFEPQIRKIVEQMdmppPGMRQTLLFSATFPKEIQALASDFLSNYVFLavgRVGSSTDL---IAQRVEYVLE 392
Cdd:PRK11634 157 EADEMLRMGFIEDVETIMAQI----PEGHQTALFSATMPEAIRRITRRFMKEPQEV---RIQSSVTTrpdISQSYWTVWG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 393 SDKRSHLMDLLHAQRETGvngkqglTLVFVETKKG----ADALEHclcvNGFPAASIHGDRTQQERELALRSFKTGNTPI 468
Cdd:PRK11634 230 MRKNEALVRFLEAEDFDA-------AIIFVRTKNAtlevAEALER----NGYNSAALNGDMNQALREQTLERLKDGRLDI 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 356530675 469 LVATDVAARGLDIPRVAHVVNFDLPNDIDDYVHRIGRTGRAGKMGLATAF 518
Cdd:PRK11634 299 LIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLF 348
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
167-367 |
2.47e-69 |
|
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: 223.06 E-value: 2.47e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 167 LNQNIQRCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIISGIMreqyaQRPRVARTAYPLALILSPTREL 246
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIM-----DQRELEKGEGPIAVIVAPTREL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 247 SCQIHDEAKKFSYQTGVKVVVAYGGAPINQQLRELERGVDILVATPGRLVDLLERARVSLQMIRYLALDEADRMLDMGFE 326
Cdd:cd17952 76 AQQIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 356530675 327 PQIRKIVEQMdMPPpgmRQTLLFSATFPKEIQALASDFLSN 367
Cdd:cd17952 156 YQVRSIVGHV-RPD---RQTLLFSATFKKKIEQLARDILSD 192
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
171-371 |
1.09e-68 |
|
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: 222.20 E-value: 1.09e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 171 IQRCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIISGIMReqYAQRPRVARTAYPLALILSPTRELSCQI 250
Cdd:cd17945 5 IRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISR--LPPLDEETKDDGPYALILAPTRELAQQI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 251 HDEAKKFSYQTGVKVVVAYGGAPINQQLRELERGVDILVATPGRLVDLLERARVSLQMIRYLALDEADRMLDMGFEPQIR 330
Cdd:cd17945 83 EEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQVT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 356530675 331 KIVEQM--DMPPPGM--------------RQTLLFSATFPKEIQALASDFLSNYVFL 371
Cdd:cd17945 163 KILDAMpvSNKKPDTeeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
144-374 |
4.75e-68 |
|
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: 221.04 E-value: 4.75e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 144 VETSGENVPPPVNTFAEIDLGEALNQNIQRCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIISGImreqy 223
Cdd:cd18049 12 ITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHI----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 224 AQRPRVARTAYPLALILSPTRELSCQIHDEAKKFSYQTGVKVVVAYGGAPINQQLRELERGVDILVATPGRLVDLLERAR 303
Cdd:cd18049 87 NHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGK 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 356530675 304 VSLQMIRYLALDEADRMLDMGFEPQIRKIVEQMdMPPpgmRQTLLFSATFPKEIQALASDFLSNYVFLAVG 374
Cdd:cd18049 167 TNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQI-RPD---RQTLMWSATWPKEVRQLAEDFLKDYIHINIG 233
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
171-362 |
3.05e-65 |
|
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: 212.11 E-value: 3.05e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 171 IQRCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIIsgimrEQYAQRPRVARTAYplALILSPTRELSCQI 250
Cdd:cd17947 5 LSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPIL-----ERLLYRPKKKAATR--VLVLVPTRELAMQC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 251 HDEAKKFSYQTGVKVVVAYGGAPINQQLRELERGVDILVATPGRLVDLLERAR-VSLQMIRYLALDEADRMLDMGFEPQI 329
Cdd:cd17947 78 FSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGFADEL 157
|
170 180 190
....*....|....*....|....*....|...
gi 356530675 330 RKIVEQMdmppPGMRQTLLFSATFPKEIQALAS 362
Cdd:cd17947 158 KEILRLC----PRTRQTMLFSATMTDEVKDLAK 186
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
144-374 |
2.05e-64 |
|
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: 212.95 E-value: 2.05e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 144 VETSGENVPPPVNTFAEIDLGEALNQNIQRCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIISGImreqy 223
Cdd:cd18050 50 ITIRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHI----- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 224 AQRPRVARTAYPLALILSPTRELSCQIHDEAKKFSYQTGVKVVVAYGGAPINQQLRELERGVDILVATPGRLVDLLERAR 303
Cdd:cd18050 125 NHQPYLERGDGPICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGK 204
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 356530675 304 VSLQMIRYLALDEADRMLDMGFEPQIRKIVEQMdMPPpgmRQTLLFSATFPKEIQALASDFLSNYVFLAVG 374
Cdd:cd18050 205 TNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQI-RPD---RQTLMWSATWPKEVRQLAEDFLRDYVQINIG 271
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
167-374 |
5.53e-62 |
|
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350715 [Multi-domain] Cd Length: 198 Bit Score: 203.59 E-value: 5.53e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 167 LNQNIQRCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIISGImreqyaQRPRvaRTAYPLALILSPTREL 246
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKL------GKPR--KKKGLRALILAPTREL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 247 SCQIHDEAKKFSYQTGVKVVV-AYGGAPINQQLRELERGVDILVATPGRLVDLLERARVSLQMIRYLALDEADRMLDMGF 325
Cdd:cd17957 73 ASQIYRELLKLSKGTGLRIVLlSKSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGF 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 356530675 326 EPQIRKIVEQMDMPppgMRQTLLFSATFPKEIQALASDFLSNYVFLAVG 374
Cdd:cd17957 153 REQTDEILAACTNP---NLQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
155-548 |
1.05e-61 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 209.68 E-value: 1.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 155 VNTFAEIDLGEALNQNIQRCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFcfpIISGIMREQYAQRPrvartay 234
Cdd:PTZ00424 27 VDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATF---VIAALQLIDYDLNA------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 235 PLALILSPTRELSCQIHDEAKKFSYQTGVKVVVAYGGAPINQQLRELERGVDILVATPGRLVDLLERARVSLQMIRYLAL 314
Cdd:PTZ00424 97 CQALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFIL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 315 DEADRMLDMGFEPQIRKIVEQMdmpPPGMrQTLLFSATFPKEIQALASDFLSNYVFLAVGRVGSSTDLIAQrveYVLESD 394
Cdd:PTZ00424 177 DEADEMLSRGFKGQIYDVFKKL---PPDV-QVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQ---FYVAVE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 395 KRSHLMDLLHAQRETgVNGKQglTLVFVETKKGADALEHCLCVNGFPAASIHGDRTQQERELALRSFKTGNTPILVATDV 474
Cdd:PTZ00424 250 KEEWKFDTLCDLYET-LTITQ--AIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDL 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 356530675 475 AARGLDIPRVAHVVNFDLPNDIDDYVHRIGRTGRAGKMGLATAFFNEGNLNLAKSLADLMQEANQEVPAWLSRY 548
Cdd:PTZ00424 327 LARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEVADY 400
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
180-360 |
2.62e-61 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 200.55 E-value: 2.62e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 180 TPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIISGIMREQYAqrprvartayPLALILSPTRELSCQIHDEAKKFSY 259
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNG----------PQALVLAPTRELAEQIYEELKKLGK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 260 QTGVKVVVAYGGAPINQQLRELeRGVDILVATPGRLVDLLERaRVSLQMIRYLALDEADRMLDMGFEPQIRKIVEQMdmp 339
Cdd:pfam00270 71 GLGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQE-RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRL--- 145
|
170 180
....*....|....*....|.
gi 356530675 340 pPGMRQTLLFSATFPKEIQAL 360
Cdd:pfam00270 146 -PKKRQILLLSATLPRNLEDL 165
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
169-367 |
2.45e-60 |
|
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: 199.23 E-value: 2.45e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 169 QNIQRCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPiisGIMREQYAQRPRVARTAyPLALILSPTRELSC 248
Cdd:cd17958 3 KEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLP---GFIHLDLQPIPREQRNG-PGVLVLTPTRELAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 249 QIHDEAKKFSYQtGVKVVVAYGGAPINQQLRELERGVDILVATPGRLVDLLERARVSLQMIRYLALDEADRMLDMGFEPQ 328
Cdd:cd17958 79 QIEAECSKYSYK-GLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQ 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 356530675 329 IRKIVeqMDMPPPgmRQTLLFSATFPKEIQALASDFLSN 367
Cdd:cd17958 158 IRKIL--LDIRPD--RQTIMTSATWPDGVRRLAQSYLKD 192
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
171-371 |
2.64e-60 |
|
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: 199.73 E-value: 2.64e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 171 IQRCKYVKPTPVQRYAIPISLA-GRDLMACAQTGSGKTAAFCFPIISGIMREQYAQRP-RVArtayplALILSPTRELSC 248
Cdd:cd17964 9 LTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRsGVS------ALIISPTRELAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 249 QIHDEAKKF-SYQTGVKVVVAYGGAPINQQLRELER-GVDILVATPGRLVDLLE--RARVSLQMIRYLALDEADRMLDMG 324
Cdd:cd17964 83 QIAAEAKKLlQGLRKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRLLDMG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 356530675 325 FEPQIRKIVEQMDMPPPGMRQTLLFSATFPKEIQALASDFL-SNYVFL 371
Cdd:cd17964 163 FRPDLEQILRHLPEKNADPRQTLLFSATVPDEVQQIARLTLkKDYKFI 210
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
158-370 |
8.74e-59 |
|
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: 195.52 E-value: 8.74e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 158 FAEIDLGEALNQNIQRCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIISGIMREQYAqrprvartayPLA 237
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYG----------IFA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 238 LILSPTRELSCQIHDEAKKFSYQTGVKVVVAYGGAPINQQLRELERGVDILVATPGRLVDLLE---RARVSLQMIRYLAL 314
Cdd:cd17955 71 LVLTPTRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 356530675 315 DEADRMLDMGFEPQIRKIVEQMdmpPPGmRQTLLFSATFPKEIQALASDFLSNYVF 370
Cdd:cd17955 151 DEADRLLTGSFEDDLATILSAL---PPK-RQTLLFSATLTDALKALKELFGNKPFF 202
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
157-371 |
4.75e-58 |
|
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: 193.68 E-value: 4.75e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 157 TFAEIDLGEALNQNIQRCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIISGIMREQyaqrPRV-ARtayp 235
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHS----PTVgAR---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 236 lALILSPTRELSCQIHDEAKKFSYQTGVKVVVAYGGAPINQQLRELERGVDILVATPGRLVDLLERARVSLQMIRYLALD 315
Cdd:cd17959 74 -ALILSPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 356530675 316 EADRMLDMGFEPQIRKIVEQMdmppPGMRQTLLFSATFPKEIQALASDFLSNYVFL 371
Cdd:cd17959 153 EADRLFEMGFAEQLHEILSRL----PENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
383-519 |
2.93e-57 |
|
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: 188.87 E-value: 2.93e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 383 IAQRVEYVLESDKRSHLMDLLHAQretgvnGKQGLTLVFVETKKGADALEHCLCVNGFPAASIHGDRTQQERELALRSFK 462
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLLLLEK------LKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFR 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 356530675 463 TGNTPILVATDVAARGLDIPRVAHVVNFDLPNDIDDYVHRIGRTGRAGKMGLATAFF 519
Cdd:cd18787 75 SGKVRVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
157-369 |
1.50e-56 |
|
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: 189.45 E-value: 1.50e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 157 TFAEIDLGEALNQNIQRCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIISGIMReqyaQRPRVartaypL 236
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLE----NPQRF------F 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 237 ALILSPTRELSCQIHDEAKKFSYQTGVKVVVAYGGAPINQQLRELERGVDILVATPGRLVDLLERAR-VSLQMIRYLALD 315
Cdd:cd17954 71 ALVLAPTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLKFLVMD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 356530675 316 EADRMLDMGFEPQIRKIVEQMdmppPGMRQTLLFSATFPKEIQALASDFLSNYV 369
Cdd:cd17954 151 EADRLLNMDFEPEIDKILKVI----PRERTTYLFSATMTTKVAKLQRASLKNPV 200
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
175-361 |
3.32e-56 |
|
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: 188.70 E-value: 3.32e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 175 KYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIISGIMREQYaqRPRVARTAYPLALILSPTRELSCQIHDEA 254
Cdd:cd17951 9 GIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEK--KLPFIKGEGPYGLIVCPSRELARQTHEVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 255 KKFSYQ------TGVKVVVAYGGAPINQQLRELERGVDILVATPGRLVDLLERARVSLQMIRYLALDEADRMLDMGFEPQ 328
Cdd:cd17951 87 EYYCKAlqeggyPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMIDMGFEED 166
|
170 180 190
....*....|....*....|....*....|...
gi 356530675 329 IRKIVEQMDmpppGMRQTLLFSATFPKEIQALA 361
Cdd:cd17951 167 IRTIFSYFK----GQRQTLLFSATMPKKIQNFA 195
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
172-371 |
1.09e-52 |
|
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1. DDX31 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350707 [Multi-domain] Cd Length: 214 Bit Score: 179.70 E-value: 1.09e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 172 QRCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIISGIMReqyaQRPRVARTAYPLALILSPTRELSCQIH 251
Cdd:cd17949 7 SKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLS----LEPRVDRSDGTLALVLVPTRELALQIY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 252 DEA----KKFSYqtgvkVVVAY--GGAPINQQLRELERGVDILVATPGRLVDLLERARV-SLQMIRYLALDEADRMLDMG 324
Cdd:cd17949 83 EVLekllKPFHW-----IVPGYliGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQSfDVSNLRWLVLDEADRLLDMG 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 356530675 325 FEPQIRKIVEQMD---------MPPPGMRQTLLFSATFPKEIQALASDFLSNYVFL 371
Cdd:cd17949 158 FEKDITKILELLDdkrskaggeKSKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
171-375 |
1.43e-52 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 178.84 E-value: 1.43e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 171 IQRCKYVKPTPVQRYAIPISLAG-RDLMACAQTGSGKTAAFCFPIISGIMREQYAQrprvartayplALILSPTRELSCQ 249
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKGGR-----------VLVLVPTRELAEQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 250 IHDEAKKFSYQTGVKVVVAYGGAPINQQLRELERGV-DILVATPGRLVDLLERARVSLQMIRYLALDEADRMLDMGFEPQ 328
Cdd:smart00487 70 WAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 356530675 329 IRKIVEQMdmppPGMRQTLLFSATFPKEIQALASDFLSNYVFLAVGR 375
Cdd:smart00487 150 LEKLLKLL----PKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGF 192
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
167-369 |
1.50e-52 |
|
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer development by promoting DNA replication. DDX59 knockdown mice showed reduced cell proliferation, anchorage-independent cell growth, and reduction of tumor formation. Recent work shows that EGFR and Ras regulate DDX59 during lung cancer development. Diseases associated with DDX59 (also called zinc finger HIT domain-containing protein 5) include orofaciodigital syndrome V and orofaciodigital syndrome. DDX59 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350720 [Multi-domain] Cd Length: 193 Bit Score: 178.51 E-value: 1.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 167 LNQNIQRCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIISGIMREQYAqrprvartayPLALILSPTREL 246
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRN----------PSALILTPTREL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 247 SCQIHDEAKKF-SYQTGVKVVVAYGGAPINQQLRELERGVDILVATPGRLVDLLERARVSLQMIRYLALDEADRMLDMGF 325
Cdd:cd17962 71 AVQIEDQAKELmKGLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGF 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 356530675 326 EPQIRKIVEQMDMPPpgmrQTLLFSATFPKEIQALASDFLSNYV 369
Cdd:cd17962 151 QQQVLDILENISHDH----QTILVSATIPRGIEQLAGQLLQNPV 190
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
169-359 |
2.65e-50 |
|
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: 173.96 E-value: 2.65e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 169 QNIQRCKYVKPTPVQRYAIPISLA-GRDLMACAQTGSGKTAAFCFPIISGIMrEQYAQRPRVARTAYPLALILSPTRELS 247
Cdd:cd17946 3 RALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLL-SQKSSNGVGGKQKPLRALILTPTRELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 248 CQIHDEAKKFSYQTGVKVVVAYGGAPINQQLRELERGVDILVATPGRLVDLLERAR---VSLQMIRYLALDEADRMLDMG 324
Cdd:cd17946 82 VQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNehlANLKSLRFLVLDEADRMLEKG 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 356530675 325 -FEpQIRKIVEQMDMPPPGM---RQTLLFSATFPKEIQA 359
Cdd:cd17946 162 hFA-ELEKILELLNKDRAGKkrkRQTFVFSATLTLDHQL 199
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
171-373 |
3.19e-49 |
|
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: 169.78 E-value: 3.19e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 171 IQRCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIISGIMREQYAQRPRVArtayplALILSPTRELSCQI 250
Cdd:cd17941 5 LKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTPEDGLG------ALIISPTRELAMQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 251 HDEAKKFSYQTGVKVVVAYGGAPINQqlrELER--GVDILVATPGRLVDLLERA----RVSLQMiryLALDEADRMLDMG 324
Cdd:cd17941 79 FEVLRKVGKYHSFSAGLIIGGKDVKE---EKERinRMNILVCTPGRLLQHMDETpgfdTSNLQM---LVLDEADRILDMG 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 356530675 325 FEPQIRKIVEQMdmppPGMRQTLLFSATFPKEIQALASDFLSNYVFLAV 373
Cdd:cd17941 153 FKETLDAIVENL----PKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
158-367 |
1.18e-48 |
|
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: 168.25 E-value: 1.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 158 FAEIDLGEALNQNIQRCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIISGI-MREQYAQrprvartaypl 236
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIdPKKDVIQ----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 237 ALILSPTRELSCQIHDEAKKFSYQTGVKVVVAYGGAPINQQLRELERGVDILVATPGRLVDLLERARVSLQMIRYLALDE 316
Cdd:cd17940 70 ALILVPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDE 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 356530675 317 ADRMLDMGFEPQIRKIVEQMdmppPGMRQTLLFSATFPKEIQALASDFLSN 367
Cdd:cd17940 150 ADKLLSQDFQPIIEKILNFL----PKERQILLFSATFPLTVKNFMDRHMHN 196
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
167-373 |
1.92e-48 |
|
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: 167.76 E-value: 1.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 167 LNQNIQRCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIISGIMREqyaqRPRVARTAYPLALILSPTREL 246
Cdd:cd17961 5 LLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKA----KAESGEEQGTRALILVPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 247 SCQIHDEAKKFSYQTGVKV-VVAYGGAPINQQLRELERGV-DILVATPGRLVDLLERARVSLQ-MIRYLALDEADRMLDM 323
Cdd:cd17961 81 AQQVSKVLEQLTAYCRKDVrVVNLSASSSDSVQRALLAEKpDIVVSTPARLLSHLESGSLLLLsTLKYLVIDEADLVLSY 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 356530675 324 GFEPQIRKIVEQMdmppPGMRQTLLFSATFPKEIQALASDFLSNYVFLAV 373
Cdd:cd17961 161 GYEEDLKSLLSYL----PKNYQTFLMSATLSEDVEALKKLVLHNPAILKL 206
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
171-369 |
1.47e-47 |
|
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: 165.44 E-value: 1.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 171 IQRCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIISGIMREQY-AQRPRVArtayplALILSPTRELSCQ 249
Cdd:cd17960 5 VAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKAnLKKGQVG------ALIISPTRELATQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 250 IHDEAKKF--SYQTGVKVVVAYGGAPINQQLRELER-GVDILVATPGRLVDLLERA--RVSLQMIRYLALDEADRMLDMG 324
Cdd:cd17960 79 IYEVLQSFleHHLPKLKCQLLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLSRKadKVKVKSLEVLVLDEADRLLDLG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 356530675 325 FEPQIRKIVEQMdmppPGMRQTLLFSATFPKEIQALASDFLSNYV 369
Cdd:cd17960 159 FEADLNRILSKL----PKQRRTGLFSATQTDAVEELIKAGLRNPV 199
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
171-361 |
1.80e-44 |
|
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: 157.14 E-value: 1.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 171 IQRCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIISGIMREQYAQRPRVArtayplALILSPTRELSCQI 250
Cdd:cd17942 5 IEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRNGTG------VIIISPTRELALQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 251 HDEAK---KFSYQTGVKVVvayGGAPINQQLRELERGVDILVATPGRLVDLLERARVSL-QMIRYLALDEADRMLDMGFE 326
Cdd:cd17942 79 YGVAKellKYHSQTFGIVI---GGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLyKNLQCLIIDEADRILEIGFE 155
|
170 180 190
....*....|....*....|....*....|....*
gi 356530675 327 PQIRKIVEQMdmppPGMRQTLLFSATFPKEIQALA 361
Cdd:cd17942 156 EEMRQIIKLL----PKRRQTMLFSATQTRKVEDLA 186
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
158-352 |
2.74e-44 |
|
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: 156.71 E-value: 2.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 158 FAEIDLGEALNQNIQRCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIISGIMreqyaqrprvartayplA 237
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIVV-----------------A 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 238 LILSPTRELSCQIHDEAKKFS-YQTGVKVVVAY--GGAPINQQLRELERGVDILVATPGRLVDLLERARVSLQMIRYLAL 314
Cdd:cd17938 64 LILEPSRELAEQTYNCIENFKkYLDNPKLRVALliGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 356530675 315 DEADRMLDMGFEPQIRKIVEQmdMPPPGMR----QTLLFSAT 352
Cdd:cd17938 144 DEADRLLSQGNLETINRIYNR--IPKITSDgkrlQVIVCSAT 183
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
173-370 |
6.62e-42 |
|
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, Component Of Gems 3, Gemin-3, and SMN-Interacting Protein) interacts directly with SMN (survival of motor neurons), the spinal muscular atrophy gene product, and may play a catalytic role in the function of the SMN complex on ribonucleoproteins. Diseases associated with DDX20 include spinal muscular atrophy and muscular atrophy. DDX20 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350701 [Multi-domain] Cd Length: 192 Bit Score: 149.72 E-value: 6.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 173 RCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIISGIMREQyaqrprvartAYPLALILSPTRELSCQIHD 252
Cdd:cd17943 7 AAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLER----------RHPQVLILAPTREIAVQIHD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 253 EAKKF-SYQTGVKVVVAYGGAPINQQLRELeRGVDILVATPGRLVDLLERARVSLQMIRYLALDEADRMLDMGFEPQIRK 331
Cdd:cd17943 77 VFKKIgKKLEGLKCEVFIGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNW 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 356530675 332 IVEQMdmppPGMRQTLLFSATFPKEIQALASDFLSNYVF 370
Cdd:cd17943 156 IFSSL----PKNKQVIAFSATYPKNLDNLLARYMRKPVL 190
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
163-371 |
1.76e-39 |
|
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: 143.10 E-value: 1.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 163 LGEALNQNIQRCKYVKPTPVQRYAIPISLAG--RDLMACAQTGSGKTAAFCFPIISgimreqyaqrpRVART-AYPLALI 239
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLS-----------RVDPTlKSPQALC 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 240 LSPTRELSCQIHDEAKKFSYQTGVKVVVA------YGGAPINQQlrelergvdILVATPGRLVDLLERARVSLQMIRYLA 313
Cdd:cd17963 70 LAPTRELARQIGEVVEKMGKFTGVKVALAvpgndvPRGKKITAQ---------IVIGTPGTVLDWLKKRQLDLKKIKILV 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 356530675 314 LDEADRMLDM-GFEPQIRKIveqMDMPPPGMrQTLLFSATFPKEIQALASDFLSNYVFL 371
Cdd:cd17963 141 LDEADVMLDTqGHGDQSIRI---KRMLPRNC-QILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
160-369 |
2.15e-39 |
|
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: 143.23 E-value: 2.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 160 EIDLGEALNQNIQRCKYVKPTPVQRYAI-PISLaGRDLMACAQTGSGKTAAFCFpiisgimreqyAQRPRVARTAY-PLA 237
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIvPIIK-GRDVIAQAQSGTGKTATFSI-----------GALQRIDTTVReTQA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 238 LILSPTRELSCQIHDEAKKFSYQTGVKVVVAYGGAPINQQLRELERGVDILVATPGRLVDLLERARVSLQMIRYLALDEA 317
Cdd:cd17939 69 LVLAPTRELAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 356530675 318 DRMLDMGFEPQIRKIVEQMdmppPGMRQTLLFSATFPKEIQALASDFLSNYV 369
Cdd:cd17939 149 DEMLSRGFKDQIYDIFQFL----PPETQVVLFSATMPHEVLEVTKKFMRDPV 196
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
394-510 |
6.66e-37 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 133.10 E-value: 6.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 394 DKRSHLMDLLHAQREtgvngkqGLTLVFVETKKGADAlEHCLCVNGFPAASIHGDRTQQERELALRSFKTGNTPILVATD 473
Cdd:pfam00271 1 EKLEALLELLKKERG-------GKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATD 72
|
90 100 110
....*....|....*....|....*....|....*..
gi 356530675 474 VAARGLDIPRVAHVVNFDLPNDIDDYVHRIGRTGRAG 510
Cdd:pfam00271 73 VAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
158-369 |
7.14e-37 |
|
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: 136.44 E-value: 7.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 158 FAEIDLGEALNQNIQRCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIISGI---MREqyaqrprvartay 234
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLdiqVRE------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 235 PLALILSPTRELSCQIHDEAKKFSYQTGVKVVVAYGGAPINQQLRELERGVDILVATPGRLVDLLERARVSLQMIRYLAL 314
Cdd:cd18045 68 TQALILSPTRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 356530675 315 DEADRMLDMGFEPQIRKIVEqmdMPPPGMrQTLLFSATFPKEIQALASDFLSNYV 369
Cdd:cd18045 148 DEADEMLNKGFKEQIYDVYR---YLPPAT-QVVLVSATLPQDILEMTNKFMTDPI 198
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
181-365 |
1.65e-36 |
|
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and nucleolar RNA helicase 2) is an RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II. It promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) and binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs. DDX50 (also called Gu-Beta, Nucleolar Protein Gu2, and malignant cell derived RNA helicase). DDX21 and DDX50 have similar genomic structures and are in tandem orientation on chromosome 10, suggesting that the two genes arose by gene duplication in evolution. Diseases associated with DDX21 include stomach disease and cerebral creatine deficiency syndrome 3. Diseases associated with DDX50 include rectal disease. Both are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. Their name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.
Pssm-ID: 350702 [Multi-domain] Cd Length: 202 Bit Score: 135.36 E-value: 1.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 181 PVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIISGIMREQYAQRprvaRTAYPLALILSPTRELSCQIHDEAKKFSYQ 260
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRK----RGRAPKVLVLAPTRELANQVTKDFKDITRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 261 tgVKVVVAYGGAPINQQLRELERGVDILVATPGRLVDLLERARVSLQMIRYLALDEADRMLDMGFEPQIRKIV-EQMDMP 339
Cdd:cd17944 91 --LSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILsVSYKKD 168
|
170 180
....*....|....*....|....*.
gi 356530675 340 PPGMRQTLLFSATFPKEIQALASDFL 365
Cdd:cd17944 169 SEDNPQTLLFSATCPDWVYNVAKKYM 194
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
167-363 |
3.43e-36 |
|
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: 135.19 E-value: 3.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 167 LNQNIQRCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIIsgimrEQYAQRPRVARTAY--PLALILSPTR 244
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPII-----QRLLRYKLLAEGPFnaPRGLVITPSR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 245 ELSCQIHDEAKKFSYQTGVKVVVAYGGAPInQQLRELERG-VDILVATPGRLVDLLERARVSLQMIRYLALDEADRMLDM 323
Cdd:cd17948 76 ELAEQIGSVAQSLTEGLGLKVKVITGGRTK-RQIRNPHFEeVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDD 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 356530675 324 GFEPQIRKIVEQ---------MDMPPPGMRQTLLFSATFPKEIQALASD 363
Cdd:cd17948 155 SFNEKLSHFLRRfplasrrseNTDGLDPGTQLVLVSATMPSGVGEVLSK 203
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
158-367 |
2.80e-35 |
|
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: 132.08 E-value: 2.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 158 FAEIDLGEALNQNIQRCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIISGIMREQyaqrPRVArtayplA 237
Cdd:cd17950 4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVD----GQVS------V 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 238 LILSPTRELSCQIHDEAKKFS-YQTGVKVVVAYGGAPINQQLRELERGV-DILVATPGRLVDLLERARVSLQMIRYLALD 315
Cdd:cd17950 74 LVICHTRELAFQISNEYERFSkYMPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 356530675 316 EADRM---LDMgfepqiRKIVEQMDMPPPGMRQTLLFSATFPKEIQALASDFLSN 367
Cdd:cd17950 154 ECDKMleqLDM------RRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQD 202
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
167-362 |
1.93e-34 |
|
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350714 [Multi-domain] Cd Length: 231 Bit Score: 130.44 E-value: 1.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 167 LNQNIQRCKYVKPTPVQRYAIPISLAG---------RDLMACAQTGSGKTAAFCFPIISGImreQYAQRPRVartaypLA 237
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQAL---SKRVVPRL------RA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 238 LILSPTRELSCQIHDEAKKFSYQTGVKVVVAYGGAPIN---QQLRELERG-----VDILVATPGRLVD-LLERARVSLQM 308
Cdd:cd17956 72 LIVVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKkeqKLLLVDTSGrylsrVDILVATPGRLVDhLNSTPGFTLKH 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 309 IRYLALDEADRMLDMGFE---PQIRKIVEQMDMPPPGMR-------------QTLLFSATFPKEIQALAS 362
Cdd:cd17956 152 LRFLVIDEADRLLNQSFQdwlETVMKALGRPTAPDLGSFgdanllersvrplQKLLFSATLTRDPEKLSS 221
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
158-369 |
4.16e-34 |
|
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: 128.72 E-value: 4.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 158 FAEIDLGEALNQNIQRCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIISGIMREQYAqrprvartayPLA 237
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKA----------TQA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 238 LILSPTRELSCQIHDEAKKFSYQTGVKVVVAYGGAPINQQLRELERGVDILVATPGRLVDLLERARVSLQMIRYLALDEA 317
Cdd:cd18046 71 LVLAPTRELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 356530675 318 DRMLDMGFEPQIRKIVEQMdmppPGMRQTLLFSATFPKEIQALASDFLSNYV 369
Cdd:cd18046 151 DEMLSRGFKDQIYDIFQKL----PPDTQVVLLSATMPNDVLEVTTKFMRDPI 198
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
165-356 |
1.43e-31 |
|
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: 122.87 E-value: 1.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 165 EALNQNIQRCKYVKPTPVQRYAIPI---SLAGRD--------------LMAcAQTGSGKTAAFCFPIISGIMREQYAQR- 226
Cdd:cd17965 17 EILKGSNKTDEEIKPSPIQTLAIKKllkTLMRKVtkqtsneepklevfLLA-AETGSGKTLAYLAPLLDYLKRQEQEPFe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 227 ---PRVA---RTAYPLALILSPTRELSCQIHDEAKKFSYQTGVKV-VVAYGGAPINQQLRELERG-VDILVATPGRLVDL 298
Cdd:cd17965 96 eaeEEYEsakDTGRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIkTFSSGFGPSYQRLQLAFKGrIDILVTTPGKLASL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 356530675 299 LERARVSLQMIRYLALDEADRMLDMGFEPQIRKIVEQMdmppPGMRQTLLFSATFPKE 356
Cdd:cd17965 176 AKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRA----PKLKHLILCSATIPKE 229
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
429-510 |
6.93e-30 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 112.69 E-value: 6.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 429 DALEHCLCVNGFPAASIHGDRTQQERELALRSFKTGNTPILVATDVAARGLDIPRVAHVVNFDLPNDIDDYVHRIGRTGR 508
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 356530675 509 AG 510
Cdd:smart00490 81 AG 82
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
144-361 |
3.87e-23 |
|
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: 98.17 E-value: 3.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 144 VETSGENVPPP---VNTFAEIDLGEALNQNIQRCKYVKPTPVQRYAIPISLAG--RDLMACAQTGSGKTAAFCFPIISgi 218
Cdd:cd18048 3 VEVLQRDPTSPlfsVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLS-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 219 mreqyaqrpRV-ARTAYPLALILSPTRELSCQ---IHDEAKKFSyqTGVKVVVAYGGapiNQQLRELERGVDILVATPGR 294
Cdd:cd18048 81 ---------RVdALKLYPQCLCLSPTFELALQtgkVVEEMGKFC--VGIQVIYAIRG---NRPGKGTDIEAQIVIGTPGT 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 356530675 295 LVDLLERAR-VSLQMIRYLALDEADRMLDM-GFEPQIRKIVEQMdmppPGMRQTLLFSATFPKEIQALA 361
Cdd:cd18048 147 VLDWCFKLRlIDVTNISVFVLDEADVMINVqGHSDHSVRVKRSM----PKECQMLLFSATFEDSVWAFA 211
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
182-488 |
4.44e-21 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 97.40 E-value: 4.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 182 VQRYAIPISLAGRDLMACAQTGSGKTAAFCFpiisgIMREQYAQRPrvartayplALILSPTRELSCQIHDEAKKFsyqt 261
Cdd:COG1061 89 LEALLAALERGGGRGLVVAPTGTGKTVLALA-----LAAELLRGKR---------VLVLVPRRELLEQWAEELRRF---- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 262 gvkvvvaYGGAPINQQLRELERgvDILVATPGRLVDLLERARVSlQMIRYLALDEADRmldmGFEPQIRKIVEQMdmpPP 341
Cdd:COG1061 151 -------LGDPLAGGGKKDSDA--PITVATYQSLARRAHLDELG-DRFGLVIIDEAHH----AGAPSYRRILEAF---PA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 342 GMRqtLLFSAT------FPKEI-------------QALASDFLSNYVFLAVGRVGSST----DLIAQRVEYVLESDKRSH 398
Cdd:COG1061 214 AYR--LGLTATpfrsdgREILLflfdgivyeyslkEAIEDGYLAPPEYYGIRVDLTDEraeyDALSERLREALAADAERK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 399 LMDLLHAQREtgvNGKQGLTLVFVETKKGADALEHCLCVNGFPAASIHGDRTQQERELALRSFKTGNTPILVATDVAARG 478
Cdd:COG1061 292 DKILRELLRE---HPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEG 368
|
330
....*....|
gi 356530675 479 LDIPRVAHVV 488
Cdd:COG1061 369 VDVPRLDVAI 378
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
274-541 |
3.16e-18 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 87.89 E-value: 3.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 274 INQQLRELERG-VDILVATPGRL-----VDLLERARVSLqmiryLALDEA--------DrmldmgFEP---QIRKIVEQM 336
Cdd:COG0514 96 RREVLRALRAGeLKLLYVAPERLlnprfLELLRRLKISL-----FAIDEAhcisqwghD------FRPdyrRLGELRERL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 337 DMPPpgmrqTLLFSATFPKEIQA-----LAsdfLSN-YVFLavgrvgSSTDL--IAQRVEYVLESDKRSHLMDLLHAQRe 408
Cdd:COG0514 165 PNVP-----VLALTATATPRVRAdiaeqLG---LEDpRVFV------GSFDRpnLRLEVVPKPPDDKLAQLLDFLKEHP- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 409 tgvnGKQGLtlVFVETKKGADALEHCLCVNGFPAASIHGDRTQQERELALRSFKTGNTPILVATdVA-ARGLDIPRVAHV 487
Cdd:COG0514 230 ----GGSGI--VYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFV 302
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 356530675 488 VNFDLPNDIDDYVHRIGRTGRAGKMGLATAFFNEGNLNLAKSLAD--LMQEANQEV 541
Cdd:COG0514 303 IHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIEqsPPDEERKRV 358
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
392-512 |
1.95e-15 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 79.77 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 392 ESDKRSHLMDLLHAQRETGVNGKqglTLVFVETKKGADALEHCLCVNGFPA------ASIHGDR--TQQERELALRSFKT 463
Cdd:COG1111 333 EHPKLSKLREILKEQLGTNPDSR---IIVFTQYRDTAEMIVEFLSEPGIKAgrfvgqASKEGDKglTQKEQIEILERFRA 409
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 356530675 464 GNTPILVATDVAARGLDIPRVAHVVNFDL-PNDIdDYVHRIGRTGR--AGKM 512
Cdd:COG1111 410 GEFNVLVATSVAEEGLDIPEVDLVIFYEPvPSEI-RSIQRKGRTGRkrEGRV 460
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
193-352 |
2.74e-15 |
|
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: 73.21 E-value: 2.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 193 GRDLMACAQTGSGKTAAFcFPIIsgimrEQYA--QRPRVartayplaLILSPTRELSCQIHDEAKKFsYQTGVKVVVAYG 270
Cdd:cd00046 1 GENVLITAPTGSGKTLAA-LLAA-----LLLLlkKGKKV--------LVLVPTKALALQTAERLREL-FGPGIRVAVLVG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 271 GAPINQQLRELERGVDILVATPGRLVDLLERA-RVSLQMIRYLALDEADRMLDMGFEPQIRKIVEQMDMPPPGmrQTLLF 349
Cdd:cd00046 66 GSSAEEREKNKLGDADIIIATPDMLLNLLLREdRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNA--QVILL 143
|
...
gi 356530675 350 SAT 352
Cdd:cd00046 144 SAT 146
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
157-361 |
3.92e-14 |
|
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: 71.67 E-value: 3.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 157 TFAEIDLGEALNQNIQRCKYVKPTPVQRYAIPISLAG--RDLMACAQTGSGKTAAFCFPIISGIMreqyaqrprvARTAY 234
Cdd:cd18047 2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVE----------PANKY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 235 PLALILSPTRELSCQ---IHDEAKKFSYQtgvkVVVAYGgapinQQLRELERGV----DILVATPGRLVDLLERAR-VSL 306
Cdd:cd18047 72 PQCLCLSPTYELALQtgkVIEQMGKFYPE----LKLAYA-----VRGNKLERGQkiseQIVIGTPGTVLDWCSKLKfIDP 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 356530675 307 QMIRYLALDEADRML-DMGFEPQIRKIveqMDMPPPGMrQTLLFSATFPKEIQALA 361
Cdd:cd18047 143 KKIKVFVLDEADVMIaTQGHQDQSIRI---QRMLPRNC-QMLLFSATFEDSVWKFA 194
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
399-509 |
1.44e-13 |
|
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: 68.00 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 399 LMDLLHAQRETGVNGKQGLTLVFVETKKGADALEHCL-----CVNGFPAASI--HGDRTQQEREL--------ALRSFKT 463
Cdd:cd18802 9 LQKLIEILREYFPKTPDFRGIIFVERRATAVVLSRLLkehpsTLAFIRCGFLigRGNSSQRKRSLmtqrkqkeTLDKFRD 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 356530675 464 GNTPILVATDVAARGLDIPRVAHVVNFDLPNDIDDYVHRIGRtGRA 509
Cdd:cd18802 89 GELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARA 133
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
385-504 |
9.10e-12 |
|
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: 62.88 E-value: 9.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 385 QRVEYVLeSDKRSHLMDLLHAQRETGvnGKqglTLVFVETKKGADALEHCLCVNGFPAASIHGDRTQQERELALRSFKTG 464
Cdd:cd18793 3 PKIEEVV-SGKLEALLELLEELREPG--EK---VLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNED 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 356530675 465 NTP--ILVATDVAARGLDIPRVAHVVNFDL---PNDID---DYVHRIG 504
Cdd:cd18793 77 PDIrvFLLSTKAGGVGLNLTAANRVILYDPwwnPAVEEqaiDRAHRIG 124
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
390-512 |
1.09e-10 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350181 [Multi-domain] Cd Length: 134 Bit Score: 59.53 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 390 VLESDKRSHLMDLLhaqRETGVNGKQGLTLVFVETKKGADALEHCLCVNGFPAASIHGDRTQQERELALRSFKTGNTPIL 469
Cdd:cd18794 8 VRPKDKKDEKLDLL---KRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVI 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 356530675 470 VATdVA-ARGLDIPRVAHVVNFDLPNDIDDYVHRIGRTGRAGKM 512
Cdd:cd18794 85 VAT-VAfGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLP 127
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
183-317 |
1.04e-09 |
|
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: 57.98 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 183 QRYAIPISLAGRDLMACAQTGSGKTAAFCFPIISGIMREQYAQrprvartayplALILSPTRELscqIHDEAKKFS---- 258
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDPGSR-----------ALYLYPTKAL---AQDQLRSLRelle 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 356530675 259 -YQTGVKVVVAYGGAPINQQLRELERGVDILVATPgrlvDLLE--------RARVSLQMIRYLALDEA 317
Cdd:cd17923 71 qLGLGIRVATYDGDTPREERRAIIRNPPRILLTNP----DMLHyallphhdRWARFLRNLRYVVLDEA 134
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
449-511 |
1.65e-09 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 54.63 E-value: 1.65e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 356530675 449 RTQQERELALRSFKtgntpILVATDVAARGLDIPRVAHVVNFDLPNDIDDYVHRIGRTGRAGK 511
Cdd:cd18785 11 NSIEHAEEIASSLE-----ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK 68
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
180-317 |
2.86e-09 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 59.91 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 180 TPVQRYAIPISL-AGRDLMACAQTGSGKTAAFCFPIISGIMREqyaqrprvartayPLALILSPTRELSCQIHDEAKKFS 258
Cdd:COG1204 24 YPPQAEALEAGLlEGKNLVVSAPTASGKTLIAELAILKALLNG-------------GKALYIVPLRALASEKYREFKRDF 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 259 YQTGVKVVVAYGGAPINqqLRELERgVDILVATPGRLvDLLERARVS-LQMIRYLALDEA 317
Cdd:COG1204 91 EELGIKVGVSTGDYDSD--DEWLGR-YDILVATPEKL-DSLLRNGPSwLRDVDLVVVDEA 146
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
375-506 |
5.17e-09 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 59.08 E-value: 5.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 375 RVGSSTDLIAQ-RVEYVLESDKRSHLMDLLHAQRETGvnGKqglTLVFVETKKGADALEHCLCVNGFPAASIHGDRTQQE 453
Cdd:COG0553 513 QICSHPALLLEeGAELSGRSAKLEALLELLEELLAEG--EK---VLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEE 587
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 356530675 454 RELALRSFKTGNTP--ILVATDVAARGLDIPRVAHVVNFDL---PNDID---DYVHRIGRT 506
Cdd:COG0553 588 RDELVDRFQEGPEApvFLISLKAGGEGLNLTAADHVIHYDLwwnPAVEEqaiDRAHRIGQT 648
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
180-317 |
7.20e-09 |
|
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: 55.73 E-value: 7.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 180 TPVQRYAI-PISLAGRDLMACAQTGSGKTAAFCFPIISGIMREQyaqrprvartayPLALILSPTRELSCQIHDEAKKFS 258
Cdd:cd17921 3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRALATSG------------GKAVYIAPTRALVNQKEADLRERF 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 259 YQTGVKVVVAYGGAPINqqlRELERGVDILVATPGRLVDLLERARV-SLQMIRYLALDEA 317
Cdd:cd17921 71 GPLGKNVGLLTGDPSVN---KLLLAEADILVATPEKLDLLLRNGGErLIQDVRLVVVDEA 127
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
419-511 |
1.07e-08 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 58.35 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 419 LVFVETKKGADALEHCLCVNGFPA------ASIHGDR--TQQERELALRSFKTGNTPILVATDVAARGLDIPRVAHVVNF 490
Cdd:PRK13766 369 IVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKgmSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFY 448
|
90 100
....*....|....*....|..
gi 356530675 491 D-LPNDIdDYVHRIGRTGRAGK 511
Cdd:PRK13766 449 EpVPSEI-RSIQRKGRTGRQEE 469
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
175-316 |
1.84e-08 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 57.59 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 175 KYVKPTPVQRYAIPISLAGRDLMACAQTGSGKT-AAFCfPIISGIMReqYAQRPRVARTAYplALILSPTRELSCQIH-- 251
Cdd:PRK13767 29 KFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFL-AIIDELFR--LGREGELEDKVY--CLYVSPLRALNNDIHrn 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 356530675 252 ---------DEAKKFSYQ-TGVKVVVAYGGAPINQQLRELERGVDILVATPGRLVDLLE--RARVSLQMIRYLALDE 316
Cdd:PRK13767 104 leeplteirEIAKERGEElPEIRVAIRTGDTSSYEKQKMLKKPPHILITTPESLAILLNspKFREKLRTVKWVIVDE 180
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
193-316 |
6.59e-08 |
|
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: 52.59 E-value: 6.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 193 GRDLMACAQTGSGKTAAFCFPIISGIMREqyaQRPRVArtayplALILSPTRELSCQIHDEAKKFS--YQTGVKVVVAYG 270
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADE---PEKGVQ------VLYISPLKALINDQERRLEEPLdeIDLEIPVAVRHG 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 356530675 271 GAPINQQLRELERGVDILVATPGRLVDLL--ERARVSLQMIRYLALDE 316
Cdd:cd17922 72 DTSQSEKAKQLKNPPGILITTPESLELLLvnKKLRELFAGLRYVVVDE 119
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
200-481 |
1.33e-07 |
|
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: 54.32 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 200 AQTGSGKT-AAFCFpiISGIMREQYAQRprvartayplaLILS-PTRELSCQIHDEAKKFSyqtGVKVVVAYGGAPIN-- 275
Cdd:COG1203 154 APTGGGKTeAALLF--ALRLAAKHGGRR-----------IIYAlPFTSIINQTYDRLRDLF---GEDVLLHHSLADLDll 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 276 ----------QQLRELERGVD--ILVATPGRLVDLLERARVSlQMIRYLAL-------DEADrMLDMGFEPQIRKIVEQM 336
Cdd:COG1203 218 eeeeeyeseaRWLKLLKELWDapVVVTTIDQLFESLFSNRKG-QERRLHNLansviilDEVQ-AYPPYMLALLLRLLEWL 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 337 DMpppgMRQTLLF-SATFPKEIqalaSDFLSNYVFLAVGRVGSSTDLIAQ----RVEYVLESDKRSHLMDLLHAQREtgv 411
Cdd:COG1203 296 KN----LGGSVILmTATLPPLL----REELLEAYELIPDEPEELPEYFRAfvrkRVELKEGPLSDEELAELILEALH--- 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 412 NGKQglTLVFVETKKGADAL----------EHCLCVNG-FPAAsihgDRTQQERELaLRSFKTGNTPILVATDVAARGLD 480
Cdd:COG1203 365 KGKS--VLVIVNTVKDAQELyealkeklpdEEVYLLHSrFCPA----DRSEIEKEI-KERLERGKPCILVSTQVVEAGVD 437
|
.
gi 356530675 481 I 481
Cdd:COG1203 438 I 438
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
194-317 |
1.60e-07 |
|
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: 51.88 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 194 RDLMACAQTGSGKTaafcfpIISgIMR-EQYAQRPRVARTAYPLALILSPTRELSCQihdEAKKFSYQTGVKVVVAYGGA 272
Cdd:cd18034 17 RNTIVVLPTGSGKT------LIA-VMLiKEMGELNRKEKNPKKRAVFLVPTVPLVAQ---QAEAIRSHTDLKVGEYSGEM 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 356530675 273 PINQQ-----LRELERgVDILVATPGRLVDLLERARVSLQMIRYLALDEA 317
Cdd:cd18034 87 GVDKWtkerwKEELEK-YDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
149-515 |
2.62e-07 |
|
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: 53.69 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 149 ENVPPPVNTFAEI--DLGEALNQNIQRCKYVKPTPVQRYAIPISLAGRDLMACAQTGSGKTAAFCFPIISGIMREqyaqr 226
Cdd:COG1205 25 RTIPAREARYAPWpdWLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLED----- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 227 pRVARtayplALILSPTRELScqiHDEAKKFS-----YQTGVKVVVAYGGAPinQQLRE--LERGvDILVATP------- 292
Cdd:COG1205 100 -PGAT-----ALYLYPTKALA---RDQLRRLRelaeaLGLGVRVATYDGDTP--PEERRwiREHP-DIVLTNPdmlhygl 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 293 ----GRLVDLLERarvslqmIRYLALDEA---------------DRMldmgfepqiRKIVEQMDMPPpgmrQTLLFSATF 353
Cdd:COG1205 168 lphhTRWARFFRN-------LRYVVIDEAhtyrgvfgshvanvlRRL---------RRICRHYGSDP----QFILASATI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 354 --PKEiqaLASDfLSNYVFLAVGRVGSSTdliaQRVEYVL-------ESDKRSH-------LMDLLHaqretgvNGKQgl 417
Cdd:COG1205 228 gnPAE---HAER-LTGRPVTVVDEDGSPR----GERTFVLwnpplvdDGIRRSAlaeaarlLADLVR-------EGLR-- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 418 TLVFVETKKGA--------DALEHclcvnGFPAASI---HGDRTQQERELALRSFKTGNTPILVAT-------DVAarGL 479
Cdd:COG1205 291 TLVFTRSRRGAellaryarRALRE-----PDLADRVaayRAGYLPEERREIERGLRSGELLGVVSTnalelgiDIG--GL 363
|
410 420 430
....*....|....*....|....*....|....*.
gi 356530675 480 DIprvahVVNFDLPNDIDDYVHRIGRTGRAGKMGLA 515
Cdd:COG1205 364 DA-----VVLAGYPGTRASFWQQAGRAGRRGQDSLV 394
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
397-520 |
4.56e-07 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 52.79 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 397 SHLMDLLHAQRetgvnGKQGLtlVFVETKKGADALEHCLCVNGFPAASIHGDRTQQERELALRSFKTGNTPILVATDVAA 476
Cdd:PRK11057 225 DQLMRYVQEQR-----GKSGI--IYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFG 297
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 356530675 477 RGLDIPRVAHVVNFDLPNDIDDYVHRIGRTGRAGKMGLATAFFN 520
Cdd:PRK11057 298 MGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYD 341
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
450-508 |
1.46e-06 |
|
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: 48.12 E-value: 1.46e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 450 TQQERELALRSFKTGNTPILVATDVAARGLDIPRVAHVVNFD-LPNDIdDYVHRIGRTGR 508
Cdd:cd18801 75 SQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDaSPSPI-RMIQRMGRTGR 133
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
418-519 |
1.82e-06 |
|
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350176 [Multi-domain] Cd Length: 153 Bit Score: 48.01 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 418 TLVFVETKkgaDALEHCLCVNGFPAasIHGDRTQQERELALRSFKTGNTPILVATDVAARGLDIP--RVAHVVNFdLPND 495
Cdd:cd18789 52 IIVFTDNV---EALYRYAKRLLKPF--ITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPeaNVAIQISG-HGGS 125
|
90 100
....*....|....*....|....
gi 356530675 496 IDDYVHRIGRTGRAGKMGLATAFF 519
Cdd:cd18789 126 RRQEAQRLGRILRPKKGGGKNAFF 149
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
175-316 |
2.16e-06 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 50.87 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 175 KYVKPTPVQRYAIPISLAGRDLMACAQTGSGKT-AAFcFPIISGIMREQYAQRPRVA-RTAY--PL-AL-------ILSP 242
Cdd:COG1201 21 RFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPRPGELPDGlRVLYisPLkALandiernLRAP 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 356530675 243 TRELSCQIHDEAKkfsyqtGVKVVVAYGGAPINQQLRELERGVDILVATPGRLVDLL--ERARVSLQMIRYLALDE 316
Cdd:COG1201 100 LEEIGEAAGLPLP------EIRVGVRTGDTPASERQRQRRRPPHILITTPESLALLLtsPDARELLRGVRTVIVDE 169
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
181-359 |
1.10e-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: 46.76 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 181 PVQRYAIPISLAGRDLMACAQTGSGKTAafCFpiisgimreqyaQRPRVARTayPLALILSPTRELscqIHDEAKKFSyQ 260
Cdd:cd17920 15 PGQLEAINAVLAGRDVLVVMPTGGGKSL--CY------------QLPALLLD--GVTLVVSPLISL---MQDQVDRLQ-Q 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 261 TGVKVVVAYGGAPINQQLRELER----GVDILVATPGRLV-----DLLERARvSLQMIRYLALDEADRMLDMG--FEP-- 327
Cdd:cd17920 75 LGIRAAALNSTLSPEEKREVLLRikngQYKLLYVTPERLLspdflELLQRLP-ERKRLALIVVDEAHCVSQWGhdFRPdy 153
|
170 180 190
....*....|....*....|....*....|...
gi 356530675 328 -QIRKIVEQMDMPPpgmrqTLLFSATFPKEIQA 359
Cdd:cd17920 154 lRLGRLRRALPGVP-----ILALTATATPEVRE 181
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
418-488 |
1.55e-05 |
|
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: 44.47 E-value: 1.55e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 356530675 418 TLVFVETKKGADALEHCLCVNGFPAASIHGDRTQQEREL-ALRSFKTGNT--PILVATDVAARGLDIPRVAHVV 488
Cdd:cd18799 9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDeALILLFFGELkpPILVTVDLLTTGVDIPEVDNVV 82
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
418-511 |
3.96e-05 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 44.18 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 418 TLVFVETKKGADALEHCL------CVNGFPAASIHGDRTQQERELALRSFKTGNTPILVATDVAARGLDIPRVAHVVNFD 491
Cdd:cd18796 41 TLVFTNTRSQAERLAQRLrelcpdRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIG 120
|
90 100
....*....|....*....|
gi 356530675 492 LPNDIDDYVHRIGRTGRAGK 511
Cdd:cd18796 121 SPKSVARLLQRLGRSGHRPG 140
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
199-317 |
2.92e-04 |
|
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350779 [Multi-domain] Cd Length: 191 Bit Score: 42.25 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 199 CAQTGSGKTAAFCFPIISGIMREQYaqrprvARTAYplaliLSPTRELSCQIHDE-AKKFSYQTGVKVVVAYGGApiNQQ 277
Cdd:cd18021 25 GAPTGSGKTVCAELALLRHWRQNPK------GRAVY-----IAPMQELVDARYKDwRAKFGPLLGKKVVKLTGET--STD 91
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 356530675 278 LRELERGvDILVATPGRLvDLLER---ARVSLQMIRYLALDEA 317
Cdd:cd18021 92 LKLLAKS-DVILATPEQW-DVLSRrwkQRKNVQSVELFIADEL 132
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
445-511 |
4.33e-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: 41.18 E-value: 4.33e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 356530675 445 IHGDRTQQERELALRSFKTGNTPILVATDVAARGLDIPR-----VAHVVNFDLPNdiddyVHRI-GRTGRAGK 511
Cdd:cd18811 67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNatvmvIEDAERFGLSQ-----LHQLrGRVGRGDH 134
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
181-357 |
7.62e-04 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 40.78 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 181 PVQRYAIPISLA-GRDLMACAQTGSGKTAAFCFPIISGIMREQyaqrprvartaypLALILSPTRELSCQIHDEAKKFsY 259
Cdd:cd18028 4 PPQAEAVRAGLLkGENLLISIPTASGKTLIAEMAMVNTLLEGG-------------KALYLVPLRALASEKYEEFKKL-E 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 260 QTGVKVVVAYGgapinqQLRELERGV---DILVATPGRLvDLLERARVS-LQMIRYLALDEADRMLDMGFEPQIRKIVEQ 335
Cdd:cd18028 70 EIGLKVGISTG------DYDEDDEWLgdyDIIVATYEKF-DSLLRHSPSwLRDVGVVVVDEIHLISDEERGPTLESIVAR 142
|
170 180
....*....|....*....|....
gi 356530675 336 MDMPPPGmRQTLLFSATF--PKEI 357
Cdd:cd18028 143 LRRLNPN-TQIIGLSATIgnPDEL 165
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
194-316 |
1.50e-03 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350781 [Multi-domain] Cd Length: 206 Bit Score: 40.42 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 194 RDLMACAQTGSGKTAAFCFPIISGIMreqyaQRPRVARTAYpLALILSPTRELSCQIHDEAK-KFSyQTGVKVVVAYGga 272
Cdd:cd18023 18 KNFVVSAPTGSGKTVLFELAILRLLK-----ERNPLPWGNR-KVVYIAPIKALCSEKYDDWKeKFG-PLGLSCAELTG-- 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 356530675 273 piNQQLRELE--RGVDILVATPGRLvDLLERARVS----LQMIRYLALDE 316
Cdd:cd18023 89 --DTEMDDTFeiQDADIILTTPEKW-DSMTRRWRDngnlVQLVALVLIDE 135
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
440-515 |
1.52e-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: 39.56 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 440 FPAASI---HGDRTQQERELALRSFKTGNTPILVATDVAARGLDIPR-----VAHVVNFDLPNdiddyVHRI-GRTGRAG 510
Cdd:cd18792 58 VPEARVallHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNantmiIEDADRFGLSQ-----LHQLrGRVGRGK 132
|
....*
gi 356530675 511 KMGLA 515
Cdd:cd18792 133 HQSYC 137
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
178-291 |
1.97e-03 |
|
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: 39.71 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 178 KPTPVQRYAIP------ISLAGRDLMACAQTGSGKTAAFCFPIISgimreqYAQRPRVartayplALILSPTRELSCQIH 251
Cdd:cd17918 15 SLTKDQAQAIKdiekdlHSPEPMDRLLSGDVGSGKTLVALGAALL------AYKNGKQ-------VAILVPTEILAHQHY 81
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 356530675 252 DEAKKFSYQTGVKVVVAYGGAPINQqlrelerGVDILVAT 291
Cdd:cd17918 82 EEARKFLPFINVELVTGGTKAQILS-------GISLLVGT 114
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
177-319 |
2.22e-03 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 39.72 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 177 VKPTPVQRYAIPISLAGRDLMACAQTGSGKTaafcfpIISGIMREQYAQRPRVARTAYplALILSPTRELSCQihdEAKK 256
Cdd:cd17927 1 FKPRNYQLELAQPALKGKNTIICLPTGSGKT------FVAVLICEHHLKKFPAGRKGK--VVFLANKVPLVEQ---QKEV 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 356530675 257 FSYQTGVKV--VVAYGGA-PINQQLRELERGVDILVATPGRLV-DLLERARVSLQMIRYLALDEADR 319
Cdd:cd17927 70 FRKHFERPGykVTGLSGDtSENVSVEQIVESSDVIIVTPQILVnDLKSGTIVSLSDFSLLVFDECHN 136
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
389-512 |
4.78e-03 |
|
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350185 [Multi-domain] Cd Length: 174 Bit Score: 38.44 E-value: 4.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 389 YVLESDKRSHLMDLLhaqRETGVNGkqgltLVFVETKKG---ADALEHCLCVNGFPAASIHGDRtqqeRELaLRSFKTGN 465
Cdd:cd18798 6 YIEDSDSLEKLLELV---KKLGDGG-----LIFVSIDYGkeyAEELKEFLERHGIKAELALSST----EKN-LEKFEEGE 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 356530675 466 TPILVAT----DVAARGLDIP-RVAHVVNFDLPndIDDYVHRIGRTGR--AGKM 512
Cdd:cd18798 73 IDVLIGVasyyGVLVRGIDLPeRIKYAIFYGVP--VTTYIQASGRTSRlyAGGL 124
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
178-291 |
6.02e-03 |
|
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350682 [Multi-domain] Cd Length: 189 Bit Score: 38.08 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 178 KPTPVQRYAIPISLAGRDLMACAQTGSGKTAafcFPIISGIMreQYAQRPRVartayplaLILSPTRELSCQIHDEAKKF 257
Cdd:cd17924 17 PPWGAQRTWAKRLLRGKSFAIIAPTGVGKTT---FGLATSLY--LASKGKRS--------YLIFPTKSLVKQAYERLSKY 83
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 356530675 258 SYQTG--VKVVVAYGGAPINQQLRELER----GVDILVAT 291
Cdd:cd17924 84 AEKAGveVKILVYHSRLKKKEKEELLEKiekgDFDILVTT 123
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
401-491 |
6.19e-03 |
|
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350177 [Multi-domain] Cd Length: 171 Bit Score: 38.00 E-value: 6.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 401 DLLHAQRETGVNGKQglTLVFVETKKGADALEHCLCVNGFPAASIHGDRTQQERELALRSFKTGNTPILVATDVAARGLD 480
Cdd:cd18790 15 DLLGEIRKRVARGER--VLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLD 92
|
90
....*....|.
gi 356530675 481 IPRVAHVVNFD 491
Cdd:cd18790 93 LPEVSLVAILD 103
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
441-515 |
6.49e-03 |
|
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350197 [Multi-domain] Cd Length: 151 Bit Score: 37.71 E-value: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 441 PAASI---HGDRTQQERELALRSFKTGNTPILVATDVAARGLDIPRvahvVNFDLPNDIDDY----VHRI-GRTGRAGKM 512
Cdd:cd18810 50 PEARIaiaHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPN----ANTIIIERADKFglaqLYQLrGRVGRSKER 125
|
...
gi 356530675 513 GLA 515
Cdd:cd18810 126 AYA 128
|
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| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
408-510 |
7.14e-03 |
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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: 37.53 E-value: 7.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530675 408 ETGVNGKQglTLVFVETKKGADAL-EHCLCVnGFpaasIHGDRTQQERELALRSFKTGNTPILVATDVAARGLDIPrvAH 486
Cdd:cd18795 38 ETVSEGKP--VLVFCSSRKECEKTaKDLAGI-AF----HHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLP--AR 108
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90 100 110
....*....|....*....|....*....|....*.
gi 356530675 487 VVNF------------DLPndIDDYVHRIGRTGRAG 510
Cdd:cd18795 109 TVIIkgtqrydgkgyrELS--PLEYLQMIGRAGRPG 142
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| SF2_C_priA |
cd18804 |
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ... |
449-514 |
8.36e-03 |
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C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350191 [Multi-domain] Cd Length: 238 Bit Score: 38.38 E-value: 8.36e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 356530675 449 RTQQERELALRSFKTGNTPILVATDVAARGLDIPRV--AHVVNFDLPNDIDDY---------VHRI-GRTGRAGKMGL 514
Cdd:cd18804 128 RKKGALEKLLDQFERGEIDILIGTQMIAKGLDFPNVtlVGILNADSGLNSPDFraserafqlLTQVsGRAGRGDKPGK 205
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