|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
149-567 |
3.77e-149 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 441.12 E-value: 3.77e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 149 SFEQMNLSRQILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERMIYRPKGAscTRVLVLVPT 228
Cdd:COG0513 3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRA--PQALILAPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 229 RELAIQVFQVFRKLSTFIQLEVCLCAGGLDLKAQEAALRSGPDVVVATPGRLIDHLHNSpSFNLSNIEVLVLDEADRMLE 308
Cdd:COG0513 81 RELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERG-ALDLSGVETLVLDEADRMLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 309 EAFRDQMNELIRLCAQNRQTLLFSATMTEEIDELASMSLQKPVKIFINENTDTALKLRQEFIRIRagrETDREAMVAALV 388
Cdd:COG0513 160 MGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVD---KRDKLELLRRLL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 389 TRTFQTNTIVFVRTKKDCQRMQILLGLLGIKVGQMQSSLTQGQRIESLSKFKKAEIDVLVSTDLASRGLDIEGVQTVINM 468
Cdd:COG0513 237 RDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 469 NMPKSIKQYIHRVGRTARAGKAGRSISLVGEDERKLLKEIvnsnaDRTLKQRL---VAPEVVEAYRRRIDELEETIQQID 545
Cdd:COG0513 317 DLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAI-----EKLIGQKIeeeELPGFEPVEEKRLERLKPKIKEKL 391
|
410 420
....*....|....*....|..
gi 392884823 546 EEDRAEKELRIAEASMAKTQNA 567
Cdd:COG0513 392 KGKKAGRGGRPGPKGERKARRG 413
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
159-354 |
3.95e-120 |
|
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: 358.11 E-value: 3.95e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 159 ILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERMIYRPKGASCTRVLVLVPTRELAIQVFQV 238
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAATRVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 239 FRKLSTFIQLEVCLCAGGLDLKAQEAALRSGPDVVVATPGRLIDHLHNSPSFNLSNIEVLVLDEADRMLEEAFRDQMNEL 318
Cdd:cd17947 81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSFDLDSIEILVLDEADRMLEEGFADELKEI 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 392884823 319 IRLCAQNRQTLLFSATMTEEIDELASMSLQKPVKIF 354
Cdd:cd17947 161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRVF 196
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
159-353 |
4.44e-88 |
|
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: 275.09 E-value: 4.44e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 159 ILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERMIYRPKGA-SCTRVLVLVPTRELAIQVFQ 237
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKgRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 238 VFRKLSTFIQLEVCLCAGGLDLKAQEAALRSGPDVVVATPGRLIDHLHNSpSFNLSNIEVLVLDEADRMLEEAFRDQMNE 317
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERG-KLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 392884823 318 LIRLCAQNRQTLLFSATMTEEIDELASMSLQKPVKI 353
Cdd:cd00268 160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
149-508 |
1.20e-86 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 280.92 E-value: 1.20e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 149 SFEQMNLSRQILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERMiyrpkGASCTRV--LVLV 226
Cdd:PRK11776 5 AFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL-----DVKRFRVqaLVLC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 227 PTRELAIQVFQVFRKLSTFIQ----LEVClcaGGLDLKAQEAALRSGPDVVVATPGRLIDHLHNSpSFNLSNIEVLVLDE 302
Cdd:PRK11776 80 PTRELADQVAKEIRRLARFIPnikvLTLC---GGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKG-TLDLDALNTLVLDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 303 ADRMLEEAFRDQMNELIRLCAQNRQTLLFSATMTEEIDELASMSLQKPVKIFInENTDTALKLRQEFIRIragRETDREA 382
Cdd:PRK11776 156 ADRMLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKV-ESTHDLPAIEQRFYEV---SPDERLP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 383 MVAALVtRTFQ-TNTIVFVRTKKDCQRMQILLGLLGIKVGQMQSSLTQGQRIESLSKFKKAEIDVLVSTDLASRGLDIEG 461
Cdd:PRK11776 232 ALQRLL-LHHQpESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKA 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 392884823 462 VQTVINMNMPKSIKQYIHRVGRTARAGKAGRSISLVGEDERKLLKEI 508
Cdd:PRK11776 311 LEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAI 357
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
150-538 |
8.37e-86 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 277.59 E-value: 8.37e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 150 FEQMNLSRQILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERMI-YRPKGASCTRVLVLVPT 228
Cdd:PRK11192 3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLdFPRRKSGPPRILILTPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 229 RELAIQVFQVFRKLSTFIQLEVCLCAGGLDLKAQEAALRSGPDVVVATPGRLIDHLHNSpSFNLSNIEVLVLDEADRMLE 308
Cdd:PRK11192 83 RELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEE-NFDCRAVETLILDEADRMLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 309 EAFRDQMNELIRLCAQNRQTLLFSATMT-EEIDELASMSLQKPVKIfineNTDTALKLR---QEFIRiRAGRETDREAMV 384
Cdd:PRK11192 162 MGFAQDIETIAAETRWRKQTLLFSATLEgDAVQDFAERLLNDPVEV----EAEPSRRERkkiHQWYY-RADDLEHKTALL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 385 AALVTRTFQTNTIVFVRTKkdcQRMQILLGLL---GIKVGQMQSSLTQGQRIESLSKFKKAEIDVLVSTDLASRGLDIEG 461
Cdd:PRK11192 237 CHLLKQPEVTRSIVFVRTR---ERVHELAGWLrkaGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDD 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392884823 462 VQTVINMNMPKSIKQYIHRVGRTARAGKAGRSISLVGEDERKLLKEIvnsnaDRTLKQRLvapevveaYRRRIDELE 538
Cdd:PRK11192 314 VSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKI-----ERYIEEPL--------KARVIDELR 377
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
148-519 |
4.68e-83 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 271.30 E-value: 4.68e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 148 VSFEQMNLSRQILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERMIYR---PKGASCTRVLV 224
Cdd:PRK10590 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRqphAKGRRPVRALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 225 LVPTRELAIQVFQVFRKLSTFIQLEVCLCAGGLDLKAQEAALRSGPDVVVATPGRLIDHLHNSpSFNLSNIEVLVLDEAD 304
Cdd:PRK10590 81 LTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQN-AVKLDQVEILVLDEAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 305 RMLEEAFRDQMNELIRLCAQNRQTLLFSATMTEEIDELASMSLQKPVKIFINENTDTALKLRQ--EFIRIRAGREtdrea 382
Cdd:PRK10590 160 RMLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQhvHFVDKKRKRE----- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 383 MVAALVTRTFQTNTIVFVRTKKDCQRMQILLGLLGIKVGQMQSSLTQGQRIESLSKFKKAEIDVLVSTDLASRGLDIEGV 462
Cdd:PRK10590 235 LLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEEL 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 392884823 463 QTVINMNMPKSIKQYIHRVGRTARAGKAGRSISLVGEDERKLLKEIvnsnaDRTLKQ 519
Cdd:PRK10590 315 PHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDI-----EKLLKK 366
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
147-662 |
9.70e-78 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 260.65 E-value: 9.70e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 147 NVSFEQMNLSRQILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERMIYRPKGASCT----RV 222
Cdd:PRK04537 8 DLTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALADRKpedpRA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 223 LVLVPTRELAIQVFQVFRKLSTFIQLEVCLCAGGLDLKAQEAALRSGPDVVVATPGRLIDHLHNSPSFNLSNIEVLVLDE 302
Cdd:PRK04537 88 LILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVVSLHACEICVLDE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 303 ADRMLEEAFRDQMNELIRLCAQ--NRQTLLFSATMTEEIDELASMSLQKPVKIFINENTDTALKLRQefiRIRAGRETDR 380
Cdd:PRK04537 168 ADRMFDLGFIKDIRFLLRRMPErgTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQ---RIYFPADEEK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 381 EAMVAALVTRTFQTNTIVFVRTKKDCQRMQILLGLLGIKVGQMQSSLTQGQRIESLSKFKKAEIDVLVSTDLASRGLDIE 460
Cdd:PRK04537 245 QTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHID 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 461 GVQTVINMNMPKSIKQYIHRVGRTARAGKAGRSISLVGED------------ERKLLKEIVNSNADRTLKQrlvAPEVVE 528
Cdd:PRK04537 325 GVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERyamslpdieayiEQKIPVEPVTAELLTPLPR---PPRVPV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 529 AYRRRIDELEETIQQIDEEDRAEKELRIAEASMAKTQNALEVGENGGAPAERRVWMMKESQIEKQRKR--EEKRQMKVDA 606
Cdd:PRK04537 402 EGEEADDEAGDSVGTIFREAREQRAAEEQRRGGGRSGPGGGSRSGSVGGGGRRDGAGADGKPRPRRKPrvEGEADAAAAG 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 607 RKK----AEAAKTPEDIQIEHEaafhvRAAKRARHSKNKRIRAVVESAGTKGAGKAAQNK 662
Cdd:PRK04537 482 AETpvvaAAAAQAPGVVAADGE-----RAPRKRRRRRNGRPVEGAEPVSTPVPAPAAPRK 536
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
144-572 |
6.30e-76 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 257.08 E-value: 6.30e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 144 TSVNVSFEQMNLSRQILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERMIYRPKGAsctRVL 223
Cdd:PRK11634 2 AEFETTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAP---QIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 224 VLVPTRELAIQVFQVFRKLSTFIQ-LEVCLCAGGLDLKAQEAALRSGPDVVVATPGRLIDHLHNSpSFNLSNIEVLVLDE 302
Cdd:PRK11634 79 VLAPTRELAVQVAEAMTDFSKHMRgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRG-TLDLSKLSGLVLDE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 303 ADRMLEEAFRDQMNELIRLCAQNRQTLLFSATMTEEIDELASMSLQKPVKIFINENTDTALKLRQEFIRIRAGRETdrEA 382
Cdd:PRK11634 158 ADEMLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKN--EA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 383 MVAALVTRTFQTnTIVFVRTKKDCQRMQILLGLLGIKVGQMQSSLTQGQRIESLSKFKKAEIDVLVSTDLASRGLDIEGV 462
Cdd:PRK11634 236 LVRFLEAEDFDA-AIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 463 QTVINMNMPKSIKQYIHRVGRTARAGKAGRSISLVGEDERKLLKeivnsNADRTLKqrLVAPEV----VEAY-RRRIDEL 537
Cdd:PRK11634 315 SLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLR-----NIERTMK--LTIPEVelpnAELLgKRRLEKF 387
|
410 420 430
....*....|....*....|....*....|....*
gi 392884823 538 EETIQQIDEedraEKELRIAEASMAKTQNALEVGE 572
Cdd:PRK11634 388 AAKVQQQLE----SSDLDQYRALLAKIQPTAEGEE 418
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
149-353 |
1.28e-73 |
|
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: 237.21 E-value: 1.28e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 149 SFEQMNLSRQILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERMIYRPKGASCtrvLVLVPT 228
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFA---LVLAPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 229 RELAIQVFQVFRKLSTFIQLEVCLCAGGLDLKAQEAALRSGPDVVVATPGRLIDHLHNSPSFNLSNIEVLVLDEADRMLE 308
Cdd:cd17954 78 RELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKGFSLKSLKFLVMDEADRLLN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 392884823 309 EAFRDQMNELIRLCAQNRQTLLFSATMTEEIDELASMSLQKPVKI 353
Cdd:cd17954 158 MDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
150-354 |
4.15e-71 |
|
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: 230.57 E-value: 4.15e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 150 FEQMNLSRQILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERMIYRPKGASCtrvLVLVPTR 229
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFA---LVLTPTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 230 ELAIQVFQVFRKLSTFIQLEVCLCAGGLDLKAQEAALRSGPDVVVATPGRLIDHLHNSPS--FNLSNIEVLVLDEADRML 307
Cdd:cd17955 78 ELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDttKVLSRVKFLVLDEADRLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 392884823 308 EEAFRDQMNELIRLCAQNRQTLLFSATMTEEIDELASMSLQKPVKIF 354
Cdd:cd17955 158 TGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFFWE 204
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
130-508 |
4.77e-70 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 237.12 E-value: 4.77e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 130 EDFFSALIDGKSldtsvnvSFEQMNLSRQILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILER 209
Cdd:PRK01297 76 EDFVVEPQEGKT-------RFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQ 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 210 MIYRP----KGASCTRVLVLVPTRELAIQVFQVFRKLSTFIQLEVCLCAGGLDLKAQEAALRSG-PDVVVATPGRLIDhL 284
Cdd:PRK01297 149 LLQTPppkeRYMGEPRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLD-F 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 285 HNSPSFNLSNIEVLVLDEADRMLEEAFRDQMNELIRLC--AQNRQTLLFSATMTEEIDELASMSLQKPVKIFINENTDTA 362
Cdd:PRK01297 228 NQRGEVHLDMVEVMVLDEADRMLDMGFIPQVRQIIRQTprKEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVAS 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 363 LKLRQefiRIRAGRETDREAMVAALVTRTFQTNTIVFVRTKKDCQRMQILLGLLGIKVGQMQSSLTQGQRIESLSKFKKA 442
Cdd:PRK01297 308 DTVEQ---HVYAVAGSDKYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREG 384
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392884823 443 EIDVLVSTDLASRGLDIEGVQTVINMNMPKSIKQYIHRVGRTARAGKAGRSISLVGEDERKLLKEI 508
Cdd:PRK01297 385 KIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEI 450
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
148-526 |
7.21e-68 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 233.13 E-value: 7.21e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 148 VSFEQMNLSRQILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLP----ILERMIYRPKGASCtrVL 223
Cdd:PTZ00110 130 VSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPaivhINAQPLLRYGDGPI--VL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 224 VLVPTRELAIQVFQVFRKLSTFIQLEVCLCAGGLDLKAQEAALRSGPDVVVATPGRLIDHLHNSPSfNLSNIEVLVLDEA 303
Cdd:PTZ00110 208 VLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVT-NLRRVTYLVLDEA 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 304 DRMLEEAFRDQMNELIRLCAQNRQTLLFSATMTEEIDELA-SMSLQKPVKIFINENTDTALK-LRQEFIRIRagrETDRE 381
Cdd:PTZ00110 287 DRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLArDLCKEEPVHVNVGSLDLTACHnIKQEVFVVE---EHEKR 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 382 AMVAALVTRTFQTNT--IVFVRTKKDCQRMQILLGLLGIKVGQMQSSLTQGQRIESLSKFKKAEIDVLVSTDLASRGLDI 459
Cdd:PTZ00110 364 GKLKMLLQRIMRDGDkiLIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDV 443
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392884823 460 EGVQTVINMNMPKSIKQYIHRVGRTARAGKAGRSISLVGEDERKLLKEIVnsNADRTLKQRlVAPEV 526
Cdd:PTZ00110 444 KDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLV--KVLREAKQP-VPPEL 507
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
150-500 |
1.67e-67 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 228.70 E-value: 1.67e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 150 FEQMNLSRQILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERMIYRPKGASCT----RVLVL 225
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDRKvnqpRALIM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 226 VPTRELAIQVFQVFRKLSTFIQLEVCLCAGGLDLKAQEAALRSGPDVVVATPGRLIDHLHNSpSFNLSNIEVLVLDEADR 305
Cdd:PRK04837 90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQN-HINLGAIQVVVLDEADR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 306 MLEEAFRDQMNELIRLC--AQNRQTLLFSATMTEEIDELASMSLQKPVKIFINENTDTALKLRQEfirIRAGRETDREAM 383
Cdd:PRK04837 169 MFDLGFIKDIRWLFRRMppANQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEE---LFYPSNEEKMRL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 384 VAALVTRTFQTNTIVFVRTKKDCQRMQILLGLLGIKVGQMQSSLTQGQRIESLSKFKKAEIDVLVSTDLASRGLDIEGVQ 463
Cdd:PRK04837 246 LQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVT 325
|
330 340 350
....*....|....*....|....*....|....*..
gi 392884823 464 TVINMNMPKSIKQYIHRVGRTARAGKAGRSISLVGED 500
Cdd:PRK04837 326 HVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEE 362
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
149-353 |
4.41e-65 |
|
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: 214.86 E-value: 4.41e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 149 SFEQMNLSRQILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERMiYRPKGASCTRVLVLVPT 228
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKL-KAHSPTVGARALILSPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 229 RELAIQVFQVFRKLSTFIQLEVCLCAGGLDLKAQEAALRSGPDVVVATPGRLIdHLHNSPSFNLSNIEVLVLDEADRMLE 308
Cdd:cd17959 81 RELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLL-HLLVEMNLKLSSVEYVVFDEADRLFE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 392884823 309 EAFRDQMNELIRLCAQNRQTLLFSATMTEEIDELASMSLQKPVKI 353
Cdd:cd17959 160 MGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
159-356 |
1.53e-63 |
|
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: 210.22 E-value: 1.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 159 ILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERMiYRPK-------GAsctrvLVLVPTREL 231
Cdd:cd17941 1 TLKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKL-YRERwtpedglGA-----LIISPTREL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 232 AIQVFQVFRKLSTFIQLEVCLCAGGLDLKaQEAALRSGPDVVVATPGRLIDHLHNSPSFNLSNIEVLVLDEADRMLEEAF 311
Cdd:cd17941 75 AMQIFEVLRKVGKYHSFSAGLIIGGKDVK-EEKERINRMNILVCTPGRLLQHMDETPGFDTSNLQMLVLDEADRILDMGF 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 392884823 312 RDQMNELIRLCAQNRQTLLFSATMTEEIDELASMSLQKPVKIFIN 356
Cdd:cd17941 154 KETLDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISVH 198
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
148-509 |
9.95e-63 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 218.50 E-value: 9.95e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 148 VSFEQMNLSRQILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILER-MIYRPKGASCTR---VL 223
Cdd:PLN00206 121 LSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRcCTIRSGHPSEQRnplAM 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 224 VLVPTRELAIQVFQVFRKLSTFIQLEVCLCAGGLDLKAQEAALRSGPDVVVATPGRLIDHL--HNspsFNLSNIEVLVLD 301
Cdd:PLN00206 201 VLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLskHD---IELDNVSVLVLD 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 302 EADRMLEEAFRDQMNELIRLCAQNrQTLLFSATMTEEIDELASMSLQKPVKIFINENTDTALKLRQEFIRIRAGREtdRE 381
Cdd:PLN00206 278 EVDCMLERGFRDQVMQIFQALSQP-QVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQK--KQ 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 382 AMVAALVTRT-FQTNTIVFVRTKKDCQrmqiLLG-----LLGIKVGQMQSSLTQGQRIESLSKFKKAEIDVLVSTDLASR 455
Cdd:PLN00206 355 KLFDILKSKQhFKPPAVVFVSSRLGAD----LLAnaitvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGR 430
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 392884823 456 GLDIEGVQTVINMNMPKSIKQYIHRVGRTARAGKAGRSISLVGEDERKLLKEIV 509
Cdd:PLN00206 431 GVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELV 484
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
149-344 |
2.13e-61 |
|
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: 205.41 E-value: 2.13e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 149 SFEQMNLSRQILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERMI-------YRPKGASCTR 221
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLedgppsvGRGRRKAYPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 222 VLVLVPTRELAIQVFQVFRKLSTFIQLEVCLCAGGLDLKAQEAALRSGPDVVVATPGRLIDHLhNSPSFNLSNIEVLVLD 301
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFI-ERGRISLSSIKFLVLD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 392884823 302 EADRMLEEAFRDQMNELIRLC----AQNRQTLLFSATMTEEIDELAS 344
Cdd:cd17967 160 EADRMLDMGFEPQIRKIVEHPdmppKGERQTLMFSATFPREIQRLAA 206
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
172-342 |
4.31e-60 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 199.78 E-value: 4.31e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 172 TPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERMIYRPKGascTRVLVLVPTRELAIQVFQVFRKLSTFIQLEVC 251
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNG---PQALVLAPTRELAEQIYEELKKLGKGLGLKVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 252 LCAGGLDLKAQEAALRsGPDVVVATPGRLIDHLHNSPsfNLSNIEVLVLDEADRMLEEAFRDQMNELIRLCAQNRQTLLF 331
Cdd:pfam00270 78 SLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERK--LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLL 154
|
170
....*....|.
gi 392884823 332 SATMTEEIDEL 342
Cdd:pfam00270 155 SATLPRNLEDL 165
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
149-510 |
6.57e-59 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 204.68 E-value: 6.57e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 149 SFEQMNLSRQILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERMIYRpkgASCTRVLVLVPT 228
Cdd:PTZ00424 29 SFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYD---LNACQALILAPT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 229 RELAIQVFQVFRKLSTFIQLEVCLCAGGLDLKAQEAALRSGPDVVVATPGRLIDHLhNSPSFNLSNIEVLVLDEADRMLE 308
Cdd:PTZ00424 106 RELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMI-DKRHLRVDDLKLFILDEADEMLS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 309 EAFRDQMNELIRLCAQNRQTLLFSATMTEEIDELASMSLQKPVKIFINENTDTALKLRQEFIRIRAgRETDREAMVAALV 388
Cdd:PTZ00424 185 RGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEK-EEWKFDTLCDLYE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 389 TRTFqTNTIVFVRTKKDCQRMQILLGLLGIKVGQMQSSLTQGQRIESLSKFKKAEIDVLVSTDLASRGLDIEGVQTVINM 468
Cdd:PTZ00424 264 TLTI-TQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINY 342
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 392884823 469 NMPKSIKQYIHRVGRTARAGKAGRSISLVGEDERKLLKEIVN 510
Cdd:PTZ00424 343 DLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIER 384
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
155-356 |
4.41e-57 |
|
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: 193.57 E-value: 4.41e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 155 LSRQILKACSGAGYSDPTPIQQACIPVAL-TGKDICACAATGTGKTAAFVLPILERMIYRPKGA--SCTRVLVLVPTREL 231
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGrrSGVSALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 232 AIQVFQVFRKLSTFIQ-LEVCLCAGGLDLKAQEAAL-RSGPDVVVATPGRLIDHLHNSPSFN-LSNIEVLVLDEADRMLE 308
Cdd:cd17964 81 ALQIAAEAKKLLQGLRkLRVQSAVGGTSRRAELNRLrRGRPDILVATPGRLIDHLENPGVAKaFTDLDYLVLDEADRLLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 392884823 309 EAFRDQMNELIRL----CAQNRQTLLFSATMTEEIDELASMSLQKPVKiFIN 356
Cdd:cd17964 161 MGFRPDLEQILRHlpekNADPRQTLLFSATVPDEVQQIARLTLKKDYK-FID 211
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
149-344 |
8.94e-57 |
|
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: 194.42 E-value: 8.94e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 149 SFEQMNLSRQILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERMIYRPKGASCTR------V 222
Cdd:cd18052 44 TFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEGLTASSFSevqepqA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 223 LVLVPTRELAIQVFQVFRKLSTFIQLEVCLCAGGLDLKAQEAALRSGPDVVVATPGRLIDHLhNSPSFNLSNIEVLVLDE 302
Cdd:cd18052 124 LIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFI-GRGKISLSKLKYLILDE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 392884823 303 ADRMLEEAFRDQMNELIRLC----AQNRQTLLFSATMTEEIDELAS 344
Cdd:cd18052 203 ADRMLDMGFGPEIRKLVSEPgmpsKEDRQTLMFSATFPEEIQRLAA 248
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
155-351 |
1.86e-56 |
|
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: 191.64 E-value: 1.86e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 155 LSRQILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERMIYRPKGA---SCTRVLVLVPTREL 231
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESgeeQGTRALILVPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 232 AIQVFQVFRKLSTFI--QLEVCLCAGGLDLKAQEAALRSGPDVVVATPGRLIDHLHNSPSFNLSNIEVLVLDEADRMLEE 309
Cdd:cd17961 81 AQQVSKVLEQLTAYCrkDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLLSTLKYLVIDEADLVLSY 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 392884823 310 AFRDQMNELIRLCAQNRQTLLFSATMTEEIDELASMSLQKPV 351
Cdd:cd17961 161 GYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
159-356 |
2.13e-55 |
|
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: 188.34 E-value: 2.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 159 ILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILErMIYRPKGA--SCTRVLVLVPTRELAIQVF 236
Cdd:cd17942 1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIE-LLYKLKFKprNGTGVIIISPTRELALQIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 237 QVFRKLSTFIQLEVCLCAGGLDLKAQEAALRSGPDVVVATPGRLIDHLHNSPSFNLSNIEVLVLDEADRMLEEAFRDQMN 316
Cdd:cd17942 80 GVAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 392884823 317 ELIRLCAQNRQTLLFSATMTEEIDELASMSLQKPvKIFIN 356
Cdd:cd17942 160 QIIKLLPKRRQTMLFSATQTRKVEDLARISLKKK-PLYVG 198
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
150-353 |
3.09e-54 |
|
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: 185.19 E-value: 3.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 150 FEQMNLSRQILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILErMIYRPKGAscTRVLVLVPTR 229
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILE-KIDPKKDV--IQALILVPTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 230 ELAIQVFQVFRKLSTFIQLEVCLCAGGLDLKAQEAALRSGPDVVVATPGRLIDhLHNSPSFNLSNIEVLVLDEADRMLEE 309
Cdd:cd17940 78 ELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILD-LAKKGVADLSHCKTLVLDEADKLLSQ 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 392884823 310 AFRDQMNELIRLCAQNRQTLLFSATMTEEIDELASMSLQKPVKI 353
Cdd:cd17940 157 DFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
166-355 |
3.33e-54 |
|
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: 185.10 E-value: 3.33e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 166 AGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERmIYRPKGASCTRVLVLVPTRELAIQVFQVFRKLSTF 245
Cdd:cd17957 8 SGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQK-LGKPRKKKGLRALILAPTRELASQIYRELLKLSKG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 246 IQLEVCLCAGGLDLKAQEAA-LRSGPDVVVATPGRLIDHLHNSPSfNLSNIEVLVLDEADRMLEEAFRDQMNELIRLC-A 323
Cdd:cd17957 87 TGLRIVLLSKSLEAKAKDGPkSITKYDILVSTPLRLVFLLKQGPI-DLSSVEYLVLDEADKLFEPGFREQTDEILAACtN 165
|
170 180 190
....*....|....*....|....*....|..
gi 392884823 324 QNRQTLLFSATMTEEIDELASMSLQKPVKIFI 355
Cdd:cd17957 166 PNLQRSLFSATIPSEVEELARSVMKDPIRIIV 197
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
167-353 |
5.66e-54 |
|
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: 185.10 E-value: 5.66e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 167 GYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILER------MIYRPKGascTRVLVLVPTRELAIQVFQVFR 240
Cdd:cd17949 10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRllslepRVDRSDG---TLALVLVPTRELALQIYEVLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 241 KL-STFIQLEVCLCAGGLDLKAQEAALRSGPDVVVATPGRLIDHLHNSPSFNLSNIEVLVLDEADRMLEEAFRDQMNELI 319
Cdd:cd17949 87 KLlKPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQSFDVSNLRWLVLDEADRLLDMGFEKDITKIL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 392884823 320 RL-------------CAQNRQTLLFSATMTEEIDELASMSLQKPVKI 353
Cdd:cd17949 167 ELlddkrskaggeksKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
167-350 |
7.47e-54 |
|
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: 185.53 E-value: 7.47e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 167 GYSDPTPIQQACIPVALTG---------KDICACAATGTGKTAAFVLPILERMIYRPkgASCTRVLVLVPTRELAIQVFQ 237
Cdd:cd17956 9 GITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKRV--VPRLRALIVVPTKELVQQVYK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 238 VFRKLSTFIQLEVCLCAGGLDLKAQEAALR--------SGPDVVVATPGRLIDHLHNSPSFNLSNIEVLVLDEADRMLEE 309
Cdd:cd17956 87 VFESLCKGTGLKVVSLSGQKSFKKEQKLLLvdtsgrylSRVDILVATPGRLVDHLNSTPGFTLKHLRFLVIDEADRLLNQ 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392884823 310 AFRDQMNELIRLCAQNR--------------------QTLLFSATMTEEIDELASMSLQKP 350
Cdd:cd17956 167 SFQDWLETVMKALGRPTapdlgsfgdanllersvrplQKLLFSATLTRDPEKLSSLKLHRP 227
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
159-353 |
4.75e-53 |
|
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: 182.01 E-value: 4.75e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 159 ILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERMIYRPKGASCTRV--LVLVPTRELAIQVF 236
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKKGQVgaLIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 237 QVFRKLSTFIQLEVC--LCAGGLDLKAQEAAL-RSGPDVVVATPGRLIDHL-HNSPSFNLSNIEVLVLDEADRMLEEAFR 312
Cdd:cd17960 81 EVLQSFLEHHLPKLKcqLLIGGTNVEEDVKKFkRNGPNILVGTPGRLEELLsRKADKVKVKSLEVLVLDEADRLLDLGFE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 392884823 313 DQMNELIRLCAQNRQTLLFSATMTEEIDELASMSLQKPVKI 353
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
166-353 |
7.09e-52 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 178.84 E-value: 7.09e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 166 AGYSDPTPIQQACIPVALTG-KDICACAATGTGKTAAFVLPILERMIYRPKGasctRVLVLVPTRELAIQVFQVFRKLST 244
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKGG----RVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 245 FIQLEVCLCAGGLDLKAQEAALRSG-PDVVVATPGRLIDHLHNSPsFNLSNIEVLVLDEADRMLEEAFRDQMNELIRLCA 323
Cdd:smart00487 80 SLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDK-LSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLP 158
|
170 180 190
....*....|....*....|....*....|
gi 392884823 324 QNRQTLLFSATMTEEIDELASMSLQKPVKI 353
Cdd:smart00487 159 KNVQLLLLSATPPEEIENLLELFLNDPVFI 188
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
159-353 |
6.04e-50 |
|
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: 174.43 E-value: 6.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 159 ILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERMIYRPK-----GASCTRVLVLVPTRELAI 233
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPldeetKDDGPYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 234 QVFQVFRKLSTFIQLEVCLCAGGLDLKAQEAALRSGPDVVVATPGRLIDHLHNSpSFNLSNIEVLVLDEADRMLEEAFRD 313
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERR-LLVLNQCTYVVLDEADRMIDMGFEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 314 QMN----------------ELIRLCA----QNRQTLLFSATMTEEIDELASMSLQKPVKI 353
Cdd:cd17945 160 QVTkildampvsnkkpdteEAEKLAAsgkhRYRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
153-354 |
9.01e-49 |
|
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: 170.20 E-value: 9.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 153 MNLSRQILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERMIYRPKGascTRVLVLVPTRELA 232
Cdd:cd17939 2 MGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRE---TQALVLAPTRELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 233 IQVFQVFRKLSTFIQLEVCLCAGGLDLKAQEAALRSGPDVVVATPGRLIDHLHNSpSFNLSNIEVLVLDEADRMLEEAFR 312
Cdd:cd17939 79 QQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRR-SLRTDKIKMFVLDEADEMLSRGFK 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 392884823 313 DQMNELIRLCAQNRQTLLFSATMTEEIDELASMSLQKPVKIF 354
Cdd:cd17939 158 DQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRIL 199
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
159-353 |
4.06e-48 |
|
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: 168.36 E-value: 4.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 159 ILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERMIYRP--KGASCTRVLVLVPTRELAIQVF 236
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRelEKGEGPIAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 237 QVFRKLSTFIQLEVCLCAGGLDLKAQEAALRSGPDVVVATPGRLIDHLHNSpSFNLSNIEVLVLDEADRMLEEAFRDQMN 316
Cdd:cd17952 81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKK-ATNLQRVTYLVLDEADRMFDMGFEYQVR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 392884823 317 ELIRLCAQNRQTLLFSATMTEEIDELASMSLQKPVKI 353
Cdd:cd17952 160 SIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
149-353 |
4.65e-47 |
|
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: 166.40 E-value: 4.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 149 SFEQMNLSRQILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERMIYRP--KGASCTRVLVLV 226
Cdd:cd17953 13 KWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRpvKPGEGPIGLIMA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 227 PTRELAIQVFQVFRKLSTFIQLEVCLCAGGLDLKAQEAALRSGPDVVVATPGRLIDHL--HNSPSFNLSNIEVLVLDEAD 304
Cdd:cd17953 93 PTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtaNNGRVTNLRRVTYVVLDEAD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 392884823 305 RMLEEAFRDQMNELIRLCAQNRQTLLFSATMTEEIDELASMSLQKPVKI 353
Cdd:cd17953 173 RMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
159-353 |
6.12e-47 |
|
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: 165.23 E-value: 6.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 159 ILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERMIYRP--KGASCTRVLVLVPTRELAIQVF 236
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPplERGDGPIVLVLAPTRELAQQIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 237 QVFRKLSTFIQLEVCLCAGGLDLKAQEAALRSGPDVVVATPGRLIDhLHNSPSFNLSNIEVLVLDEADRMLEEAFRDQMN 316
Cdd:cd17966 81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLID-FLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 392884823 317 ELIRLCAQNRQTLLFSATMTEEIDELASMSLQKPVKI 353
Cdd:cd17966 160 KIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
159-359 |
1.40e-46 |
|
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box protein, which shows little similarity to any of the other known human DEAD box proteins, but shows a high similarity to mouse Ddx24 at the amino acid level. MDM2 mediates nonproteolytic polyubiquitylation of the DEAD-Box RNA helicase DDX24. DDX24 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.
Pssm-ID: 350704 [Multi-domain] Cd Length: 235 Bit Score: 165.49 E-value: 1.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 159 ILKACSGAGYSDPTPIQQACIPVALT-GKDICACAATGTGKTAAFVLPILERMIYRPKGASCT------RVLVLVPTREL 231
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLLSQKSSNGVGgkqkplRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 232 AIQVFQVFRKLSTFIQLEVCLCAGGLDLKAQEAALRSGPDVVVATPGRLIDHLHNSPSF--NLSNIEVLVLDEADRMLEE 309
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHlaNLKSLRFLVLDEADRMLEK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 392884823 310 AFRDQMNELIRL-------CAQNRQTLLFSATMTeeidelasMSLQKPVKIFINENT 359
Cdd:cd17946 161 GHFAELEKILELlnkdragKKRKRQTFVFSATLT--------LDHQLPLKLNSKKKK 209
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
159-353 |
4.68e-46 |
|
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: 162.43 E-value: 4.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 159 ILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERMIyrpKGASCTRVLVLVPTRELAIQVFQV 238
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLD---LERRHPQVLILAPTREIAVQIHDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 239 FRKLSTFIQ-LEVCLCAGGLDLKAQEAALRsGPDVVVATPGRlIDHLHNSPSFNLSNIEVLVLDEADRMLEEAFRDQMNE 317
Cdd:cd17943 78 FKKIGKKLEgLKCEVFIGGTPVKEDKKKLK-GCHIAVGTPGR-IKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNW 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 392884823 318 LIRLCAQNRQTLLFSATMTEEIDELASMSLQKPVKI 353
Cdd:cd17943 156 IFSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLV 191
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
149-343 |
7.71e-46 |
|
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: 164.06 E-value: 7.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 149 SFEQMNLSRQILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERMIYRPKGASCTRV------ 222
Cdd:cd18051 22 TFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQGPGESLPSEsgyygr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 223 -------LVLVPTRELAIQVFQVFRKLSTFIQLEVCLCAGGLDLKAQEAALRSGPDVVVATPGRLIDHLHNSpSFNLSNI 295
Cdd:cd18051 102 rkqyplaLVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERG-KIGLDYC 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 392884823 296 EVLVLDEADRMLEEAFRDQMNELIRLCAQ----NRQTLLFSATMTEEIDELA 343
Cdd:cd18051 181 KYLVLDEADRMLDMGFEPQIRRIVEQDTMpptgERQTLMFSATFPKEIQMLA 232
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
166-353 |
2.90e-45 |
|
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer development by promoting DNA replication. DDX59 knockdown mice showed reduced cell proliferation, anchorage-independent cell growth, and reduction of tumor formation. Recent work shows that EGFR and Ras regulate DDX59 during lung cancer development. Diseases associated with DDX59 (also called zinc finger HIT domain-containing protein 5) include orofaciodigital syndrome V and orofaciodigital syndrome. DDX59 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350720 [Multi-domain] Cd Length: 193 Bit Score: 160.41 E-value: 2.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 166 AGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERMIYRPKGASctrVLVLVPTRELAIQVFQVFRKL-ST 244
Cdd:cd17962 8 AGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPS---ALILTPTRELAVQIEDQAKELmKG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 245 FIQLEVCLCAGGLDLKAQEAALRSGPDVVVATPGRLIDHLHNSpSFNLSNIEVLVLDEADRMLEEAFRDQMNELIRLCAQ 324
Cdd:cd17962 85 LPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQS-SVELDNIKIVVVDEADTMLKMGFQQQVLDILENISH 163
|
170 180
....*....|....*....|....*....
gi 392884823 325 NRQTLLFSATMTEEIDELASMSLQKPVKI 353
Cdd:cd17962 164 DHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
365-497 |
4.33e-45 |
|
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350174 [Multi-domain] Cd Length: 131 Bit Score: 157.67 E-value: 4.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 365 LRQEFIRIRAgrETDREAMVAALVTRTFQTNTIVFVRTKKDCQRMQILLGLLGIKVGQMQSSLTQGQRIESLSKFKKAEI 444
Cdd:cd18787 1 IKQLYVVVEE--EEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKV 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 392884823 445 DVLVSTDLASRGLDIEGVQTVINMNMPKSIKQYIHRVGRTARAGKAGRSISLV 497
Cdd:cd18787 79 RVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
150-353 |
1.48e-44 |
|
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: 158.76 E-value: 1.48e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 150 FEQMNLSRQILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERMIYRPKGascTRVLVLVPTR 229
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKA---TQALVLAPTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 230 ELAIQVFQVFRKLSTFIQLEVCLCAGGLDLKAQEAALRSGPDVVVATPGRLIDHLhNSPSFNLSNIEVLVLDEADRMLEE 309
Cdd:cd18046 78 ELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMI-NRRYLRTDYIKMFVLDEADEMLSR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 392884823 310 AFRDQMNELIRLCAQNRQTLLFSATMTEEIDELASMSLQKPVKI 353
Cdd:cd18046 157 GFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
159-353 |
1.55e-44 |
|
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: 158.66 E-value: 1.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 159 ILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPIL-------ERMIYR----PKGasctrvLVLVP 227
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLImfaleqeKKLPFIkgegPYG------LIVCP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 228 TRELAIQVFQV----FRKLST--FIQLEVCLCAGGLDLKAQEAALRSGPDVVVATPGRLIDHLhNSPSFNLSNIEVLVLD 301
Cdd:cd17951 75 SRELARQTHEVieyyCKALQEggYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDML-NKKKINLDICRYLCLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 392884823 302 EADRMLEEAFRDQMNELIRLCAQNRQTLLFSATMTEEIDELASMSLQKPVKI 353
Cdd:cd17951 154 EADRMIDMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
149-355 |
7.81e-43 |
|
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: 154.04 E-value: 7.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 149 SFEQMNLSRQILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERMIYRPKGASCtrvLVLVPT 228
Cdd:cd17950 3 GFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSV---LVICHT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 229 RELAIQVFQVFRKLSTFI-QLEVCLCAGGLDLKAQEAALRS-GPDVVVATPGRLIDhLHNSPSFNLSNIEVLVLDEADRM 306
Cdd:cd17950 80 RELAFQISNEYERFSKYMpNVKTAVFFGGVPIKKDIEVLKNkCPHIVVGTPGRILA-LVREKKLKLSHVKHFVLDECDKM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 392884823 307 LEEA-FRDQMNELIRLCAQNRQTLLFSATMTEEIDELASMSLQKPVKIFI 355
Cdd:cd17950 159 LEQLdMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
150-343 |
6.50e-42 |
|
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: 151.32 E-value: 6.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 150 FEQMNLSRQILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILErmiyrpkgasCTRVLVLVPTR 229
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQ----------IVVALILEPSR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 230 ELAIQVFQVFRKLSTFI---QLEVCLCAGGLDLKAQEAALRSGPDVVVATPGRLIDhLHNSPSFNLSNIEVLVLDEADRM 306
Cdd:cd17938 71 ELAEQTYNCIENFKKYLdnpKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLED-LIKTGKLDLSSVRFFVLDEADRL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 392884823 307 LEEAFRDQMNEL------IRLCAQNRQTLLFSATM-TEEIDELA 343
Cdd:cd17938 150 LSQGNLETINRIynripkITSDGKRLQVIVCSATLhSFEVKKLA 193
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
159-354 |
9.35e-39 |
|
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: 142.22 E-value: 9.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 159 ILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERMIYRP------KGASctrVLVLVPTRELA 232
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPipreqrNGPG---VLVLTPTRELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 233 IQVFQVFRKLSTFIQLEVCLCAGGlDLKAQEAALRSGPDVVVATPGRLIDhLHNSPSFNLSNIEVLVLDEADRMLEEAFR 312
Cdd:cd17958 78 LQIEAECSKYSYKGLKSVCVYGGG-NRNEQIEDLSKGVDIIIATPGRLND-LQMNNVINLKSITYLVLDEADRMLDMGFE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 392884823 313 DQMNELIRLCAQNRQTLLFSATMTEEIDELASMSLQKPVKIF 354
Cdd:cd17958 156 PQIRKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIVY 197
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
155-353 |
2.08e-38 |
|
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: 141.17 E-value: 2.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 155 LSRQILKACSGAGYSDPTPIQQACIPVALTG--KDICACAATGTGKTAAFVLPILERMIYRPKgasCTRVLVLVPTRELA 232
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLK---SPQALCLAPTRELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 233 IQVFQVFRKLSTFIQLEVCLCAGGLDLKAQEaalRSGPDVVVATPGRLIDHLhNSPSFNLSNIEVLVLDEADRMLEEA-F 311
Cdd:cd17963 78 RQIGEVVEKMGKFTGVKVALAVPGNDVPRGK---KITAQIVIGTPGTVLDWL-KKRQLDLKKIKILVLDEADVMLDTQgH 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 392884823 312 RDQMNELIRLCAQNRQTLLFSATMTEEIDELASMSLQKPVKI 353
Cdd:cd17963 154 GDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
148-355 |
1.55e-37 |
|
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: 140.14 E-value: 1.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 148 VSFEQMNLSRQILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERMIYRP-----KGASCtrv 222
Cdd:cd18049 24 LNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPflergDGPIC--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 223 LVLVPTRELAIQVFQVFRKLSTFIQLEVCLCAGGLDLKAQEAALRSGPDVVVATPGRLIDHLHNSPSfNLSNIEVLVLDE 302
Cdd:cd18049 101 LVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKT-NLRRCTYLVLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 392884823 303 ADRMLEEAFRDQMNELIRLCAQNRQTLLFSATMTEEIDELASMSLQKPVKIFI 355
Cdd:cd18049 180 ADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINI 232
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
149-355 |
6.73e-35 |
|
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: 133.98 E-value: 6.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 149 SFEQMNLSRQILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERMIYRP-----KGASCtrvL 223
Cdd:cd18050 63 AFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPylergDGPIC---L 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 224 VLVPTRELAIQVFQVFRKLSTFIQLEVCLCAGGLDLKAQEAALRSGPDVVVATPGRLIDHLHNSPSfNLSNIEVLVLDEA 303
Cdd:cd18050 140 VLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKT-NLRRCTYLVLDEA 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 392884823 304 DRMLEEAFRDQMNELIRLCAQNRQTLLFSATMTEEIDELASMSLQKPVKIFI 355
Cdd:cd18050 219 DRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINI 270
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
150-353 |
2.62e-33 |
|
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: 127.20 E-value: 2.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 150 FEQMNLSRQILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERMIYRPKGascTRVLVLVPTR 229
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRE---TQALILSPTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 230 ELAIQVFQVFRKLSTFIQLEVCLCAGGLDLKAQEAALRSGPDVVVATPGRLIDHLHNSpSFNLSNIEVLVLDEADRMLEE 309
Cdd:cd18045 78 ELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRR-SLRTRHIKMLVLDEADEMLNK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 392884823 310 AFRDQMNELIRLCAQNRQTLLFSATMTEEIDELASMSLQKPVKI 353
Cdd:cd18045 157 GFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
160-334 |
4.98e-32 |
|
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: 123.42 E-value: 4.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 160 LKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERMIY----RPKGAScTRVLVLVPTRELAIQV 235
Cdd:cd17944 2 IKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEdqqpRKRGRA-PKVLVLAPTRELANQV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 236 FQVFRKLSTfiQLEVCLCAGGLDLKAQEAALRSGPDVVVATPGRLIDHLHNSpSFNLSNIEVLVLDEADRMLEEAFRDQM 315
Cdd:cd17944 81 TKDFKDITR--KLSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNG-RLDLTKLKHVVLDEVDQMLDMGFAEQV 157
|
170 180
....*....|....*....|....
gi 392884823 316 NELIRL-----CAQNRQTLLFSAT 334
Cdd:cd17944 158 EEILSVsykkdSEDNPQTLLFSAT 181
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
379-488 |
1.62e-29 |
|
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: 112.69 E-value: 1.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 379 DREAMVAALVTRTFQTNTIVFVRTKKDCQrMQILLGLLGIKVGQMQSSLTQGQRIESLSKFKKAEIDVLVSTDLASRGLD 458
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 392884823 459 IEGVQTVINMNMPKSIKQYIHRVGRTARAG 488
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
158-344 |
1.34e-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: 108.61 E-value: 1.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 158 QILKacsGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERMIYRPKGAS----CTRVLVLVPTRELAI 233
Cdd:cd17948 3 EILQ---RQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEgpfnAPRGLVITPSRELAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 234 QVFQVFRKLSTFIQLEVCLCAGGLDLKAQEAALRSGPDVVVATPGrLIDHLHNSPSFNLSNIEVLVLDEADRMLEEAFRD 313
Cdd:cd17948 80 QIGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPG-ALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 392884823 314 QMNELIRLC-------------AQNRQTLLFSATMTEEIDELAS 344
Cdd:cd17948 159 KLSHFLRRFplasrrsentdglDPGTQLVLVSATMPSGVGEVLS 202
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
149-368 |
2.90e-24 |
|
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: 102.02 E-value: 2.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 149 SFEQMNLSRQILKACSGAGYSDPTPIQQACIPVALTG--KDICACAATGTGKTAAFVLPILERMIYRPKGASCtrvLVLV 226
Cdd:cd18048 19 SFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQC---LCLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 227 PTRELAIQVFQVFRKLSTFiqlevclCAG--------------GLDLKAQeaalrsgpdVVVATPGRLIDHLHNSPSFNL 292
Cdd:cd18048 96 PTFELALQTGKVVEEMGKF-------CVGiqviyairgnrpgkGTDIEAQ---------IVIGTPGTVLDWCFKLRLIDV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392884823 293 SNIEVLVLDEADRMLE-EAFRDQMNELIRLCAQNRQTLLFSATMTEEIDELASMSLQKPvkifinentdTALKLRQE 368
Cdd:cd18048 160 TNISVFVLDEADVMINvQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDP----------NIIKLKKE 226
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
407-488 |
1.21e-23 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 94.97 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 407 QRMQILLGLLGIKVGQMQSSLTQGQRIESLSKFKKAEIDVLVSTDLASRGLDIEGVQTVINMNMPKSIKQYIHRVGRTAR 486
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 392884823 487 AG 488
Cdd:smart00490 81 AG 82
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
185-644 |
1.20e-21 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 99.71 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 185 GKDICACAATGTGKT--AAFVLpileRMIYRPKgasctRVLVLVPTRELAIQVFQVFRKLSTfiqlevclcagglDLKAQ 262
Cdd:COG1061 100 GGRGLVVAPTGTGKTvlALALA----AELLRGK-----RVLVLVPRRELLEQWAEELRRFLG-------------DPLAG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 263 EAALRSGPDVVVATpgrlIDHLHNSPSFNL--SNIEVLVLDEADRMLEEAFRDQMNELirlcaQNRQTLLFSAT------ 334
Cdd:COG1061 158 GGKKDSDAPITVAT----YQSLARRAHLDElgDRFGLVIIDEAHHAGAPSYRRILEAF-----PAAYRLGLTATpfrsdg 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 335 ------------MTEEIDELASMSLQKPVKIFI------NENTDTALKLRQEFIRIRAGRETDREAMVAALVTRTFQTNT 396
Cdd:COG1061 229 reillflfdgivYEYSLKEAIEDGYLAPPEYYGirvdltDERAEYDALSERLREALAADAERKDKILRELLREHPDDRKT 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 397 IVFVRTKKDCQRMQILLGLLGIKVGQMQSSLTQGQRIESLSKFKKAEIDVLVSTDLASRGLDIEGVQTVInMNMP-KSIK 475
Cdd:COG1061 309 LVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI-LLRPtGSPR 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 476 QYIHRVGRTARAGKAGRS---ISLVGEDeRKLLKEIVNSNADRTLKqRLVAPEVVEAYRRRIDELEETIQQIDEEDRAEK 552
Cdd:COG1061 388 EFIQRLGRGLRPAPGKEDalvYDFVGND-VPVLEELAKDLRDLAGY-RVEFLDEEESEELALLIAVKPALEVKGELEEEL 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 553 ELRIAEASMAKTQNALEVGENGGAPAERRVWMMKESQIEKQRKREEKRQMKVDARKKAEAAKTPEDIQIEHEAAFHVRAA 632
Cdd:COG1061 466 LEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLLLLLLLELLELLAAL 545
|
490
....*....|..
gi 392884823 633 KRARHSKNKRIR 644
Cdd:COG1061 546 LRLEELAALLLK 557
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
149-350 |
1.61e-21 |
|
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: 93.25 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 149 SFEQMNLSRQILKACSGAGYSDPTPIQQACIPVALTG--KDICACAATGTGKTAAFVLPILERMIYRPKGASCtrvLVLV 226
Cdd:cd18047 2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQC---LCLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 227 PTRELAIQVFQVFRKLSTFIQlEVCLcAGGLDLKAQEAALRSGPDVVVATPGRLIDHLHNSPSFNLSNIEVLVLDEADRM 306
Cdd:cd18047 79 PTYELALQTGKVIEQMGKFYP-ELKL-AYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVM 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 392884823 307 L-EEAFRDQMNELIRLCAQNRQTLLFSATMTEEIDELASMSLQKP 350
Cdd:cd18047 157 IaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
154-500 |
1.17e-19 |
|
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: 93.75 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 154 NLSRQILKACSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERMIYRPKGasctRVLVLVPTRELAI 233
Cdd:COG1205 40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPGA----TALYLYPTKALAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 234 -QVfqvfRKLSTFIQlevclcAGGLDLKA--------QEA--ALRSGPDVVVATPgrliDHLH-----NSPSF--NLSNI 295
Cdd:COG1205 116 dQL----RRLRELAE------ALGLGVRVatydgdtpPEErrWIREHPDIVLTNP----DMLHygllpHHTRWarFFRNL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 296 EVLVLDEA---------------DRMLeeafrdqmneliRLCAQNRQTLLF---SATmteeID---ELASMSLQKPVKIf 354
Cdd:COG1205 182 RYVVIDEAhtyrgvfgshvanvlRRLR------------RICRHYGSDPQFilaSAT----IGnpaEHAERLTGRPVTV- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 355 INENT------DTAL---KLRQEFIRIRAGRETDReaMVAALVTRTFQtnTIVFVRTKKDCQRM------QILLGLLGIK 419
Cdd:COG1205 245 VDEDGsprgerTFVLwnpPLVDDGIRRSALAEAAR--LLADLVREGLR--TLVFTRSRRGAELLaryarrALREPDLADR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 420 VGQMQSSLTQGQRIESLSKFKKAEIDVLVST---DLasrGLDIEGVQTVINMNMPKSIKQYIHRVGRTARAGKAGRSISL 496
Cdd:COG1205 321 VAAYRAGYLPEERREIERGLRSGELLGVVSTnalEL---GIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVLV 397
|
....
gi 392884823 497 VGED 500
Cdd:COG1205 398 AGDD 401
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
171-340 |
5.16e-19 |
|
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: 87.05 E-value: 5.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 171 PTPIQQACIPV---ALTGK------------DICACAA-TGTGKTAAFVLPI---LERMIYRP-----------KGASCT 220
Cdd:cd17965 31 PSPIQTLAIKKllkTLMRKvtkqtsneepklEVFLLAAeTGSGKTLAYLAPLldyLKRQEQEPfeeaeeeyesaKDTGRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 221 RVLVLVPTRELAIQVFQVFRKLSTFIQLEVCLCAGGLDLKAQEAAL--RSGPDVVVATPGrLIDHLHNSPSFNLSNIEVL 298
Cdd:cd17965 111 RSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGPSYQRLQLafKGRIDILVTTPG-KLASLAKSRPKILSRVTHL 189
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 392884823 299 VLDEADRMLEEAFRDQMNELIRLCAQNRQTLLFSATMTEEID 340
Cdd:cd17965 190 VVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFD 231
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
185-334 |
1.38e-16 |
|
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: 77.06 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 185 GKDICACAATGTGKTAAFVLPILERMIYRPKgasctRVLVLVPTRELAIQVFQVFRKLStFIQLEVCLCAGGLDLKAQEA 264
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLKKGK-----KVLVLVPTKALALQTAERLRELF-GPGIRVAVLVGGSSAEEREK 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392884823 265 ALRSGPDVVVATPGRLIDHLHNSPSFNLSNIEVLVLDEADRMLEEAFRDQMnELIRLCAQNR---QTLLFSAT 334
Cdd:cd00046 75 NKLGDADIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALI-LDLAVRKAGLknaQVILLSAT 146
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
172-345 |
2.49e-12 |
|
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: 66.13 E-value: 2.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 172 TPIQQACI-PVALTGKDICACAATGTGKTAafvlpILERMIYRPKGASCTRVLVLVPTRELAIQVFQVFRKLSTFIQLEV 250
Cdd:cd17921 3 NPIQREALrALYLSGDSVLVSAPTSSGKTL-----IAELAILRALATSGGKAVYIAPTRALVNQKEADLRERFGPLGKNV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 251 CLCAGGLDLKAQEAAlrsGPDVVVATPGRLIDHLHNSPSFNLSNIEVLVLDEA------DR--MLEEAfrdqmneLIRLC 322
Cdd:cd17921 78 GLLTGDPSVNKLLLA---EADILVATPEKLDLLLRNGGERLIQDVRLVVVDEAhligdgERgvVLELL-------LSRLL 147
|
170 180
....*....|....*....|....
gi 392884823 323 AQNRQT-LLFSATMTEEIDELASM 345
Cdd:cd17921 148 RINKNArFVGLSATLPNAEDLAEW 171
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
185-335 |
6.03e-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: 64.91 E-value: 6.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 185 GKDICACAATGTGKTAAFVLPILERMIYRPKgascTRVLVLVPTRELAIQVFQVFRKL--STFIQLEVCLCAGGLDLKAQ 262
Cdd:cd17923 15 GRSVVVTTGTASGKSLCYQLPILEALLRDPG----SRALYLYPTKALAQDQLRSLRELleQLGLGIRVATYDGDTPREER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 263 EAALRSGPDVVVATPGRL---IDHLHNSPSFNLSNIEVLVLDEAdRMLEEAFRDQMNELIR----LCAQNRQTLLF---S 332
Cdd:cd17923 91 RAIIRNPPRILLTNPDMLhyaLLPHHDRWARFLRNLRYVVLDEA-HTYRGVFGSHVALLLRrlrrLCRRYGADPQFiltS 169
|
...
gi 392884823 333 ATM 335
Cdd:cd17923 170 ATI 172
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
387-622 |
2.14e-11 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 67.45 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 387 LVTRTFQTN----TIVFVRTKKDCQRMQILLGLLGIKVGQM--QSS------LTQGQRIESLSKFKKAEIDVLVSTDLAS 454
Cdd:COG1111 343 ILKEQLGTNpdsrIIVFTQYRDTAEMIVEFLSEPGIKAGRFvgQASkegdkgLTQKEQIEILERFRAGEFNVLVATSVAE 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 455 RGLDIEGVQTVINM-NMPKSIKqYIHRVGRTARAGkAGRSISLVGED-------------ERKLLKEIVNSNADrtLKQR 520
Cdd:COG1111 423 EGLDIPEVDLVIFYePVPSEIR-SIQRKGRTGRKR-EGRVVVLIAKGtrdeayywssrrkEKKMKSILKKLKKL--LDKQ 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 521 LVAPEVVEAyRRRIDELEETIQQIDEEDRAEKELRIAEASMAKTQNALEVGENGGAPAERRVwmMKESQIEKQRKREEKR 600
Cdd:COG1111 499 EKEKLKESA-QATLDEFESIKELAEDEINEKDLDEIESSENGAHVDWREPVLLQVIVSTLAE--SLELRELGEKVDDEVN 575
|
250 260
....*....|....*....|..
gi 392884823 601 QMKVDARKKAEAAKTPEDIQIE 622
Cdd:COG1111 576 LILEIDRVDVVDDGSVLRVSRL 597
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
168-487 |
5.21e-11 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 66.28 E-value: 5.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 168 YSDPTPIQQACIPVALTGKDICACAATGTGKT-AAFvLPILERMIYRP---KGASCTRVLVLVPTRELA--IQvfqvfRK 241
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPrpgELPDGLRVLYISPLKALAndIE-----RN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 242 LSTFIQlEVCLCAgGLDLKAQEAALRSG--------------PDVVVATPgrliDHLH---NSPSF--NLSNIEVLVLDE 302
Cdd:COG1201 96 LRAPLE-EIGEAA-GLPLPEIRVGVRTGdtpaserqrqrrrpPHILITTP----ESLAlllTSPDAreLLRGVRTVIVDE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 303 ----AD--R------MLEeafRdqmneLIRLCAQNRQTLLFSATMtEEIDE----LASMSLQKPVKIfINENTDTALKLR 366
Cdd:COG1201 170 ihalAGskRgvhlalSLE---R-----LRALAPRPLQRIGLSATV-GPLEEvarfLVGYEDPRPVTI-VDAGAGKKPDLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 367 -----QEFIRIRAGRETDREAMVAALVTRTFQ-TNTIVFVRTKKDCQRM-QILLGLLGIKVGQMQ---SSLTQGQRIESL 436
Cdd:COG1201 240 vlvpvEDLIERFPWAGHLWPHLYPRVLDLIEAhRTTLVFTNTRSQAERLfQRLNELNPEDALPIAahhGSLSREQRLEVE 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392884823 437 SKFKKAEIDVLVST---DLasrGLDIEGVQTVINMNMPKSIK---QYI----HRVGRTARA 487
Cdd:COG1201 320 EALKAGELRAVVATsslEL---GIDIGDVDLVIQVGSPKSVArllQRIgragHRVGEVSKG 377
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
186-303 |
1.51e-09 |
|
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: 58.43 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 186 KDICACAATGTGKTAAFVLPILErMIY--RPKGASCTRVLVLVPTRELAIQVFQVFRKLSTFIQLEVClCAGGLDLKAQE 263
Cdd:cd18034 17 RNTIVVLPTGSGKTLIAVMLIKE-MGElnRKEKNPKKRAVFLVPTVPLVAQQAEAIRSHTDLKVGEYS-GEMGVDKWTKE 94
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 392884823 264 AALR--SGPDVVVATPGRLIDHLHNSpSFNLSNIEVLVLDEA 303
Cdd:cd18034 95 RWKEelEKYDVLVMTAQILLDALRHG-FLSLSDINLLIFDEC 135
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
182-324 |
5.89e-09 |
|
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: 56.67 E-value: 5.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 182 ALTGKDICACAATGTGKTAAFVLpILERMIYRPKGASCTRVLVLVPTRELAIQVFQVFRKLSTFIQLEVCLCAGGLDLKA 261
Cdd:cd17927 14 ALKGKNTIICLPTGSGKTFVAVL-ICEHHLKKFPAGRKGKVVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGDTSENV 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392884823 262 QEAALRSGPDVVVATPGRLIDHLHNSPSFNLSNIEVLVLDEADRMLEEAfrdQMNELIRLCAQ 324
Cdd:cd17927 93 SVEQIVESSDVIIVTPQILVNDLKSGTIVSLSDFSLLVFDECHNTTKNH---PYNEIMFRYLD 152
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
427-567 |
9.80e-09 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 58.73 E-value: 9.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 427 LTQGQRIESLSKFKKAEIDVLVSTDLASRGLDIEGVQTVINMN-MPKSIKQyIHRVGRTARaGKAGRSISLVGEDER--- 502
Cdd:PRK13766 407 MSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEpVPSEIRS-IQRKGRTGR-QEEGRVVVLIAKGTRdea 484
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392884823 503 ---------KLLKEIVNsNADRTLKQRLVAPEVVEAYRRRIDELEETIQQIDEEDRAEKELRIAEASMAKTQNA 567
Cdd:PRK13766 485 yywssrrkeKKMKEELK-NLKGILNKKLQELDEEQKGEEEEKDEQLSLDDFVKSKGKEEEEEEEKEEKDKETEE 557
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
396-494 |
3.06e-08 |
|
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: 52.98 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 396 TIVFVRTKKDCQRMQILLGLLGIKVGQMQSSLTQGQRIESLSKFKKAEIDVLVSTDLASRGLDIEGVQTVINMNMPKSIK 475
Cdd:cd18794 33 GIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSME 112
|
90
....*....|....*....
gi 392884823 476 QYIHRVGRTARAGKAGRSI 494
Cdd:cd18794 113 SYYQESGRAGRDGLPSECI 131
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
441-489 |
5.98e-08 |
|
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: 50.40 E-value: 5.98e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 392884823 441 KAEIDVLVSTDLASRGLDIEGVQTVINMNMPKSIKQYIHRVGRTARAGK 489
Cdd:cd18785 20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK 68
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
263-520 |
7.01e-08 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 55.53 E-value: 7.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 263 EAALRSG-PDVVVATPGRLidhlhNSPSFN--LSNIEV--LVLDEA--------DrmleeaFR-D--QMNELIRLCAqNR 326
Cdd:COG0514 100 LRALRAGeLKLLYVAPERL-----LNPRFLelLRRLKIslFAIDEAhcisqwghD------FRpDyrRLGELRERLP-NV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 327 QTLLFSATMTEEI--DELASMSLQKPvKIFIN----ENtdtalkLRqefIRIRAGRETDREAMVAALVTRTFQTNTIVFV 400
Cdd:COG0514 168 PVLALTATATPRVraDIAEQLGLEDP-RVFVGsfdrPN------LR---LEVVPKPPDDKLAQLLDFLKEHPGGSGIVYC 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 401 RTKKDCQRMQILLGLLGIKVGQMQSSLTQGQRIESLSKFKKAEIDVLVSTdlaSR---GLDIEGVQTVINMNMPKSIKQY 477
Cdd:COG0514 238 LSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT---IAfgmGIDKPDVRFVIHYDLPKSIEAY 314
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 392884823 478 IHRVGRTARAGKAGRSISLVG-EDERKLLKEIVNSNADRTLKQR 520
Cdd:COG0514 315 YQEIGRAGRDGLPAEALLLYGpEDVAIQRFFIEQSPPDEERKRV 358
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
427-496 |
2.46e-07 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350188 [Multi-domain] Cd Length: 143 Bit Score: 50.43 E-value: 2.46e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 427 LTQGQRIESLSKFKKAEIDVLVSTDLASRGLDIEGVQTVINMNMPKSIKQYIHRVGRTARaGKAGRSISL 496
Cdd:cd18801 74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR-KRQGRVVVL 142
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
425-487 |
2.54e-07 |
|
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: 50.28 E-value: 2.54e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392884823 425 SSLTQGQRIESLSKFKKAEIDVLVSTDLASRGLDIEGVQTVINMNMPKSIKQYIHRVGRtARA 487
Cdd:cd18802 72 SLMTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARA 133
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
174-459 |
4.18e-07 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 53.16 E-value: 4.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 174 IQQACIPVALTGKDIC-ACAATGTGKTAAFVLPILERMIYRPKgascTRVLVLVPTRELAIQVFQVFRKLSTF------- 245
Cdd:COG1203 135 ALELALEAAEEEPGLFiLTAPTGGGKTEAALLFALRLAAKHGG----RRIIYALPFTSIINQTYDRLRDLFGEdvllhhs 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 246 -IQLEVCLCAGGLDLKAQEAALR----SGPdVVVATpgrlIDHL-----HNSPSF-----NLSNiEVLVLDEADrMLEEA 310
Cdd:COG1203 211 lADLDLLEEEEEYESEARWLKLLkelwDAP-VVVTT----IDQLfeslfSNRKGQerrlhNLAN-SVIILDEVQ-AYPPY 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 311 FRDQMNELIR-LCAQNRQTLLFSATMTEEIDELasmsLQKPVKIfINENTDTALKLRQEFIRIR---AGRETDREAMVAA 386
Cdd:COG1203 284 MLALLLRLLEwLKNLGGSVILMTATLPPLLREE----LLEAYEL-IPDEPEELPEYFRAFVRKRvelKEGPLSDEELAEL 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 387 LVTRTFQTNTIVFVR-TKKDCQRM--QILLGLLGIKVGQMQSSLTQGQR--IES--LSKFKKAEIDVLVSTDLASRGLDI 459
Cdd:COG1203 359 ILEALHKGKSVLVIVnTVKDAQELyeALKEKLPDEEVYLLHSRFCPADRseIEKeiKERLERGKPCILVSTQVVEAGVDI 438
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
370-490 |
4.22e-07 |
|
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: 49.95 E-value: 4.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 370 IRIRAGRETDReaMVAALVTRTFQTntIVFVRTKKDCQRM-----QILL--GLLGIKVGQMQSSLTQGQRIESLSKFKKA 442
Cdd:cd18797 16 ERGSARREAAR--LFADLVRAGVKT--IVFCRSRKLAELLlrylkARLVeeGPLASKVASYRAGYLAEDRREIEAELFNG 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 392884823 443 EIDVLVSTDLASRGLDIEGVQTVINMNMPKSIKQYIHRVGRTARAGKA 490
Cdd:cd18797 92 ELLGVVATNALELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKD 139
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
191-334 |
7.69e-07 |
|
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: 49.23 E-value: 7.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 191 CAATGTGKTAAFVLPILERmiyrpkgaSCTRVLVLVPTRELAIQVFQVFRKLSTFIQLEVclcAGGLDLKAQEAAlrsgp 270
Cdd:cd17926 24 VLPTGSGKTLTALALIAYL--------KELRTLIVVPTDALLDQWKERFEDFLGDSSIGL---IGGGKKKDFDDA----- 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392884823 271 DVVVATPgRLIDHLHNSPSFNLSNIEVLVLDEADRMLEEAFRdqmnELIRLCAQNRQtLLFSAT 334
Cdd:cd17926 88 NVVVATY-QSLSNLAEEEKDLFDQFGLLIVDEAHHLPAKTFS----EILKELNAKYR-LGLTAT 145
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
183-343 |
1.43e-06 |
|
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: 49.25 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 183 LTGKDICACAATGTGKTAAFVLPILERMIyrpKGAsctRVLVLVPTRELAIQVFQVFRKLSTfIQLEVCLCAGglDLKAQ 262
Cdd:cd18028 15 LKGENLLISIPTASGKTLIAEMAMVNTLL---EGG---KALYLVPLRALASEKYEEFKKLEE-IGLKVGISTG--DYDED 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 263 EAALrSGPDVVVATPGRLIDHLHNSPSFnLSNIEVLVLDEAdRMLEEAFRDQMNELI----RLCAQNRQTLLFSATMTeE 338
Cdd:cd18028 86 DEWL-GDYDIIVATYEKFDSLLRHSPSW-LRDVGVVVVDEI-HLISDEERGPTLESIvarlRRLNPNTQIIGLSATIG-N 161
|
....*
gi 392884823 339 IDELA 343
Cdd:cd18028 162 PDELA 166
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
378-490 |
2.14e-06 |
|
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: 48.03 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 378 TDREAMVAALVTRtfQTNTIVFVRTKKDCQRMQILLGLL------GIKVGQMQSSLTQGQRIESLSKFKKAEIDVLVST- 450
Cdd:cd18796 25 ADAYAEVIFLLER--HKSTLVFTNTRSQAERLAQRLRELcpdrvpPDFIALHHGSLSRELREEVEAALKRGDLKVVVATs 102
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 392884823 451 --DLasrGLDIEGVQTVINMNMPKSIKQYIHRVGRTARAGKA 490
Cdd:cd18796 103 slEL---GIDIGDVDLVIQIGSPKSVARLLQRLGRSGHRPGA 141
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
169-302 |
2.62e-06 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350794 [Multi-domain] Cd Length: 204 Bit Score: 49.01 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 169 SDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLPILERMIYRPKGASCTRVLVLVPTRELAIQ----VFQVFRKLst 244
Cdd:cd18036 1 LELRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKRRSAGEKGRVVVLVNKVPLVEQqlekFFKYFRKG-- 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392884823 245 fiqLEVCLCAGGLDLKAQEAALRSGPDVVVATPGRLIDHLHN---SPSFNLSNIEVLVLDE 302
Cdd:cd18036 79 ---YKVTGLSGDSSHKVSFGQIVKASDVIICTPQILINNLLSgreEERVYLSDFSLLIFDE 136
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
377-547 |
3.33e-06 |
|
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350185 [Multi-domain] Cd Length: 174 Bit Score: 48.07 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 377 ETDREAMVAALVtRTFQTNTIVFVRTKKDCQRMQILLGLL---GIKVGQMQSSltqgqRIESLSKFKKAEIDVLVSTdlA 453
Cdd:cd18798 9 DSDSLEKLLELV-KKLGDGGLIFVSIDYGKEYAEELKEFLerhGIKAELALSS-----TEKNLEKFEEGEIDVLIGV--A 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 454 S------RGLDI-EGVQTVINMNMPksIKQYIHRVGRTAR--AGKAGRSISLVGEDERKLLkeivnsnadRTLKQRL--V 522
Cdd:cd18798 81 SyygvlvRGIDLpERIKYAIFYGVP--VTTYIQASGRTSRlyAGGLTKGLSVVLVDDPELF---------EALKKRLklI 149
|
170 180
....*....|....*....|....*
gi 392884823 523 APEvVEAYRRRIDELEETIQQIDEE 547
Cdd:cd18798 150 LDE-FIFKELEEVDLEELLSEIDES 173
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
171-276 |
5.57e-06 |
|
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: 47.41 E-value: 5.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 171 PTPIQQACIPVALtgKDICA--------CAATGTGKTAAFVLPILerMIY-RPKgasctRVLVLVPTRELAIQVFQVFRK 241
Cdd:cd17918 16 LTKDQAQAIKDIE--KDLHSpepmdrllSGDVGSGKTLVALGAAL--LAYkNGK-----QVAILVPTEILAHQHYEEARK 86
|
90 100 110
....*....|....*....|....*....|....*
gi 392884823 242 LSTFIQLEvcLCAGGldlkaQEAALRSGPDVVVAT 276
Cdd:cd17918 87 FLPFINVE--LVTGG-----TKAQILSGISLLVGT 114
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
157-351 |
8.79e-06 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 47.14 E-value: 8.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 157 RQILKacSGAGYSDPTPIQQACIPVALTGKDICACAATGTGKTAAFVLP-ILERMIyrpkgasctrVLVLVPTreLAIQV 235
Cdd:cd17920 1 EQILK--EVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPaLLLDGV----------TLVVSPL--ISLMQ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 236 FQVFRKLSTFIQLeVCLCAGGLDLKAQEAALRSG---PDVVVATPGRL-----IDHLHNSPSFNLsnIEVLVLDEADRML 307
Cdd:cd17920 67 DQVDRLQQLGIRA-AALNSTLSPEEKREVLLRIKngqYKLLYVTPERLlspdfLELLQRLPERKR--LALIVVDEAHCVS 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 392884823 308 E--EAFRDQMNELIRLCAQNR--QTLLFSATMTEEI--DELASMSLQKPV 351
Cdd:cd17920 144 QwgHDFRPDYLRLGRLRRALPgvPILALTATATPEVreDILKRLGLRNPV 193
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
175-305 |
1.09e-05 |
|
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: 46.74 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 175 QQACIPVALTGKDICAcAATGTGKTAAFVLPILERMiyRPKGAsctRVLVLVPTRELAIQVFQVFRKLSTfIQLEVCLCA 254
Cdd:cd18035 7 QVLIAAVALNGNTLIV-LPTGLGKTIIAILVAADRL--TKKGG---KVLILAPSRPLVEQHAENLKRVLN-IPDKITSLT 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 392884823 255 GGLDLKAQEAALRSGpDVVVATPGRLIDHLHNSpSFNLSNIEVLVLDEADR 305
Cdd:cd18035 80 GEVKPEERAERWDAS-KIIVATPQVIENDLLAG-RITLDDVSLLIFDEAHH 128
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
185-302 |
1.26e-05 |
|
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: 46.04 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 185 GKDICACAATGTGKTAAFVLPILERMIYRPKGAscTRVLVLVPTRELAIQVFQVFRKLSTFIQLEVCLCAGGLDLKAQE- 263
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKG--VQVLYISPLKALINDQERRLEEPLDEIDLEIPVAVRHGDTSQSEk 78
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 392884823 264 -AALRSGPDVVVATPGRLiDHLHNSPSFN--LSNIEVLVLDE 302
Cdd:cd17922 79 aKQLKNPPGILITTPESL-ELLLVNKKLRelFAGLRYVVVDE 119
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
486-716 |
1.96e-05 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 48.06 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 486 RAGKAGrSISLVGEDERkLLKEIVNSNADRTLKQR------LVA---PEVVEAYRRRIDELEETIQQIdEEDRAekelRI 556
Cdd:PRK14900 831 RVPLAG-VIDLAAETAR-VDKEIGKVDQDLAVLERklqnpsFVQnapPAVVEKDRARAEELREKRGKL-EAHRA----ML 903
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 557 AEASMAKTQNALEVGENGGAPAERRVWMMKESQIEKQRKREEKRQMKVdARKKAEAAKTPEDIQIEheaafHVRAAKRAR 636
Cdd:PRK14900 904 SGSEANSARRDTMEIQNEQKPTQDGPAAEAQPAQENTVVESAEKAVAA-VSEAAQQAATAVASGIE-----KVAEAVRKT 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 637 HSKNKRIRAVVESAGTKGAGKAAQNKK---KASSNSKTSLRDIPLVNAGSRGVQKaqkgqKPGAKKgftsalasVSKKSV 713
Cdd:PRK14900 978 VRRSVKKAAATRAAMKKKVAKKAPAKKaaaKKAAAKKAAAKKKVAKKAPAKKVAR-----KPAAKK--------AAKKPA 1044
|
...
gi 392884823 714 KAA 716
Cdd:PRK14900 1045 RKA 1047
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
396-486 |
1.54e-04 |
|
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350177 [Multi-domain] Cd Length: 171 Bit Score: 43.00 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 396 TIVFVRTKKDCQRMQILLGLLGIKVGQMQSSLTQGQRIESLSKFKKAEIDVLVSTDLASRGLDIEGVQTVINMNMPK--- 472
Cdd:cd18790 30 VLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDADKegf 109
|
90
....*....|....*.
gi 392884823 473 --SIKQYIHRVGRTAR 486
Cdd:cd18790 110 lrSETSLIQTIGRAAR 125
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
168-483 |
2.01e-04 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 44.88 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 168 YSDPTPIQQACIPVALTGKDICACAATGTGKT-AAFVLPILERMIYRPKGASCTRVLVLV--PTRELA--IQvfqvfRKL 242
Cdd:PRK13767 30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFLAIIDELFRLGREGELEDKVYCLYvsPLRALNndIH-----RNL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 243 STFIQ-LEVCLCAGGLDLKAQEAALRSG--------------PDVVVATPGRLIDHLhNSPSFN--LSNIEVLVLDE--- 302
Cdd:PRK13767 105 EEPLTeIREIAKERGEELPEIRVAIRTGdtssyekqkmlkkpPHILITTPESLAILL-NSPKFRekLRTVKWVIVDEihs 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 303 -ADR--------MLEEAFRDQMNELIR--LCA-------------------QNRQTLLFSATMTEEIDelasMSLQKPVK 352
Cdd:PRK13767 184 lAENkrgvhlslSLERLEELAGGEFVRigLSAtiepleevakflvgyeddgEPRDCEIVDARFVKPFD----IKVISPVD 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 353 IFINentDTALKLRQEFIRiragretdreaMVAALVTRtfQTNTIVFVRTKKDCQRM-----QILLGLLGI-KVGQMQSS 426
Cdd:PRK13767 260 DLIH---TPAEEISEALYE-----------TLHELIKE--HRTTLIFTNTRSGAERVlynlrKRFPEEYDEdNIGAHHSS 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 392884823 427 LTQGQRIESLSKFKKAEIDVLVSTDLASRGLDIEGVQTVINMNMPKSIKQYIHRVGR 483
Cdd:PRK13767 324 LSREVRLEVEEKLKRGELKVVVSSTSLELGIDIGYIDLVVLLGSPKSVSRLLQRIGR 380
|
|
| DEXHc_DHX36 |
cd17981 |
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ... |
194-338 |
3.88e-04 |
|
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as G4-resolvase 1 or G4R1, MLE-like protein 1 and RNA helicase associated with AU-rich element or RHAU) unwinds a G4-quadruplex in human telomerase RNA. DHX36 belongs to 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: 350739 [Multi-domain] Cd Length: 180 Bit Score: 42.14 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 194 TGTGKTAAFVLPILERMIYRPKGASCtRVLVLVPTRELAIQVfqvfrklSTFIQLEVCLCAG-----GLDLKAQEAALRS 268
Cdd:cd17981 26 TGCGKTTQVTQFILDDAIERGKGSSC-RIVCTQPRRISAISV-------AERVAAERAESCGlgnstGYQIRLESRKPRK 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392884823 269 GPDVVVATPGRLIDHLHNSPsfNLSNIEVLVLDEA-DRMLEEafrDQMNELIRLCAQNRQTL---LFSATMTEE 338
Cdd:cd17981 98 QGSILYCTTGIVLQWLQSDP--HLSNVSHLVLDEIhERNLQS---DVLMGIVKDLLPFRSDLkviLMSATLNAE 166
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
528-735 |
4.70e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 528 EAYRRRIDELEETIQQIDEEDRAEK---ELRIAEASMAKTQNALEVGENGGAPAERRVWMMKESQIEKQRKREEKRQMKV 604
Cdd:PTZ00121 1414 AAAKKKADEAKKKAEEKKKADEAKKkaeEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE 1493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 605 DARKKAEAAKTPEDIQIEHEAAFHVRAAKRARHSKNkriravVESAGTKGAGKAAQNKKKASSnsktslrdiplvnagsr 684
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK------AEEAKKADEAKKAEEKKKADE----------------- 1550
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 392884823 685 gVQKAQKGQKPGAKKGFTSALASVSKKSVkAARHGPEDSKFQKARVAHRMK 735
Cdd:PTZ00121 1551 -LKKAEELKKAEEKKKAEEAKKAEEDKNM-ALRKAEEAKKAEEARIEEVMK 1599
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
397-489 |
7.27e-04 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 42.96 E-value: 7.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 397 IVFVRTKKDCQRMQILLGLLGIKVGQMQSSLTQGQRIESLSKFKKAEIDVLVSTDLASRGLDIEGVQTVINMNMPKSIKQ 476
Cdd:PLN03137 684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEG 763
|
90
....*....|...
gi 392884823 477 YIHRVGRTARAGK 489
Cdd:PLN03137 764 YHQECGRAGRDGQ 776
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
486-724 |
1.12e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 486 RAGKAGRSISLVGEDERKLLKEIVNSNADRTLKQRLVAPEVveayRRRIDELE-ETIQQIDEEDRAEKELRIAEasmaKT 564
Cdd:PTZ00121 1177 KAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEA----RKAEDAKKaEAVKKAEEAKKDAEEAKKAE----EE 1248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 565 QNALEVGENGGAPAERRVWMMKESQIEKQRKREEKRQM----KVDARKKAEAAKTPEDIQIEHEAAFHVRAAKRARHSKN 640
Cdd:PTZ00121 1249 RNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAeekkKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAK 1328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 641 KRIRAVVESAgtKGAGKAAQNKKKASSNSKTSLRdiplvnaGSRGVQKAQKGQKPGAKKGFTSA--LASVSKKSVKAARH 718
Cdd:PTZ00121 1329 KKADAAKKKA--EEAKKAAEAAKAEAEAAADEAE-------AAEEKAEAAEKKKEEAKKKADAAkkKAEEKKKADEAKKK 1399
|
....*.
gi 392884823 719 GPEDSK 724
Cdd:PTZ00121 1400 AEEDKK 1405
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
500-735 |
1.62e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 500 DERKLLKEIVNSNADRTLKQRLVAPEVVEAYRRRIdelEETIQQIDEEDRAEKELRIAEASMAKTQNALEVGEN-GGAPA 578
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK---EEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADElKKAAA 1415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 579 ERRVWMMKESQIEKQRKREEKRQMKVDARKKAEAAKTPEDIQIEHEAAFHVRAAKRARHSKNKriravvesagTKGAGKA 658
Cdd:PTZ00121 1416 AKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK----------AEEAKKA 1485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392884823 659 AQNKKKASSNSKTSLRdiplVNAGSRGVQKAQKGQKPGAKKGFTSALASVSKKSVKAARHGPEDSKFQKARVAHRMK 735
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADE----AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK 1558
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
485-737 |
1.81e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 485 ARAGKAGRSISLVGEDERKLLKEIVNSNADRTLKQRLVAPEVVEA-YRRRIDELE--ETIQQIDEEDRAEKELRIAEASM 561
Cdd:PTZ00121 1242 AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAeEKKKADEAKkaEEKKKADEAKKKAEEAKKADEAK 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 562 AKTQNALEVGENGGAPAERRVWMMKESQIEKQRKREE----KRQMKVDARKKAEAAKTPEDIQIEHEAAFHVRAAKRARH 637
Cdd:PTZ00121 1322 KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEaeaaEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAE 1401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 638 SKNKRIRAVVESAGTKgaGKAAQNKKKASSNSKTslrdiplvNAGSRGVQKAQKGQKpGAKKGFTSALASVSKKSVKAAR 717
Cdd:PTZ00121 1402 EDKKKADELKKAAAAK--KKADEAKKKAEEKKKA--------DEAKKKAEEAKKADE-AKKKAEEAKKAEEAKKKAEEAK 1470
|
250 260
....*....|....*....|.
gi 392884823 718 HGPE-DSKFQKARVAHRMKTK 737
Cdd:PTZ00121 1471 KADEaKKKAEEAKKADEAKKK 1491
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
192-312 |
2.03e-03 |
|
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350790 [Multi-domain] Cd Length: 163 Bit Score: 39.47 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 192 AATGTGKT--AAFvlpilerMIYR-PKGASCTRVLVLVPTRELAIQVFQVFRKLSTFIQLEVclcAGGLDLKAQEAalrs 268
Cdd:cd18032 27 MATGTGKTytAAF-------LIKRlLEANRKKRILFLAHREELLEQAERSFKEVLPDGSFGN---LKGGKKKPDDA---- 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 392884823 269 gpDVVVATPGRL--IDHLHNSPS--FNLsnievLVLDEADRMLEEAFR 312
Cdd:cd18032 93 --RVVFATVQTLnkRKRLEKFPPdyFDL-----IIIDEAHHAIASSYR 133
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
519-648 |
7.13e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 39.82 E-value: 7.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 519 QRLVAPEVV---EAYRRRIDELEETIQ-QIDEEDRAEKELRIAEASMAKTQNALEVGENGGAPAE---RRVWMMKES-QI 590
Cdd:pfam12128 588 KRIDVPEWAaseEELRERLDKAEEALQsAREKQAAAEEQLVQANGELEKASREETFARTALKNARldlRRLFDEKQSeKD 667
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 392884823 591 EKQRKREEKRQMKVDARKKAEAAKTPEDIQIEHEAAFHVRAAKRARHSKNKRIRAVVE 648
Cdd:pfam12128 668 KKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEG 725
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
186-312 |
9.68e-03 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 37.65 E-value: 9.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392884823 186 KDICACAATGTGKT---AAFVLPILERMIYRpkgasctRVLVLVPTRELAIQVFQVFRKLSTFiQLEVCLCAGGLDLKAQ 262
Cdd:pfam04851 24 KRGLIVMATGSGKTltaAKLIARLFKKGPIK-------KVLFLVPRKDLLEQALEEFKKFLPN-YVEIGEIISGDKKDES 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 392884823 263 EAALRsgpdVVVATPGRLIDHLHNSPSFNLSN-IEVLVLDEADRMLEEAFR 312
Cdd:pfam04851 96 VDDNK----IVVTTIQSLYKALELASLELLPDfFDVIIIDEAHRSGASSYR 142
|
|
| |
