|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
123-538 |
5.49e-120 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 361.77 E-value: 5.49e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 123 DFKMLPRLQQNLLSRNFDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGLRAHKTTGLRALVLAPTRELAQ 202
Cdd:COG0513 6 DLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAPQALILAPTRELAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 203 QIYRECAELTRETGLRTH-FISKVSEAKQKhgAECKQRYDILVSTPNRVRFLLQQEppLLDLSHVEWFVLDEADRLMEEG 281
Cdd:COG0513 86 QVAEELRKLAKYLGLRVAtVYGGVSIGRQI--RALKRGVDIVVATPGRLLDLIERG--ALDLSGVETLVLDEADRMLDMG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 282 qnnFKEQLDDIYAACSnPTKCVAFFSATYTVPVAKWALRHLKNLVRITIGVQNSATETVQQELLFVgSEGGKLVAIRDLV 361
Cdd:COG0513 162 ---FIEDIERILKLLP-KERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLV-DKRDKLELLRRLL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 362 RQGLQPPVLVFVQSKERAKQLFEELLYDGINVDVIHAERSQHQRDNCVKAFREGSIWVLICTELMGRGIDFKGVNLVINY 441
Cdd:COG0513 237 RDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 442 DFPPTTISYIHRIGRTGRAGRPGRAITFFTQEDTSNLRGIALIIKNsggTVPEYML----QMKKVRKSEAKMRAKKPLDR 517
Cdd:COG0513 317 DLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQ---KIEEEELpgfePVEEKRLERLKPKIKEKLKG 393
|
410 420
....*....|....*....|.
gi 24666101 518 EDISTKIRPETKGDEKHKSTK 538
Cdd:COG0513 394 KKAGRGGRPGPKGERKARRGK 414
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
130-331 |
4.73e-106 |
|
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: 317.61 E-value: 4.73e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 130 LQQNLLSRNFDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGLRAHKTT-GLRALVLAPTRELAQQIYREC 208
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKkGLRALILAPTRELASQIYREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 209 AELTRETGLRTHFISKVSEAKQKHGAECKQRYDILVSTPNRVRFLLQQEPplLDLSHVEWFVLDEADRLMEegqNNFKEQ 288
Cdd:cd17957 81 LKLSKGTGLRIVLLSKSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGP--IDLSSVEYLVLDEADKLFE---PGFREQ 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 24666101 289 LDDIYAACSNPTKCVAFFSATYTVPVAKWALRHLKNLVRITIG 331
Cdd:cd17957 156 TDEILAACTNPNLQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
90-513 |
9.70e-70 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 234.30 E-value: 9.70e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 90 AAEEANETRKQYGIRVLGKNVPPPVDSFGtltrDFKMLPRLQQNLLSRNFDHPTPIQMQALPVLLQRRALMACAPTGSGK 169
Cdd:PLN00206 96 SSSQAELLRRKLEIHVKGEAVPPPILSFS----SCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 170 TLAFLTPIIN---GLRAHKTTGLR---ALVLAPTRELAQQIYRECAELTRETGLRTHF-ISKVSEAKQKHgaECKQRYDI 242
Cdd:PLN00206 172 TASFLVPIISrccTIRSGHPSEQRnplAMVLTPTRELCVQVEDQAKVLGKGLPFKTALvVGGDAMPQQLY--RIQQGVEL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 243 LVSTPNRVRFLLQQEPplLDLSHVEWFVLDEADRLMEEGqnnFKEQLDDIYAACSNPTkcVAFFSATYTVPVAKWALRHL 322
Cdd:PLN00206 250 IVGTPGRLIDLLSKHD--IELDNVSVLVLDEVDCMLERG---FRDQVMQIFQALSQPQ--VLLFSATVSPEVEKFASSLA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 323 KNLVRITIGVQNSATETVQQELLFVGSEGGKlVAIRDLV--RQGLQPPVLVFVQSKERAKQLFEEL-LYDGINVDVIHAE 399
Cdd:PLN00206 323 KDIILISIGNPNRPNKAVKQLAIWVETKQKK-QKLFDILksKQHFKPPAVVFVSSRLGADLLANAItVVTGLKALSIHGE 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 400 RSQHQRDNCVKAFREGSIWVLICTELMGRGIDFKGVNLVINYDFPPTTISYIHRIGRTGRAGRPGRAITFFTQEDTSNLR 479
Cdd:PLN00206 402 KSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFP 481
|
410 420 430
....*....|....*....|....*....|....
gi 24666101 480 GIALIIKNSGGTVPEYMLQMKKVRKSEAKMRAKK 513
Cdd:PLN00206 482 ELVALLKSSGAAIPRELANSRYLGSGRKRKKKRR 515
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
90-510 |
6.22e-64 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 219.26 E-value: 6.22e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 90 AAEEANETRKQYGIRVL-GKNVPPPVDSFGTLTRDFKMLPRLQQNllsrNFDHPTPIQMQALPVLLQRRALMACAPTGSG 168
Cdd:PTZ00110 104 SSKEVDEIRKEKEITIIaGENVPKPVVSFEYTSFPDYILKSLKNA----GFTEPTPIQVQGWPIALSGRDMIGIAETGSG 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 169 KTLAFLTPIINGLRAH----KTTGLRALVLAPTRELAQQIYRECAELTRETGLRTHFI-SKVSEAKQKhgAECKQRYDIL 243
Cdd:PTZ00110 180 KTLAFLLPAIVHINAQpllrYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAyGGVPKRGQI--YALRRGVEIL 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 244 VSTPNRVRFLLQQEppLLDLSHVEWFVLDEADRLMEEGqnnFKEQLDDIYAACsNPTKCVAFFSATYTVPVAKWALRHLK 323
Cdd:PTZ00110 258 IACPGRLIDFLESN--VTNLRRVTYLVLDEADRMLDMG---FEPQIRKIVSQI-RPDRQTLMWSATWPKEVQSLARDLCK 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 324 N-LVRITIG-VQNSATETVQQELlFVGSEGGKLVAIRDLVRQGLQP--PVLVFVQSKERAKQLFEELLYDGINVDVIHAE 399
Cdd:PTZ00110 332 EePVHVNVGsLDLTACHNIKQEV-FVVEEHEKRGKLKMLLQRIMRDgdKILIFVETKKGADFLTKELRLDGWPALCIHGD 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 400 RSQHQRDNCVKAFREGSIWVLICTELMGRGIDFKGVNLVINYDFPPTTISYIHRIGRTGRAGRPGRAITFFTQEDTSNLR 479
Cdd:PTZ00110 411 KKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLAR 490
|
410 420 430
....*....|....*....|....*....|.
gi 24666101 480 GIALIIKNSGGTVPEYMLQMKKVRKSEAKMR 510
Cdd:PTZ00110 491 DLVKVLREAKQPVPPELEKLSNERSNGTERR 521
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
123-498 |
2.42e-62 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 213.24 E-value: 2.42e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 123 DFKMLPRLQQNLLSRNFDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGL-----RAHKTTG-LRALVLAP 196
Cdd:PRK01297 91 DFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLlqtppPKERYMGePRALIIAP 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 197 TRELAQQIYRECAELTRETGLRT-HFISKVSEAKQKHGAECKQrYDILVSTPNRVRFLLQQEPPLLDLshVEWFVLDEAD 275
Cdd:PRK01297 171 TRELVVQIAKDAAALTKYTGLNVmTFVGGMDFDKQLKQLEARF-CDILVATPGRLLDFNQRGEVHLDM--VEVMVLDEAD 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 276 RLMEEGqnnFKEQLDDIYAacSNPTKC---VAFFSATYTVPVAKWALRHLKNLVRITIGVQNSATETVQQELLFV-GSEG 351
Cdd:PRK01297 248 RMLDMG---FIPQVRQIIR--QTPRKEerqTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVaGSDK 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 352 GKLvaIRDLVRQGLQPPVLVFVQSKERAKQLFEELLYDGINVDVIHAERSQHQRDNCVKAFREGSIWVLICTELMGRGID 431
Cdd:PRK01297 323 YKL--LYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIH 400
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24666101 432 FKGVNLVINYDFPPTTISYIHRIGRTGRAGRPGRAITFFTQEDTSNLRGIALII--KNSGGTVPEYMLQ 498
Cdd:PRK01297 401 IDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLgrKISCEMPPAELLK 469
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
130-329 |
2.93e-62 |
|
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: 203.83 E-value: 2.93e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 130 LQQNLLSRNFDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGL---RAHKTTGLRALVLAPTRELAQQIYR 206
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLlpePKKKGRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 207 ECAELTRETGLRTH-FISKVSEAKQKhgAECKQRYDILVSTPNRVRFLLQQEPplLDLSHVEWFVLDEADRLMEEGqnnF 285
Cdd:cd00268 81 VARKLGKGTGLKVAaIYGGAPIKKQI--EALKKGPDIVVGTPGRLLDLIERGK--LDLSNVKYLVLDEADRMLDMG---F 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 24666101 286 KEQLDDIYAACsNPTKCVAFFSATYTVPVAKWALRHLKNLVRIT 329
Cdd:cd00268 154 EEDVEKILSAL-PKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
116-531 |
3.80e-60 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 206.96 E-value: 3.80e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 116 SFGTLTrdfkMLPRLQQNLLSRNFDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGLRAhKTTGLRALVLA 195
Cdd:PRK11776 5 AFSTLP----LPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDV-KRFRVQALVLC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 196 PTRELAQQIYRECAELTRetglRTHFIsKV-----------SEAKQKHGAEckqrydILVSTPNRVRFLLQQEppLLDLS 264
Cdd:PRK11776 80 PTRELADQVAKEIRRLAR----FIPNI-KVltlcggvpmgpQIDSLEHGAH------IIVGTPGRILDHLRKG--TLDLD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 265 HVEWFVLDEADRLMEEGqnnFKEQLDDIYAACsnPTKC-VAFFSATYTVPVAKWALRHLKNLVRITIGVQNSATeTVQQE 343
Cdd:PRK11776 147 ALNTLVLDEADRMLDMG---FQDAIDAIIRQA--PARRqTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLP-AIEQR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 344 LLFVgSEGGKLVAIRDLVRQgLQP-PVLVFVQSKERAKQLFEELLYDGINVDVIHAERSQHQRDNCVKAFREGSIWVLIC 422
Cdd:PRK11776 221 FYEV-SPDERLPALQRLLLH-HQPeSCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 423 TELMGRGIDFKGVNLVINYDFPPTTISYIHRIGRTGRAGRPGRAITFFTQEDTSNLRGIaliiknsggtvpEYMLQMKKV 502
Cdd:PRK11776 299 TDVAARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAI------------EDYLGRKLN 366
|
410 420 430
....*....|....*....|....*....|....*....
gi 24666101 503 RKS--EAKMRAKKPLDREDIS--------TKIRPetkGD 531
Cdd:PRK11776 367 WEPlpSLSPLSGVPLLPEMVTlcidggkkDKLRP---GD 402
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
123-578 |
5.64e-59 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 203.25 E-value: 5.64e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 123 DFKMLPRLQQNLLSRNFDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGL---RAHKTTGLRALVLAPTRE 199
Cdd:PRK11192 5 ELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLldfPRRKSGPPRILILTPTRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 200 LAQQIYRECAELTRETGLRTHFISKvSEAKQKHGAECKQRYDILVSTPNRVRFLLQQEppLLDLSHVEWFVLDEADRLME 279
Cdd:PRK11192 85 LAMQVADQARELAKHTHLDIATITG-GVAYMNHAEVFSENQDIVVATPGRLLQYIKEE--NFDCRAVETLILDEADRMLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 280 EGqnnFKEQLDDIYAACSNpTKCVAFFSATYTVP-VAKWALRHLKNLVRITIGVQNSATETVQQELLFVGSEGGKLVAIR 358
Cdd:PRK11192 162 MG---FAQDIETIAAETRW-RKQTLLFSATLEGDaVQDFAERLLNDPVEVEAEPSRRERKKIHQWYYRADDLEHKTALLC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 359 DLVRQGLQPPVLVFVQSKERAKQLFEELLYDGINVDVIHAERSQHQRDNCVKAFREGSIWVLICTELMGRGIDFKGVNLV 438
Cdd:PRK11192 238 HLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 439 INYDFPPTTISYIHRIGRTGRAGRPGRAITFFTQEDtsnlrgiALIIknsgGTVPEYMlqmkkvrkseakmraKKPLDRE 518
Cdd:PRK11192 318 INFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHD-------HLLL----GKIERYI---------------EEPLKAR 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24666101 519 DIStKIRPETKG-DEKHKSTKLKKVERTEKILKNRKGYEKDLNSKQKKLGNIKTELKPAGK 578
Cdd:PRK11192 372 VID-ELRPKTKApSEKKTGKPSKKVLAKRAEKKEKEKEKPKVKKRHRDTKNIGKRRKPSGT 431
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
139-486 |
2.97e-55 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 193.87 E-value: 2.97e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 139 FDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGLRAHKTTG-----LRALVLAPTRELAQQIYRECAELTR 213
Cdd:PRK10590 21 YREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAkgrrpVRALILTPTRELAAQIGENVRDYSK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 214 ETGLRTHFI-SKVSEAKQKhgAECKQRYDILVSTPNRVRFLLQQEPplLDLSHVEWFVLDEADRLMEEGqnnFKEQLDDI 292
Cdd:PRK10590 101 YLNIRSLVVfGGVSINPQM--MKLRGGVDVLVATPGRLLDLEHQNA--VKLDQVEILVLDEADRMLDMG---FIHDIRRV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 293 YAACSnPTKCVAFFSATYTVPVAKWALRHLKNLVRITIGVQNSATETVQQELLFVGSEGgKLVAIRDLVRQGLQPPVLVF 372
Cdd:PRK10590 174 LAKLP-AKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKR-KRELLSQMIGKGNWQQVLVF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 373 VQSKERAKQLFEELLYDGINVDVIHAERSQHQRDNCVKAFREGSIWVLICTELMGRGIDFKGVNLVINYDFPPTTISYIH 452
Cdd:PRK10590 252 TRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPEDYVH 331
|
330 340 350
....*....|....*....|....*....|....
gi 24666101 453 RIGRTGRAGRPGRAITFFTQEDTSNLRGIALIIK 486
Cdd:PRK10590 332 RIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLK 365
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
340-470 |
3.67e-53 |
|
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: 177.70 E-value: 3.67e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 340 VQQELLFVGSEGGKLVAIRDLVRQGLQPPVLVFVQSKERAKQLFEELLYDGINVDVIHAERSQHQRDNCVKAFREGSIWV 419
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 24666101 420 LICTELMGRGIDFKGVNLVINYDFPPTTISYIHRIGRTGRAGRPGRAITFF 470
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
123-488 |
3.44e-51 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 181.71 E-value: 3.44e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 123 DFKMLPRLQQNLLSRNFDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGLRAH------KTTGLRALVLAP 196
Cdd:PRK04837 12 DFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHpapedrKVNQPRALIMAP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 197 TRELAQQIYRECAELTRETGLRTHfISKVSEAKQKHGAECKQRYDILVSTPNRVRFLLQQEppLLDLSHVEWFVLDEADR 276
Cdd:PRK04837 92 TRELAVQIHADAEPLAQATGLKLG-LAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQN--HINLGAIQVVVLDEADR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 277 LMEEGqnnFkeqLDDI---YAACSNPTKCVA-FFSATYTVPVAKWALRHLKNLVRITIGVQNSATETVQQELlFVGSEGG 352
Cdd:PRK04837 169 MFDLG---F---IKDIrwlFRRMPPANQRLNmLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEEL-FYPSNEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 353 KLVAIRDLVRQGLQPPVLVFVQSKERAKQLFEELLYDGINVDVIHAERSQHQRDNCVKAFREGSIWVLICTELMGRGIDF 432
Cdd:PRK04837 242 KMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHI 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 24666101 433 KGVNLVINYDFPPTTISYIHRIGRTGRAGRPGRAITFFTQEDTSNLRGIALIIKNS 488
Cdd:PRK04837 322 PAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIGHS 377
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
92-481 |
9.58e-51 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 180.02 E-value: 9.58e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 92 EEANETRKQYGIRVLGKNVPPPVDSFGTLTRDFKMLprlqQNLLSRNFDHPTPIQMQALPVLLQRRALMACAPTGSGKTL 171
Cdd:PTZ00424 5 EQKNQSEQVASTGTIESNYDEIVDSFDALKLNEDLL----RGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 172 AFLTPIINgLRAHKTTGLRALVLAPTRELAQQIYRECAELTRETGLRTHFI---SKVSEAKQKhgaeCKQRYDILVSTPN 248
Cdd:PTZ00424 81 TFVIAALQ-LIDYDLNACQALILAPTRELAQQIQKVVLALGDYLKVRCHACvggTVVRDDINK----LKAGVHMVVGTPG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 249 RVRFLLQQEPPLLDlsHVEWFVLDEADRLMEEGqnnFKEQLDDIYAACSnPTKCVAFFSATYTVPVAKWALRHLKNLVRI 328
Cdd:PTZ00424 156 RVYDMIDKRHLRVD--DLKLFILDEADEMLSRG---FKGQIYDVFKKLP-PDVQVALFSATMPNEILELTTKFMRDPKRI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 329 TIGVQNSATETVQQELLFVGSEGGKLVAIRDLVRQGLQPPVLVFVQSKERAKQLFEELLYDGINVDVIHAERSQHQRDNC 408
Cdd:PTZ00424 230 LVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLI 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24666101 409 VKAFREGSIWVLICTELMGRGIDFKGVNLVINYDFPPTTISYIHRIGRTGRAGRPGRAITFFTQEDTSNLRGI 481
Cdd:PTZ00424 310 MREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEI 382
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
124-469 |
5.10e-46 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 170.90 E-value: 5.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 124 FKMLPRLQQNLLSRNFDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIIN------GLRAHKTTGLRALVLAPT 197
Cdd:PRK04537 14 FDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNrllsrpALADRKPEDPRALILAPT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 198 RELAQQIYRECAELTRETGLRTHFI-SKVSEAKQKHgaECKQRYDILVSTPNR-VRFLLQQEppLLDLSHVEWFVLDEAD 275
Cdd:PRK04537 94 RELAIQIHKDAVKFGADLGLRFALVyGGVDYDKQRE--LLQQGVDVIIATPGRlIDYVKQHK--VVSLHACEICVLDEAD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 276 RLMEEG-QNNFKEQLDDIYAACSNPTkcvAFFSATYTVPVAKWALRHLKNLVRITIGVQNSATETVQQELLFvGSEGGKL 354
Cdd:PRK04537 170 RMFDLGfIKDIRFLLRRMPERGTRQT---LLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYF-PADEEKQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 355 VAIRDLVRQGLQPPVLVFVQSKERAKQLFEELLYDGINVDVIHAERSQHQRDNCVKAFREGSIWVLICTELMGRGIDFKG 434
Cdd:PRK04537 246 TLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDG 325
|
330 340 350
....*....|....*....|....*....|....*
gi 24666101 435 VNLVINYDFPPTTISYIHRIGRTGRAGRPGRAITF 469
Cdd:PRK04537 326 VKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISF 360
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
128-331 |
2.77e-44 |
|
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: 156.88 E-value: 2.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 128 PRLQQNLLSRNFDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGL---------RAHKTTGLRALVLAPTR 198
Cdd:cd17967 9 ELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLledgppsvgRGRRKAYPSALILAPTR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 199 ELAQQIYRECAELTRETGLRTHFI----SKVSEAKQ-KHGAeckqryDILVSTPNRVRFLLQQEppLLDLSHVEWFVLDE 273
Cdd:cd17967 89 ELAIQIYEEARKFSYRSGVRSVVVyggaDVVHQQLQlLRGC------DILVATPGRLVDFIERG--RISLSSIKFLVLDE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24666101 274 ADRLMEEGqnnFKEQLDDIYAACSNPTKCV---AFFSATYTVPVAKWALRHLKNLVRITIG 331
Cdd:cd17967 161 ADRMLDMG---FEPQIRKIVEHPDMPPKGErqtLMFSATFPREIQRLAADFLKNYIFLTVG 218
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
139-532 |
8.23e-44 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 165.79 E-value: 8.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 139 FDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGLRAHkttgLRA---LVLAPTRELAQQIYRECAELtret 215
Cdd:PRK11634 26 YEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPE----LKApqiLVLAPTRELAVQVAEAMTDF---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 216 glrthfiskvseAKQKHGAEC-----KQRYD-----------ILVSTPNRVRFLLQQEPplLDLSHVEWFVLDEADRLME 279
Cdd:PRK11634 98 ------------SKHMRGVNVvalygGQRYDvqlralrqgpqIVVGTPGRLLDHLKRGT--LDLSKLSGLVLDEADEMLR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 280 EGqnnFKEQLDDIYAACSNPTKcVAFFSATYTVPVAKWALRHLKN--LVRItigvQNSATE--TVQQELLFVGSEGGKLV 355
Cdd:PRK11634 164 MG---FIEDVETIMAQIPEGHQ-TALFSATMPEAIRRITRRFMKEpqEVRI----QSSVTTrpDISQSYWTVWGMRKNEA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 356 AIRDLVRQGLQPPVlVFVQSKERAKQLFEELLYDGINVDVIHAERSQHQRDNCVKAFREGSIWVLICTELMGRGIDFKGV 435
Cdd:PRK11634 236 LVRFLEAEDFDAAI-IFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 436 NLVINYDFPPTTISYIHRIGRTGRAGRPGRAITFFTQEDTSNLRGIALIIKNsggTVPEY------MLQMKKVRKSEAKM 509
Cdd:PRK11634 315 SLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKL---TIPEVelpnaeLLGKRRLEKFAAKV 391
|
410 420
....*....|....*....|....*....
gi 24666101 510 RAKkpLDREDIS------TKIRPETKGDE 532
Cdd:PRK11634 392 QQQ--LESSDLDqyrallAKIQPTAEGEE 418
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
143-316 |
6.60e-43 |
|
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: 151.24 E-value: 6.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 143 TPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGLRaHKTTGLRALVLAPTRELAQQIYRECAELTRETGLRTHFI 222
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALD-KLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 223 skVSEAKQKHGAECKQRYDILVSTPNRVRFLLQQEPpllDLSHVEWFVLDEADRLMEEGqnnFKEQLDDIYAACsNPTKC 302
Cdd:pfam00270 80 --LGGDSRKEQLEKLKGPDILVGTPGRLLDLLQERK---LLKNLKLLVLDEAHRLLDMG---FGPDLEEILRRL-PKKRQ 150
|
170
....*....|....
gi 24666101 303 VAFFSATYTVPVAK 316
Cdd:pfam00270 151 ILLLSATLPRNLED 164
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
128-309 |
1.58e-42 |
|
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: 151.69 E-value: 1.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 128 PRLQQNLLSRNFDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGLRAH-KTTGLRALVLAPTRELAQQIYR 206
Cdd:cd17959 10 PPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHsPTVGARALILSPTRELALQTLK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 207 ECAELTRETGLRTHFISKVSEAKQKHGAECKQRyDILVSTPNRVRFLLQQEPplLDLSHVEWFVLDEADRLMEEGqnnFK 286
Cdd:cd17959 90 VTKELGKFTDLRTALLVGGDSLEEQFEALASNP-DIIIATPGRLLHLLVEMN--LKLSSVEYVVFDEADRLFEMG---FA 163
|
170 180
....*....|....*....|...
gi 24666101 287 EQLDDIYAACSNPTKCVaFFSAT 309
Cdd:cd17959 164 EQLHEILSRLPENRQTL-LFSAT 185
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
138-328 |
8.59e-40 |
|
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: 143.93 E-value: 8.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 138 NFDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGL--RAHKTTGLRALVLAPTRELAQQIYRECAELTRET 215
Cdd:cd17947 9 GFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLlyRPKKKAATRVLVLVPTRELAMQCFSVLQQLAQFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 216 GLRTHFISKVSEAKQkHGAECKQRYDILVSTPNRVRFLLQQEPPlLDLSHVEWFVLDEADRLMEEGqnnFKEQLDDIYAA 295
Cdd:cd17947 89 DITFALAVGGLSLKA-QEAALRARPDIVIATPGRLIDHLRNSPS-FDLDSIEILVLDEADRMLEEG---FADELKEILRL 163
|
170 180 190
....*....|....*....|....*....|...
gi 24666101 296 CSNpTKCVAFFSATYTVPVAKWALRHLKNLVRI 328
Cdd:cd17947 164 CPR-TRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
138-329 |
1.10e-36 |
|
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: 136.30 E-value: 1.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 138 NFDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGLRA-------HKTTGLRALVLAPTRELAQQIYRECAE 210
Cdd:cd17945 9 GYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRlppldeeTKDDGPYALILAPTRELAQQIEEETQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 211 LTRETGLRThfISKV-SEAKQKHGAECKQRYDILVSTPNRVRFLLqqEPPLLDLSHVEWFVLDEADRLMEEGqnnFKEQL 289
Cdd:cd17945 89 FAKPLGIRV--VSIVgGHSIEEQAFSLRNGCEILIATPGRLLDCL--ERRLLVLNQCTYVVLDEADRMIDMG---FEPQV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 24666101 290 DDI-------------------YAACSNPTKCVAFFSATYTVPVAKWALRHLKNLVRIT 329
Cdd:cd17945 162 TKIldampvsnkkpdteeaeklAASGKHRYRQTMMFTATMPPAVEKIAKGYLRRPVVVT 220
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
104-329 |
1.87e-36 |
|
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: 135.58 E-value: 1.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 104 RVLGKNVPPPVDSFGTLTrdfkMLPRLQQNLLSRNFDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGLRA 183
Cdd:cd17953 1 KVRGKDCPKPIQKWSQCG----LSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 184 HKT----TGLRALVLAPTRELAQQIYRECAELTRETGLRTHFISKVSEAKQKHgAECKQRYDILVSTPNR-VRFLLQQEP 258
Cdd:cd17953 77 QRPvkpgEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQI-AELKRGAEIVVCTPGRmIDILTANNG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24666101 259 PLLDLSHVEWFVLDEADRLMEEGqnnFKEQLDDIYAACsNPTKCVAFFSATYTVPVAKWALRHLKNLVRIT 329
Cdd:cd17953 156 RVTNLRRVTYVVLDEADRMFDMG---FEPQIMKIVNNI-RPDRQTVLFSATFPRKVEALARKVLHKPIEIT 222
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
103-332 |
3.99e-36 |
|
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: 135.87 E-value: 3.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 103 IRVLGKNVPPPVDSFgtltRDFKMLPRLQQNLLSRNFDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGLR 182
Cdd:cd18052 31 VEVTGRNPPPAILTF----EEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 183 AHKTTGLR--------ALVLAPTRELAQQIYRECAELTRETGLRTHFI-SKVSEAKQKhgAECKQRYDILVSTPNRvrfl 253
Cdd:cd18052 107 KEGLTASSfsevqepqALIVAPTRELANQIFLEARKFSYGTCIRPVVVyGGVSVGHQI--RQIEKGCHILVATPGR---- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 254 lqqeppLLD--------LSHVEWFVLDEADRLMEEGqnnFKEQLDDIYAACSNPTKC---VAFFSATYTVPVAKWALRHL 322
Cdd:cd18052 181 ------LLDfigrgkisLSKLKYLILDEADRMLDMG---FGPEIRKLVSEPGMPSKEdrqTLMFSATFPEEIQRLAAEFL 251
|
250
....*....|.
gi 24666101 323 K-NLVRITIGV 332
Cdd:cd18052 252 KeDYLFLTVGR 262
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
137-343 |
5.11e-36 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 133.77 E-value: 5.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 137 RNFDHPTPIQMQALPVLLQR-RALMACAPTGSGKTLAFLTPIINglRAHKTTGLRALVLAPTRELAQQIYRECAELTRET 215
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALE--ALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 216 GLRTHFISKVSEAKQKHGAECKQRYDILVSTPNRVRFLLQQEPplLDLSHVEWFVLDEADRLMEegqNNFKEQLDDIYAA 295
Cdd:smart00487 82 GLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDK--LSLSNVDLVILDEAHRLLD---GGFGDQLEKLLKL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 24666101 296 CSNPTKCVaFFSATYTVPVAKWALRHLKNLVRITIGVqnSATETVQQE 343
Cdd:smart00487 157 LPKNVQLL-LLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
130-321 |
2.20e-35 |
|
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: 132.76 E-value: 2.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 130 LQQNLLSRNFDHPTPIQMQALPVLLQ---------RRALMACAPTGSGKTLAFLTPIINGLRAHKTTGLRALVLAPTREL 200
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPsskstppyrPGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPRLRALIVVPTKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 201 AQQIYRECAELTRETGLRT-------HFISKVSEAKQKHGAECKQRYDILVSTPNR-VRFLlqQEPPLLDLSHVEWFVLD 272
Cdd:cd17956 81 VQQVYKVFESLCKGTGLKVvslsgqkSFKKEQKLLLVDTSGRYLSRVDILVATPGRlVDHL--NSTPGFTLKHLRFLVID 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24666101 273 EADRLMEEGQNNFKEQLD---------------DIYAACSNPTKCVA-FFSATYTVPVAK---WALRH 321
Cdd:cd17956 159 EADRLLNQSFQDWLETVMkalgrptapdlgsfgDANLLERSVRPLQKlLFSATLTRDPEKlssLKLHR 226
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
128-331 |
3.16e-35 |
|
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: 131.94 E-value: 3.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 128 PRLQQNLLSRNFDHPTPIQMQALPVLLQ-RRALMACAPTGSGKTLAFLTP----IINGLRAHKTTGLRALVLAPTRELAQ 202
Cdd:cd17964 3 PSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPaiqsLLNTKPAGRRSGVSALIISPTRELAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 203 QIYRECAELTR-ETGLRTH-FI--SKVSEAKQKHGaecKQRYDILVSTPNRVRFLLQQEPPLLDLSHVEWFVLDEADRLM 278
Cdd:cd17964 83 QIAAEAKKLLQgLRKLRVQsAVggTSRRAELNRLR---RGRPDILVATPGRLIDHLENPGVAKAFTDLDYLVLDEADRLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 24666101 279 EEGqnnFKEQLDDIYAA----CSNPTKCVaFFSAtyTVPvakwalRHLKNLVRITIG 331
Cdd:cd17964 160 DMG---FRPDLEQILRHlpekNADPRQTL-LFSA--TVP------DEVQQIARLTLK 204
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
139-329 |
4.02e-34 |
|
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: 128.46 E-value: 4.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 139 FDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGLRAHKT----TGLRALVLAPTRELAQQIYRECAELTRE 214
Cdd:cd17960 10 FTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKAnlkkGQVGALIISPTRELATQIYEVLQSFLEH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 215 TG--LRTHFISKVSEAKQKHGAECKQRYDILVSTPNRVRFLLQQEPPLLDLSHVEWFVLDEADRLMEEGqnnFKEQLDDI 292
Cdd:cd17960 90 HLpkLKCQLLIGGTNVEEDVKKFKRNGPNILVGTPGRLEELLSRKADKVKVKSLEVLVLDEADRLLDLG---FEADLNRI 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 24666101 293 YAACsnP-TKCVAFFSATYTVPVAKWALRHLKNLVRIT 329
Cdd:cd17960 167 LSKL--PkQRRTGLFSATQTDAVEELIKAGLRNPVRVV 202
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
128-326 |
8.03e-34 |
|
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: 127.70 E-value: 8.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 128 PRLQQNLLSRNFDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGLRAHKTT-----GLRALVLAPTRELAQ 202
Cdd:cd17961 3 PRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAEsgeeqGTRALILVPTRELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 203 QIYRECAELTreTGLRTH-----FISKVSEAKQKHGAECKQryDILVSTPNRVRFLLQQEpPLLDLSHVEWFVLDEADRL 277
Cdd:cd17961 83 QVSKVLEQLT--AYCRKDvrvvnLSASSSDSVQRALLAEKP--DIVVSTPARLLSHLESG-SLLLLSTLKYLVIDEADLV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 24666101 278 MEEGqnnFKEQLDDIyaACSNPTKCVAFF-SATYTVPVAKwalrhLKNLV 326
Cdd:cd17961 158 LSYG---YEEDLKSL--LSYLPKNYQTFLmSATLSEDVEA-----LKKLV 197
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
131-328 |
1.36e-33 |
|
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: 127.02 E-value: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 131 QQNLLSRNFDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGLRAHKTT---GLRALVLAPTRELAQQIYRE 207
Cdd:cd17941 2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTpedGLGALIISPTRELAMQIFEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 208 CAELTRETGLRTHFISKVSEAKQKhgAECKQRYDILVSTPNRvrfLLQ--QEPPLLDLSHVEWFVLDEADRLMEEGqnnF 285
Cdd:cd17941 82 LRKVGKYHSFSAGLIIGGKDVKEE--KERINRMNILVCTPGR---LLQhmDETPGFDTSNLQMLVLDEADRILDMG---F 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 24666101 286 KEQLDDIYAACSnPTKCVAFFSATYTVPVAKWALRHLKNLVRI 328
Cdd:cd17941 154 KETLDAIVENLP-KSRQTLLFSATQTKSVKDLARLSLKNPEYI 195
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
130-311 |
2.83e-33 |
|
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: 126.18 E-value: 2.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 130 LQQNLLSRNFDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGLrAHKTTGLRALVLAPTRELAQQIYRECA 209
Cdd:cd17955 10 LVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRL-SEDPYGIFALVLTPTRELAYQIAEQFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 210 ELTRETGLRTHFI----SKVSEAKqkhgaECKQRYDILVSTPNRVRFLLQQEPPLL-DLSHVEWFVLDEADRLMEEgqnN 284
Cdd:cd17955 89 ALGAPLGLRCCVIvggmDMVKQAL-----ELSKRPHIVVATPGRLADHLRSSDDTTkVLSRVKFLVLDEADRLLTG---S 160
|
170 180
....*....|....*....|....*..
gi 24666101 285 FKEQLDDIYAACSnPTKCVAFFSATYT 311
Cdd:cd17955 161 FEDDLATILSALP-PKRQTLLFSATLT 186
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
132-311 |
3.40e-32 |
|
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box protein, which shows little similarity to any of the other known human DEAD box proteins, but shows a high similarity to mouse Ddx24 at the amino acid level. MDM2 mediates nonproteolytic polyubiquitylation of the DEAD-Box RNA helicase DDX24. DDX24 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.
Pssm-ID: 350704 [Multi-domain] Cd Length: 235 Bit Score: 124.27 E-value: 3.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 132 QNLLSRNFDHPTPIQMQALPV-LLQRRALMACAPTGSGKTLAFLTPIINGL--------RAHKTTGLRALVLAPTRELAQ 202
Cdd:cd17946 3 RALADLGFSEPTPIQALALPAaIRDGKDVIGAAETGSGKTLAFGIPILERLlsqkssngVGGKQKPLRALILTPTRELAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 203 QIYRECAELTRETGLRThfISKV---SEAKQKHgaECKQRYDILVSTPNRVRFLLQQEPPLLD-LSHVEWFVLDEADRLM 278
Cdd:cd17946 83 QVKDHLKAIAKYTNIKI--ASIVgglAVQKQER--LLKKRPEIVVATPGRLWELIQEGNEHLAnLKSLRFLVLDEADRML 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 24666101 279 EEGqnNFKEqLDDIYAACSNPTKCVA------FFSATYT 311
Cdd:cd17946 159 EKG--HFAE-LEKILELLNKDRAGKKrkrqtfVFSATLT 194
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
352-461 |
4.86e-32 |
|
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: 119.24 E-value: 4.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 352 GKLVAIRDLVRQGLQPPVLVFVQSKERAKqlFEELL-YDGINVDVIHAERSQHQRDNCVKAFREGSIWVLICTELMGRGI 430
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLE--AELLLeKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
|
90 100 110
....*....|....*....|....*....|.
gi 24666101 431 DFKGVNLVINYDFPPTTISYIHRIGRTGRAG 461
Cdd:pfam00271 79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
130-329 |
5.49e-32 |
|
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: 123.08 E-value: 5.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 130 LQQNLLSR-NFDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGL-----RAHKTTGLRALVLAPTRELAQQ 203
Cdd:cd17949 1 LVSHLKSKmGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLlslepRVDRSDGTLALVLVPTRELALQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 204 IYRECAELTRetglRTHFIskVS------EAKQKHGAECKQRYDILVSTPNRVRFLLQ--QEpplLDLSHVEWFVLDEAD 275
Cdd:cd17949 81 IYEVLEKLLK----PFHWI--VPgyliggEKRKSEKARLRKGVNILIATPGRLLDHLKntQS---FDVSNLRWLVLDEAD 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24666101 276 RLMEEGqnnFKEQLDDIY-------AACSNPTKCVAFF-----SATYTVPVAKWALRHLKNLVRIT 329
Cdd:cd17949 152 RLLDMG---FEKDITKILellddkrSKAGGEKSKPSRRqtvlvSATLTDGVKRLAGLSLKDPVYID 214
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
107-331 |
3.06e-31 |
|
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: 122.07 E-value: 3.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 107 GKNVPPPVDSFgtltRDFKMLPRLQQNLLSRNFDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGL----- 181
Cdd:cd18051 13 GENCPPHIETF----SDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIyeqgp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 182 -----RAHKTTGLR-----ALVLAPTRELAQQIYREcaelTRETGLRthfiSKVSEAKQKHGAECKQRY-------DILV 244
Cdd:cd18051 89 geslpSESGYYGRRkqyplALVLAPTRELASQIYDE----ARKFAYR----SRVRPCVVYGGADIGQQMrdlergcHLLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 245 STPNRVRFLLQQEPPLLDlsHVEWFVLDEADRLMEEGqnnFKEQLDDIYAACSNPTKCV---AFFSATYTVPVAKWALRH 321
Cdd:cd18051 161 ATPGRLVDMLERGKIGLD--YCKYLVLDEADRMLDMG---FEPQIRRIVEQDTMPPTGErqtLMFSATFPKEIQMLARDF 235
|
250
....*....|
gi 24666101 322 LKNLVRITIG 331
Cdd:cd18051 236 LDNYIFLAVG 245
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
123-328 |
4.90e-30 |
|
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: 117.01 E-value: 4.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 123 DFKMLPRLQQNLLSRNFDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGLRAhKTTGLRALVLAPTRELAQ 202
Cdd:cd17940 3 DYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDP-KKDVIQALILVPTRELAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 203 QIYRECAELTRETGLRTHFISKVSEAKQKHgAECKQRYDILVSTPNRVRFLLQQEppLLDLSHVEWFVLDEADRLMEEgq 282
Cdd:cd17940 82 QTSQVCKELGKHMGVKVMVTTGGTSLRDDI-MRLYQTVHVLVGTPGRILDLAKKG--VADLSHCKTLVLDEADKLLSQ-- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 24666101 283 nNFKEQLDDIYAACSnPTKCVAFFSATYTVPVAKWALRHLKNLVRI 328
Cdd:cd17940 157 -DFQPIIEKILNFLP-KERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
130-329 |
6.82e-30 |
|
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: 116.49 E-value: 6.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 130 LQQNLLSRNFDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGLRAHKTTGLrALVLAPTRELAQQIYRECA 209
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPS-ALILTPTRELAVQIEDQAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 210 ELTR-ETGLRTHF-ISKVSEAKQKHgaECKQRYDILVSTPNRVRFLLQQEPplLDLSHVEWFVLDEADRLMEEGqnnFKE 287
Cdd:cd17962 80 ELMKgLPPMKTALlVGGLPLPPQLY--RLQQGVKVIIATPGRLLDILKQSS--VELDNIKIVVVDEADTMLKMG---FQQ 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 24666101 288 QLDDIYAACSNPTKcVAFFSATYTVPVAKWALRHLKNLVRIT 329
Cdd:cd17962 153 QVLDILENISHDHQ-TILVSATIPRGIEQLAGQLLQNPVRIT 193
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
134-329 |
4.44e-29 |
|
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: 114.39 E-value: 4.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 134 LLSRNFDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGLRAH----KTTGLRALVLAPTRELAQQIYRECA 209
Cdd:cd17966 5 LKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQppleRGDGPIVLVLAPTRELAQQIQQEAN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 210 ELTRETGLRTHFI-SKVSEAKQKhgAECKQRYDILVSTPNRVRFLLQQEPplLDLSHVEWFVLDEADRLMEEGqnnFKEQ 288
Cdd:cd17966 85 KFGGSSRLRNTCVyGGAPKGPQI--RDLRRGVEICIATPGRLIDFLDQGK--TNLRRVTYLVLDEADRMLDMG---FEPQ 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 24666101 289 LDDIYAACsNPTKCVAFFSATYTVPVAKWALRHLKNLVRIT 329
Cdd:cd17966 158 IRKIVDQI-RPDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
138-328 |
5.72e-29 |
|
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: 113.95 E-value: 5.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 138 NFDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGLrAHKTTGLRALVLAPTRELAQQIYRECAELTRETGL 217
Cdd:cd17954 19 GWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQAL-LENPQRFFALVLAPTRELAQQISEQFEALGSSIGL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 218 RTHFI----SKVSEAKQkhgaeCKQRYDILVSTPNRVRFLLQQEPPlLDLSHVEWFVLDEADRLMEEgqnNFKEQLDDIY 293
Cdd:cd17954 98 KSAVLvggmDMMAQAIA-----LAKKPHVIVATPGRLVDHLENTKG-FSLKSLKFLVMDEADRLLNM---DFEPEIDKIL 168
|
170 180 190
....*....|....*....|....*....|....*.
gi 24666101 294 AACsnPTKCVAF-FSATYTVPVAKWALRHLKNLVRI 328
Cdd:cd17954 169 KVI--PRERTTYlFSATMTTKVAKLQRASLKNPVKI 202
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
130-329 |
7.83e-29 |
|
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: 113.66 E-value: 7.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 130 LQQNLLSRNFDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGLRAH----KTTGLRALVLAPTRELAQQIY 205
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQreleKGEGPIAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 206 RECAELTRETGLRTHFISKvSEAKQKHGAECKQRYDILVSTPNRVRFLLQQEPplLDLSHVEWFVLDEADRLMEEGqnnF 285
Cdd:cd17952 81 LEAKKFGKAYNLRVVAVYG-GGSKWEQAKALQEGAEIVVATPGRLIDMVKKKA--TNLQRVTYLVLDEADRMFDMG---F 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 24666101 286 KEQLDDIyAACSNPTKCVAFFSATYTVPVAKWALRHLKNLVRIT 329
Cdd:cd17952 155 EYQVRSI-VGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRVV 197
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
128-329 |
8.00e-29 |
|
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: 113.44 E-value: 8.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 128 PRLQQNLLSRNFDHPTPIQMQALPVLLQ--RRALMACAPTGSGKTLAF----LTPIINGLRAhkttgLRALVLAPTRELA 201
Cdd:cd17963 3 PELLKGLYAMGFNKPSKIQETALPLILSdpPENLIAQSQSGTGKTAAFvlamLSRVDPTLKS-----PQALCLAPTRELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 202 QQIYRECAELTRETGLRTHFISKVSEAKQKHGAEckqrYDILVSTPNRVRFLLQQEppLLDLSHVEWFVLDEADRLMEeg 281
Cdd:cd17963 78 RQIGEVVEKMGKFTGVKVALAVPGNDVPRGKKIT----AQIVIGTPGTVLDWLKKR--QLDLKKIKILVLDEADVMLD-- 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 24666101 282 QNNFKEQLDDIYAACSNPTKcVAFFSATYTVPVAKWALRHLKNLVRIT 329
Cdd:cd17963 150 TQGHGDQSIRIKRMLPRNCQ-ILLFSATFPDSVRKFAEKIAPNANTIK 196
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
134-310 |
1.32e-28 |
|
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: 112.74 E-value: 1.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 134 LLSRNFDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGLRAHkTTGLRALVLAPTRELAQQI---YRECAE 210
Cdd:cd17943 5 LKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLE-RRHPQVLILAPTREIAVQIhdvFKKIGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 211 LTRetGLRTH-FISKVSEAKQKHGAECKQrydILVSTPNRVRFLLqqEPPLLDLSHVEWFVLDEADRLMEEgqnNFKEQL 289
Cdd:cd17943 84 KLE--GLKCEvFIGGTPVKEDKKKLKGCH---IAVGTPGRIKQLI--ELGALNVSHVRLFVLDEADKLMEG---SFQKDV 153
|
170 180
....*....|....*....|.
gi 24666101 290 DDIYAACSNpTKCVAFFSATY 310
Cdd:cd17943 154 NWIFSSLPK-NKQVIAFSATY 173
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
123-309 |
5.40e-28 |
|
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: 111.26 E-value: 5.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 123 DFKMLPRLQQNLLSRNFDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINglrahkttGLRALVLAPTRELAQ 202
Cdd:cd17938 3 ELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQ--------IVVALILEPSRELAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 203 QIYrEC-----AELTRETgLRTHFI---SKVSEAKQKHGAECkqryDILVSTPNRVRFLLQQEppLLDLSHVEWFVLDEA 274
Cdd:cd17938 75 QTY-NCienfkKYLDNPK-LRVALLiggVKAREQLKRLESGV----DIVVGTPGRLEDLIKTG--KLDLSSVRFFVLDEA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 24666101 275 DRLMEEGQNNFkeqLDDIYAACSNPTKC-----VAFFSAT 309
Cdd:cd17938 147 DRLLSQGNLET---INRIYNRIPKITSDgkrlqVIVCSAT 183
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
92-331 |
3.52e-27 |
|
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: 110.10 E-value: 3.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 92 EEANETRKQYGIRVLGKNVPPPVDSFGTLTrdfkmLPRLQQNLLSR-NFDHPTPIQMQALPVLLQRRALMACAPTGSGKT 170
Cdd:cd18049 1 QEVEQYRRSKEITVRGHNCPKPVLNFYEAN-----FPANVMDVIARqNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 171 LAFLTPIINGLRAH----KTTGLRALVLAPTRELAQQIYRECAELTRETGLRTHFISKvSEAKQKHGAECKQRYDILVST 246
Cdd:cd18049 76 LSYLLPAIVHINHQpfleRGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYG-GAPKGPQIRDLERGVEICIAT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 247 PNR-VRFLlqqEPPLLDLSHVEWFVLDEADRLMEEGqnnFKEQLDDIYAACsNPTKCVAFFSATYTVPVAKWALRHLKNL 325
Cdd:cd18049 155 PGRlIDFL---EAGKTNLRRCTYLVLDEADRMLDMG---FEPQIRKIVDQI-RPDRQTLMWSATWPKEVRQLAEDFLKDY 227
|
....*.
gi 24666101 326 VRITIG 331
Cdd:cd18049 228 IHINIG 233
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
130-292 |
8.20e-26 |
|
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350706 [Multi-domain] Cd Length: 231 Bit Score: 105.91 E-value: 8.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 130 LQQNLLSRNFDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGLRAHK------TTGLRALVLAPTRELAQQ 203
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKllaegpFNAPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 204 IYRECAELTRETGLRTHFISkvseakqkhGAECKQRY--------DILVSTPNRVRFLLQQEppLLDLSHVEWFVLDEAD 275
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVIT---------GGRTKRQIrnphfeevDILVATPGALSKLLTSR--IYSLEQLRHLVLDEAD 149
|
170
....*....|....*..
gi 24666101 276 RLMEEgqnNFKEQLDDI 292
Cdd:cd17948 150 TLLDD---SFNEKLSHF 163
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
139-329 |
1.35e-25 |
|
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: 104.47 E-value: 1.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 139 FDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGLRAHKTT-----GLRALVLAPTRELAQQIYRECAELTR 213
Cdd:cd17958 10 FEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPreqrnGPGVLVLTPTRELALQIEAECSKYSY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 214 EtGLRTHFI-----SKVSEAKQKHGAeckqryDILVSTPNRVRFLlqQEPPLLDLSHVEWFVLDEADRLMEEG-QNNFKE 287
Cdd:cd17958 90 K-GLKSVCVygggnRNEQIEDLSKGV------DIIIATPGRLNDL--QMNNVINLKSITYLVLDEADRMLDMGfEPQIRK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 24666101 288 QLDDIyaacsNPTKCVAFFSATYTVPVAKWALRHLKNLVRIT 329
Cdd:cd17958 161 ILLDI-----RPDRQTIMTSATWPDGVRRLAQSYLKDPMIVY 197
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
380-461 |
1.49e-25 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 100.36 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 380 KQLFEELLYDGINVDVIHAERSQHQRDNCVKAFREGSIWVLICTELMGRGIDFKGVNLVINYDFPPTTISYIHRIGRTGR 459
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 24666101 460 AG 461
Cdd:smart00490 81 AG 82
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
130-328 |
4.47e-25 |
|
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: 102.79 E-value: 4.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 130 LQQNLL----SRNFDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGL-RAHKTTglRALVLAPTRELAQQI 204
Cdd:cd17939 4 LSEDLLrgiyAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIdTTVRET--QALVLAPTRELAQQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 205 YRECAELTRETGLRTH-FI--SKVSEAKQKhgaeCKQRYDILVSTPNRVRFLLQQEPplLDLSHVEWFVLDEADRLMEEG 281
Cdd:cd17939 82 QKVVKALGDYMGVKVHaCIggTSVREDRRK----LQYGPHIVVGTPGRVFDMLQRRS--LRTDKIKMFVLDEADEMLSRG 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 24666101 282 qnnFKEQLDDIYAACsnPTKC-VAFFSATYTVPVAKWALRHLKNLVRI 328
Cdd:cd17939 156 ---FKDQIYDIFQFL--PPETqVVLFSATMPHEVLEVTKKFMRDPVRI 198
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
93-331 |
7.62e-24 |
|
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: 101.24 E-value: 7.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 93 EANETRKQYGIRVLGKNVPPPVDSFGTLTrdfkmLPRLQQN-LLSRNFDHPTPIQMQALPVLLQRRALMACAPTGSGKTL 171
Cdd:cd18050 40 DVEELRRKKEITIRGVGCPKPVFAFHQAN-----FPQYVMDvLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 172 AFLTPIINGLRAH----KTTGLRALVLAPTRELAQQIYRECAELTRETGLRTHFISKvSEAKQKHGAECKQRYDILVSTP 247
Cdd:cd18050 115 AYLLPAIVHINHQpyleRGDGPICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYG-GAPKGPQIRDLERGVEICIATP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 248 NR-VRFLlqqEPPLLDLSHVEWFVLDEADRLMEEGqnnFKEQLDDIYAACsNPTKCVAFFSATYTVPVAKWALRHLKNLV 326
Cdd:cd18050 194 GRlIDFL---EAGKTNLRRCTYLVLDEADRMLDMG---FEPQIRKIVDQI-RPDRQTLMWSATWPKEVRQLAEDFLRDYV 266
|
....*
gi 24666101 327 RITIG 331
Cdd:cd18050 267 QINIG 271
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
128-468 |
1.21e-22 |
|
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: 102.61 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 128 PRLQQNLLSRNFDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGLRAHKTTglRALVLAPTRELAQQIYRE 207
Cdd:COG1205 43 PELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPGA--TALYLYPTKALARDQLRR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 208 CAELTRETGLRThfisKV------SEAKQKHGAecKQRYDILVSTP---NR---------VRFLlqqepplldlSHVEWF 269
Cdd:COG1205 121 LRELAEALGLGV----RVatydgdTPPEERRWI--REHPDIVLTNPdmlHYgllphhtrwARFF----------RNLRYV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 270 VLDEA---------------DRLmeegqNNFKEQL--DDIYAACS----NPtkcVAFFSATYTVPVA----KWALRHLKN 324
Cdd:COG1205 185 VIDEAhtyrgvfgshvanvlRRL-----RRICRHYgsDPQFILASatigNP---AEHAERLTGRPVTvvdeDGSPRGERT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 325 LV-----RITIGVQNSATetvqqellfvgSEGGKLVAirDLVRQGLQppVLVFVQSKERAKQLFEEL---LYDGINVDVI 396
Cdd:COG1205 257 FVlwnppLVDDGIRRSAL-----------AEAARLLA--DLVREGLR--TLVFTRSRRGAELLARYArraLREPDLADRV 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24666101 397 HAERSQH---QRDNCVKAFREGSIWVLICT---ELmgrGIDFKGVNLVINYDFPPTTISYIHRIGRTGRAGRPGRAIT 468
Cdd:COG1205 322 AAYRAGYlpeERREIERGLRSGELLGVVSTnalEL---GIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVL 396
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
134-320 |
3.60e-22 |
|
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: 94.35 E-value: 3.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 134 LLSRNFDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPII---NGLRAHKTTGLRALVLAPTRELAQQIYRECAE 210
Cdd:cd17942 5 IEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIellYKLKFKPRNGTGVIIISPTRELALQIYGVAKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 211 LTREtGLRTHFISKVSEAKQKHGAECKQRYDILVSTPNRVRFLLQQEPPLLdLSHVEWFVLDEADRLMEEGqnnFKEQLD 290
Cdd:cd17942 85 LLKY-HSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFL-YKNLQCLIIDEADRILEIG---FEEEMR 159
|
170 180 190
....*....|....*....|....*....|...
gi 24666101 291 DIYAACSNpTKCVAFFSATYTVPV---AKWALR 320
Cdd:cd17942 160 QIIKLLPK-RRQTMLFSATQTRKVedlARISLK 191
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
134-309 |
1.09e-21 |
|
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: 93.56 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 134 LLSRNFDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIING-------LRAHKTTGLRALVLAPTRELAQQIYR 206
Cdd:cd17951 5 LKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFaleqekkLPFIKGEGPYGLIVCPSRELARQTHE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 207 EC---AELTRETG---LRTHF-ISKVSEAKQKHgaECKQRYDILVSTPNRVRFLLQQEPPLLDLshVEWFVLDEADRLME 279
Cdd:cd17951 85 VIeyyCKALQEGGypqLRCLLcIGGMSVKEQLE--VIRKGVHIVVATPGRLMDMLNKKKINLDI--CRYLCLDEADRMID 160
|
170 180 190
....*....|....*....|....*....|
gi 24666101 280 EGqnnFKEQLDDIYAACSNPTKCVaFFSAT 309
Cdd:cd17951 161 MG---FEEDIRTIFSYFKGQRQTL-LFSAT 186
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
156-470 |
1.52e-21 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 98.56 E-value: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 156 RRALMACAPTGSGKTLAFLTPIinglrAHKTTGLRALVLAPTRELAQQIYRECAELTRETGLrthfiskvseakqkHGAE 235
Cdd:COG1061 100 GGRGLVVAPTGTGKTVLALALA-----AELLRGKRVLVLVPRRELLEQWAEELRRFLGDPLA--------------GGGK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 236 CKQRYDILVSTPNRVRFLLQQEPPLLDLSHVewfVLDEADRLmeeGQNNFKEQLDDIYAAC------------SNPTKCV 303
Cdd:COG1061 161 KDSDAPITVATYQSLARRAHLDELGDRFGLV---IIDEAHHA---GAPSYRRILEAFPAAYrlgltatpfrsdGREILLF 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 304 AFFSATYTVPvAKWALR--HLKNLVRITIGVQ--------NSATETVQQELlfVGSEGGKLVAIRDLVRQ-GLQPPVLVF 372
Cdd:COG1061 235 LFDGIVYEYS-LKEAIEdgYLAPPEYYGIRVDltderaeyDALSERLREAL--AADAERKDKILRELLREhPDDRKTLVF 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 373 VQSKERAKQLFEELLYDGINVDVIHAERSQHQRDNCVKAFREGSIWVLICTELMGRGIDFKGVNLVINYDfpPTT--ISY 450
Cdd:COG1061 312 CSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLR--PTGspREF 389
|
330 340
....*....|....*....|
gi 24666101 451 IHRIGRTGRAGRPGRAITFF 470
Cdd:COG1061 390 IQRLGRGLRPAPGKEDALVY 409
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
141-329 |
1.74e-21 |
|
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: 93.98 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 141 HPTPIQMQALPVLLQ----------------RRALMACAPTGSGKTLAFLTPIINGLR---------------AHKTTG- 188
Cdd:cd17965 30 KPSPIQTLAIKKLLKtlmrkvtkqtsneepkLEVFLLAAETGSGKTLAYLAPLLDYLKrqeqepfeeaeeeyeSAKDTGr 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 189 LRALVLAPTRELAQQIYRECAELTRETGLRTHFIS-KVSEAKQKHGAECKQRYDILVSTPNRVRFLLQQEPPLldLSHVE 267
Cdd:cd17965 110 PRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSsGFGPSYQRLQLAFKGRIDILVTTPGKLASLAKSRPKI--LSRVT 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24666101 268 WFVLDEADRLMEegqnnfKEQLDDIYAACSN--PTKCVAFFSATYTVPVAKWALRHLKNLVRIT 329
Cdd:cd17965 188 HLVVDEADTLFD------RSFLQDTTSIIKRapKLKHLILCSATIPKEFDKTLRKLFPDVVRIA 245
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
122-311 |
3.90e-21 |
|
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: 92.02 E-value: 3.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 122 RDFKMLPRLQQNLLSRNFDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGLRaHKTTGLRALVLAPTRELA 201
Cdd:cd17950 5 RDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLE-PVDGQVSVLVICHTRELA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 202 QQIYRECAELTRE-TGLRTH-FISKVSEAKQKHGAECKQRyDILVSTPNRVRFLLQQEPplLDLSHVEWFVLDEADRLME 279
Cdd:cd17950 84 FQISNEYERFSKYmPNVKTAvFFGGVPIKKDIEVLKNKCP-HIVVGTPGRILALVREKK--LKLSHVKHFVLDECDKMLE 160
|
170 180 190
....*....|....*....|....*....|..
gi 24666101 280 egQNNFKEQLDDIYAACSnPTKCVAFFSATYT 311
Cdd:cd17950 161 --QLDMRRDVQEIFRATP-HDKQVMMFSATLS 189
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
123-328 |
2.31e-20 |
|
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: 89.43 E-value: 2.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 123 DFKMLPRLQQNLLSRNFDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGLRaHKTTGLRALVLAPTRELAQ 202
Cdd:cd18046 3 DMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQID-TSLKATQALVLAPTRELAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 203 QIYRECAELTRETGLRTHFI---SKVSEAKQKHGAECKqrydILVSTPNRVRFLLQQEppLLDLSHVEWFVLDEADRLME 279
Cdd:cd18046 82 QIQKVVMALGDYMGIKCHACiggTSVRDDAQKLQAGPH----IVVGTPGRVFDMINRR--YLRTDYIKMFVLDEADEMLS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 24666101 280 EGqnnFKEQLDDIYAACsNPTKCVAFFSATYTVPVAKWALRHLKNLVRI 328
Cdd:cd18046 156 RG---FKDQIYDIFQKL-PPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
132-323 |
1.52e-18 |
|
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: 84.13 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 132 QNLLSRNFDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGLRAHKTTGLRA-----LVLAPTRELAQQIYR 206
Cdd:cd17944 3 KLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRGrapkvLVLAPTRELANQVTK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 207 ECAELTRETGLrTHFISKVSEAKQKHgaECKQRYDILVSTPNRVRFLLQQEPplLDLSHVEWFVLDEADRLMEEGqnnFK 286
Cdd:cd17944 83 DFKDITRKLSV-ACFYGGTPYQQQIF--AIRNGIDILVGTPGRIKDHLQNGR--LDLTKLKHVVLDEVDQMLDMG---FA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 24666101 287 EQLDDI----YAACSNPTKCVAFFSATYTVPVAKWALRHLK 323
Cdd:cd17944 155 EQVEEIlsvsYKKDSEDNPQTLLFSATCPDWVYNVAKKYMK 195
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
143-274 |
9.73e-18 |
|
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: 81.15 E-value: 9.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 143 TPIQMQAL-PVLLQRRALMACAPTGSGKTLAFLTPIINGLRAHKTtglRALVLAPTRELAQQIYRECAELTRETGLR-TH 220
Cdd:cd17921 3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRALATSGG---KAVYIAPTRALVNQKEADLRERFGPLGKNvGL 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 24666101 221 FISKVSEAKQKhgaecKQRYDILVSTPNRVRFLLQQEPPLLdLSHVEWFVLDEA 274
Cdd:cd17921 80 LTGDPSVNKLL-----LAEADILVATPEKLDLLLRNGGERL-IQDVRLVVVDEA 127
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
161-309 |
4.40e-17 |
|
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: 78.21 E-value: 4.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 161 ACAPTGSGKTLAFLTPIINGLRahkTTGLRALVLAPTRELAQQIYRECAELTREtGLRTHFISKVSEAKQKHGAEcKQRY 240
Cdd:cd00046 6 ITAPTGSGKTLAALLAALLLLL---KKGKKVLVLVPTKALALQTAERLRELFGP-GIRVAVLVGGSSAEEREKNK-LGDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24666101 241 DILVSTPNRVRFLLQQEpPLLDLSHVEWFVLDEADRLMEEGQNNFKEQLDDIYAACSNPTkcVAFFSAT 309
Cdd:cd00046 81 DIIIATPDMLLNLLLRE-DRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQ--VILLSAT 146
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
127-527 |
1.05e-16 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 83.41 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 127 LPRLQQNLLSRNFDHPTPIQMQALP-VLLQRRALMACAPTGSGKTL-AFLtPIINGLRahktTGLRALVLAPTRELAQQI 204
Cdd:COG1204 8 LEKVIEFLKERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLiAEL-AILKALL----NGGKALYIVPLRALASEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 205 YRECAELTRETGLRthfISKVSEAKQKHGAEcKQRYDILVSTPNRVRFLLQQEPPLLDlsHVEWFVLDEAdrlmeegqnn 284
Cdd:COG1204 83 YREFKRDFEELGIK---VGVSTGDYDSDDEW-LGRYDILVATPEKLDSLLRNGPSWLR--DVDLVVVDEA---------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 285 fkEQLDD------IYAACS-----NPTKCVAFFSAtyTVP----VAKWalrhLK-NLVRIT-------IGVQNSATETVQ 341
Cdd:COG1204 147 --HLIDDesrgptLEVLLArlrrlNPEAQIVALSA--TIGnaeeIAEW----LDaELVKSDwrpvplnEGVLYDGVLRFD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 342 QELLFVGSEGGKLVAirDLVRQGLQppVLVFVQSK-------ERAKQLFEELL-------YDGINVDVIHAERSQHQRD- 406
Cdd:COG1204 219 DGSRRSKDPTLALAL--DLLEEGGQ--VLVFVSSRrdaeslaKKLADELKRRLtpeereeLEELAEELLEVSEETHTNEk 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 407 --NCVK--------------------AFREGSIWVLICTE-LMgrgidfKGVNL----VInydfppttISYIHRIGRT-- 457
Cdd:COG1204 295 laDCLEkgvafhhaglpselrrlvedAFREGLIKVLVATPtLA------AGVNLparrVI--------IRDTKRGGMVpi 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 458 ---------GRAGRPGRaitfftqeDTsnlRGIALIIKNSggtvpeymlqmkkvrKSEAKMRAKKPLDR--EDISTKIRP 526
Cdd:COG1204 361 pvlefkqmaGRAGRPGY--------DP---YGEAILVAKS---------------SDEADELFERYILGepEPIRSKLAN 414
|
.
gi 24666101 527 E 527
Cdd:COG1204 415 E 415
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
138-328 |
2.96e-16 |
|
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: 77.51 E-value: 2.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 138 NFDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFltpIINGLRAHKTT--GLRALVLAPTRELAQQIYRECAELTRET 215
Cdd:cd18045 18 GFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATF---SISVLQCLDIQvrETQALILSPTRELAVQIQKVLLALGDYM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 216 GLRTHF----------ISKVSEAKQkhgaeckqrydILVSTPNRVRFLLQQEPplLDLSHVEWFVLDEADRLMEEGqnnF 285
Cdd:cd18045 95 NVQCHAciggtsvgddIRKLDYGQH-----------IVSGTPGRVFDMIRRRS--LRTRHIKMLVLDEADEMLNKG---F 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 24666101 286 KEQLDDIYAACSNPTKCVaFFSATYTVPVAKWALRHLKNLVRI 328
Cdd:cd18045 159 KEQIYDVYRYLPPATQVV-LVSATLPQDILEMTNKFMTDPIRI 200
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
142-467 |
3.09e-14 |
|
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box helicases found associated with a bacterial ATP-dependent DNA ligase, part of a four-gene system that occurs in about 12 % of prokaryotic reference genomes. The actual motif in this family is DE[VILW]H.
Pssm-ID: 274994 [Multi-domain] Cd Length: 804 Bit Score: 76.05 E-value: 3.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 142 PTPIQMQALPVLLQRRALMACAPTGSGKTLA-FLTPIIN--GLRAHKTTGLRALVLAPTRELAQQIYRECAELTRETGL- 217
Cdd:TIGR04121 14 PRPFQLEMWAAALEGRSGLLIAPTGSGKTLAgFLPSLIDlaGPEAPKEKGLHTLYITPLRALAVDIARNLQAPIEELGLp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 218 -----RTHFISKVSEAKQKhgaecKQRYDILVSTPNRVRFLLQQE--PPLL-DLSHVewfVLDEADRLMEEGQNNFKE-- 287
Cdd:TIGR04121 94 irvetRTGDTSSSERARQR-----KKPPDILLTTPESLALLLSYPdaARLFkDLRCV---VVDEWHELAGSKRGDQLEla 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 288 --QLddiyaACSNPTKCVAFFSATytvpvakwaLRHLKNLVRITIGVQNSATETVQqellfvGSEGGKLVAIRDLVRQGL 365
Cdd:TIGR04121 166 laRL-----RRLAPGLRRWGLSAT---------IGNLEEARRVLLGVGGAPAVLVR------GKLPKAIEVISLLPESEE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 366 QPP----------------------VLVFVQSKERAKQLFEELLYdgINVD---VI---HAERSQHQRDNCVKAFREGSI 417
Cdd:TIGR04121 226 RFPwaghlglralpevyaeidqartTLVFTNTRSQAELWFQALWE--ANPEfalPIalhHGSLDREQRRWVEAAMAAGRL 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 24666101 418 WVLICTELMGRGIDFKGVNLVINYDFPPTTISYIHRIGRTG-RAGRPGRAI 467
Cdd:TIGR04121 304 RAVVCTSSLDLGVDFGPVDLVIQIGSPKGVARLLQRAGRSNhRPGEPSRAL 354
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
139-464 |
1.04e-13 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 74.15 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 139 FDHptpiQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGLRAhkttGLRALVLAPTRELAQQIYRECAELtRETGLR 218
Cdd:PRK01172 24 YDH----QRMAIEQLRKGENVIVSVPTAAGKTLIAYSAIYETFLA----GLKSIYIVPLRSLAMEKYEELSRL-RSLGMR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 219 ThfisKVSEAKQKHGAECKQRYDILVSTPNRVRFLLQQEPPLLDlsHVEWFVLDEADRLMEEGQNNFKEQLDDIyAACSN 298
Cdd:PRK01172 95 V----KISIGDYDDPPDFIKRYDVVILTSEKADSLIHHDPYIIN--DVGLIVADEIHIIGDEDRGPTLETVLSS-ARYVN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 299 PTKCVAFFSATYT--VPVAKW----ALRHLKNLVRITIGVqnsateTVQQELLFVGSEGGKL---VAIRDLVRQGLQppV 369
Cdd:PRK01172 168 PDARILALSATVSnaNELAQWlnasLIKSNFRPVPLKLGI------LYRKRLILDGYERSQVdinSLIKETVNDGGQ--V 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 370 LVFVQSKERAK-------QLFEEL-----------LYDGINVDVI-------HAERSQHQRDNCVKAFREGSIWVLICTE 424
Cdd:PRK01172 240 LVFVSSRKNAEdyaemliQHFPEFndfkvssennnVYDDSLNEMLphgvafhHAGLSNEQRRFIEEMFRNRYIKVIVATP 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 24666101 425 LMGRGIDFKGvNLVINYD---FPPTTISYIHRI---GRTGRAGRPG 464
Cdd:PRK01172 320 TLAAGVNLPA-RLVIVRDitrYGNGGIRYLSNMeikQMIGRAGRPG 364
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
124-467 |
3.76e-13 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 72.44 E-value: 3.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 124 FKMLPRLQQNLLSRNFDHPTPIQMQALPVLLQRRALMACAPTGSGKTLA-FLTPIINGLRAHKTT----GLRALVLAPTR 198
Cdd:COG1201 7 LSLLHPAVRAWFAARFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTLAaFLPALDELARRPRPGelpdGLRVLYISPLK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 199 ELAQQIYRE----CAELTRETGLRTHFIS--------KVSE-AKQKhgaecKQRYDILVSTPNRVRFLLQQEPPLLDLSH 265
Cdd:COG1201 87 ALANDIERNlrapLEEIGEAAGLPLPEIRvgvrtgdtPASErQRQR-----RRPPHILITTPESLALLLTSPDARELLRG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 266 VEWFVLDEadrlmeegqnnfkeqlddIYAACSNptKCVAFFSATytvpVAKwaLRHL--KNLVRITIgvqnSAT----ET 339
Cdd:COG1201 162 VRTVIVDE------------------IHALAGS--KRGVHLALS----LER--LRALapRPLQRIGL----SATvgplEE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 340 VQQELlfVGSEGGKLVAIrdlVRQGLQPP----VLVFVQSKERAKQLFEEL---LYDGInVDVIH--------------A 398
Cdd:COG1201 212 VARFL--VGYEDPRPVTI---VDAGAGKKpdleVLVPVEDLIERFPWAGHLwphLYPRV-LDLIEahrttlvftntrsqA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 399 ER-----------------------SQHQRDNCVKAFREGSIWVLICT---ELmgrGIDFKGVNLVINYDFPPTTISYIH 452
Cdd:COG1201 286 ERlfqrlnelnpedalpiaahhgslSREQRLEVEEALKAGELRAVVATsslEL---GIDIGDVDLVIQVGSPKSVARLLQ 362
|
410
....*....|....*.
gi 24666101 453 RIGRTG-RAGRPGRAI 467
Cdd:COG1201 363 RIGRAGhRVGEVSKGR 378
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
365-469 |
2.15e-12 |
|
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: 62.72 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 365 LQPPVLVFVQSKERAKQLFEELLydginvdvihaersqhqrdncvkafregsiwVLICTELMGRGIDFKGVNLVINYDFP 444
Cdd:cd18785 2 MVVKIIVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDPP 50
|
90 100
....*....|....*....|....*.
gi 24666101 445 PTTISYIHRIGRTGRAG-RPGRAITF 469
Cdd:cd18785 51 SSAASYIQRVGRAGRGGkDEGEVILF 76
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
146-274 |
3.45e-12 |
|
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: 65.30 E-value: 3.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 146 QMQALPVLLQRRALMACAPTGSGKTLAFLTPIINglRAHKTTGLRALVLAPTRELAQQIYRECAELTRETGLRTHFIS-- 223
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILE--ALLRDPGSRALYLYPTKALAQDQLRSLRELLEQLGLGIRVATyd 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24666101 224 --KVSEAKQKHGaecKQRYDILVSTP------------NRVRFllqqepplldLSHVEWFVLDEA 274
Cdd:cd17923 83 gdTPREERRAII---RNPPRILLTNPdmlhyallphhdRWARF----------LRNLRYVVLDEA 134
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
336-474 |
4.05e-12 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 68.63 E-value: 4.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 336 ATETVQQELL----------FVGS--------------EGGKLVAIRDLVRQGLQPPVLVFVQSKERAKQLFEELLYDGI 391
Cdd:COG0514 176 ATPRVRADIAeqlgledprvFVGSfdrpnlrlevvpkpPDDKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGI 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 392 NVDVIHA-----ERSQHQRDncvkaFREGSIWVLICTELMGRGIDFKGVNLVINYDFPPTTISYIHRIGRTGRAGRPGRA 466
Cdd:COG0514 256 RAAAYHAgldaeEREANQDR-----FLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEA 330
|
....*...
gi 24666101 467 ITFFTQED 474
Cdd:COG0514 331 LLLYGPED 338
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
353-467 |
4.67e-12 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 68.99 E-value: 4.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 353 KLVAIRDLVRQGLQPP----VLVFVQSKERAKQLFEELLYDGINVD--VIHAER------SQHQRDNCVKAFREGSIWVL 420
Cdd:COG1111 336 KLSKLREILKEQLGTNpdsrIIVFTQYRDTAEMIVEFLSEPGIKAGrfVGQASKegdkglTQKEQIEILERFRAGEFNVL 415
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 24666101 421 ICTELMGRGIDFKGVNLVINYDFPPTTISYIHRIGRTGRaGRPGRAI 467
Cdd:COG1111 416 VATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGR-KREGRVV 461
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
353-558 |
5.15e-12 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 68.75 E-value: 5.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 353 KLVAIRDLVRQGLQ----PPVLVFVQSKERAKQLFEELLYDGINvdvihAER-------------SQHQRDNCVKAFREG 415
Cdd:PRK13766 348 KLEKLREIVKEQLGknpdSRIIVFTQYRDTAEKIVDLLEKEGIK-----AVRfvgqaskdgdkgmSQKEQIEILDKFRAG 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 416 SIWVLICTELMGRGIDFKGVNLVINYDFPPTTISYIHRIGRTGRaGRPGRAITfftqedtsnlrgiaLIIKnsgGTVPE- 494
Cdd:PRK13766 423 EFNVLVSTSVAEEGLDIPSVDLVIFYEPVPSEIRSIQRKGRTGR-QEEGRVVV--------------LIAK---GTRDEa 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24666101 495 -YMLQMKKVRKSEAKMRA-KKPLDREDISTKIRPETKGDEKHKSTKLKKVERTEKILKNRKGYEKD 558
Cdd:PRK13766 485 yYWSSRRKEKKMKEELKNlKGILNKKLQELDEEQKGEEEEKDEQLSLDDFVKSKGKEEEEEEEKEE 550
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
343-470 |
8.83e-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: 62.61 E-value: 8.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 343 ELLFVGSEGGKLVAIRDLVRQGLQPPVLVFVQSKERAKQLFEELLYDGINVDVIHAERSQHQRDNCVKAFREGSIWVLIC 422
Cdd:cd18794 7 SVRPKDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVA 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 24666101 423 TELMGRGIDFKGVNLVINYDFPPTTISYIHRIGRTGRAGRPGRAITFF 470
Cdd:cd18794 87 TVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
157-273 |
1.17e-11 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 63.37 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 157 RALMACAPTGSGKTLAFLTPIINGLRAHKTTGLRALVLAPTRELAQQIYR------ECAELTRETGLRTHFISKVSEAKQ 230
Cdd:cd17922 2 RNVLIAAPTGSGKTEAAFLPALSSLADEPEKGVQVLYISPLKALINDQERrleeplDEIDLEIPVAVRHGDTSQSEKAKQ 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 24666101 231 KhgaecKQRYDILVSTPNRVRFLLQQEPPLLDLSHVEWFVLDE 273
Cdd:cd17922 82 L-----KNPPGILITTPESLELLLVNKKLRELFAGLRYVVVDE 119
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
101-320 |
2.29e-11 |
|
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: 63.89 E-value: 2.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 101 YGIRVLGKNVPPPVDSFGTLtRDFKMLPRLQQNLLSRNFDHPTPIQMQALPVLLQR--RALMACAPTGSGKTLAFLTPII 178
Cdd:cd18048 1 HRVEVLQRDPTSPLFSVKSF-EELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAML 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 179 NGLRAHKTTGlRALVLAPTRELA-------QQIYRECAELTRETGLRTHFISKVSEAKQKhgaeckqrydILVSTPNRVR 251
Cdd:cd18048 80 SRVDALKLYP-QCLCLSPTFELAlqtgkvvEEMGKFCVGIQVIYAIRGNRPGKGTDIEAQ----------IVIGTPGTVL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24666101 252 ---FLLQqeppLLDLSHVEWFVLDEADRLME-EGQNNfkeqlDDIYAACSNPTKC-VAFFSATYTVPVAKWALR 320
Cdd:cd18048 149 dwcFKLR----LIDVTNISVFVLDEADVMINvQGHSD-----HSVRVKRSMPKECqMLLFSATFEDSVWAFAER 213
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
369-467 |
3.39e-11 |
|
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: 61.22 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 369 VLVFVQSKERAKQLFEELLYDGINVDVI----HAER------SQHQRDNCVKAFREGSIWVLICTELMGRGIDFKGVNLV 438
Cdd:cd18801 33 VIIFSEFRDSAEEIVNFLSKIRPGIRATrfigQASGksskgmSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLI 112
|
90 100
....*....|....*....|....*....
gi 24666101 439 INYDFPPTTISYIHRIGRTGRaGRPGRAI 467
Cdd:cd18801 113 ICYDASPSPIRMIQRMGRTGR-KRQGRVV 140
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
352-455 |
2.27e-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: 58.64 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 352 GKLVAIRDLVRQGLQPP--VLVFVQSKERAKQLFEELLYDGINVDVIHAERSQHQRDNCVKAFREG-SIWV-LICTELMG 427
Cdd:cd18793 11 GKLEALLELLEELREPGekVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDpDIRVfLLSTKAGG 90
|
90 100 110
....*....|....*....|....*....|....
gi 24666101 428 RGIDFKGVNLVINYDFP--PTT----ISYIHRIG 455
Cdd:cd18793 91 VGLNLTAANRVILYDPWwnPAVeeqaIDRAHRIG 124
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
369-467 |
2.92e-10 |
|
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: 58.81 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 369 VLVFVQSKERAKQLFEEL------LYDGINVDVIHAERSQHQRDNCVKAFREGSIWVLICTELMGRGIDFKGVNLVINYD 442
Cdd:cd18796 41 TLVFTNTRSQAERLAQRLrelcpdRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIG 120
|
90 100
....*....|....*....|....*
gi 24666101 443 FPPTTISYIHRIGRTGRagRPGRAI 467
Cdd:cd18796 121 SPKSVARLLQRLGRSGH--RPGAAS 143
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
144-273 |
4.62e-10 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 58.88 E-value: 4.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 144 PIQMQAL-PVLLQRRALMACAPTGSGKTLAFLTPIINGLRAHKttglRALVLAPTRELAQQIYRECAELtRETGLRThfi 222
Cdd:cd18028 4 PPQAEAVrAGLLKGENLLISIPTASGKTLIAEMAMVNTLLEGG----KALYLVPLRALASEKYEEFKKL-EEIGLKV--- 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 24666101 223 sKVSEAKQKHGAECKQRYDILVSTPNRVRFLLQQEPPLLDLshVEWFVLDE 273
Cdd:cd18028 76 -GISTGDYDEDDEWLGDYDIIVATYEKFDSLLRHSPSWLRD--VGVVVVDE 123
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
352-457 |
1.62e-09 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 60.62 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 352 GKLVAIRDLVRQGLQP--PVLVFVQSKERAKQLFEELLYDGINVDVIHAERSQHQRDNCVKAFREGS-IWV-LICTELMG 427
Cdd:COG0553 533 AKLEALLELLEELLAEgeKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeAPVfLISLKAGG 612
|
90 100 110
....*....|....*....|....*....|....*.
gi 24666101 428 RGIDFKGVNLVINYDFP--PTT----ISYIHRIGRT 457
Cdd:COG0553 613 EGLNLTAADHVIHYDLWwnPAVeeqaIDRAHRIGQT 648
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
349-467 |
1.85e-09 |
|
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: 56.50 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 349 SEGGKLVAirDLVRQGLQppVLVFVQSKERAKQLF----EELLYDGINVDVIHA--------ERSQHQRDncvkaFREGS 416
Cdd:cd18797 22 REAARLFA--DLVRAGVK--TIVFCRSRKLAELLLrylkARLVEEGPLASKVASyragylaeDRREIEAE-----LFNGE 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 24666101 417 IWVLICT---ELmgrGIDFKGVNLVINYDFPPTTISYIHRIGRTGRAGRPGRAI 467
Cdd:cd18797 93 LLGVVATnalEL---GIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKDSLVI 143
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
144-309 |
3.44e-09 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 55.77 E-value: 3.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 144 PIQMQALPVLLQ----RRALMaCAPTGSGKTLAFLTpIINGLRAHKTtglraLVLAPTRELAQQIYRECAELtretgLRT 219
Cdd:cd17926 3 PYQEEALEAWLAhknnRRGIL-VLPTGSGKTLTALA-LIAYLKELRT-----LIVVPTDALLDQWKERFEDF-----LGD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 220 HFISKVSEAKQKHGAECkqryDILVSTPNRVRFLLQQEPPLLDLSHVewFVLDEADRLMEEGqnnFKEQLDDIYAacsnp 299
Cdd:cd17926 71 SSIGLIGGGKKKDFDDA----NVVVATYQSLSNLAEEEKDLFDQFGL--LIVDEAHHLPAKT---FSEILKELNA----- 136
|
170
....*....|
gi 24666101 300 tKCVAFFSAT 309
Cdd:cd17926 137 -KYRLGLTAT 145
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
368-485 |
1.30e-08 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350182 [Multi-domain] Cd Length: 154 Bit Score: 54.10 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 368 PVLVFVQSKERAKQLFEELlydgINVDVIHAERSQHQRDNCVKAFREGSIWVLICTELMGRGID-------FKGVNLVIN 440
Cdd:cd18795 45 PVLVFCSSRKECEKTAKDL----AGIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNlpartviIKGTQRYDG 120
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 24666101 441 YDFPPTTISYIHRIgrTGRAGRPGRaitfftqeDTsnlRGIALII 485
Cdd:cd18795 121 KGYRELSPLEYLQM--IGRAGRPGF--------DT---RGEAIIM 152
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
161-274 |
2.95e-08 |
|
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: 54.19 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 161 ACAPTGSGKTL-------AFLTPIINGLRAHKttglRALVLAPTRELAQQiyrECAELTRETGLRTHFIS---KVSEAKQ 230
Cdd:cd18034 21 VVLPTGSGKTLiavmlikEMGELNRKEKNPKK----RAVFLVPTVPLVAQ---QAEAIRSHTDLKVGEYSgemGVDKWTK 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 24666101 231 KHGAECKQRYDILVSTPNRVRFLLQQEppLLDLSHVEWFVLDEA 274
Cdd:cd18034 94 ERWKEELEKYDVLVMTAQILLDALRHG--FLSLSDINLLIFDEC 135
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
123-320 |
3.45e-08 |
|
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: 53.96 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 123 DFKMLPRLQQNLLSRNFDHPTPIQMQALPVLLQR--RALMACAPTGSGKTLAFLTPIINGLR-AHKTTglRALVLAPTRE 199
Cdd:cd18047 5 ELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEpANKYP--QCLCLSPTYE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 200 LA-------QQIYRECAELTRETGLRTHfiskvseaKQKHGAECKQRydILVSTPNRV-RFLLQQEppLLDLSHVEWFVL 271
Cdd:cd18047 83 LAlqtgkviEQMGKFYPELKLAYAVRGN--------KLERGQKISEQ--IVIGTPGTVlDWCSKLK--FIDPKKIKVFVL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 24666101 272 DEADRLM-EEGQNNFKEQLDDIYaacsnPTKC-VAFFSATYTVPVAKWALR 320
Cdd:cd18047 151 DEADVMIaTQGHQDQSIRIQRML-----PRNCqMLLFSATFEDSVWKFAQK 196
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
370-479 |
3.45e-08 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 56.26 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 370 LVFVQSKERAKQLFEELLYDGINVDVIHAERSQHQRDNCVKAFREGSIWVLICTELMGRGIDFKGVNLVINYDFPPTTIS 449
Cdd:PRK11057 240 IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIES 319
|
90 100 110
....*....|....*....|....*....|
gi 24666101 450 YIHRIGRTGRAGRPGRAITFFTQEDTSNLR 479
Cdd:PRK11057 320 YYQETGRAGRDGLPAEAMLFYDPADMAWLR 349
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
370-460 |
5.52e-08 |
|
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: 52.21 E-value: 5.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 370 LVFVqsKERA-----KQLFEE--LLYDGINVDVI--HAERSQHQRDN--------CVKAFREGSIWVLICTELMGRGIDF 432
Cdd:cd18802 29 IIFV--ERRAtavvlSRLLKEhpSTLAFIRCGFLigRGNSSQRKRSLmtqrkqkeTLDKFRDGELNLLIATSVLEEGIDV 106
|
90 100
....*....|....*....|....*...
gi 24666101 433 KGVNLVINYDFPPTTISYIHRIGRtGRA 460
Cdd:cd18802 107 PACNLVIRFDLPKTLRSYIQSRGR-ARA 133
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
125-432 |
6.68e-08 |
|
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: 55.47 E-value: 6.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 125 KMLPRLQQNLLSRNFDHPTPIQMQALPvlLQRRALMAC--------------APTGSGKTLAFLTPIINGLRAHKttGLR 190
Cdd:COG1203 104 QALDHLLAERLERLLPKKSKPRTPINP--LQNEALELAleaaeeepglfiltAPTGGGKTEAALLFALRLAAKHG--GRR 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 191 ALVLAPTRELAQQIYRECAELTRET-----GLRTHFISKVSEAKQKHGAECKQR-----YDILVSTPnrVRFLL------ 254
Cdd:COG1203 180 IIYALPFTSIINQTYDRLRDLFGEDvllhhSLADLDLLEEEEEYESEARWLKLLkelwdAPVVVTTI--DQLFEslfsnr 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 255 -QQEPPLLDLSH-VewFVLDEAD-----------RLMEEGQN--------------NFKEQLDDIY-AACSNPTKCVAFF 306
Cdd:COG1203 258 kGQERRLHNLANsV--IILDEVQayppymlalllRLLEWLKNlggsvilmtatlppLLREELLEAYeLIPDEPEELPEYF 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 307 SAtytvpvakwALRHlknlvRITIGVQNSATETVQQELLFVGSEGGKlvairdlvrqglqppVLVFVQSKERAKQLFEEL 386
Cdd:COG1203 336 RA---------FVRK-----RVELKEGPLSDEELAELILEALHKGKS---------------VLVIVNTVKDAQELYEAL 386
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 24666101 387 LYDGINVDVIH-------AERSqhQRDNCVKA-FREGSIWVLICTEL--MGRGIDF 432
Cdd:COG1203 387 KEKLPDEEVYLlhsrfcpADRS--EIEKEIKErLERGKPCILVSTQVveAGVDIDF 440
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
137-273 |
1.92e-07 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 54.12 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 137 RNFDHPTPIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGL-RAHKTTGLR----ALVLAPTRELAQQIYR----- 206
Cdd:PRK13767 28 EKFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIIDELfRLGREGELEdkvyCLYVSPLRALNNDIHRnleep 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 207 --ECAELTRETGL---------RThfiSKVSEA-KQK------HgaeckqrydILVSTPNRVRFLLQQEPPLLDLSHVEW 268
Cdd:PRK13767 108 ltEIREIAKERGEelpeirvaiRT---GDTSSYeKQKmlkkppH---------ILITTPESLAILLNSPKFREKLRTVKW 175
|
....*
gi 24666101 269 FVLDE 273
Cdd:PRK13767 176 VIVDE 180
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
145-217 |
3.15e-07 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350781 [Multi-domain] Cd Length: 206 Bit Score: 51.20 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 145 IQMQALPVLLQ-RRALMACAPTGSGKTLAFLTPIINGLR---AHKTTGLRALVLAPTRELAQQIYRE-----------CA 209
Cdd:cd18023 5 IQSEVFPDLLYsDKNFVVSAPTGSGKTVLFELAILRLLKernPLPWGNRKVVYIAPIKALCSEKYDDwkekfgplglsCA 84
|
....*...
gi 24666101 210 ELTRETGL 217
Cdd:cd18023 85 ELTGDTEM 92
|
|
| ComFA |
COG4098 |
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ... |
368-475 |
3.97e-07 |
|
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, recombination and repair];
Pssm-ID: 443274 [Multi-domain] Cd Length: 451 Bit Score: 52.57 E-value: 3.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 368 PVLVFVQSKERAKQLFEEL--LYDGINVDVIHAERSQhqRDNCVKAFREGSIWVLICTELMGRGIDFKGVN-LVINYDfp 444
Cdd:COG4098 321 QLLIFVPTIELLEQLVALLqkLFPEERIAGVHAEDPE--RKEKVQAFRDGEIPILVTTTILERGVTFPNVDvAVLGAD-- 396
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 24666101 445 pttisyiHRI----------GRTGR-AGRPGRAITFFTQEDT 475
Cdd:COG4098 397 -------HPVfteaalvqiaGRVGRsADYPTGEVIFFHHGKT 431
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
132-246 |
9.15e-07 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 49.34 E-value: 9.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 132 QNLLSRNFDHPTPIQMQALPVLLQ------RRALMACAPTGSGKTLAFLTPIINGLRAHKttglRALVLAPTRELAQQIY 205
Cdd:cd17918 6 QELCKSLPFSLTKDQAQAIKDIEKdlhspePMDRLLSGDVGSGKTLVALGAALLAYKNGK----QVAILVPTEILAHQHY 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 24666101 206 RECAELTREtgLRTHFISKVSEAKQKHGAeckqryDILVST 246
Cdd:cd17918 82 EEARKFLPF--INVELVTGGTKAQILSGI------SLLVGT 114
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
129-478 |
1.96e-06 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 50.97 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 129 RLQQNLLSRNFDHPTPIQMQALPV-LLQRRALMACAPTGSGKTLAFLTPIINGLRahkTTGLRALVLAPTRELAQQIYRE 207
Cdd:PRK00254 11 RIKRVLKERGIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIVMVNKLL---REGGKAVYLVPLKALAEEKYRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 208 CAELtRETGLRTHFISKVSEAKQkhgaECKQRYDILVSTPNRVRFLLQQEPPLldLSHVEWFVLDEADRLmeeGQNNFKE 287
Cdd:PRK00254 88 FKDW-EKLGLRVAMTTGDYDSTD----EWLGKYDIIIATAEKFDSLLRHGSSW--IKDVKLVVADEIHLI---GSYDRGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 288 QLDDIYAACSNPTKCVAfFSATYTVP--VAKWALRHLK----NLVRITIGVQNSAtetvqqellFVGSEGGKLVA----- 356
Cdd:PRK00254 158 TLEMILTHMLGRAQILG-LSATVGNAeeLAEWLNAELVvsdwRPVKLRKGVFYQG---------FLFWEDGKIERfpnsw 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 357 ---IRDLVRQGLQppVLVFVQSKERA-----------------------KQLFEELLYDGIN----------VDVIHAER 400
Cdd:PRK00254 228 eslVYDAVKKGKG--ALVFVNTRRSAekealelakkikrfltkpelralKELADSLEENPTNeklkkalrggVAFHHAGL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 401 SQHQRDNCVKAFREGSIWVLICTELMGRGIDFKGVNLVIN-----YDFPPTTISYIHRIGRTGRAGRP-----GRAITFF 470
Cdd:PRK00254 306 GRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRdtkrySNFGWEDIPVLEIQQMMGRAGRPkydevGEAIIVA 385
|
....*...
gi 24666101 471 TQEDTSNL 478
Cdd:PRK00254 386 TTEEPSKL 393
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
163-458 |
2.57e-06 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 50.69 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 163 APTGSGKTLA-FLTPIINGLR--------AHKTTGLRALVLAPTRELAQQIYREC----------------AELTRETGL 217
Cdd:PRK09751 3 APTGSGKTLAaFLYALDRLFReggedtreAHKRKTSRILYISPIKALGTDVQRNLqiplkgiaderrrrgeTEVNLRVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 218 RTHFISKVSEAKQkhgaeCKQRYDILVSTPNRVrFLLQQEPPLLDLSHVEWFVLDEADRLMEEGQNNFK----EQLDDIY 293
Cdd:PRK09751 83 RTGDTPAQERSKL-----TRNPPDILITTPESL-YLMLTSRARETLRGVETVIIDEVHAVAGSKRGAHLalslERLDALL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 294 ---------AACSNPTKCVAFF--SATYTVPVAKWALRHLKnlVRITIGVQNSATETVQQELLFVGSEGGKLVAIRDLVR 362
Cdd:PRK09751 157 htsaqriglSATVRSASDVAAFlgGDRPVTVVNPPAMRHPQ--IRIVVPVANMDDVSSVASGTGEDSHAGREGSIWPYIE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 363 QGLQPPVL------VFVQSKERAKQLFEEL--LY-------DGINVDVIHAE------------------RSQH------ 403
Cdd:PRK09751 235 TGILDEVLrhrstiVFTNSRGLAEKLTARLneLYaarlqrsPSIAVDAAHFEstsgatsnrvqssdvfiaRSHHgsvske 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 24666101 404 QRDNCVKAFREGSIWVLICTELMGRGIDFKGVNLVINYDFPPTTISYIHRIGRTG 458
Cdd:PRK09751 315 QRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
127-276 |
1.64e-05 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 48.01 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 127 LPRLQQNLLSRNFDhPTPIQMQALPVLLQRRALMACAPTGSGKTLAfltpiinGLRAHKT---TGLRALVLAPTRELAQQ 203
Cdd:COG4581 12 LEALADFAEERGFE-LDPFQEEAILALEAGRSVLVAAPTGSGKTLV-------AEFAIFLalaRGRRSFYTAPIKALSNQ 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24666101 204 IYRE-CAELTRET-GLRTHFISKVSEAkqkhgaeckqryDILVSTPNRVRFLLQQEPPllDLSHVEWFVLDE----ADR 276
Cdd:COG4581 84 KFFDlVERFGAENvGLLTGDASVNPDA------------PIVVMTTEILRNMLYREGA--DLEDVGVVVMDEfhylADP 148
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
142-285 |
2.05e-05 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 45.89 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 142 PTPIQMQ-ALPVLLQRRALMaCAPTGSGKTLAFLTPIINGLRAHKTT-GLRALVLAPTRELAQQIYRECAELTRETGLRT 219
Cdd:cd17927 3 PRNYQLElAQPALKGKNTII-CLPTGSGKTFVAVLICEHHLKKFPAGrKGKVVFLANKVPLVEQQKEVFRKHFERPGYKV 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24666101 220 HFISKVSEAKQKHGAECKqRYDILVSTPNR-VRFLLQQEPPllDLSHVEWFVLDEADRLMEEGQNNF 285
Cdd:cd17927 82 TGLSGDTSENVSVEQIVE-SSDVIIVTPQIlVNDLKSGTIV--SLSDFSLLVFDECHNTTKNHPYNE 145
|
|
| DinG |
COG1199 |
Rad3-related DNA helicase DinG [Replication, recombination and repair]; |
153-206 |
3.41e-04 |
|
Rad3-related DNA helicase DinG [Replication, recombination and repair];
Pssm-ID: 440812 [Multi-domain] Cd Length: 629 Bit Score: 43.76 E-value: 3.41e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 24666101 153 LLQRRALMACAPTGSGKTLAFLTPiinGLRAHKTTGLRALVLAPTRELAQQIYR 206
Cdd:COG1199 30 LAEGRHLLIEAGTGTGKTLAYLVP---ALLAARETGKKVVISTATKALQEQLVE 80
|
|
| Cas3_I-D |
cd09710 |
CRISPR/Cas system-associated protein Cas3; Distinct diverged subfamily of Cas3 helicase domain; ... |
163-218 |
4.27e-04 |
|
CRISPR/Cas system-associated protein Cas3; Distinct diverged subfamily of Cas3 helicase domain; 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; Diverged DNA helicase Cas3'; signature gene for Type I and subtype I-D
Pssm-ID: 187841 [Multi-domain] Cd Length: 353 Bit Score: 42.94 E-value: 4.27e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 24666101 163 APTGSGKTLAFLTPIINGlrahkttGLRALVLAPTRELAQQIYRECAELTRETGLR 218
Cdd:cd09710 21 APTGAGKTLAWLTPLLHG-------ENKAIALYPTNALIEDQTEAIKEFVDDANPR 69
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
142-293 |
4.43e-04 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 41.12 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 142 PTPIQMQALPVLL-----QRRALMACAPTGSGKTLAFLTpIINGLRaHKTTGLRALVLAPTRELAQQIYRECAELTREtg 216
Cdd:pfam04851 4 LRPYQIEAIENLLesiknGQKRGLIVMATGSGKTLTAAK-LIARLF-KKGPIKKVLFLVPRKDLLEQALEEFKKFLPN-- 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24666101 217 lrTHFISKVSEAKQKHgaECKQRYDILVSTPNRV--RFLLQQEPPLLDLSHVewFVLDEADRLMEEGQNNFKEQLDDIY 293
Cdd:pfam04851 80 --YVEIGEIISGDKKD--ESVDDNKIVVTTIQSLykALELASLELLPDFFDV--IIIDEAHRSGASSYRNILEYFKPAF 152
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
139-207 |
4.65e-04 |
|
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350779 [Multi-domain] Cd Length: 191 Bit Score: 41.48 E-value: 4.65e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24666101 139 FDHPTPIQMQALPVLLQRRA-LMACAPTGSGKT----LAFltpiingLRAHKTTG-LRALVLAPTRELAQQIYRE 207
Cdd:cd18021 1 FKFFNPIQTQVFNSLYNTDDnVFVGAPTGSGKTvcaeLAL-------LRHWRQNPkGRAVYIAPMQELVDARYKD 68
|
|
| VirD4 |
COG3505 |
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ... |
160-214 |
4.97e-04 |
|
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442728 [Multi-domain] Cd Length: 402 Bit Score: 42.66 E-value: 4.97e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 24666101 160 MACAPTGSGKTLAFLTPIINGLRAhkttGLRALVLAPTRELAQQIYRECAELTRE 214
Cdd:COG3505 3 LVIGPTGSGKTVGLVIPNLTQLAR----GESVVVTDPKGDLAELTAGFRRRAGYD 53
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
341-470 |
7.60e-04 |
|
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: 40.31 E-value: 7.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 341 QQELLFVGSEGgKLVAIRDLVRQGLQP-PVLVFVQSKERAKQLFEELLYDGINVDVIHAERSQHqrdncVKAFREGSIWV 419
Cdd:cd18789 24 KRRLLAAMNPN-KLRALEELLKRHEQGdKIIVFTDNVEALYRYAKRLLKPFITGETPQSEREEI-----LQNFREGEYNT 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 24666101 420 LICTELMGRGIDFKGVNLVInydfpptTIS--------YIHRIGRTGRAGRPGRAITFF 470
Cdd:cd18789 98 LVVSKVGDEGIDLPEANVAI-------QISghggsrrqEAQRLGRILRPKKGGGKNAFF 149
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
346-474 |
9.36e-04 |
|
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: 40.02 E-value: 9.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 346 FVGSEGGKLV--AIRDLVRQGLQppvlVF-----VQSKERAKQLFEELLYDgINVDVIHAERSQHQRDNCVKAFREGSIW 418
Cdd:cd18810 5 YVMPYDDELIreAIERELLRGGQ----VFyvhnrIESIEKLATQLRQLVPE-ARIAIAHGQMTENELEEVMLEFAKGEYD 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 24666101 419 VLICTELMGRGIDFKGVNLVINYDFPPTTISYIHRI-GRTGRAGRpgRAITFFTQED 474
Cdd:cd18810 80 ILVCTTIIESGIDIPNANTIIIERADKFGLAQLYQLrGRVGRSKE--RAYAYFLYPD 134
|
|
| cas3_cyano |
TIGR03158 |
CRISPR-associated helicase Cas3, subtype CYANO; CRISPR (Clustered Regularly Interspaced Short ... |
163-211 |
1.28e-03 |
|
CRISPR-associated helicase Cas3, subtype CYANO; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) is a widespread family of prokaryotic direct repeats with spacers of unique sequence between consecutive repeats. This protein family is a CRISPR-associated (Cas) family strictly associated with the Cyano subtype of CRISPR/Cas locus, found in several species of Cyanobacteria and several archaeal species. It contains helicase motifs and appears to represent the Cas3 protein of the Cyano subtype of CRISPR/Cas system.
Pssm-ID: 274457 [Multi-domain] Cd Length: 357 Bit Score: 41.42 E-value: 1.28e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 24666101 163 APTGSGKTLAFLTPIINGlrahkttGLRALVLAPTRELAQQIYRECAEL 211
Cdd:TIGR03158 21 APTGAGKTLAWLTPLLHG-------ENDTIALYPTNALIEDQTEAIKEF 62
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
146-289 |
1.28e-03 |
|
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an IFN-inducible cytoplasmic helicase that plays a role in RIG-I-mediated type I interferon (IFN) nuclease-mediated viral RNA degradation. DDX60 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: 350783 [Multi-domain] Cd Length: 192 Bit Score: 40.43 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 146 QMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGLRAHKTtglRALV-LAPTRELAQQIYRE-CAELTRETGLRTHFIS 223
Cdd:cd18025 6 QRELLDIVDRRESALIVAPTSSGKTFISYYCMEKVLRESDD---GVVVyVAPTKALVNQVVAEvYARFSKKYPPSGKSLW 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24666101 224 KVseAKQKHGAECKQRYDILVSTPNRVRFLLQQEPPLLDLSHVEWFVLDEADRLMEEGQNNFKEQL 289
Cdd:cd18025 83 GV--FTRDYRHNNPMNCQVLITVPECLEILLLSPHNASWVPRIKYVIFDEIHSIGQSEDGAVWEQL 146
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
153-276 |
1.45e-03 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 41.48 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 153 LLQRRALMACAPTGSGKTL----AFLTPIINGlrahkttGlRALVLAPTRELAQQIYRECAELTrETGLRThfisKVSEA 228
Cdd:PRK02362 36 LLDGKNLLAAIPTASGKTLiaelAMLKAIARG-------G-KALYIVPLRALASEKFEEFERFE-ELGVRV----GISTG 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 24666101 229 KQKHGAECKQRYDILVSTPNRVRFLLQQEPPLL-DLSHV---EWFVLDEADR 276
Cdd:PRK02362 103 DYDSRDEWLGDNDIIVATSEKVDSLLRNGAPWLdDITCVvvdEVHLIDSANR 154
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
357-459 |
1.47e-03 |
|
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350177 [Multi-domain] Cd Length: 171 Bit Score: 39.92 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 357 IRDLVRQGLQppVLVFVQSKERAKQLFEELLYDGINVDVIHAERSQHQRDNCVKAFREGSIWVLICTELMGRGIDFKGVN 436
Cdd:cd18790 20 IRKRVARGER--VLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVS 97
|
90 100
....*....|....*....|....*...
gi 24666101 437 LVINYD-----FPPTTISYIHRIGRTGR 459
Cdd:cd18790 98 LVAILDadkegFLRSETSLIQTIGRAAR 125
|
|
| SF2_C_priA |
cd18804 |
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ... |
377-467 |
1.50e-03 |
|
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350191 [Multi-domain] Cd Length: 238 Bit Score: 40.69 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 377 ERAKQLFEELLYDGINVDVIhaeRSQHQRDNCVKAFREGSIWVLICTELMGRGIDFKGVNLV--INYDFPPTTISY---- 450
Cdd:cd18804 108 EELKTLFPEARIARIDRDTT---RKKGALEKLLDQFERGEIDILIGTQMIAKGLDFPNVTLVgiLNADSGLNSPDFrase 184
|
90 100
....*....|....*....|...
gi 24666101 451 -----IHRI-GRTGRAGRPGRAI 467
Cdd:cd18804 185 rafqlLTQVsGRAGRGDKPGKVI 207
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
376-467 |
1.55e-03 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350179 [Multi-domain] Cd Length: 160 Bit Score: 39.56 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 376 KERAKQLFEELlydgiNVDVIHAERSQHQRDNCVKAFREGSIWVLICTELMGRGIDFKGVNLVINYDFPPTTISYIHRI- 454
Cdd:cd18792 51 AEELKELVPEA-----RVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFGLSQLHQLr 125
|
90
....*....|...
gi 24666101 455 GRTGRAGRPGRAI 467
Cdd:cd18792 126 GRVGRGKHQSYCY 138
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
145-276 |
1.55e-03 |
|
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: 39.81 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 145 IQMQALPVLLQRRALMACAPTGSGKTLAFLTPIINGLRAHKTtglRALVLAPTRELAQQIYrecAELTRETGLRTHFISK 224
Cdd:cd18035 5 LYQVLIAAVALNGNTLIVLPTGLGKTIIAILVAADRLTKKGG---KVLILAPSRPLVEQHA---ENLKRVLNIPDKITSL 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 24666101 225 VSEAKQKHGAECKQRYDILVSTPNRVRFLLQQEPplLDLSHVEWFVLDEADR 276
Cdd:cd18035 79 TGEVKPEERAERWDASKIIVATPQVIENDLLAGR--ITLDDVSLLIFDEAHH 128
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|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
392-463 |
2.72e-03 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 38.86 E-value: 2.72e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24666101 392 NVDVIHAERSQHQRDNCVKAFREGSIWVLICTELMGRGIDFKGVNLVINYDFPPTTISYIHRI-GRTGRAGRP 463
Cdd:cd18811 63 NVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLHQLrGRVGRGDHQ 135
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
159-207 |
3.03e-03 |
|
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 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: 350688 [Multi-domain] Cd Length: 186 Bit Score: 39.20 E-value: 3.03e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 24666101 159 LMACAPTGSGKTLAFLTPiinGLRAHKTTGLRALVLA-PTRELAQQIYRE 207
Cdd:cd17930 4 VILEAPTGSGKTEAALLW---ALKLAARGGKRRIIYAlPTRATINQMYER 50
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|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
133-283 |
3.20e-03 |
|
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: 39.16 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 133 NLLSRNFDHPT--PIQMQALPVLLQRRALMACAPTGSGKTLAFLTPIIngLRAHKTTGLrALVLAP--------TRELAQ 202
Cdd:cd18018 2 KLLRRVFGHPSfrPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPAL--LLRRRGPGL-TLVVSPlialmkdqVDALPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 203 QIYRECAELTRETGLRTHFISKVseakqkHGAECKqrydILVSTPNR-----VRFLLQQEPPlldlshVEWFVLDEADRL 277
Cdd:cd18018 79 AIKAAALNSSLTREERRRILEKL------RAGEVK----ILYVSPERlvnesFRELLRQTPP------ISLLVVDEAHCI 142
|
....*.
gi 24666101 278 MEEGQN 283
Cdd:cd18018 143 SEWSHN 148
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
153-283 |
4.02e-03 |
|
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350682 [Multi-domain] Cd Length: 189 Bit Score: 38.85 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 153 LLQRRALMACAPTGSGKTlAFLTpIINGLRAHKttGLRALVLAPTRELAQQIYRECAELTRETGLRTH--FISKVSEAKQ 230
Cdd:cd17924 29 LLRGKSFAIIAPTGVGKT-TFGL-ATSLYLASK--GKRSYLIFPTKSLVKQAYERLSKYAEKAGVEVKilVYHSRLKKKE 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666101 231 KHGAECKQR---YDILVST----PNRVRFLLQQEPPLLdlshvewFVlDEADRLMEEGQN 283
Cdd:cd17924 105 KEELLEKIEkgdFDILVTTnqflSKNFDLLSNKKFDFV-------FV-DDVDAVLKSSKN 156
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