|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
6-507 |
0e+00 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 664.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 6 SDRDRGRDRGFGAPRFGGSRAG-PLSGKKFG----------NPGEKLVKKKWNLDELPKFEKNFYQEHPDLARRTAQEVE 74
Cdd:PTZ00110 30 SSNPYGNYQANHQDNYGGFRPGyGNYSGGYGgfgmnsygssTLGKRLQPIDWKSINLVPFEKNFYKEHPEVSALSSKEVD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 75 TYRRSKEIT-VRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAI 153
Cdd:PTZ00110 110 EIRKEKEITiIAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 154 VHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLE 233
Cdd:PTZ00110 190 VHINAQPLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLE 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 234 CGKTNLRRTTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDY-IHINIGALELSANHN 312
Cdd:PTZ00110 270 SNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEEpVHVNVGSLDLTACHN 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 313 ILQIVDVCHDVEKDEKLIRLMEEIMSEKeNKTIVFVETKRRCDELTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKA 392
Cdd:PTZ00110 350 IKQEVFVVEEHEKRGKLKMLLQRIMRDG-DKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKS 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 393 PILIATDVASRGLDVEDVKFVINYDYPNSSEDYIHRIGRTARSTKTGTAYTFFTPNNIKQVSDLISVLREANQAINPKLL 472
Cdd:PTZ00110 429 PIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELE 508
|
490 500 510
....*....|....*....|....*....|....*
gi 1002095822 473 QLVEDRGSGRsrgrggmkddRRDRYSAGKRGGFNT 507
Cdd:PTZ00110 509 KLSNERSNGT----------ERRRWGGYGRFSNNV 533
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
71-304 |
0e+00 |
|
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: 535.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 71 QEVETYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLL 150
Cdd:cd18049 1 QEVEQYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 151 PAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLID 230
Cdd:cd18049 81 PAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLID 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002095822 231 FLECGKTNLRRTTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGA 304
Cdd:cd18049 161 FLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGA 234
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
33-303 |
0e+00 |
|
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: 523.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 33 KFGNPGEKLVKKKWNLDELPKFEKNFYQEHPDLARRTAQEVETYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQ 112
Cdd:cd18050 1 KFGNPGERLRKKKWDLSELPKFEKNFYVEHPEVARMTQYDVEELRRKKEITIRGVGCPKPVFAFHQANFPQYVMDVLLDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 113 NFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYCR 192
Cdd:cd18050 81 NFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQVQQVADDYGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 193 ACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRMLDMGFEPQIRKIVDQIRPD 272
Cdd:cd18050 161 SSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPD 240
|
250 260 270
....*....|....*....|....*....|.
gi 1002095822 273 RQTLMWSATWPKEVRQLAEDFLKDYIHINIG 303
Cdd:cd18050 241 RQTLMWSATWPKEVRQLAEDFLRDYVQINIG 271
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
95-512 |
2.14e-164 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 475.79 E-value: 2.14e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 95 NFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHqpflERGDGPICLVLA 174
Cdd:COG0513 3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDP----SRPRAPQALILA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 175 PTRELAQQVQQVAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRML 254
Cdd:COG0513 79 PTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRML 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 255 DMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGALELSANhNILQIVDVCHDVEKDEKLIRLME 334
Cdd:COG0513 159 DMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAE-TIEQRYYLVDKRDKLELLRRLLR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 335 EimsEKENKTIVFVETKRRCDELTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKAPILIATDVASRGLDVEDVKFVI 414
Cdd:COG0513 238 D---EDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 415 NYDYPNSSEDYIHRIGRTARSTKTGTAYTFFTPNNIKQVSDLisvLREANQAINPKLLQLVEDRGSGRSRGRGGMKDDRR 494
Cdd:COG0513 315 NYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAI---EKLIGQKIEEEELPGFEPVEEKRLERLKPKIKEKL 391
|
410
....*....|....*...
gi 1002095822 495 DRYSAGKRGGFNTFRDRE 512
Cdd:COG0513 392 KGKKAGRGGRPGPKGERK 409
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
105-301 |
5.44e-156 |
|
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: 445.66 E-value: 5.44e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 105 VMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGDGPICLVLAPTRELAQQVQ 184
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGDGPIVLVLAPTRELAQQIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 185 QVAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRMLDMGFEPQIRK 264
Cdd:cd17966 81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1002095822 265 IVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHIN 301
Cdd:cd17966 161 IVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
105-300 |
2.47e-105 |
|
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: 316.31 E-value: 2.47e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 105 VMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFlERGDGPICLVLAPTRELAQQVQ 184
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPK-KKGRGPQALVLAPTRELAMQIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 185 QVAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRMLDMGFEPQIRK 264
Cdd:cd00268 80 EVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 1002095822 265 IVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHI 300
Cdd:cd00268 160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
83-300 |
1.61e-100 |
|
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: 304.69 E-value: 1.61e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 83 TVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFL 162
Cdd:cd17953 1 KVRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 163 ERGDGPICLVLAPTRELAQQVQQVAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFL--ECGK-TNL 239
Cdd:cd17953 81 KPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtaNNGRvTNL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002095822 240 RRTTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHI 300
Cdd:cd17953 161 RRVTYVVLDEADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
96-448 |
4.65e-99 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 309.81 E-value: 4.65e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 96 FYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFlergdGPICLVLAP 175
Cdd:PRK11776 6 FSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRF-----RVQALVLCP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 176 TRELAQQVqqvAAEYCRACR----LKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEAD 251
Cdd:PRK11776 81 TRELADQV---AKEIRRLARfipnIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEAD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 252 RMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHInigalELSANHNILQIVDVCHDVEKDEKLIR 331
Cdd:PRK11776 158 RMLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEV-----KVESTHDLPAIEQRFYEVSPDERLPA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 332 LMEEIMSEKENKTIVFVETKRRCDELTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKAPILIATDVASRGLDVEDVK 411
Cdd:PRK11776 233 LQRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALE 312
|
330 340 350
....*....|....*....|....*....|....*..
gi 1002095822 412 FVINYDYPNSSEDYIHRIGRTARSTKTGTAYTFFTPN 448
Cdd:PRK11776 313 AVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPE 349
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
105-300 |
6.54e-95 |
|
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: 289.31 E-value: 6.54e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 105 VMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGDGPICLVLAPTRELAQQVQ 184
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGEGPIAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 185 QVAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRMLDMGFEPQIRK 264
Cdd:cd17952 81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1002095822 265 IVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHI 300
Cdd:cd17952 161 IVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
95-441 |
6.25e-87 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 277.21 E-value: 6.25e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 95 NFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHInhQPFLERGDGPI-CLVL 173
Cdd:PRK11192 2 TFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHL--LDFPRRKSGPPrILIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 174 APTRELAQQVQQVAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRM 253
Cdd:PRK11192 80 TPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 254 LDMGFEPQIRKIVDQIRPDRQTLMWSATWPKE-VRQLAEDFLKDYIHINIGAlELSANHNILQIVDVCHDVE-KDEKLIR 331
Cdd:PRK11192 160 LDMGFAQDIETIAAETRWRKQTLLFSATLEGDaVQDFAERLLNDPVEVEAEP-SRRERKKIHQWYYRADDLEhKTALLCH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 332 LMEEimsEKENKTIVFVETKRRCDELTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKAPILIATDVASRGLDVEDVK 411
Cdd:PRK11192 239 LLKQ---PEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVS 315
|
330 340 350
....*....|....*....|....*....|
gi 1002095822 412 FVINYDYPNSSEDYIHRIGRTARSTKTGTA 441
Cdd:PRK11192 316 HVINFDMPRSADTYLHRIGRTGRAGRKGTA 345
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
103-461 |
8.53e-86 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 275.15 E-value: 8.53e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 103 ANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGDGPI-CLVLAPTRELAQ 181
Cdd:PRK10590 10 PDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVrALILTPTRELAA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 182 QVQQVAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRMLDMGFEPQ 261
Cdd:PRK10590 90 QIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFIHD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 262 IRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIgALELSANHNILQIVdvcHDVEKDEKLIRLMEEIMSEKE 341
Cdd:PRK10590 170 IRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEV-ARRNTASEQVTQHV---HFVDKKRKRELLSQMIGKGNW 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 342 NKTIVFVETKRRCDELTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKAPILIATDVASRGLDVEDVKFVINYDYPNS 421
Cdd:PRK10590 246 QQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNV 325
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1002095822 422 SEDYIHRIGRTARSTKTGTAYTFFTPNNIKQVSDLISVLR 461
Cdd:PRK10590 326 PEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLK 365
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
96-303 |
1.70e-84 |
|
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: 263.58 E-value: 1.70e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 96 FYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHI-NHQPFLERGDG----PIC 170
Cdd:cd17967 2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLlEDGPPSVGRGRrkayPSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 171 LVLAPTRELAQQVQQVAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEA 250
Cdd:cd17967 82 LILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDEA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1002095822 251 DRMLDMGFEPQIRKIVDQ----IRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIG 303
Cdd:cd17967 162 DRMLDMGFEPQIRKIVEHpdmpPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVG 218
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
105-300 |
8.91e-84 |
|
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: 260.86 E-value: 8.91e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 105 VMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFL-ERGDGPICLVLAPTRELAQQV 183
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPrEQRNGPGVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 184 QQVAAEYCRAcRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRMLDMGFEPQIR 263
Cdd:cd17958 81 EAECSKYSYK-GLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 1002095822 264 KIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHI 300
Cdd:cd17958 160 KILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
69-472 |
1.15e-80 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 263.57 E-value: 1.15e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 69 TAQEVETYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSY 148
Cdd:PLN00206 96 SSSQAELLRRKLEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASF 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 149 LLPAIVH---INHQPFLERgDGPICLVLAPTRELAQQVQQVAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVEICIATP 225
Cdd:PLN00206 176 LVPIISRcctIRSGHPSEQ-RNPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTP 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 226 GRLIDFLECGKTNLRRTTYLVLDEADRMLDMGFEPQIRKIVdQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGAL 305
Cdd:PLN00206 255 GRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIF-QALSQPQVLLFSATVSPEVEKFASSLAKDIILISIGNP 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 306 ElSANHNILQIVDVchdVEKDEKLIRLMEEIMSEKENK--TIVFVETKRRCDELTRKMRR-DGWPAMGIHGDKSQQERDW 382
Cdd:PLN00206 334 N-RPNKAVKQLAIW---VETKQKKQKLFDILKSKQHFKppAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERRE 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 383 VLNEFKHGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYIHRIGRTARSTKTGTAYTFFTPNNIKQVSDLISVLRE 462
Cdd:PLN00206 410 VMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKS 489
|
410
....*....|
gi 1002095822 463 ANQAInPKLL 472
Cdd:PLN00206 490 SGAAI-PREL 498
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
84-303 |
1.99e-78 |
|
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: 249.11 E-value: 1.99e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 84 VRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQ---- 159
Cdd:cd18052 33 VTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEglta 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 160 PFLERGDGPICLVLAPTRELAQQVQQVAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNL 239
Cdd:cd18052 113 SSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISL 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002095822 240 RRTTYLVLDEADRMLDMGFEPQIRKIVDQI----RPDRQTLMWSATWPKEVRQLAEDFLK-DYIHINIG 303
Cdd:cd18052 193 SKLKYLILDEADRMLDMGFGPEIRKLVSEPgmpsKEDRQTLMFSATFPEEIQRLAAEFLKeDYLFLTVG 261
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
96-444 |
1.66e-74 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 250.15 E-value: 1.66e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 96 FYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINhqPFLErgdGPICLVLAP 175
Cdd:PRK11634 8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLD--PELK---APQILVLAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 176 TRELAQQVQQVAAEYCRACR-LKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRML 254
Cdd:PRK11634 83 TRELAVQVAEAMTDFSKHMRgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEML 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 255 DMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGAlELSANHNILQIVDVCHDVEKDEKLIRLME 334
Cdd:PRK11634 163 RMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQS-SVTTRPDISQSYWTVWGMRKNEALVRFLE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 335 eimSEKENKTIVFVETKRRCDELTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKAPILIATDVASRGLDVEDVKFVI 414
Cdd:PRK11634 242 ---AEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVV 318
|
330 340 350
....*....|....*....|....*....|
gi 1002095822 415 NYDYPNSSEDYIHRIGRTARSTKTGTAYTF 444
Cdd:PRK11634 319 NYDIPMDSESYVHRIGRTGRAGRAGRALLF 348
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
86-303 |
3.36e-74 |
|
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: 237.63 E-value: 3.36e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 86 GHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQ---PFL 162
Cdd:cd18051 13 GENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQgpgESL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 163 ERGDG--------PICLVLAPTRELAQQVQQVAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEC 234
Cdd:cd18051 93 PSESGyygrrkqyPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLER 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002095822 235 GKTNLRRTTYLVLDEADRMLDMGFEPQIRKIVDQI----RPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIG 303
Cdd:cd18051 173 GKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDtmppTGERQTLMFSATFPKEIQMLARDFLDNYIFLAVG 245
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
99-444 |
5.37e-74 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 242.95 E-value: 5.37e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 99 ANFPAN--VMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHI--NHQPFLERGDGPICLVLA 174
Cdd:PRK04837 11 SDFALHpqVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLlsHPAPEDRKVNQPRALIMA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 175 PTRELAQQVQQVAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRML 254
Cdd:PRK04837 91 PTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 255 DMGFEPQIRKIVDQIRP--DRQTLMWSATWPKEVRQLAEDFLKDYIHINIGALELSAnHNILQIVDVCHDVEKDEKLIRL 332
Cdd:PRK04837 171 DLGFIKDIRWLFRRMPPanQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTG-HRIKEELFYPSNEEKMRLLQTL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 333 MEEimsEKENKTIVFVETKRRCDELTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKAPILIATDVASRGLDVEDVKF 412
Cdd:PRK04837 250 IEE---EWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTH 326
|
330 340 350
....*....|....*....|....*....|..
gi 1002095822 413 VINYDYPNSSEDYIHRIGRTARSTKTGTAYTF 444
Cdd:PRK04837 327 VFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
96-444 |
1.93e-73 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 243.28 E-value: 1.93e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 96 FYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLE---RGDgPICLV 172
Cdd:PRK01297 89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKeryMGE-PRALI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 173 LAPTRELAQQVQQVAAEYCRACRLKSTCIYGGAPKGPQIRDLE-RGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEAD 251
Cdd:PRK01297 168 IAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEAD 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 252 RMLDMGFEPQIRKIVDQIRP--DRQTLMWSATWPKEVRQLAEDFLKDYIHINIGAlELSANHNILQIVdvcHDVEKDEKL 329
Cdd:PRK01297 248 RMLDMGFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEP-ENVASDTVEQHV---YAVAGSDKY 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 330 IRLMEEIMSEKENKTIVFVETKRRCDELTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKAPILIATDVASRGLDVED 409
Cdd:PRK01297 324 KLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDG 403
|
330 340 350
....*....|....*....|....*....|....*
gi 1002095822 410 VKFVINYDYPNSSEDYIHRIGRTARSTKTGTAYTF 444
Cdd:PRK01297 404 ISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISF 438
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
91-444 |
2.81e-72 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 242.93 E-value: 2.81e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 91 KPV--LNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFL--ERGD 166
Cdd:PRK04537 4 KPLtdLTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALadRKPE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 167 GPICLVLAPTRELAQQVQQVAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKT-NLRRTTYL 245
Cdd:PRK04537 84 DPRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVvSLHACEIC 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 246 VLDEADRMLDMGFEPQIRKIVDQI--RPDRQTLMWSATWPKEVRQLAedflkdYIHIN-----IGALELSANHNILQIVD 318
Cdd:PRK04537 164 VLDEADRMFDLGFIKDIRFLLRRMpeRGTRQTLLFSATLSHRVLELA------YEHMNepeklVVETETITAARVRQRIY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 319 VCHDVEKdeklIRLMEEIMSEKEN-KTIVFVETKRRCDELTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKAPILIA 397
Cdd:PRK04537 238 FPADEEK----QTLLLGLLSRSEGaRTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVA 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1002095822 398 TDVASRGLDVEDVKFVINYDYPNSSEDYIHRIGRTARSTKTGTAYTF 444
Cdd:PRK04537 314 TDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISF 360
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
93-456 |
6.39e-69 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 228.94 E-value: 6.39e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 93 VLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHqpflergDGPIC-- 170
Cdd:PTZ00424 27 VDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDY-------DLNACqa 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 171 LVLAPTRELAQQVQQVAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEA 250
Cdd:PTZ00424 100 LILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 251 DRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGALELSAnHNILQIVDVchdVEKDE-KL 329
Cdd:PTZ00424 180 DEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTL-EGIRQFYVA---VEKEEwKF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 330 IRLMEEIMSEKENKTIVFVETKRRCDELTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKAPILIATDVASRGLDVED 409
Cdd:PTZ00424 256 DTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQ 335
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1002095822 410 VKFVINYDYPNSSEDYIHRIGRTARSTKTGTAYTFFTPNNIKQVSDL 456
Cdd:PTZ00424 336 VSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEI 382
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
105-300 |
3.82e-67 |
|
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: 218.34 E-value: 3.82e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 105 VMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLE---RGDGPICLVLAPTRELAQ 181
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDeetKDDGPYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 182 QVQQVAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRMLDMGFEPQ 261
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002095822 262 IRKIVDQI-----RPD---------------RQTLMWSATWPKEVRQLAEDFLKDYIHI 300
Cdd:cd17945 161 VTKILDAMpvsnkKPDteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
118-289 |
6.90e-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: 199.78 E-value: 6.90e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 118 TAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINhqpflERGDGPICLVLAPTRELAQQVQQVAAEYCRACRLK 197
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALD-----KLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 198 STCIYGGAPKGPQIRDLeRGVEICIATPGRLIDFLECGKTnLRRTTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLM 277
Cdd:pfam00270 76 VASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILL 153
|
170
....*....|..
gi 1002095822 278 WSATWPKEVRQL 289
Cdd:pfam00270 154 LSATLPRNLEDL 165
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
105-301 |
1.09e-60 |
|
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: 200.64 E-value: 1.09e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 105 VMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQ----PFLeRGDGPICLVLAPTRELA 180
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQekklPFI-KGEGPYGLIVCPSRELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 181 QQVQQVAAEYCRAC------RLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRML 254
Cdd:cd17951 80 RQTHEVIEYYCKALqeggypQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1002095822 255 DMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHIN 301
Cdd:cd17951 160 DMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTVN 206
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
313-445 |
1.50e-59 |
|
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350174 [Multi-domain] Cd Length: 131 Bit Score: 194.65 E-value: 1.50e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 313 ILQIVDVCHDVEKDEKLIRLmeEIMSEKENKTIVFVETKRRCDELTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKA 392
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLL--LLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKV 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1002095822 393 PILIATDVASRGLDVEDVKFVINYDYPNSSEDYIHRIGRTARSTKTGTAYTFF 445
Cdd:cd18787 79 RVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
109-316 |
1.83e-56 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 189.24 E-value: 1.83e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 109 IARQNFTEPTAIQAQGWPVALSGL-DMVGVAQTGSGKTLSYLLPAIVHinhqpfLERGDGPICLVLAPTRELAQQVQQVA 187
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEA------LKRGKGGRVLVLVPTRELAEQWAEEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 188 AEYCRACRLKSTCIYGGAPKGPQIRDLERGV-EICIATPGRLIDFLECGKTNLRRTTYLVLDEADRMLDMGFEPQIRKIV 266
Cdd:smart00487 75 KKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1002095822 267 DQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGAlelSANHNILQI 316
Cdd:smart00487 155 KLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGF---TPLEPIEQF 201
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
113-300 |
7.04e-56 |
|
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: 188.18 E-value: 7.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 113 NFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHI-NHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYC 191
Cdd:cd17949 10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLlSLEPRVDRSDGTLALVLVPTRELALQIYEVLEKLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 192 RACR-LKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGK----TNLRrttYLVLDEADRMLDMGFEPQIRKIV 266
Cdd:cd17949 90 KPFHwIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQsfdvSNLR---WLVLDEADRLLDMGFEKDITKIL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1002095822 267 DQIR-------------PDRQTLMWSATWPKEVRQLAEDFLKDYIHI 300
Cdd:cd17949 167 ELLDdkrskaggekskpSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
103-301 |
3.53e-54 |
|
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: 183.55 E-value: 3.53e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 103 ANVMDVIARQNFTEPTAIQAQGWPVALS-GLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGDGPICLVLAPTRELAQ 181
Cdd:cd17964 3 PSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGVSALIISPTRELAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 182 QVQQVAAEYCRACR-LKSTCIYGGAPKGPQIRDLER-GVEICIATPGRLIDFLE-CG-KTNLRRTTYLVLDEADRMLDMG 257
Cdd:cd17964 83 QIAAEAKKLLQGLRkLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLEnPGvAKAFTDLDYLVLDEADRLLDMG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1002095822 258 FEPQIRKIVDQIRP----DRQTLMWSATWPKEVRQLAEDFL-KDYIHIN 301
Cdd:cd17964 163 FRPDLEQILRHLPEknadPRQTLLFSATVPDEVQQIARLTLkKDYKFID 211
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
107-300 |
1.74e-52 |
|
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: 178.66 E-value: 1.74e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 107 DVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHI--NHQPFLergdgpiCLVLAPTRELAQQVQ 184
Cdd:cd17954 13 EACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALleNPQRFF-------ALVLAPTRELAQQIS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 185 QVAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKT-NLRRTTYLVLDEADRMLDMGFEPQIR 263
Cdd:cd17954 86 EQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKGfSLKSLKFLVMDEADRLLNMDFEPEID 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1002095822 264 KIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHI 300
Cdd:cd17954 166 KILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
105-303 |
1.22e-50 |
|
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: 173.54 E-value: 1.22e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 105 VMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQpflERGDGPICLVLAPTRELAQQVQ 184
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKP---RKKKGLRALILAPTRELASQIY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 185 QVAAEYCRACRLKSTCIYGG-APKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRMLDMGFEPQIR 263
Cdd:cd17957 78 RELLKLSKGTGLRIVLLSKSlEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1002095822 264 KIVDQIR-PDRQTLMWSATWPKEVRQLAEDFLKDYIHINIG 303
Cdd:cd17957 158 EILAACTnPNLQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
109-300 |
1.08e-49 |
|
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: 170.90 E-value: 1.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 109 IARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPflerGDGPIC--LVLAPTRELAQQVQQV 186
Cdd:cd17947 5 LSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRP----KKKAATrvLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 187 AAEYCRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKT-NLRRTTYLVLDEADRMLDMGFEPQIRKI 265
Cdd:cd17947 81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSfDLDSIEILVLDEADRMLEEGFADELKEI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1002095822 266 VDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHI 300
Cdd:cd17947 161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
106-290 |
2.27e-47 |
|
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: 164.84 E-value: 2.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 106 MDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERgDGPICLVLAPTRELAQQVQQ 185
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPR-NGTGVIIISPTRELALQIYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 186 VAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGK----TNLRrttYLVLDEADRMLDMGFEPQ 261
Cdd:cd17942 81 VAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKgflyKNLQ---CLIIDEADRILEIGFEEE 157
|
170 180
....*....|....*....|....*....
gi 1002095822 262 IRKIVDQIRPDRQTLMWSATWPKEVRQLA 290
Cdd:cd17942 158 MRQIIKLLPKRRQTMLFSATQTRKVEDLA 186
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
105-281 |
4.06e-47 |
|
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: 165.49 E-value: 4.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 105 VMDVIARQNFTEPTAIQAQGWPVALS-GLDMVGVAQTGSGKTLSYLLPAIVHI----NHQPFLERGDGPICLVLAPTREL 179
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLlsqkSSNGVGGKQKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 180 AQQVQQVAAEYCRACRLKSTCIYGG--APKgpQIRDLERGVEICIATPGRLIDFLECGKT---NLRRTTYLVLDEADRML 254
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGlaVQK--QERLLKKRPEIVVATPGRLWELIQEGNEhlaNLKSLRFLVLDEADRML 158
|
170 180 190
....*....|....*....|....*....|....*
gi 1002095822 255 DMG-FEpQIRKIVDQI-------RPDRQTLMWSAT 281
Cdd:cd17946 159 EKGhFA-ELEKILELLnkdragkKRKRQTFVFSAT 192
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
117-300 |
6.51e-47 |
|
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: 163.49 E-value: 6.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 117 PTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHInhqpfLERGDGPICLVLAPTRELAQQVQQVAAEYCRAC-R 195
Cdd:cd17962 13 PTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRC-----LTEHRNPSALILTPTRELAVQIEDQAKELMKGLpP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 196 LKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQT 275
Cdd:cd17962 88 MKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILENISHDHQT 167
|
170 180
....*....|....*....|....*
gi 1002095822 276 LMWSATWPKEVRQLAEDFLKDYIHI 300
Cdd:cd17962 168 ILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
95-301 |
5.77e-46 |
|
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: 161.32 E-value: 5.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 95 NFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHI-NHQPFLergdGPICLVL 173
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLkAHSPTV----GARALIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 174 APTRELAQQVQQVAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRM 253
Cdd:cd17959 78 SPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1002095822 254 LDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHIN 301
Cdd:cd17959 158 FEMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
109-302 |
9.37e-45 |
|
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: 157.84 E-value: 9.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 109 IARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFlERGDGPICLVLAPTRELAQQVQQVAA 188
Cdd:cd17941 5 LKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERW-TPEDGLGALIISPTRELAMQIFEVLR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 189 EYCRACRLKSTCIYGGapKGPQIrDLER--GVEICIATPGRLIDFLE----CGKTNLRrttYLVLDEADRMLDMGFEPQI 262
Cdd:cd17941 84 KVGKYHSFSAGLIIGG--KDVKE-EKERinRMNILVCTPGRLLQHMDetpgFDTSNLQ---MLVLDEADRILDMGFKETL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1002095822 263 RKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINI 302
Cdd:cd17941 158 DAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
107-296 |
1.77e-44 |
|
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: 157.39 E-value: 1.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 107 DVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFlergdGPICLVLAPTRELAQQV-QQ 185
Cdd:cd17955 12 KQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPY-----GIFALVLTPTRELAYQIaEQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 186 VAAeYCRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLE---CGKTNLRRTTYLVLDEADRMLDMGFEPQI 262
Cdd:cd17955 87 FRA-LGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEADRLLTGSFEDDL 165
|
170 180 190
....*....|....*....|....*....|....
gi 1002095822 263 RKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKD 296
Cdd:cd17955 166 ATILSALPPKRQTLLFSATLTDALKALKELFGNK 199
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
105-290 |
6.88e-43 |
|
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: 152.73 E-value: 6.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 105 VMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHI-NHQPFLERGDgPICLVLAPTRELAQQV 183
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlKRKANLKKGQ-VGALIISPTRELATQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 184 QQVAAEYCRAC--RLKSTCIYGGAPKGPQIRDLER-GVEICIATPGRLIDFLE--CGKTNLRRTTYLVLDEADRMLDMGF 258
Cdd:cd17960 80 YEVLQSFLEHHlpKLKCQLLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLSrkADKVKVKSLEVLVLDEADRLLDLGF 159
|
170 180 190
....*....|....*....|....*....|..
gi 1002095822 259 EPQIRKIVDQIRPDRQTLMWSATWPKEVRQLA 290
Cdd:cd17960 160 EADLNRILSKLPKQRRTGLFSATQTDAVEELI 191
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
106-301 |
1.44e-39 |
|
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: 143.59 E-value: 1.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 106 MDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPflergDGPICLVLAPTRELAQQVQQ 185
Cdd:cd17940 11 LMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKK-----DVIQALILVPTRELALQTSQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 186 VAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRMLDMGFEPQIRKI 265
Cdd:cd17940 86 VCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQPIIEKI 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 1002095822 266 VDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHIN 301
Cdd:cd17940 166 LNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEIN 201
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
120-301 |
2.04e-38 |
|
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: 140.75 E-value: 2.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 120 IQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAI--VHINHQPfLERGDGPICLVLAPTRELAQQVQQVAAEYCRacRLK 197
Cdd:cd17944 16 IQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIekLQEDQQP-RKRGRAPKVLVLAPTRELANQVTKDFKDITR--KLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 198 STCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRMLDMGFEPQIRKIVD-QIRPDR--- 273
Cdd:cd17944 93 VACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSvSYKKDSedn 172
|
170 180 190
....*....|....*....|....*....|
gi 1002095822 274 -QTLMWSATWPKEVRQLAEDFLKD-YIHIN 301
Cdd:cd17944 173 pQTLLFSATCPDWVYNVAKKYMKSqYEQVD 202
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
109-296 |
8.05e-38 |
|
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: 138.87 E-value: 8.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 109 IARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHI-NHQPFLERGDGPICLVLAPTRELAQQVQQVA 187
Cdd:cd17961 9 IAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlKAKAESGEEQGTRALILVPTRELAQQVSKVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 188 ---AEYCRAcRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRT-TYLVLDEADRMLDMGFEPQIR 263
Cdd:cd17961 89 eqlTAYCRK-DVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLLSTlKYLVIDEADLVLSYGYEEDLK 167
|
170 180 190
....*....|....*....|....*....|...
gi 1002095822 264 KIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKD 296
Cdd:cd17961 168 SLLSYLPKNYQTFLMSATLSEDVEALKKLVLHN 200
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
327-434 |
6.25e-36 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 130.41 E-value: 6.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 327 EKLIRLMEEIMSEKENKTIVFVETKRRCDElTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKAPILIATDVASRGLD 406
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100
....*....|....*....|....*...
gi 1002095822 407 VEDVKFVINYDYPNSSEDYIHRIGRTAR 434
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGR 107
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
105-292 |
4.10e-35 |
|
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: 132.49 E-value: 4.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 105 VMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERG--DGPICLVLAPTRELAQQ 182
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGpfNAPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 183 VQQVAAEYCRACRLKSTCIYGGAPKGpQIRDLERG-VEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRMLDMGFEPQ 261
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITGGRTKR-QIRNPHFEeVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1002095822 262 IRKIV-------------DQIRPDRQTLMWSATWPKEVRQLAED 292
Cdd:cd17948 160 LSHFLrrfplasrrsentDGLDPGTQLVLVSATMPSGVGEVLSK 203
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
114-300 |
2.06e-34 |
|
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: 129.37 E-value: 2.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 114 FTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPflergDGPICLVLAPTRELAQQVQQVAAEYCRA 193
Cdd:cd17939 17 FEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTV-----RETQALVLAPTRELAQQIQKVVKALGDY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 194 CRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRMLDMGFEPQIRKIVDQIRPDR 273
Cdd:cd17939 92 MGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQIYDIFQFLPPET 171
|
170 180
....*....|....*....|....*..
gi 1002095822 274 QTLMWSATWPKEVRQLAEDFLKDYIHI 300
Cdd:cd17939 172 QVVLFSATMPHEVLEVTKKFMRDPVRI 198
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
102-300 |
2.68e-34 |
|
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: 128.85 E-value: 2.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 102 PANVMDVIARQNFTEPTAIQAQGWPVALSGLD--MVGVAQTGSGKTLSYLLPaivhinhqpFLERGDG----PICLVLAP 175
Cdd:cd17963 2 KPELLKGLYAMGFNKPSKIQETALPLILSDPPenLIAQSQSGTGKTAAFVLA---------MLSRVDPtlksPQALCLAP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 176 TRELAQQVQQVAAEYCRACRLKSTCiyggAPKGPQIRDLERGVE-ICIATPGRLIDFLECGKTNLRRTTYLVLDEADRML 254
Cdd:cd17963 73 TRELARQIGEVVEKMGKFTGVKVAL----AVPGNDVPRGKKITAqIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVML 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1002095822 255 DM-GFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHI 300
Cdd:cd17963 149 DTqGHGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
105-300 |
5.47e-34 |
|
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: 127.77 E-value: 5.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 105 VMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINhqpfLERGdGPICLVLAPTRELAQQVQ 184
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLD----LERR-HPQVLILAPTREIAVQIH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 185 QVAAEYCRACRLKSTCIY-GGAPKGPQIRDLeRGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRMLDMGFEPQIR 263
Cdd:cd17943 76 DVFKKIGKKLEGLKCEVFiGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVN 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 1002095822 264 KIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHI 300
Cdd:cd17943 155 WIFSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLV 191
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
114-300 |
2.56e-33 |
|
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: 126.41 E-value: 2.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 114 FTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPflergDGPICLVLAPTRELAQQVQQVAAEYCRA 193
Cdd:cd18046 19 FEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSL-----KATQALVLAPTRELAQQIQKVVMALGDY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 194 CRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRMLDMGFEPQIRKIVDQIRPDR 273
Cdd:cd18046 94 MGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKDQIYDIFQKLPPDT 173
|
170 180
....*....|....*....|....*..
gi 1002095822 274 QTLMWSATWPKEVRQLAEDFLKDYIHI 300
Cdd:cd18046 174 QVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
117-291 |
5.74e-32 |
|
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: 122.81 E-value: 5.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 117 PTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPaIVHInhqpflergdgPICLVLAPTRELAQQVQQVA---AEYCRA 193
Cdd:cd17938 22 PTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLP-VLQI-----------VVALILEPSRELAEQTYNCIenfKKYLDN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 194 CRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRMLDMGFEPQIRKIVDQI---- 269
Cdd:cd17938 90 PKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQGNLETINRIYNRIpkit 169
|
170 180
....*....|....*....|....*
gi 1002095822 270 -RPDR-QTLMWSATWPK-EVRQLAE 291
Cdd:cd17938 170 sDGKRlQVIVCSATLHSfEVKKLAD 194
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
114-296 |
6.41e-29 |
|
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: 114.36 E-value: 6.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 114 FTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPflergdGPI-CLVLAPTRELAQQVQQvaaEYCR 192
Cdd:cd17950 22 FEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVD------GQVsVLVICHTRELAFQISN---EYER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 193 ACR----LKSTCIYGGAPKGPQIRDLERGV-EICIATPGRLIDFLECGKTNLRRTTYLVLDEADRML-DMGFEPQIRKIV 266
Cdd:cd17950 93 FSKympnVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLeQLDMRRDVQEIF 172
|
170 180 190
....*....|....*....|....*....|
gi 1002095822 267 DQIRPDRQTLMWSATWPKEVRQLAEDFLKD 296
Cdd:cd17950 173 RATPHDKQVMMFSATLSKEIRPVCKKFMQD 202
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
355-434 |
7.57e-28 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 106.91 E-value: 7.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 355 DELTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYIHRIGRTAR 434
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
113-300 |
3.15e-27 |
|
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: 109.09 E-value: 3.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 113 NFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIvhinhQPFLERGDGPICLVLAPTRELAQQVQQVA---AE 189
Cdd:cd18045 18 GFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVL-----QCLDIQVRETQALILSPTRELAVQIQKVLlalGD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 190 Y----CRACrlkstciYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRMLDMGFEPQIRKI 265
Cdd:cd18045 93 YmnvqCHAC-------IGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKEQIYDV 165
|
170 180 190
....*....|....*....|....*....|....*
gi 1002095822 266 VDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHI 300
Cdd:cd18045 166 YRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
105-259 |
1.77e-25 |
|
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: 105.02 E-value: 1.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 105 VMDVIARQNFTEPTAIQAQGWPVALSGL---------DMVGVAQTGSGKTLSYLLPaIVhinhQPFLERGDGPI-CLVLA 174
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSSkstppyrpgDLCVSAPTGSGKTLAYVLP-IV----QALSKRVVPRLrALIVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 175 PTRELAQQVQQVAAEYCRACRLKsTCIYGG----APKGPQIRDLERG-----VEICIATPGRLIDFLECGKT----NLRr 241
Cdd:cd17956 76 PTKELVQQVYKVFESLCKGTGLK-VVSLSGqksfKKEQKLLLVDTSGrylsrVDILVATPGRLVDHLNSTPGftlkHLR- 153
|
170
....*....|....*...
gi 1002095822 242 ttYLVLDEADRMLDMGFE 259
Cdd:cd17956 154 --FLVIDEADRLLNQSFQ 169
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
138-300 |
9.67e-22 |
|
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: 94.75 E-value: 9.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 138 AQTGSGKTLSYLLPAIVHINHQ---PFLERGDG---------PICLVLAPTRELAQQVQQVAAeycracRLKSTCIYGGA 205
Cdd:cd17965 68 AETGSGKTLAYLAPLLDYLKRQeqePFEEAEEEyesakdtgrPRSVILVPTHELVEQVYSVLK------KLSHTVKLGIK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 206 P----KGPQIRDLER----GVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLM 277
Cdd:cd17965 142 TfssgFGPSYQRLQLafkgRIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLIL 221
|
170 180
....*....|....*....|...
gi 1002095822 278 WSATWPKEVRQLAEDFLKDYIHI 300
Cdd:cd17965 222 CSATIPKEFDKTLRKLFPDVVRI 244
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
137-461 |
1.73e-20 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 95.48 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 137 VAQTGSGKTlsYLLPAIVHinhqpflERGDGPICLVLAPTRELaqqVQQVAAEYCRacrlkstcIYGGAPKGPQIRDLER 216
Cdd:COG1061 106 VAPTGTGKT--VLALALAA-------ELLRGKRVLVLVPRREL---LEQWAEELRR--------FLGDPLAGGGKKDSDA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 217 GVEIC-IATPGRLIDFLECGktnlRRTTYLVLDEADRmldmGFEPQIRKIVDQIRPDRQTLMwSAT-------WPKEVR- 287
Cdd:COG1061 166 PITVAtYQSLARRAHLDELG----DRFGLVIIDEAHH----AGAPSYRRILEAFPAAYRLGL-TATpfrsdgrEILLFLf 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 288 -----------QLAEDFLKDYIHINI------GALELSANHNILQIVDVCHDVEKDEKLIRLMEEIMSEKenKTIVFVET 350
Cdd:COG1061 237 dgivyeyslkeAIEDGYLAPPEYYGIrvdltdERAEYDALSERLREALAADAERKDKILRELLREHPDDR--KTLVFCSS 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 351 KRRCDELTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKAPILIATDVASRGLDVEDVKFVInYDYPNSSE-DYIHRI 429
Cdd:COG1061 315 VDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI-LLRPTGSPrEFIQRL 393
|
330 340 350
....*....|....*....|....*....|....
gi 1002095822 430 GRTARSTKTGTAYTFFT--PNNIKQVSDLISVLR 461
Cdd:COG1061 394 GRGLRPAPGKEDALVYDfvGNDVPVLEELAKDLR 427
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
93-308 |
9.76e-17 |
|
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: 79.68 E-value: 9.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 93 VLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSG--LDMVGVAQTGSGKTLSYLLPAIVHINHQPFLergdgPIC 170
Cdd:cd18048 17 VKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLY-----PQC 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 171 LVLAPTRELAQQVQQVAAEYCRACrLKSTCIYG----GAPKGPQIRdlergVEICIATPGRLIDFleCGK---TNLRRTT 243
Cdd:cd18048 92 LCLSPTFELALQTGKVVEEMGKFC-VGIQVIYAirgnRPGKGTDIE-----AQIVIGTPGTVLDW--CFKlrlIDVTNIS 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002095822 244 YLVLDEADRMLDM-GFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGALELS 308
Cdd:cd18048 164 VFVLDEADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
306-437 |
3.55e-15 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 79.00 E-value: 3.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 306 ELSANHNILQIVDVC--HDVE--KDEKLIRLMEEIMSEK-ENKTIVFVETKRRCDELTRKMRRDGWPAM------GIHGD 374
Cdd:COG1111 313 RLVSDPRFRKAMRLAeeADIEhpKLSKLREILKEQLGTNpDSRIIVFTQYRDTAEMIVEFLSEPGIKAGrfvgqaSKEGD 392
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002095822 375 K--SQQERDWVLNEFKHGKAPILIATDVASRGLDVEDVKFVINYDyPNSSE-DYIHRIGRTARSTK 437
Cdd:COG1111 393 KglTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYE-PVPSEiRSIQRKGRTGRKRE 457
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
119-458 |
6.92e-15 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 77.49 E-value: 6.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 119 AIQAqgwpvALSGLDMVGVAQTGSGKTLSYLLPAIVhinhqpflerGDGPiCLVLAPTreLAQQVQQVAAeyCRACRLKS 198
Cdd:COG0514 25 IIEA-----VLAGRDALVVMPTGGGKSLCYQLPALL----------LPGL-TLVVSPL--IALMKDQVDA--LRAAGIRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 199 TCIYGGAPKGPQ---IRDLERG-VEICIATPGRL-----IDFLECGKTNLrrttyLVLDEA--------DrmldmgFEP- 260
Cdd:COG0514 85 AFLNSSLSAEERrevLRALRAGeLKLLYVAPERLlnprfLELLRRLKISL-----FAIDEAhcisqwghD------FRPd 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 261 --QIRKIVDQIrPDRQTLMWSATWPKEVR-----QLAedfLKDyihinigALELSAN---HNI-LQIVDVCHDvEKDEKL 329
Cdd:COG0514 154 yrRLGELRERL-PNVPVLALTATATPRVRadiaeQLG---LED-------PRVFVGSfdrPNLrLEVVPKPPD-DKLAQL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 330 IRLMEEImseKENKTIVFVETKRRCDELTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKAPILIATdVA-SRGLDVE 408
Cdd:COG0514 222 LDFLKEH---PGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKP 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1002095822 409 DVKFVINYDYPNSSEDYIHRIGRTARSTKTGTAYTFFTPNNIKQVSDLIS 458
Cdd:COG0514 298 DVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIE 347
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
96-296 |
1.95e-13 |
|
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: 69.36 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 96 FYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSG--LDMVGVAQTGSGKTLSYLLPAIVHINhqPFLERGDgpiCLVL 173
Cdd:cd18047 3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVE--PANKYPQ---CLCL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 174 APTRELAQQVQQVAAEycrACRLKSTCIYGGAPKGPQirdLERGV----EICIATPGRLIDFleCGKTNL---RRTTYLV 246
Cdd:cd18047 78 SPTYELALQTGKVIEQ---MGKFYPELKLAYAVRGNK---LERGQkiseQIVIGTPGTVLDW--CSKLKFidpKKIKVFV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1002095822 247 LDEADRML-DMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKD 296
Cdd:cd18047 150 LDEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPD 200
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
137-281 |
7.26e-13 |
|
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: 66.27 E-value: 7.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 137 VAQTGSGKTLSYLLPAIvhinhQPFLERGDGpiCLVLAPTRELAqqvQQVAAEYCRACRLKSTC--IYGGAPKGPQIRDL 214
Cdd:cd00046 7 TAPTGSGKTLAALLAAL-----LLLLKKGKK--VLVLVPTKALA---LQTAERLRELFGPGIRVavLVGGSSAEEREKNK 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 215 ERGVEICIATPGRLI-DFLECGKTNLRRTTYLVLDEADRMLDMGFEPQIRKIVDQ--IRPDRQTLMWSAT 281
Cdd:cd00046 77 LGDADIIIATPDMLLnLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRkaGLKNAQVILLSAT 146
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
327-432 |
1.81e-12 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 70.25 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 327 EKLIRLMEEIMSEKEnKTIVFVETKRRCDELTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKAP--ILIATDVASRG 404
Cdd:COG0553 536 EALLELLEELLAEGE-KVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEApvFLISLKAGGEG 614
|
90 100 110
....*....|....*....|....*....|....
gi 1002095822 405 LDVEDVKFVINYDYP------NSSEDYIHRIGRT 432
Cdd:COG0553 615 LNLTAADHVIHYDLWwnpaveEQAIDRAHRIGQT 648
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
128-450 |
1.90e-12 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 70.13 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 128 ALSGLDMVGVAQTGSGKTLSYLLPAIVHinhqpflergDGpICLVLAPTRELAQ-QVQQVAAEYCRACRLKST------- 199
Cdd:PRK11057 37 VLSGRDCLVVMPTGGGKSLCYQIPALVL----------DG-LTLVVSPLISLMKdQVDQLLANGVAAACLNSTqtreqql 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 200 CIYGGAPKGpQIRDLergveicIATPGRLI--DFLE-CGKTNLrrtTYLVLDEADRMLDMG--FEPQIRKIvDQIR---P 271
Cdd:PRK11057 106 EVMAGCRTG-QIKLL-------YIAPERLMmdNFLEhLAHWNP---ALLAVDEAHCISQWGhdFRPEYAAL-GQLRqrfP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 272 DRQTLMWSATWPKEVRQlaeDFLK----DYIHINIGALElsaNHNILQIVdvchdVEKDEKLIRLMEEIMSEKENKTIVF 347
Cdd:PRK11057 174 TLPFMALTATADDTTRQ---DIVRllglNDPLIQISSFD---RPNIRYTL-----VEKFKPLDQLMRYVQEQRGKSGIIY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 348 VETKRRCDELTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYIH 427
Cdd:PRK11057 243 CNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQ 322
|
330 340
....*....|....*....|...
gi 1002095822 428 RIGRTARSTKTGTAYTFFTPNNI 450
Cdd:PRK11057 323 ETGRAGRDGLPAEAMLFYDPADM 345
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
325-445 |
2.13e-12 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350181 [Multi-domain] Cd Length: 134 Bit Score: 64.54 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 325 KDEKLIRLMEEIMSEKENKTIVFVETKRRCDELTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKAPILIATDVASRG 404
Cdd:cd18794 14 KDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMG 93
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1002095822 405 LDVEDVKFVINYDYPNSSEDYIHRIGRTARSTKTGTAYTFF 445
Cdd:cd18794 94 IDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
325-446 |
2.40e-11 |
|
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: 61.84 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 325 KDEKLIRLMEEIMSEKEN----KTIVFVETKRRCDELTRKMR-----RDGWPA---MGiHGDKSQQERDW--------VL 384
Cdd:cd18802 5 VIPKLQKLIEILREYFPKtpdfRGIIFVERRATAVVLSRLLKehpstLAFIRCgflIG-RGNSSQRKRSLmtqrkqkeTL 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002095822 385 NEFKHGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYIHRIGRtARstKTGTAYTFFT 446
Cdd:cd18802 84 DKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-AR--APNSKYILMV 142
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
328-430 |
1.32e-10 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 59.41 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 328 KLIRLMEEIMSEKEN--KTIVFVETKRRCDELTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKAP--ILIATDVASR 403
Cdd:cd18793 12 KLEALLELLEELREPgeKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGV 91
|
90 100 110
....*....|....*....|....*....|...
gi 1002095822 404 GLDVEDVKFVINYDYP-NSS-----EDYIHRIG 430
Cdd:cd18793 92 GLNLTAANRVILYDPWwNPAveeqaIDRAHRIG 124
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
343-446 |
2.57e-10 |
|
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: 56.94 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 343 KTIVFVETKRRCDELTRKMRrdgwpamgihgdksqqerdwvlnefkhgkapILIATDVASRGLDVEDVKFVINYDYPNSS 422
Cdd:cd18785 5 KIIVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDPPSSA 53
|
90 100
....*....|....*....|....
gi 1002095822 423 EDYIHRIGRTARSTKTGTAYTFFT 446
Cdd:cd18785 54 ASYIQRVGRAGRGGKDEGEVILFV 77
|
|
| P68HR |
pfam08061 |
P68HR (NUC004) repeat; This short region is found in two copies in p68-like RNA helicases. |
498-532 |
2.83e-10 |
|
P68HR (NUC004) repeat; This short region is found in two copies in p68-like RNA helicases.
Pssm-ID: 429808 Cd Length: 35 Bit Score: 55.49 E-value: 2.83e-10
10 20 30
....*....|....*....|....*....|....*
gi 1002095822 498 SAGKRGGFNTFRDRENYDRGYSSLLKRDFGAKTQN 532
Cdd:pfam08061 1 AAGKQAGFRAFNEAEAFENGYDALGKQDFGAKAAN 35
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
318-437 |
2.76e-09 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 60.27 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 318 DVCHdvEKDEKLIRLMEEIMSEKEN-KTIVFVETKRRCDELTRKMRRDGWPA---MG---IHGDK--SQQERDWVLNEFK 388
Cdd:PRK13766 343 DIEH--PKLEKLREIVKEQLGKNPDsRIIVFTQYRDTAEKIVDLLEKEGIKAvrfVGqasKDGDKgmSQKEQIEILDKFR 420
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1002095822 389 HGKAPILIATDVASRGLDVEDVKFVINYDyPNSSE-DYIHRIGRTARSTK 437
Cdd:PRK13766 421 AGEFNVLVSTSVAEEGLDIPSVDLVIFYE-PVPSEiRSIQRKGRTGRQEE 469
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
329-437 |
5.29e-09 |
|
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: 55.35 E-value: 5.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 329 LIRLMEEImsEKENKTIVFVETKRRCDELTRKMRR----DGWP--AMGIHGDKSQQERDWVLNEFKHGKAPILIATDVAS 402
Cdd:cd18796 28 YAEVIFLL--ERHKSTLVFTNTRSQAERLAQRLRElcpdRVPPdfIALHHGSLSRELREEVEAALKRGDLKVVVATSSLE 105
|
90 100 110
....*....|....*....|....*....|....*
gi 1002095822 403 RGLDVEDVKFVINYDYPNSSEDYIHRIGRTARSTK 437
Cdd:cd18796 106 LGIDIGDVDLVIQIGSPKSVARLLQRLGRSGHRPG 140
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
98-250 |
4.49e-08 |
|
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: 56.38 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 98 EANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHInhqpflERGDGPICLVLAPTR 177
Cdd:COG1205 38 PDWLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEAL------LEDPGATALYLYPTK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 178 ELAQ-QVQQVaAEYCRACRLK-STCIY-GGAPkgPQIRD--LERGvEICIATP-----------GRLIDFLEcgktNLRr 241
Cdd:COG1205 112 ALARdQLRRL-RELAEALGLGvRVATYdGDTP--PEERRwiREHP-DIVLTNPdmlhygllphhTRWARFFR----NLR- 182
|
....*....
gi 1002095822 242 ttYLVLDEA 250
Cdd:COG1205 183 --YVVIDEA 189
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
339-445 |
9.80e-08 |
|
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: 51.48 E-value: 9.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 339 EKENKTIVFVETKrrcDELTRKMRRDGWPAmgIHGDKSQQERDWVLNEFKHGKAPILIATDVASRGLDVED--VKFVINY 416
Cdd:cd18789 47 EQGDKIIVFTDNV---EALYRYAKRLLKPF--ITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPEanVAIQISG 121
|
90 100
....*....|....*....|....*....
gi 1002095822 417 DYpNSSEDYIHRIGRTARStKTGTAYTFF 445
Cdd:cd18789 122 HG-GSRRQEAQRLGRILRP-KKGGGKNAF 148
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
121-250 |
1.07e-07 |
|
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: 52.20 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 121 QAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPflergdGPICLVLAPTRELAQQVQQVAAEYCRACRLKSTC 200
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDP------GSRALYLYPTKALAQDQLRSLRELLEQLGLGIRV 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002095822 201 -IYGG-APKGPQIRDLERGVEICIATP-----------GRLIDFLEcgktNLRrttYLVLDEA 250
Cdd:cd17923 79 aTYDGdTPREERRAIIRNPPRILLTNPdmlhyallphhDRWARFLR----NLR---YVVLDEA 134
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
245-434 |
1.15e-07 |
|
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
Pssm-ID: 187770 [Multi-domain] Cd Length: 353 Bit Score: 53.97 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 245 LVLDEADRMLD--MGFepqIRKIVDQIRPDRQTLM-WSATWPKEVRQLAEDFLKDYIHInigALELSANHNILQIVDVCH 321
Cdd:cd09639 127 LIFDEVHFYDEytLAL---ILAVLEVLKDNDVPILlMSATLPKFLKEYAEKIGYVEENE---PLDLKPNERAPFIKIESD 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 322 DVEKDEKLIRLMEEIMSEKenKTIVFVETKRRCDELTRKMRRDG--WPAMGIHG-----DKSQQERDwVLNEFKHGKAPI 394
Cdd:cd09639 201 KVGEISSLERLLEFIKKGG--SVAIIVNTVDRAQEFYQQLKEKGpeEEIMLIHSrftekDRAKKEAE-LLLEFKKSEKFV 277
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1002095822 395 LIATDVASRGLDVeDVKFVINYDYPNSSedYIHRIGRTAR 434
Cdd:cd09639 278 IVATQVIEASLDI-SVDVMITELAPIDS--LIQRLGRLHR 314
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
111-185 |
1.22e-07 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 54.72 E-value: 1.22e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002095822 111 RQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVH-INHQPFLERGDGPICLVLAPTRELAQQVQQ 185
Cdd:COG1201 19 AARFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTLAAFLPALDElARRPRPGELPDGLRVLYISPLKALANDIER 94
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
325-434 |
1.41e-07 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350188 [Multi-domain] Cd Length: 143 Bit Score: 50.82 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 325 KDEKLIRLMEEI-MSEKENKT---IVFVETKRRCDELTRKMRRDGW---PAMGI-HGDK------SQQERDWVLNEFKHG 390
Cdd:cd18801 10 KLEKLEEIVKEHfKKKQEGSDtrvIIFSEFRDSAEEIVNFLSKIRPgirATRFIgQASGksskgmSQKEQKEVIEQFRKG 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1002095822 391 KAPILIATDVASRGLDVEDVKFVINYDyPNSSE-DYIHRIGRTAR 434
Cdd:cd18801 90 GYNVLVATSIGEEGLDIGEVDLIICYD-ASPSPiRMIQRMGRTGR 133
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
332-434 |
1.63e-06 |
|
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350177 [Multi-domain] Cd Length: 171 Bit Score: 48.40 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 332 LMEEIMSEKENKTIVFVE--TKRRCDELTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKAPILIATDVASRGLDVED 409
Cdd:cd18790 16 LLGEIRKRVARGERVLVTtlTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPE 95
|
90 100 110
....*....|....*....|....*....|
gi 1002095822 410 VKFVINYD-----YPNSSEDYIHRIGRTAR 434
Cdd:cd18790 96 VSLVAILDadkegFLRSETSLIQTIGRAAR 125
|
|
| P68HR |
pfam08061 |
P68HR (NUC004) repeat; This short region is found in two copies in p68-like RNA helicases. |
551-583 |
1.96e-06 |
|
P68HR (NUC004) repeat; This short region is found in two copies in p68-like RNA helicases.
Pssm-ID: 429808 Cd Length: 35 Bit Score: 44.71 E-value: 1.96e-06
10 20 30
....*....|....*....|....*....|....*
gi 1002095822 551 SAGIQTSFRTGNPTGTYQNGYDS--TQQYGSNVPN 583
Cdd:pfam08061 1 AAGKQAGFRAFNEAEAFENGYDAlgKQDFGAKAAN 35
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
129-458 |
6.13e-06 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 49.51 E-value: 6.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 129 LSGLDMVGVAQTGSGKTLSYLLPAIVHinhqpflergdGPICLVLAPTRELAQQ-------------------------- 182
Cdd:PLN03137 473 MSGYDVFVLMPTGGGKSLTYQLPALIC-----------PGITLVISPLVSLIQDqimnllqanipaaslsagmewaeqle 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 183 -VQQVAAEYCracrlKSTCIYGGAPKGPQIRDLERGVEICIAtpgrlidflecgKTNLRRttyLVLDEADRMLDMG--FE 259
Cdd:PLN03137 542 iLQELSSEYS-----KYKLLYVTPEKVAKSDSLLRHLENLNS------------RGLLAR---FVIDEAHCVSQWGhdFR 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 260 PQIRK--IVDQIRPDRQTLMWSATWPKEVRqlaEDFLKDYIHINIGALELSANH-NILQIVdvchdVEKDEKLIRLMEEI 336
Cdd:PLN03137 602 PDYQGlgILKQKFPNIPVLALTATATASVK---EDVVQALGLVNCVVFRQSFNRpNLWYSV-----VPKTKKCLEDIDKF 673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 337 MseKENK----TIVFVETKRRCDELTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKAPILIATDVASRGLDVEDVKF 412
Cdd:PLN03137 674 I--KENHfdecGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRF 751
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1002095822 413 VINYDYPNSSEDYIHRIGRTARSTKTGTAYTFFTPNNIKQVSDLIS 458
Cdd:PLN03137 752 VIHHSLPKSIEGYHQECGRAGRDGQRSSCVLYYSYSDYIRVKHMIS 797
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
138-414 |
1.11e-05 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 48.15 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 138 AQTGSGKTLSYLLPAIVHINHQpfleRGDGpICLVLaPTRELAQQVQQVAAEycracrlkstcIYGGA----------PK 207
Cdd:COG1203 154 APTGGGKTEAALLFALRLAAKH----GGRR-IIYAL-PFTSIINQTYDRLRD-----------LFGEDvllhhsladlDL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 208 GPQIRDLERGVE------------ICIATPGRLIDFLECGKT-NLRR-----TTYLVLDEADrMLDMGFEPQIRKIVDQI 269
Cdd:COG1203 217 LEEEEEYESEARwlkllkelwdapVVVTTIDQLFESLFSNRKgQERRlhnlaNSVIILDEVQ-AYPPYMLALLLRLLEWL 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 270 RPDRQT--LMwSATWPKEVRQLAEDFLkDYIHINIGALELSANHNILQIVDVCHDVEKDEKLIRLMEEIMsEKENKTIVF 347
Cdd:COG1203 296 KNLGGSviLM-TATLPPLLREELLEAY-ELIPDEPEELPEYFRAFVRKRVELKEGPLSDEELAELILEAL-HKGKSVLVI 372
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002095822 348 VETKRRCDELTRKMRRDGW--PAMGIHG-----DKSQQERDwVLNEFKHGKAPILIATDVASRGLDVeDVKFVI 414
Cdd:COG1203 373 VNTVKDAQELYEALKEKLPdeEVYLLHSrfcpaDRSEIEKE-IKERLERGKPCILVSTQVVEAGVDI-DFDVVI 444
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
119-288 |
3.10e-05 |
|
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.
Pssm-ID: 350776 [Multi-domain] Cd Length: 201 Bit Score: 45.32 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 119 AIQAqgwpvALSGLDMVGVAQTGSGKTLSYLLPAIvhinhqpFLERGDGPICLVLAPTRELAQ-QVQQVAAeycracRLK 197
Cdd:cd18018 20 AIAR-----LLSGRSTLVVLPTGAGKSLCYQLPAL-------LLRRRGPGLTLVVSPLIALMKdQVDALPR------AIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 198 STCIYGGAPKGPQIRDLER----GVEICIATPGRLI--DFLECGKTnLRRTTYLVLDEADRMLDMG--FEP---QIRKIV 266
Cdd:cd18018 82 AAALNSSLTREERRRILEKlragEVKILYVSPERLVneSFRELLRQ-TPPISLLVVDEAHCISEWShnFRPdylRLCRVL 160
|
170 180
....*....|....*....|..
gi 1002095822 267 DQIRPDRQTLMWSATWPKEVRQ 288
Cdd:cd18018 161 RELLGAPPVLALTATATKRVVE 182
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
119-288 |
1.03e-04 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 43.68 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 119 AIQAqgwpvALSGLDMVGVAQTGSGKTLSYLLPAIVhinhqpflergDGPICLVLAPTRELAQ-QVQQvaaeyCRACRLK 197
Cdd:cd17920 20 AINA-----VLAGRDVLVVMPTGGGKSLCYQLPALL-----------LDGVTLVVSPLISLMQdQVDR-----LQQLGIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 198 STCIYGGAPKGPQIRDLER----GVEICIATPGRL-----IDFLEcGKTNLRRTTYLVLDEADRMLDMG--FEPQIRKIV 266
Cdd:cd17920 79 AAALNSTLSPEEKREVLLRikngQYKLLYVTPERLlspdfLELLQ-RLPERKRLALIVVDEAHCVSQWGhdFRPDYLRLG 157
|
170 180
....*....|....*....|....
gi 1002095822 267 DQIR--PDRQTLMWSATWPKEVRQ 288
Cdd:cd17920 158 RLRRalPGVPILALTATATPEVRE 181
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
127-252 |
1.71e-04 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 42.89 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 127 VALSGLDMVgVAQTGSGKTLSYLLPAIVHinhqpfLERGDGPIcLVLAPTRELaqqVQQVAAEYCRACRLKSTCIYGGAP 206
Cdd:cd18035 13 VALNGNTLI-VLPTGLGKTIIAILVAADR------LTKKGGKV-LILAPSRPL---VEQHAENLKRVLNIPDKITSLTGE 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1002095822 207 KGPQIR-DLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADR 252
Cdd:cd18035 82 VKPEERaERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
343-437 |
4.46e-04 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 41.09 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 343 KTIVFVETKRRCdELTRKMRRDGWPAMGIHGDK--------SQQERDWVLNEFKHGKAPILIATDVASRGLDVEDVKFVI 414
Cdd:cd18797 37 KTIVFCRSRKLA-ELLLRYLKARLVEEGPLASKvasyragyLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVV 115
|
90 100
....*....|....*....|...
gi 1002095822 415 NYDYPNSSEDYIHRIGRTARSTK 437
Cdd:cd18797 116 LAGYPGSLASLWQQAGRAGRRGK 138
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
343-414 |
1.18e-03 |
|
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: 39.08 E-value: 1.18e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002095822 343 KTIVFVETKRRCDELTRKMRRDGWPAMGIHGDKSQQER-DWVLNEFKHG--KAPILIATDVASRGLDVEDVKFVI 414
Cdd:cd18799 8 KTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERgDEALILLFFGelKPPILVTVDLLTTGVDIPEVDNVV 82
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
140-250 |
2.42e-03 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 39.56 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 140 TGSGKTL-SYLLpaIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYcraCRLKSTCIYGGAPKGPQIRD----L 214
Cdd:cd18034 25 TGSGKTLiAVML--IKEMGELNRKEKNPKKRAVFLVPTVPLVAQQAEAIRSH---TDLKVGEYSGEMGVDKWTKErwkeE 99
|
90 100 110
....*....|....*....|....*....|....*.
gi 1002095822 215 ERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEA 250
Cdd:cd18034 100 LEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
128-249 |
2.46e-03 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350794 [Multi-domain] Cd Length: 204 Bit Score: 39.77 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 128 ALSGLDMVGVAQTGSGKTLSYLLPAIVHInhQPFLERGDGPICLVLAPTRELAQQVQQVAAEYCRACrLKSTCIYGGAPK 207
Cdd:cd18036 14 ALRGKNTIICAPTGSGKTRVAVYICRHHL--EKRRSAGEKGRVVVLVNKVPLVEQQLEKFFKYFRKG-YKVTGLSGDSSH 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1002095822 208 GPQIRDLERGVEICIATPGRLIDFLECGKTNLRRT----TYLVLDE 249
Cdd:cd18036 91 KVSFGQIVKASDVIICTPQILINNLLSGREEERVYlsdfSLLIFDE 136
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
371-461 |
3.66e-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: 38.48 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002095822 371 IHGDKSQQERDWVLNEFKHGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYIHRI-GRTARSTKTGTAYtFFTPNN 449
Cdd:cd18810 57 AHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIERADKFGLAQLYQLrGRVGRSKERAYAY-FLYPDQ 135
|
90
....*....|..
gi 1002095822 450 IKQVSDLISVLR 461
Cdd:cd18810 136 KKLTEDALKRLE 147
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
120-183 |
4.15e-03 |
|
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: 38.78 E-value: 4.15e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002095822 120 IQAQGW-PVALSGLDMVGVAQTGSGKTLSYLLpAIVHinhqpfLERGDGPICLVLAPTRELAQQV 183
Cdd:cd17921 5 IQREALrALYLSGDSVLVSAPTSSGKTLIAEL-AILR------ALATSGGKAVYIAPTRALVNQK 62
|
|
| |
