|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
380-793 |
9.35e-111 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 348.29 E-value: 9.35e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 380 TSWTNSGLHPTILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKILRmdeetrNKARQddgP 459
Cdd:COG0513 2 MSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDP------SRPRA---P 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 460 LALILAPTRELAAQIHEALRTYCQNTDIIVLLSYGQSDRARSLNEIRNGCDILIGTCGRIMDFTVKSHISLLHLRFLVFD 539
Cdd:COG0513 73 QALILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 540 EADRLLqDMkkdplghlgaiikdaGFMES--------AATRQTIMTSATFNASVMTVANELMKRlPgqdEMIKiVLANGR 611
Cdd:COG0513 153 EADRML-DM---------------GFIEDierilkllPKERQTLLFSATMPPEIRKLAKRYLKN-P---VRIE-VAPENA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 612 LSKRVNLEFFECKGlAEKNAKLREILKQNVNGktlKTIIFVQKKDQCDACAAKLTSGGMLAQTLHGDRSQDMREKLINDF 691
Cdd:COG0513 212 TAETIEQRYYLVDK-RDKLELLRRLLRDEDPE---RAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAF 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 692 KSNRVNLLVTTDLLSRGIDVSDLDRVINFDLPDgDPdqgaDTFIHRAGRTGRTGRKenGLCVSFVDPQsDRDSLlapKLV 771
Cdd:COG0513 288 RNGKIRVLVATDVAARGIDIDDVSHVINYDLPE-DP----EDYVHRIGRTGRAGAE--GTAISLVTPD-ERRLL---RAI 356
|
410 420
....*....|....*....|..
gi 392921583 772 ELIISQNLPDLKVPDFLDAMAK 793
Cdd:COG0513 357 EKLIGQKIEEEELPGFEPVEEK 378
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
387-756 |
3.73e-60 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 212.11 E-value: 3.73e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 387 LHPTILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKILrmdeetrNKARQDDGP-LALILA 465
Cdd:PRK11192 8 LDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLL-------DFPRRKSGPpRILILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 466 PTRELAAQIHEALRTYCQNT--DIIVL---LSYGQSDRARSLNEirngcDILIGTCGRIMDFTVKSHISLLHLRFLVFDE 540
Cdd:PRK11192 81 PTRELAMQVADQARELAKHThlDIATItggVAYMNHAEVFSENQ-----DIVVATPGRLLQYIKEENFDCRAVETLILDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 541 ADRLLqDMkkdplghlgaiikdaGFME-----SAATR---QTIMTSATFNAS-VMTVANELMKrlpgqdEMIKI-VLANG 610
Cdd:PRK11192 156 ADRML-DM---------------GFAQdietiAAETRwrkQTLLFSATLEGDaVQDFAERLLN------DPVEVeAEPSR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 611 RLSKRVNLEFFECKGLAEKNAKLREILKQNvngKTLKTIIFVQKKDQCDACAAKLTSGGMLAQTLHGDRSQDMREKLIND 690
Cdd:PRK11192 214 RERKKIHQWYYRADDLEHKTALLCHLLKQP---EVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKR 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392921583 691 FKSNRVNLLVTTDLLSRGIDVSDLDRVINFDLPdgdpdQGADTFIHRAGRTGRTGRKenGLCVSFV 756
Cdd:PRK11192 291 LTDGRVNVLVATDVAARGIDIDDVSHVINFDMP-----RSADTYLHRIGRTGRAGRK--GTAISLV 349
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
380-783 |
1.51e-59 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 210.81 E-value: 1.51e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 380 TSWTNSGLHPTILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKIlrmdeETRNKARQddgp 459
Cdd:PRK11776 4 TAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL-----DVKRFRVQ---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 460 lALILAPTRELAAQIHEALRT---YCQNTDIIVlLSYGQSDRARsLNEIRNGCDILIGTCGRIMDFTVKSHISLLHLRFL 536
Cdd:PRK11776 75 -ALVLCPTRELADQVAKEIRRlarFIPNIKVLT-LCGGVPMGPQ-IDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 537 VFDEADRLLqDMkkdplG---HLGAIIKDAgfmesAATRQTIMTSATFNASVMTVANELMKrlpgQDEMIKI--VLANGR 611
Cdd:PRK11776 152 VLDEADRML-DM-----GfqdAIDAIIRQA-----PARRQTLLFSATYPEGIAAISQRFQR----DPVEVKVesTHDLPA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 612 LSKRvnleFFECKGlAEKNAKLREILKQNvngKTLKTIIFVQKKDQCDACAAKLTSGGMLAQTLHGDRSQDMREKLINDF 691
Cdd:PRK11776 217 IEQR----FYEVSP-DERLPALQRLLLHH---QPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRF 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 692 --KSNRVnlLVTTDLLSRGIDVSDLDRVINFDLPdgdPDqgADTFIHRAGRTGRTGRKenGLCVSFVdpqSDRDSLLAPK 769
Cdd:PRK11776 289 anRSCSV--LVATDVAARGLDIKALEAVINYELA---RD--PEVHVHRIGRTGRAGSK--GLALSLV---APEEMQRANA 356
|
410
....*....|....*...
gi 392921583 770 LVEL----IISQNLPDLK 783
Cdd:PRK11776 357 IEDYlgrkLNWEPLPSLS 374
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
230-799 |
5.97e-59 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 211.56 E-value: 5.97e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 230 DNHQGGHDSYRGQNSGGYSGNNSgeyrndYRSQQDSrdHRSGGNNSSSGFKNDGGFGGndnrgfgnngggsfgnpnnSYR 309
Cdd:PTZ00110 1 MRSTDGSSSNGSVSSGPSNNYNS------YGPYPDS--SNPYGNYQANHQDNYGGFRP-------------------GYG 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 310 GNSNNIGGF-HRSDGSNSEGVNApvrAPRDW-----VPVTR-------DIDELVRETADRLADCDvgQDRAVEIRNAEKD 376
Cdd:PTZ00110 54 NYSGGYGGFgMNSYGSSTLGKRL---QPIDWksinlVPFEKnfykehpEVSALSSKEVDEIRKEK--EITIIAGENVPKP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 377 VrlTSWTNSGLHPTILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKILrmdeeTRNKARQD 456
Cdd:PTZ00110 129 V--VSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHIN-----AQPLLRYG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 457 DGPLALILAPTRELAAQIHEALRTYCQNTDIIVLLSYGQSDRARSLNEIRNGCDILIGTCGRIMDFTVKSHISLLHLRFL 536
Cdd:PTZ00110 202 DGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 537 VFDEADRLLqDMKKDPlghlgAIIKDAGfmESAATRQTIMTSATFNASVMTVANELMKRLPGQDEMIKIVL-ANGRLSKR 615
Cdd:PTZ00110 282 VLDEADRML-DMGFEP-----QIRKIVS--QIRPDRQTLMWSATWPKEVQSLARDLCKEEPVHVNVGSLDLtACHNIKQE 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 616 VNL--EFfeckglaEKNAKLREILKQnVNGKTLKTIIFVQKKDQCDACAAKLTSGGMLAQTLHGDRSQDMREKLINDFKS 693
Cdd:PTZ00110 354 VFVveEH-------EKRGKLKMLLQR-IMRDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKT 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 694 NRVNLLVTTDLLSRGIDVSDLDRVINFDLPDGDPDqgadtFIHRAGRTGRTGRKenGLCVSFVDPQSDRdslLAPKLVEL 773
Cdd:PTZ00110 426 GKSPIMIATDVASRGLDVKDVKYVINFDFPNQIED-----YVHRIGRTGRAGAK--GASYTFLTPDKYR---LARDLVKV 495
|
570 580
....*....|....*....|....*.
gi 392921583 774 IISQNLPdlkVPDFLDAMAKSSRGKS 799
Cdd:PTZ00110 496 LREAKQP---VPPELEKLSNERSNGT 518
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
391-595 |
2.16e-56 |
|
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: 193.04 E-value: 2.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 391 ILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKILRmdeetrNKARQDDGPLALILAPTREL 470
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLP------EPKKKGRGPQALVLAPTREL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 471 AAQIHEALRTYCQNTDIIVLLSYGQSDRARSLNEIRNGCDILIGTCGRIMDFTVKSHISLLHLRFLVFDEADRLLqDMkk 550
Cdd:cd00268 75 AMQIAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRML-DM-- 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 392921583 551 dplGHLGAIIKDAGFMEsaATRQTIMTSATFNASVMTVANELMKR 595
Cdd:cd00268 152 ---GFEEDVEKILSALP--KDRQTLLFSATLPEEVKELAKKFLKN 191
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
386-755 |
1.85e-55 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 198.27 E-value: 1.85e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 386 GLHPTILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKILRMDEetrNKARQDDGPLALILA 465
Cdd:PRK04837 14 ALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPA---PEDRKVNQPRALIMA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 466 PTRELAAQIHEALRTYCQNTDIIVLLSYGQSDRARSLNEIRNGCDILIGTCGRIMDFTVKSHISLLHLRFLVFDEADRLL 545
Cdd:PRK04837 91 PTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 546 QdmkkdpLGhlgaIIKDAGF----MESAATRQTIMTSATFNASVMTVANELMkrlpgqDEMIKIVLA-NGRLSKRVNLEF 620
Cdd:PRK04837 171 D------LG----FIKDIRWlfrrMPPANQRLNMLFSATLSYRVRELAFEHM------NNPEYVEVEpEQKTGHRIKEEL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 621 FeckgLAEKNAKLREILkqnvngkTL-------KTIIFVQKKDQCDACAAKLTSGGMLAQTLHGDRSQDMREKLINDFKS 693
Cdd:PRK04837 235 F----YPSNEEKMRLLQ-------TLieeewpdRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTR 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392921583 694 NRVNLLVTTDLLSRGIDVSDLDRVINFDLPDGDPDqgadtFIHRAGRTGRTGrkENGLCVSF 755
Cdd:PRK04837 304 GDLDILVATDVAARGLHIPAVTHVFNYDLPDDCED-----YVHRIGRTGRAG--ASGHSISL 358
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
381-595 |
1.51e-54 |
|
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: 188.85 E-value: 1.51e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 381 SWTNSGLHPTILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKILRMDEETRNKARQDDGPL 460
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGRRKAYPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 461 ALILAPTRELAAQIHEALRTYCQNTDIIVLLSYGQSDRARSLNEIRNGCDILIGTCGRIMDFTVKSHISLLHLRFLVFDE 540
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 392921583 541 ADRLLqDMkkdplGHLGAI--IKDAGFMESAATRQTIMTSATFNASVMTVANELMKR 595
Cdd:cd17967 161 ADRML-DM-----GFEPQIrkIVEHPDMPPKGERQTLMFSATFPREIQRLAADFLKN 211
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
387-774 |
3.78e-53 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 193.21 E-value: 3.78e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 387 LHPTILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKILRMDEEtrnKARQDDGPLALILAP 466
Cdd:PRK01297 94 LAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPP---KERYMGEPRALIIAP 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 467 TRELAAQIHEALRTYCQNTDIIVLLSYGQSDRARSLNEIR-NGCDILIGTCGRIMDFTVKSHISLLHLRFLVFDEADRLL 545
Cdd:PRK01297 171 TRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEADRML 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 546 qDMKKDPlgHLGAIIKdagFMESAATRQTIMTSATFNASVMTVANELMKRlPGQDEMIKIVLANGRLSKRVnlefFECKG 625
Cdd:PRK01297 251 -DMGFIP--QVRQIIR---QTPRKEERQTLLFSATFTDDVMNLAKQWTTD-PAIVEIEPENVASDTVEQHV----YAVAG 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 626 lAEKNAKLREILKQNvngKTLKTIIFVQKKDQCDACAAKLTSGGMLAQTLHGDRSQDMREKLINDFKSNRVNLLVTTDLL 705
Cdd:PRK01297 320 -SDKYKLLYNLVTQN---PWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVA 395
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392921583 706 SRGIDVSDLDRVINFDLPDgDPDQgadtFIHRAGRTGRTGRKenGLCVSFVdpqSDRDSLLAPKLVELI 774
Cdd:PRK01297 396 GRGIHIDGISHVINFTLPE-DPDD----YVHRIGRTGRAGAS--GVSISFA---GEDDAFQLPEIEELL 454
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
381-787 |
2.89e-48 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 178.46 E-value: 2.89e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 381 SWTNSGLHPTILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDkiLRMDEETRNKARQddgPL 460
Cdd:PRK10590 2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQ--HLITRQPHAKGRR---PV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 461 -ALILAPTRELAAQIHEALRTYCQNTDIIVLLSYGQSDRARSLNEIRNGCDILIGTCGRIMDFTVKSHISLLHLRFLVFD 539
Cdd:PRK10590 77 rALILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 540 EADRLLqdmkkdplghlgaiikDAGFMES--------AATRQTIMTSATFNASVMTVANELMKRlPGQDEMIKIVLANGR 611
Cdd:PRK10590 157 EADRML----------------DMGFIHDirrvlaklPAKRQNLLFSATFSDDIKALAEKLLHN-PLEIEVARRNTASEQ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 612 LSKRVNLeffeckglAEKNAKlREILKQNV-NGKTLKTIIFVQKKDQCDACAAKLTSGGMLAQTLHGDRSQDMREKLIND 690
Cdd:PRK10590 220 VTQHVHF--------VDKKRK-RELLSQMIgKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALAD 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 691 FKSNRVNLLVTTDLLSRGIDVSDLDRVINFDLPDGDPDqgadtFIHRAGRTGR---TGRKENGLCVsfvdpqsDRDSLLa 767
Cdd:PRK10590 291 FKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPED-----YVHRIGRTGRaaaTGEALSLVCV-------DEHKLL- 357
|
410 420
....*....|....*....|
gi 392921583 768 pKLVELIISQNLPDLKVPDF 787
Cdd:PRK10590 358 -RDIEKLLKKEIPRIAIPGY 376
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
376-796 |
9.51e-48 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 179.76 E-value: 9.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 376 DVRLTSWTNSG--LHPTILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKILrmdeeTRNKA 453
Cdd:PRK04537 3 DKPLTDLTFSSfdLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLL-----SRPAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 454 --RQDDGPLALILAPTRELAAQIHEALRTYCQNTDIIVLLSYGQSDRARSLNEIRNGCDILIGTCGRIMDFtVKSH--IS 529
Cdd:PRK04537 78 adRKPEDPRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDY-VKQHkvVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 530 LLHLRFLVFDEADRLLQdmkkdpLGhlgaIIKDAGF----MESAATRQTIMTSATFNASVMTVANELM---KRLPGQDEM 602
Cdd:PRK04537 157 LHACEICVLDEADRMFD------LG----FIKDIRFllrrMPERGTRQTLLFSATLSHRVLELAYEHMnepEKLVVETET 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 603 IkivlANGRLSKRVnleFFECKglAEKNAKLREILKQNvngKTLKTIIFVQKKDQCDACAAKLTSGGMLAQTLHGDRSQD 682
Cdd:PRK04537 227 I----TAARVRQRI---YFPAD--EEKQTLLLGLLSRS---EGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQK 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 683 MREKLINDFKSNRVNLLVTTDLLSRGIDVSDLDRVINFDLPdgdpdQGADTFIHRAGRTGRTGrkENGLCVSFVdpqSDR 762
Cdd:PRK04537 295 KRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVYNYDLP-----FDAEDYVHRIGRTARLG--EEGDAISFA---CER 364
|
410 420 430
....*....|....*....|....*....|....*
gi 392921583 763 DSLLAPKlVELIISQNLPDLKV-PDFLDAMAKSSR 796
Cdd:PRK04537 365 YAMSLPD-IEAYIEQKIPVEPVtAELLTPLPRPPR 398
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
367-594 |
7.87e-47 |
|
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: 168.61 E-value: 7.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 367 AVEIRNAEKDVRLTSWTNSGLHPTILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKILRmd 446
Cdd:cd18052 30 PVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMK-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 447 eeTRNKARQDDG---PLALILAPTRELAAQIHEALRTYCQNTDIIVLLSYGQSDRARSLNEIRNGCDILIGTCGRIMDFT 523
Cdd:cd18052 108 --EGLTASSFSEvqePQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFI 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392921583 524 VKSHISLLHLRFLVFDEADRLLqDMKKDPlgHLGAIIKDAGfMESAATRQTIMTSATFNASVMTVANELMK 594
Cdd:cd18052 186 GRGKISLSKLKYLILDEADRML-DMGFGP--EIRKLVSEPG-MPSKEDRQTLMFSATFPEEIQRLAAEFLK 252
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
404-588 |
6.41e-45 |
|
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: 159.33 E-value: 6.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 404 RTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKIlrmdeetrnkARQDDGPLALILAPTRELAAQIHEALRTYCQ 483
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAL----------DKLDNGPQALVLAPTRELAEQIYEELKKLGK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 484 NTDIIVLLSYGQSDRARSLNEIRnGCDILIGTCGRIMDFTVKSHiSLLHLRFLVFDEADRLLQDMKKDplgHLGAIIKDA 563
Cdd:pfam00270 71 GLGLKVASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGP---DLEEILRRL 145
|
170 180
....*....|....*....|....*
gi 392921583 564 GfmesaATRQTIMTSATFNASVMTV 588
Cdd:pfam00270 146 P-----KKRQILLLSATLPRNLEDL 165
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
380-786 |
1.57e-44 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 171.18 E-value: 1.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 380 TSWTNSGLHPTILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKIlrmDEETRnkarqddGP 459
Cdd:PRK11634 6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNL---DPELK-------AP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 460 LALILAPTRELAAQIHEALRTYCQNT-DIIVLLSYGQSDRARSLNEIRNGCDILIGTCGRIMDFTVKSHISLLHLRFLVF 538
Cdd:PRK11634 76 QILVLAPTRELAVQVAEAMTDFSKHMrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 539 DEADRLLQdmkkdplghlgaiikdAGFMESA--------ATRQTIMTSATFNASVMTVANELMKRlPGQDEMIKIVLANG 610
Cdd:PRK11634 156 DEADEMLR----------------MGFIEDVetimaqipEGHQTALFSATMPEAIRRITRRFMKE-PQEVRIQSSVTTRP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 611 RLSKrvnlEFFECKGLAEKNAKLREILKQNVNGktlkTIIFVQKKDQCDACAAKLTSGGMLAQTLHGDRSQDMREKLIND 690
Cdd:PRK11634 219 DISQ----SYWTVWGMRKNEALVRFLEAEDFDA----AIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLER 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 691 FKSNRVNLLVTTDLLSRGIDVSDLDRVINFDLPdgdpdQGADTFIHRAGRTGRTGRKenGLCVSFVDPQSDRdsLLapKL 770
Cdd:PRK11634 291 LKDGRLDILIATDVAARGLDVERISLVVNYDIP-----MDSESYVHRIGRTGRAGRA--GRALLFVENRERR--LL--RN 359
|
410
....*....|....*.
gi 392921583 771 VELIISQNLPDLKVPD 786
Cdd:PRK11634 360 IERTMKLTIPEVELPN 375
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
387-594 |
3.07e-42 |
|
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: 153.51 E-value: 3.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 387 LHPTILETLKRIKYNNVRTIQGAMIPQVL-DGHDVLGQAETSAGKTAAFGLPIIDKILRmdeetRNKARQDDGPLALILA 465
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPAIQSLLN-----TKPAGRRSGVSALIIS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 466 PTRELAAQIHEALRTYCQN-TDIIVLLSYGQSDRARSLNEI-RNGCDILIGTCGRIMDF--TVKSHISLLHLRFLVFDEA 541
Cdd:cd17964 76 PTRELALQIAAEAKKLLQGlRKLRVQSAVGGTSRRAELNRLrRGRPDILVATPGRLIDHleNPGVAKAFTDLDYLVLDEA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 392921583 542 DRLLqDMkkdplGHLGAI--IKDAGFMESAATRQTIMTSATFNASVMTVANELMK 594
Cdd:cd17964 156 DRLL-DM-----GFRPDLeqILRHLPEKNADPRQTLLFSATVPDEVQQIARLTLK 204
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
616-756 |
1.80e-41 |
|
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350174 [Multi-domain] Cd Length: 131 Bit Score: 148.04 E-value: 1.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 616 VNLEFFECKGLAEKNAKLREILKQNVNGKTlktIIFVQKKDQCDACAAKLTSGGMLAQTLHGDRSQDMREKLINDFKSNR 695
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKA---IIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGK 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392921583 696 VNLLVTTDLLSRGIDVSDLDRVINFDLPDgdpdqGADTFIHRAGRTGRTGRKenGLCVSFV 756
Cdd:cd18787 78 VRVLVATDVAARGLDIPGVDHVINYDLPR-----DAEDYVHRIGRTGRAGRK--GTAITFV 131
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
381-776 |
2.32e-41 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 159.95 E-value: 2.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 381 SWTNSGLHPTILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDK--ILRMDEETRNKarqddG 458
Cdd:PLN00206 122 SFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRccTIRSGHPSEQR-----N 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 459 PLALILAPTRELAAQIHEALRTYCQNTDIIVLLSYGQSDRARSLNEIRNGCDILIGTCGRIMDFTVKSHISLLHLRFLVF 538
Cdd:PLN00206 197 PLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVL 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 539 DEADRLLQDMKKDPLGHLgaiikdagfMESAATRQTIMTSATFNASVMTVANELMKrlpgqdEMIKIVLAN-GRLSKRVN 617
Cdd:PLN00206 277 DEVDCMLERGFRDQVMQI---------FQALSQPQVLLFSATVSPEVEKFASSLAK------DIILISIGNpNRPNKAVK 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 618 --LEFFECKglaEKNAKLREILKQNVNGKTlKTIIFVQKKDQCDACAAKLT-SGGMLAQTLHGDRSQDMREKLINDFKSN 694
Cdd:PLN00206 342 qlAIWVETK---QKKQKLFDILKSKQHFKP-PAVVFVSSRLGADLLANAITvVTGLKALSIHGEKSMKERREVMKSFLVG 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 695 RVNLLVTTDLLSRGIDVSDLDRVINFDLPDgdpdqGADTFIHRAGRTGRTGrkENGLCVSFVDPQSDRdslLAPKLVELI 774
Cdd:PLN00206 418 EVPVIVATGVLGRGVDLLRVRQVIIFDMPN-----TIKEYIHQIGRASRMG--EKGTAIVFVNEEDRN---LFPELVALL 487
|
..
gi 392921583 775 IS 776
Cdd:PLN00206 488 KS 489
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
391-596 |
2.16e-40 |
|
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: 147.74 E-value: 2.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 391 ILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKILRmdeetrnkARQDDGPLALILAPTREL 470
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGK--------PRKKKGLRALILAPTREL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 471 AAQIHEALRTYCQNTDI-IVLLSYGQSDRARSLNEIRNGCDILIGTCGRIMDFTVKSHISLLHLRFLVFDEADRLLqdmk 549
Cdd:cd17957 73 ASQIYRELLKLSKGTGLrIVLLSKSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLF---- 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 392921583 550 kdplghlgaiikDAGFME---------SAATRQTIMTSATFNASVMTVANELMKRL 596
Cdd:cd17957 149 ------------EPGFREqtdeilaacTNPNLQRSLFSATIPSEVEELARSVMKDP 192
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
396-585 |
6.37e-40 |
|
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: 146.96 E-value: 6.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 396 KRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKILRMDeetrNKARQDDGPLALILAPTRELAAQIH 475
Cdd:cd17949 7 SKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLE----PRVDRSDGTLALVLVPTRELALQIY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 476 EALRTYCQNTDIIV--LLSYGQ---SDRARslneIRNGCDILIGTCGRIMDftvksHI------SLLHLRFLVFDEADRL 544
Cdd:cd17949 83 EVLEKLLKPFHWIVpgYLIGGEkrkSEKAR----LRKGVNILIATPGRLLD-----HLkntqsfDVSNLRWLVLDEADRL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 392921583 545 LqDMK-----KDPLGHLGAIIKDAGFMESA-ATRQTIMTSATFNASV 585
Cdd:cd17949 154 L-DMGfekdiTKILELLDDKRSKAGGEKSKpSRRQTVLVSATLTDGV 199
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
406-759 |
5.46e-39 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 149.98 E-value: 5.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 406 IQGAMIPQVLDGHDVLGQAETSAGKTAAFglpIIDKILRMDEETRNKArqddgplALILAPTRELAAQIHE---ALRTYC 482
Cdd:PTZ00424 54 IQQRGIKPILDGYDTIGQAQSGTGKTATF---VIAALQLIDYDLNACQ-------ALILAPTRELAQQIQKvvlALGDYL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 483 qntDIIVLLSYGQSDRARSLNEIRNGCDILIGTCGRIMDFTVKSHISLLHLRFLVFDEADRLLQDMKKDPlghlgaiIKD 562
Cdd:PTZ00424 124 ---KVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFKGQ-------IYD 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 563 AgFMESAATRQTIMTSATFNASVMTVANELMkRLPgqdemIKIVLANGRLSKRVNLEFFEckgLAEKNAKLREILKQNVN 642
Cdd:PTZ00424 194 V-FKKLPPDVQVALFSATMPNEILELTTKFM-RDP-----KRILVKKDELTLEGIRQFYV---AVEKEEWKFDTLCDLYE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 643 GKTL-KTIIFVQKKDQCDACAAKLTSGGMLAQTLHGDRSQDMREKLINDFKSNRVNLLVTTDLLSRGIDVSDLDRVINFD 721
Cdd:PTZ00424 264 TLTItQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYD 343
|
330 340 350
....*....|....*....|....*....|....*...
gi 392921583 722 LPdgdpdQGADTFIHRAGRTGRTGRKenGLCVSFVDPQ 759
Cdd:PTZ00424 344 LP-----ASPENYIHRIGRSGRFGRK--GVAINFVTPD 374
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
391-595 |
1.02e-38 |
|
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: 143.61 E-value: 1.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 391 ILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKILR---MDEETRnkarqDDGPLALILAPT 467
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRlppLDEETK-----DDGPYALILAPT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 468 RELAAQIHEALRTYCQNTDI-IVLLSYGQSDRARSLnEIRNGCDILIGTCGRIMDFTVKSHISLLHLRFLVFDEADRLLq 546
Cdd:cd17945 76 RELAQQIEEETQKFAKPLGIrVVSIVGGHSIEEQAF-SLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMI- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392921583 547 DMKKDP-----LGHLGAIIK--DAGFMESAAT------RQTIMTSATFNASVMTVANELMKR 595
Cdd:cd17945 154 DMGFEPqvtkiLDAMPVSNKkpDTEEAEKLAAsgkhryRQTMMFTATMPPAVEKIAKGYLRR 215
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
379-595 |
3.00e-37 |
|
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: 139.43 E-value: 3.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 379 LTSWTNSGLHPTILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKILRMDeetrnKARQDDG 458
Cdd:cd17953 11 IQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQR-----PVKPGEG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 459 PLALILAPTRELAAQIHEALRTYCQNTDIIVLLSYGQSDRARSLNEIRNGCDILIGTCGRIMDFTVKSHISLLHLR---F 535
Cdd:cd17953 86 PIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNGRVTNLRrvtY 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 536 LVFDEADRLLqDMKKDPlgHLGAIIKDAgfmesAATRQTIMTSATFNASVMTVANELMKR 595
Cdd:cd17953 166 VVLDEADRMF-DMGFEP--QIMKIVNNI-----RPDRQTVLFSATFPRKVEALARKVLHK 217
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
406-595 |
3.93e-36 |
|
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: 135.46 E-value: 3.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 406 IQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKILRmdeetrnKARQDDGPLALILAPTRELAAQIHEALRTYCQNT 485
Cdd:cd17947 16 IQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLY-------RPKKKAATRVLVLVPTRELAMQCFSVLQQLAQFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 486 DIIVLLSYGQSDRARSLNEIRNGCDILIGTCGRIMDFTVKSH-ISLLHLRFLVFDEADRLLQDMKKDplgHLGAIIKdag 564
Cdd:cd17947 89 DITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGFAD---ELKEILR--- 162
|
170 180 190
....*....|....*....|....*....|.
gi 392921583 565 fmESAATRQTIMTSATFNASVMTVANELMKR 595
Cdd:cd17947 163 --LCPRTRQTMLFSATMTDEVKDLAKLSLNK 191
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
379-581 |
7.18e-36 |
|
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: 136.32 E-value: 7.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 379 LTSWTNSGLHPTILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKILR------MDEETRNK 452
Cdd:cd18051 20 IETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEqgpgesLPSESGYY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 453 ARQDDGPLALILAPTRELAAQIHEALRTYCQNTDIIVLLSYGQSDRARSLNEIRNGCDILIGTCGRIMDFTVKSHISLLH 532
Cdd:cd18051 100 GRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDY 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 392921583 533 LRFLVFDEADRLLqDMKKDPlgHLGAII-KDAgfMESAATRQTIMTSATF 581
Cdd:cd18051 180 CKYLVLDEADRML-DMGFEP--QIRRIVeQDT--MPPTGERQTLMFSATF 224
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
386-595 |
7.91e-35 |
|
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: 131.96 E-value: 7.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 386 GLHPTILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKiLRMDEEtrnkarqddGPLALILA 465
Cdd:cd17955 5 GLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQR-LSEDPY---------GIFALVLT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 466 PTRELAAQIHEALRTYCQNTDIIVLLSYGQSDRARSLNEIRNGCDILIGTCGRIMDftvksHI--------SLLHLRFLV 537
Cdd:cd17955 75 PTRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLAD-----HLrssddttkVLSRVKFLV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 392921583 538 FDEADRLLQDMKKDPLGHLGAIIKdagfmesaATRQTIMTSATFNASVMTVANELMKR 595
Cdd:cd17955 150 LDEADRLLTGSFEDDLATILSALP--------PKRQTLLFSATLTDALKALKELFGNK 199
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
391-621 |
1.14e-34 |
|
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: 132.36 E-value: 1.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 391 ILETLKRIKYNNVRTIQGAMIPQ-VLDGHDVLGQAETSAGKTAAFGLPIIDKILRmDEETRNKARQDDGPLALILAPTRE 469
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAaIRDGKDVIGAAETGSGKTLAFGIPILERLLS-QKSSNGVGGKQKPLRALILTPTRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 470 LAAQIHEALRTYCQNTDI-IVLLSYGQS--DRARSLNeirNGCDILIGTCGRIMDFTVKSH---ISLLHLRFLVFDEADR 543
Cdd:cd17946 80 LAVQVKDHLKAIAKYTNIkIASIVGGLAvqKQERLLK---KRPEIVVATPGRLWELIQEGNehlANLKSLRFLVLDEADR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 544 LLQDmkkdplGH---LGAIIKDAGFMESAAT--RQTIMTSATFN-ASVMTVANELMKRLPGQDEMIKIVLANGRLSKRVN 617
Cdd:cd17946 157 MLEK------GHfaeLEKILELLNKDRAGKKrkRQTFVFSATLTlDHQLPLKLNSKKKKKKKEKKQKLELLIEKVGFRKK 230
|
....
gi 392921583 618 LEFF 621
Cdd:cd17946 231 PKVI 234
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
391-594 |
1.24e-34 |
|
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: 130.95 E-value: 1.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 391 ILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKILrmdeeTRNKARQDDGPLALILAPTREL 470
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHIN-----AQPPLERGDGPIVLVLAPTREL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 471 AAQIHEALRTYCQNTDIIVLLSYGQSDRARSLNEIRNGCDILIGTCGRIMDFTVKSHISLLHLRFLVFDEADRLLqDMKK 550
Cdd:cd17966 76 AQQIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRML-DMGF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 392921583 551 DPlgHLGAIIKdagfmESAATRQTIMTSATFNASVMTVANELMK 594
Cdd:cd17966 155 EP--QIRKIVD-----QIRPDRQTLMWSATWPKEVRRLAEDFLK 191
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
395-596 |
4.84e-34 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 129.53 E-value: 4.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 395 LKRIKYNNVRTIQGAMIPQVLDG-HDVLGQAETSAGKTAAFGLPIIDKILRmdeetrnkarqDDGPLALILAPTRELAAQ 473
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKR-----------GKGGRVLVLVPTRELAEQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 474 IHEALRTYCQNTDIIVLLSYGQSDRARSLNEIRNGC-DILIGTCGRIMDFTVKSHISLLHLRFLVFDEADRLLQDMKKDP 552
Cdd:smart00487 70 WAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 392921583 553 LGHLGAIIKDAgfmesaatRQTIMTSATFNASVMTVANELMKRL 596
Cdd:smart00487 150 LEKLLKLLPKN--------VQLLLLSATPPEEIENLLELFLNDP 185
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
387-596 |
6.45e-34 |
|
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of infectious West Nile virus particles. New research suggests that DDX56 relocalizes to the site of virus assembly during WNV infection and that its interaction with WNV capsid in the cytoplasm may occur transiently during virion morphogenesis. DDX56 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350719 [Multi-domain] Cd Length: 206 Bit Score: 129.24 E-value: 6.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 387 LHPTILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKILRMDEETRNKarqdDGPLALILAP 466
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGEE----QGTRALILVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 467 TRELAAQIHEALR---TYCqnTDIIVLLSYGQSDRARSLNEIRNGC-DILIGTCGRIMDFTVKSHISLL-HLRFLVFDEA 541
Cdd:cd17961 77 TRELAQQVSKVLEqltAYC--RKDVRVVNLSASSSDSVQRALLAEKpDIVVSTPARLLSHLESGSLLLLsTLKYLVIDEA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 542 DRLL-----QDMKKdPLGHLGAIIkdagfmesaatrQTIMTSATFNASVmtvanELMKRL 596
Cdd:cd17961 155 DLVLsygyeEDLKS-LLSYLPKNY------------QTFLMSATLSEDV-----EALKKL 196
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
391-594 |
2.02e-33 |
|
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis antigen 13 or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 is also called cancer/testis antigen 26 or DEAD-Box Protein CAGE. Both DDX46 and DDX53 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350716 [Multi-domain] Cd Length: 197 Bit Score: 127.58 E-value: 2.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 391 ILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPiidKILRMDEETRNKArQDDGPLALILAPTREL 470
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLP---GFIHLDLQPIPRE-QRNGPGVLVLTPTREL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 471 AAQIHEALRTYCQNtDIIVLLSYGQSDRARSLNEIRNGCDILIGTCGRIMDFTVKSHISLLHLRFLVFDEADRLLqDMKK 550
Cdd:cd17958 77 ALQIEAECSKYSYK-GLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRML-DMGF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 392921583 551 DPlghlgAIIKDagFMESAATRQTIMTSATFNASVMTVANELMK 594
Cdd:cd17958 155 EP-----QIRKI--LLDIRPDRQTIMTSATWPDGVRRLAQSYLK 191
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
391-593 |
2.42e-33 |
|
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: 127.53 E-value: 2.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 391 ILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKIlrMDEETRNKarqDDGPLALILAPTREL 470
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHI--MDQRELEK---GEGPIAVIVAPTREL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 471 AAQIHEALRTYCQNTDIIVLLSYGQSDRARSLNEIRNGCDILIGTCGRIMDFTVKSHISLLHLRFLVFDEADRLLqDMKK 550
Cdd:cd17952 76 AQQIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMF-DMGF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 392921583 551 DP--LGHLGAIIKDagfmesaatRQTIMTSATFNASVMTVANELM 593
Cdd:cd17952 155 EYqvRSIVGHVRPD---------RQTLLFSATFKKKIEQLARDIL 190
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
386-595 |
3.82e-33 |
|
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: 127.05 E-value: 3.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 386 GLHPTILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIdKILRmdeetrnkarqddgplALILA 465
Cdd:cd17938 5 GVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL-QIVV----------------ALILE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 466 PTRELAAQIHEALRT---YCQNTDIIVLLSYGQSDRARSLNEIRNGCDILIGTCGRIMDFTVKSHISLLHLRFLVFDEAD 542
Cdd:cd17938 68 PSRELAEQTYNCIENfkkYLDNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEAD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 392921583 543 RLLQDMKKDPLGHLGAIIKDAGfmeSAATR-QTIMTSATFNA-SVMTVANELMKR 595
Cdd:cd17938 148 RLLSQGNLETINRIYNRIPKIT---SDGKRlQVIVCSATLHSfEVKKLADKIMHF 199
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
386-580 |
7.72e-33 |
|
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: 126.27 E-value: 7.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 386 GLHPTILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKIlrMDEETRNKARqddgplALILA 465
Cdd:cd17959 7 GLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKL--KAHSPTVGAR------ALILS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 466 PTRELAAQIHEALRTYCQNTDIIVLLSYGQSDRARSLNEIRNGCDILIGTCGRIMDFTVKSHISLLHLRFLVFDEADRL- 544
Cdd:cd17959 79 PTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLf 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 392921583 545 ---LQDMKKDPLGHLgaiikdagfmesAATRQTIMTSAT 580
Cdd:cd17959 159 emgFAEQLHEILSRL------------PENRQTLLFSAT 185
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
391-580 |
1.20e-32 |
|
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: 125.91 E-value: 1.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 391 ILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIdkILRMDEETRNKARQDDGPLALILAPTREL 470
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLI--MFALEQEKKLPFIKGEGPYGLIVCPSREL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 471 AAQIHEALRTYCQNTD------IIVLLSYGQSDRARSLNEIRNGCDILIGTCGRIMDFTVKSHISLLHLRFLVFDEADRL 544
Cdd:cd17951 79 ARQTHEVIEYYCKALQeggypqLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 392921583 545 LqdmkkdplghlgaiikDAGFMESAAT--------RQTIMTSAT 580
Cdd:cd17951 159 I----------------DMGFEEDIRTifsyfkgqRQTLLFSAT 186
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
406-594 |
3.21e-32 |
|
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: 124.33 E-value: 3.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 406 IQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKIlrmdeETRNKARQddgplALILAPTRELAAQIHEALRTYCQNT 485
Cdd:cd17940 25 IQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKI-----DPKKDVIQ-----ALILVPTRELALQTSQVCKELGKHM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 486 DIIVLLSYGQSDRARSLNEIRNGCDILIGTCGRIMDFTVKSHISLLHLRFLVFDEADRLL----QDMKKDPLGHLgaiik 561
Cdd:cd17940 95 GVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLsqdfQPIIEKILNFL----- 169
|
170 180 190
....*....|....*....|....*....|...
gi 392921583 562 dagfmesAATRQTIMTSATFNASVMTVANELMK 594
Cdd:cd17940 170 -------PKERQILLFSATFPLTVKNFMDRHMH 195
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
391-556 |
9.56e-32 |
|
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: 123.90 E-value: 9.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 391 ILETLKRIKYNNVRTIQGAMIPQVLDG---------HDVLGQAETSAGKTAAFGLPIIDKIL-RMDEETRnkarqddgpl 460
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSkRVVPRLR---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 461 ALILAPTRELAAQIHEALRTYCQNTDIIVLLSYGQSDRARSLNEIRNGC--------DILIGTCGRIMD-FTVKSHISLL 531
Cdd:cd17956 71 ALIVVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTsgrylsrvDILVATPGRLVDhLNSTPGFTLK 150
|
170 180
....*....|....*....|....*
gi 392921583 532 HLRFLVFDEADRLLQDMKKDPLGHL 556
Cdd:cd17956 151 HLRFLVIDEADRLLNQSFQDWLETV 175
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
391-594 |
1.62e-31 |
|
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: 122.30 E-value: 1.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 391 ILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKILRMDEETRNKarqddGPLALILAPTREL 470
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKKG-----QVGALIISPTREL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 471 AAQIHEALRTYCQNTDI---IVLLSYGQSDRARSLNEIRNGCDILIGTCGRIMDFTVKSH--ISLLHLRFLVFDEADRLL 545
Cdd:cd17960 76 ATQIYEVLQSFLEHHLPklkCQLLIGGTNVEEDVKKFKRNGPNILVGTPGRLEELLSRKAdkVKVKSLEVLVLDEADRLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 392921583 546 qDM--KKDPLGHLGAIIKdagfmesaaTRQTIMTSATFNASVmtvaNELMK 594
Cdd:cd17960 156 -DLgfEADLNRILSKLPK---------QRRTGLFSATQTDAV----EELIK 192
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
391-589 |
1.25e-30 |
|
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: 119.70 E-value: 1.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 391 ILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKILrmdeetRNKARQDDGPLALILAPTREL 470
Cdd:cd17941 1 TLKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLY------RERWTPEDGLGALIISPTREL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 471 AAQIHEALRTYCQNTDIIVLLSYGQSDRARSLNEIrNGCDILIGTCGRI---MDFTVKSHISllHLRFLVFDEADRLLqD 547
Cdd:cd17941 75 AMQIFEVLRKVGKYHSFSAGLIIGGKDVKEEKERI-NRMNILVCTPGRLlqhMDETPGFDTS--NLQMLVLDEADRIL-D 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 392921583 548 MK-KDPlghLGAIIKDAGfmesaATRQTIMTSATFNASVMTVA 589
Cdd:cd17941 151 MGfKET---LDAIVENLP-----KSRQTLLFSATQTKSVKDLA 185
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
386-585 |
2.77e-29 |
|
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can shuttle between the nucleus and the cytoplasm, and has an RNA-independent ATPase activity. DX47 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350712 [Multi-domain] Cd Length: 203 Bit Score: 115.88 E-value: 2.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 386 GLHPTILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKILRmdeetrnkARQddgPL-ALIL 464
Cdd:cd17954 6 GVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLE--------NPQ---RFfALVL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 465 APTRELAAQIHEALRTYCQNTDIIVLLSYGQSDRARSLNEIRNGCDILIGTCGRIMDftvksHI------SLLHLRFLVF 538
Cdd:cd17954 75 APTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVD-----HLentkgfSLKSLKFLVM 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 392921583 539 DEADRLLqDMKKDPlgHLGAIIKdagfmESAATRQTIMTSATFNASV 585
Cdd:cd17954 150 DEADRLL-NMDFEP--EIDKILK-----VIPRERTTYLFSATMTTKV 188
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
391-594 |
6.95e-29 |
|
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: 114.28 E-value: 6.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 391 ILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDkilRMDEETRnkarqddGPLALILAPTREL 470
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALE---SLDLERR-------HPQVLILAPTREI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 471 AAQIHEALRTYCQN-TDIIVLLSYGQSDRARSLNEIrNGCDILIGTCGRIMDFTVKSHISLLHLRFLVFDEADRLLQdmk 549
Cdd:cd17943 71 AVQIHDVFKKIGKKlEGLKCEVFIGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLME--- 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 392921583 550 kdplghlGAIIKDAGFMESA--ATRQTIMTSATFNASVMTVANELMK 594
Cdd:cd17943 147 -------GSFQKDVNWIFSSlpKNKQVIAFSATYPKNLDNLLARYMR 186
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
628-745 |
7.40e-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: 111.15 E-value: 7.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 628 EKNAKLREILKQNVNGKTlktIIFVQKKDQCDACAAkLTSGGMLAQTLHGDRSQDMREKLINDFKSNRVNLLVTTDLLSR 707
Cdd:pfam00271 1 EKLEALLELLKKERGGKV---LIFSQTKKTLEAELL-LEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAER 76
|
90 100 110
....*....|....*....|....*....|....*...
gi 392921583 708 GIDVSDLDRVINFDLPDgdpdqGADTFIHRAGRTGRTG 745
Cdd:pfam00271 77 GLDLPDVDLVINYDLPW-----NPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
391-591 |
9.10e-29 |
|
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: 115.54 E-value: 9.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 391 ILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKILRMDEetrNKARQDDGPLALILAPTREL 470
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKL---LAEGPFNAPRGLVITPSREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 471 AAQIHEALRTYCQNTDIIVLLSYGQSDRARSLNEIRNGCDILIGTCGRIMDFTVKSHISLLHLRFLVFDEADRLLQD--- 547
Cdd:cd17948 78 AEQIGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDsfn 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 392921583 548 ------MKKDPLgHLGAIIKDAGFMESAatrQTIMTSATFNASVMTVANE 591
Cdd:cd17948 158 eklshfLRRFPL-ASRRSENTDGLDPGT---QLVLVSATMPSGVGEVLSK 203
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
391-597 |
2.81e-27 |
|
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: 110.14 E-value: 2.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 391 ILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKIlrmdeeTRNKARQDDGPLALILAPTREL 470
Cdd:cd17942 1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELL------YKLKFKPRNGTGVIIISPTREL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 471 AAQIHEALRTYCQNTDIIVLLSYGQSDRARSLNEIRNGCDILIGTCGRIMD-------FTVKshisllHLRFLVFDEADR 543
Cdd:cd17942 75 ALQIYGVAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDhlqntkgFLYK------NLQCLIIDEADR 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 392921583 544 LLQ-----DMKKdplghlgaIIKDAgfmesAATRQTIMTSATFNASVMTVANELMKRLP 597
Cdd:cd17942 149 ILEigfeeEMRQ--------IIKLL-----PKRRQTMLFSATQTRKVEDLARISLKKKP 194
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
391-594 |
4.94e-27 |
|
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, G17P1, or HUMP68) is involved in pathways that include the alteration of RNA structures, plays a role as a coregulator of transcription, a regulator of splicing, and in the processing of small noncoding RNAs. It synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. Dysregulation of this gene may play a role in cancer development. DDX5 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350807 [Multi-domain] Cd Length: 234 Bit Score: 110.48 E-value: 4.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 391 ILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKIlrmdeETRNKARQDDGPLALILAPTREL 470
Cdd:cd18049 35 VMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHI-----NHQPFLERGDGPICLVLAPTREL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 471 AAQIHEALRTYCQNTDIIVLLSYGQSDRARSLNEIRNGCDILIGTCGRIMDFTVKSHISLLHLRFLVFDEADRLLqDMKK 550
Cdd:cd18049 110 AQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRML-DMGF 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 392921583 551 DPlgHLGAIIKdagfmESAATRQTIMTSATFNASVMTVANELMK 594
Cdd:cd18049 189 EP--QIRKIVD-----QIRPDRQTLMWSATWPKEVRQLAEDFLK 225
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
387-594 |
1.41e-25 |
|
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: 104.96 E-value: 1.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 387 LHPTILETLKRIKYNNVRTIQGAMIPQVLDG--HDVLGQAETSAGKTAAFGLPIIDKIlrmdeETRNKARQddgplALIL 464
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRV-----DPTLKSPQ-----ALCL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 465 APTRELAAQIHEALRTYCQNTDIIVLLSYGQSDRARSlNEIRNgcDILIGTCGRIMDFTVKSHISLLHLRFLVFDEADRL 544
Cdd:cd17963 71 APTRELARQIGEVVEKMGKFTGVKVALAVPGNDVPRG-KKITA--QIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVM 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 392921583 545 LqdmKKDPLGHLGAIIKDagFMESAAtrQTIMTSATFNASVMTVANELMK 594
Cdd:cd17963 148 L---DTQGHGDQSIRIKR--MLPRNC--QILLFSATFPDSVRKFAEKIAP 190
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
406-594 |
3.66e-25 |
|
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: 104.16 E-value: 3.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 406 IQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKiLRMDEETRNKARqddGPLALILAPTRELAAQIHEALRtycqnt 485
Cdd:cd17944 16 IQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEK-LQEDQQPRKRGR---APKVLVLAPTRELANQVTKDFK------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 486 DIIVLLS----YGQSDRARSLNEIRNGCDILIGTCGRIMDFTVKSHISLLHLRFLVFDEADRLLqDMKKDPlgHLGAIIK 561
Cdd:cd17944 86 DITRKLSvacfYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQML-DMGFAE--QVEEILS 162
|
170 180 190
....*....|....*....|....*....|...
gi 392921583 562 DAGFMESAATRQTIMTSATFNASVMTVANELMK 594
Cdd:cd17944 163 VSYKKDSEDNPQTLLFSATCPDWVYNVAKKYMK 195
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
391-594 |
1.40e-24 |
|
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: 102.24 E-value: 1.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 391 ILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKILrmdEETRNkarqddgPLALILAPTREL 470
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCL---TEHRN-------PSALILTPTREL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 471 AAQIHEALRTYCQNT-DIIVLLSYGQSDRARSLNEIRNGCDILIGTCGRIMDFTVKSHISLLHLRFLVFDEADRLLQ-DM 548
Cdd:cd17962 71 AVQIEDQAKELMKGLpPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKmGF 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 392921583 549 KKDPLGHLGAIIKDAgfmesaatrQTIMTSATFNASVMTVANELMK 594
Cdd:cd17962 151 QQQVLDILENISHDH---------QTILVSATIPRGIEQLAGQLLQ 187
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
345-594 |
1.78e-24 |
|
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or DEAD Box Protein P82) has a wide variety of functions including regulating the alternative splicing of exons exhibiting specific features such as the inclusion of AC-rich alternative exons in CD44 transcripts, playing a role in innate immunity, and promoting mRNA degradation mediated by the antiviral zinc-finger protein ZC3HAV1 in an ATPase-dependent manner. DDX17 synergizes with DDX5 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. DDX17 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350808 [Multi-domain] Cd Length: 271 Bit Score: 104.32 E-value: 1.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 345 DIDELVREtadrladcdvgqdRAVEIRNAEKDVRLTSWTNSGLHPTILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQA 424
Cdd:cd18050 40 DVEELRRK-------------KEITIRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 425 ETSAGKTAAFGLPIIDKILRMDEETRNkarqdDGPLALILAPTRELAAQIHEALRTYCQNTDIIVLLSYGQSDRARSLNE 504
Cdd:cd18050 107 QTGSGKTLAYLLPAIVHINHQPYLERG-----DGPICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 505 IRNGCDILIGTCGRIMDFTVKSHISLLHLRFLVFDEADRLLqDMKKDPlgHLGAIIKdagfmESAATRQTIMTSATFNAS 584
Cdd:cd18050 182 LERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRML-DMGFEP--QIRKIVD-----QIRPDRQTLMWSATWPKE 253
|
250
....*....|
gi 392921583 585 VMTVANELMK 594
Cdd:cd18050 254 VRQLAEDFLR 263
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
407-594 |
1.58e-22 |
|
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: 96.36 E-value: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 407 QGAMIPqVLDGHDVLGQAETSAGKTAAFGLPIIDKIlrmdeETRNKARQddgplALILAPTRELAAQIHE---ALRTYCq 483
Cdd:cd18046 27 QRAIMP-CIKGYDVIAQAQSGTGKTATFSISILQQI-----DTSLKATQ-----ALVLAPTRELAQQIQKvvmALGDYM- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 484 ntDIIVLLSYGQSDRARSLNEIRNGCDILIGTCGRIMDFTVKSHISLLHLRFLVFDEADRLLQDMKKDPlghlgaiIKDA 563
Cdd:cd18046 95 --GIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKDQ-------IYDI 165
|
170 180 190
....*....|....*....|....*....|.
gi 392921583 564 gFMESAATRQTIMTSATFNASVMTVANELMK 594
Cdd:cd18046 166 -FQKLPPDTQVVLLSATMPNDVLEVTTKFMR 195
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
406-594 |
3.37e-22 |
|
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: 95.49 E-value: 3.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 406 IQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKILRMDEETRnkarqddgplALILAPTRELAAQI-HEALR--TYC 482
Cdd:cd17950 28 VQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVS----------VLVICHTRELAFQIsNEYERfsKYM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 483 QNTDIIVLlsYGQSDRARSLNEIRNGC-DILIGTCGRIMDFTVKSHISLLHLRFLVFDEADRLLQ--DMKKDplghlgai 559
Cdd:cd17950 98 PNVKTAVF--FGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLEqlDMRRD-------- 167
|
170 180 190
....*....|....*....|....*....|....*
gi 392921583 560 IKDAgFMESAATRQTIMTSATFNASVMTVANELMK 594
Cdd:cd17950 168 VQEI-FRATPHDKQVMMFSATLSKEIRPVCKKFMQ 201
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
659-745 |
9.07e-21 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 87.27 E-value: 9.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 659 DACAAKLTSGGMLAQTLHGDRSQDMREKLINDFKSNRVNLLVTTDLLSRGIDVSDLDRVINFDLPdgdpdQGADTFIHRA 738
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLP-----WSPASYIQRI 75
|
....*..
gi 392921583 739 GRTGRTG 745
Cdd:smart00490 76 GRAGRAG 82
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
416-777 |
2.60e-19 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 92.78 E-value: 2.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 416 DGHDVLGQAETSAGKT--AAFglpIIDKILRmdeetrnkarqddGPLALILAPTRELAAQIHEALRTYcqntdiivllsy 493
Cdd:COG1061 99 GGGRGLVVAPTGTGKTvlALA---LAAELLR-------------GKRVLVLVPRRELLEQWAEELRRF------------ 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 494 gQSDRARSLNEIRNGCDILIGTcgrIMDFTVKSHISLLHLRF--LVFDEA--------DRLLQ----------------- 546
Cdd:COG1061 151 -LGDPLAGGGKKDSDAPITVAT---YQSLARRAHLDELGDRFglVIIDEAhhagapsyRRILEafpaayrlgltatpfrs 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 547 DMKKDPLGHLGAIIKDAGFmeSAATRQTIMTSATFnasvMTVANELmkrlpgQDEMIKIVLANGRLSKRVNleffecKGL 626
Cdd:COG1061 227 DGREILLFLFDGIVYEYSL--KEAIEDGYLAPPEY----YGIRVDL------TDERAEYDALSERLREALA------ADA 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 627 AEKNAKLREILKQNVNGKtlKTIIFVQKKDQCDACAAKLTSGGMLAQTLHGDRSQDMREKLINDFKSNRVNLLVTTDLLS 706
Cdd:COG1061 289 ERKDKILRELLREHPDDR--KTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLN 366
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392921583 707 RGIDVSDLDRVINFDlPDGDPDQgadtFIHRAGRTGRTGR-KENGLCVSFVDPQSDRDSLLAPKLVELIISQ 777
Cdd:COG1061 367 EGVDVPRLDVAILLR-PTGSPRE----FIQRLGRGLRPAPgKEDALVYDFVGNDVPVLEELAKDLRDLAGYR 433
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
406-593 |
8.52e-19 |
|
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: 85.45 E-value: 8.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 406 IQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKIlrmdeETRNKARQddgplALILAPTRELAAQIHEALRTYCQNT 485
Cdd:cd17939 23 IQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRI-----DTTVRETQ-----ALVLAPTRELAQQIQKVVKALGDYM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 486 DIIVLLSYGqSDRARSLNEI-RNGCDILIGTCGRIMDFTVKSHISLLHLRFLVFDEADRLLQDMKKDplgHLGAIIKdag 564
Cdd:cd17939 93 GVKVHACIG-GTSVREDRRKlQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKD---QIYDIFQ--- 165
|
170 180
....*....|....*....|....*....
gi 392921583 565 FMESAAtrQTIMTSATFNASVMTVANELM 593
Cdd:cd17939 166 FLPPET--QVVLFSATMPHEVLEVTKKFM 192
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
386-593 |
7.20e-17 |
|
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: 80.20 E-value: 7.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 386 GLHPTILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKIlrmDEETRNkarqddgPLALILA 465
Cdd:cd18045 5 GLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCL---DIQVRE-------TQALILS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 466 PTRELAAQIHEALRTYCQNTDIIVLLSYGQSDRARSLNEIRNGCDILIGTCGRIMDFTVKSHISLLHLRFLVFDEADRLL 545
Cdd:cd18045 75 PTRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEML 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 392921583 546 QDMKKDplghlgaIIKDAGFMESAATrQTIMTSATFNASVMTVANELM 593
Cdd:cd18045 155 NKGFKE-------QIYDVYRYLPPAT-QVVLVSATLPQDILEMTNKFM 194
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
344-746 |
8.29e-17 |
|
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: 85.27 E-value: 8.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 344 RDIDELVretaDRLADCDVGQDRAVEIRN-AEKDVRLTSWtNSGLHPTILETLKRIKYNNVRTIQGAMIPQVLDGHDVLG 422
Cdd:COG1205 2 ARLEELL----ERLRASPRYGDQIVHVRTiPAREARYAPW-PDWLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 423 QAETSAGKTAAFGLPIIDKILRMDEETrnkarqddgplALILAPTRELAAQIHEALRTYCQNTDIIVLLS--YGQSDRA- 499
Cdd:COG1205 77 ATPTASGKSLAYLLPVLEALLEDPGAT-----------ALYLYPTKALARDQLRRLRELAEALGLGVRVAtyDGDTPPEe 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 500 RSlnEIRNGCDILIGTcgriMDFTvksHISLLH-----------LRFLVFDEA---------------DRLLQDMKkdpl 553
Cdd:COG1205 146 RR--WIREHPDIVLTN----PDML---HYGLLPhhtrwarffrnLRYVVIDEAhtyrgvfgshvanvlRRLRRICR---- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 554 gHLGaiikdagfmesaATRQTIMTSAtfnasvmTVAN--ELMKRLPGQDemIKIVLANGRLSKRVNLEFFECKGLAEK-- 629
Cdd:COG1205 213 -HYG------------SDPQFILASA-------TIGNpaEHAERLTGRP--VTVVDEDGSPRGERTFVLWNPPLVDDGir 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 630 ---NAKLREILKQNV-NGktLKTIIFVQ-KKdqcdacAAKLTS---GGMLAQTLHGDR--------SQDMREKLINDFKS 693
Cdd:COG1205 271 rsaLAEAARLLADLVrEG--LRTLVFTRsRR------GAELLAryaRRALREPDLADRvaayragyLPEERREIERGLRS 342
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 392921583 694 NRVNLLVTTDLLSRGIDVSDLDRVINfdlpDGDPDQGADtFIHRAGRTGRTGR 746
Cdd:COG1205 343 GELLGVVSTNALELGIDIGGLDAVVL----AGYPGTRAS-FWQQAGRAGRRGQ 390
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
424-596 |
1.85e-15 |
|
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: 77.03 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 424 AETSAGKTAAFGLPIIDKILRMDEETRNKARQDDGPL-------ALILAPTRELAAQIHEALRTYCQNTDI-IVLLSYGQ 495
Cdd:cd17965 68 AETGSGKTLAYLAPLLDYLKRQEQEPFEEAEEEYESAkdtgrprSVILVPTHELVEQVYSVLKKLSHTVKLgIKTFSSGF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 496 SDRARSLNE-IRNGCDILIGTCGRIMDFTVKSHISLLHLRFLVFDEADRLlqdMKKDPLGHLGAIIKDAgfmesAATRQT 574
Cdd:cd17965 148 GPSYQRLQLaFKGRIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTL---FDRSFLQDTTSIIKRA-----PKLKHL 219
|
170 180
....*....|....*....|..
gi 392921583 575 IMTSAtfnasvmTVANELMKRL 596
Cdd:cd17965 220 ILCSA-------TIPKEFDKTL 234
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
417-571 |
5.35e-14 |
|
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: 70.12 E-value: 5.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 417 GHDVLGQAETSAGKTAAFGLPIIDKILrmdeetrnkarqDDGPLALILAPTRELAAQIHEALRTYCQNTDIIVLLSYGQS 496
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLL------------KKGKKVLVLVPTKALALQTAERLRELFGPGIRVAVLVGGSS 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392921583 497 DRARSLNEIRNGcDILIGTCGRI-MDFTVKSHISLLHLRFLVFDEADRLLQDMKK---DPLGHLGAIIKDAGFMESAAT 571
Cdd:cd00046 69 AEEREKNKLGDA-DIIIATPDMLlNLLLREDRLFLKDLKLIIVDEAHALLIDSRGaliLDLAVRKAGLKNAQVILLSAT 146
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
594-750 |
7.22e-11 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 66.29 E-value: 7.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 594 KRLPGQDEMIKIVlangRLSKrvnleffECKGLAEKNAKLREILKQ--NVNGKTlKTIIFVQKKDQCDACAAKLTSGGML 671
Cdd:COG1111 312 KRLVSDPRFRKAM----RLAE-------EADIEHPKLSKLREILKEqlGTNPDS-RIIVFTQYRDTAEMIVEFLSEPGIK 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 672 AQTLHG--DR------SQDMREKLINDFKSNRVNLLVTTDLLSRGIDVSDLDRVINFDlpdgdPDQGADTFIHRAGRTGr 743
Cdd:COG1111 380 AGRFVGqaSKegdkglTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYE-----PVPSEIRSIQRKGRTG- 453
|
....*..
gi 392921583 744 tgRKENG 750
Cdd:COG1111 454 --RKREG 458
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
387-593 |
8.08e-10 |
|
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: 60.03 E-value: 8.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 387 LHPTILETLKRIKYNNVRTIQGAMIPQVLDG--HDVLGQAETSAGKTAAFGLPIIDkilRMDEETRNkarqddgPLALIL 464
Cdd:cd18048 25 LKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLS---RVDALKLY-------PQCLCL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 465 APTRELAAQ---IHEALRTYCQNTDIIVLLSYGQSDRARSLNEirngcDILIGTCGRIMDFTVKSH-ISLLHLRFLVFDE 540
Cdd:cd18048 95 SPTFELALQtgkVVEEMGKFCVGIQVIYAIRGNRPGKGTDIEA-----QIVIGTPGTVLDWCFKLRlIDVTNISVFVLDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 392921583 541 ADRLLqdmkkDPLGHLGAIIKDAGFMESAAtrQTIMTSATFNASVMTVANELM 593
Cdd:cd18048 170 ADVMI-----NVQGHSDHSVRVKRSMPKEC--QMLLFSATFEDSVWAFAERIV 215
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
407-541 |
3.21e-09 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 57.21 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 407 QGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKILRmDEETRnkarqddgplALILAPTRELAAQIHEALRTY-CQNT 485
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLR-DPGSR----------ALYLYPTKALAQDQLRSLRELlEQLG 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 486 DIIVLLSY-GQSDRARSLNEIRNGCDILigtcgrimdFT--VKSHISLL-----------HLRFLVFDEA 541
Cdd:cd17923 74 LGIRVATYdGDTPREERRAIIRNPPRIL---------LTnpDMLHYALLphhdrwarflrNLRYVVLDEA 134
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
629-723 |
9.55e-09 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 54.79 E-value: 9.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 629 KNAKLREILKQNVNGKTlKTIIFVQKKDQCDACAAKLTSGGMLAQTLHGDRSQDMREKLINDFKSN---RVnLLVTTDLL 705
Cdd:cd18793 12 KLEALLELLEELREPGE-KVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDpdiRV-FLLSTKAG 89
|
90
....*....|....*...
gi 392921583 706 SRGIDVSDLDRVINFDLP 723
Cdd:cd18793 90 GVGLNLTAANRVILYDPW 107
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
628-756 |
1.43e-08 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350189 [Multi-domain] Cd Length: 142 Bit Score: 54.52 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 628 EKNAKLREIL-KQNVNGKTLKTIIFVQKKDQCDACA-----AKLTSGGMLAQTL--HGDRSQDMREKL--------INDF 691
Cdd:cd18802 7 PKLQKLIEILrEYFPKTPDFRGIIFVERRATAVVLSrllkeHPSTLAFIRCGFLigRGNSSQRKRSLMtqrkqketLDKF 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392921583 692 KSNRVNLLVTTDLLSRGIDVSDLDRVINFDLPDgdpdqGADTFIHRAGRtgrtGRKENGLCVSFV 756
Cdd:cd18802 87 RDGELNLLIATSVLEEGIDVPACNLVIRFDLPK-----TLRSYIQSRGR----ARAPNSKYILMV 142
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
679-756 |
2.20e-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: 51.94 E-value: 2.20e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392921583 679 RSQDMREKLindfkSNRVNLLVTTDLLSRGIDVSDLDRVINFdlpdgDPDQGADTFIHRAGRTGRTGrKENGLCVSFV 756
Cdd:cd18785 11 NSIEHAEEI-----ASSLEILVATNVLGEGIDVPSLDTVIFF-----DPPSSAASYIQRVGRAGRGG-KDEGEVILFV 77
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
424-795 |
1.58e-07 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 55.70 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 424 AETSAGKTAAFGLPIIDKILRMDEETRNKARQDDGPLALILAPTRELAAQIHEALRTYCQ------------NTDIIVLL 491
Cdd:PRK09751 3 APTGSGKTLAAFLYALDRLFREGGEDTREAHKRKTSRILYISPIKALGTDVQRNLQIPLKgiaderrrrgetEVNLRVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 492 SYGQSDRARSLNEIRNGCDILIGTCGRI-MDFTVKSHISLLHLRFLVFDEADRLLQDMKKdplGHLGAIIK--DAGFMES 568
Cdd:PRK09751 83 RTGDTPAQERSKLTRNPPDILITTPESLyLMLTSRARETLRGVETVIIDEVHAVAGSKRG---AHLALSLErlDALLHTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 569 AatrQTIMTSATFNAS------------VMTVANELMKRL--------------------PGQDE----------MIKIV 606
Cdd:PRK09751 160 A---QRIGLSATVRSAsdvaaflggdrpVTVVNPPAMRHPqirivvpvanmddvssvasgTGEDShagregsiwpYIETG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 607 LANGRLSKRVNLEFFECKGLAEK-NAKLREILKQNVNGKTLKTIIFVQKKDQCDACAAKLTSGG-MLAQTLHGDRSQDMR 684
Cdd:PRK09751 237 ILDEVLRHRSTIVFTNSRGLAEKlTARLNELYAARLQRSPSIAVDAAHFESTSGATSNRVQSSDvFIARSHHGSVSKEQR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 685 EKLINDFKSNRVNLLVTTDLLSRGIDVSDLDRVINFDLPdgdPDQGADTfihraGRTGRTGRKENGLCVSFVDPQSDRDS 764
Cdd:PRK09751 317 AITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATP---LSVASGL-----QRIGRAGHQVGGVSKGLFFPRTRRDL 388
|
410 420 430
....*....|....*....|....*....|..
gi 392921583 765 LLAPKLVELIISQNLPDLKVP-DFLDAMAKSS 795
Cdd:PRK09751 389 VDSAVIVECMFAGRLENLTPPhNPLDVLAQQT 420
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
387-593 |
8.56e-07 |
|
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: 50.87 E-value: 8.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 387 LHPTILETLKRIKYNNVRTIQGAMIPQVL--DGHDVLGQAETSAGKTAAFGLPIIDKIlrmdeETRNKARQddgplALIL 464
Cdd:cd18047 8 LKPQLLQGVYAMGFNRPSKIQENALPLMLaePPQNLIAQSQSGTGKTAAFVLAMLSQV-----EPANKYPQ-----CLCL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 465 APTRELAAQIHEALRTYCQNTDIIVLLSYGQSDRARSLNEIRNgcDILIGTCGRIMDFTVK-SHISLLHLRFLVFDEADR 543
Cdd:cd18047 78 SPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISE--QIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 392921583 544 LLQDMkkdplGHLGAIIKDAGFMESAAtrQTIMTSATFNASVMTVANELM 593
Cdd:cd18047 156 MIATQ-----GHQDQSIRIQRMLPRNC--QMLLFSATFEDSVWKFAQKVV 198
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
633-750 |
9.98e-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: 49.28 E-value: 9.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 633 LREILKQNVNGKTLKTIIFVQKKDQCDACAAKLTS-----------GGMLAQTLHGdRSQDMREKLINDFKSNRVNLLVT 701
Cdd:cd18801 18 VKEHFKKKQEGSDTRVIIFSEFRDSAEEIVNFLSKirpgiratrfiGQASGKSSKG-MSQKEQKEVIEQFRKGGYNVLVA 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 392921583 702 TDLLSRGIDVSDLDRVINFDlPDGDPdqgadtfIHRAGRTGRTGRKENG 750
Cdd:cd18801 97 TSIGEEGLDIGEVDLIICYD-ASPSP-------IRMIQRMGRTGRKRQG 137
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
417-540 |
2.19e-06 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 48.73 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 417 GHDVLGQAETSAGKTAAFGLPIIDKILRmdeetrnkaRQDDGPLALILAPTRELAAQIHEALRTYCQ--NTDIIVLLSYG 494
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLAD---------EPEKGVQVLYISPLKALINDQERRLEEPLDeiDLEIPVAVRHG 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 392921583 495 ---QSDRARSLneiRNGCDILIGT--CGRIMdFTVKSHISLL-HLRFLVFDE 540
Cdd:cd17922 72 dtsQSEKAKQL---KNPPGILITTpeSLELL-LVNKKLRELFaGLRYVVVDE 119
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
426-541 |
4.44e-06 |
|
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: 48.42 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 426 TSAGKTaafgLPIIDKILRMDEETRNKARQddGPLALILAPTRELAAQIHEALRTYcqnTDIIVLLSYGQS-----DRAR 500
Cdd:cd18034 25 TGSGKT----LIAVMLIKEMGELNRKEKNP--KKRAVFLVPTVPLVAQQAEAIRSH---TDLKVGEYSGEMgvdkwTKER 95
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 392921583 501 SLNEIRNGcDILIGTCGRIMDFTVKSHISLLHLRFLVFDEA 541
Cdd:cd18034 96 WKEELEKY-DVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
629-749 |
7.36e-06 |
|
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350176 [Multi-domain] Cd Length: 153 Bit Score: 46.86 E-value: 7.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 629 KNAKLREILKQNVNGKtlKTIIFVQKKDQCDACAAKLtsggmLAQTLHGDRSQDMREKLINDFKSNRVNLLVTTDLLSRG 708
Cdd:cd18789 35 KLRALEELLKRHEQGD--KIIVFTDNVEALYRYAKRL-----LKPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEG 107
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 392921583 709 IDVSDLDRVINFDLPDGDPDQgadtFIHRAGRTGRTGRKEN 749
Cdd:cd18789 108 IDLPEANVAIQISGHGGSRRQ----EAQRLGRILRPKKGGG 144
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
622-746 |
1.03e-05 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 49.49 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 622 ECKGLAEKNAKLREILKQNVNGK-TLKTIIFVQKKDQCDACAAKLTSGGMLAQTLHG--DRSQD--MREK----LINDFK 692
Cdd:PRK13766 341 ELDIEHPKLEKLREIVKEQLGKNpDSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGqaSKDGDkgMSQKeqieILDKFR 420
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 392921583 693 SNRVNLLVTTDLLSRGIDVSDLDRVINFdlpdgDPDQGADTFIHRAGRTGR--TGR 746
Cdd:PRK13766 421 AGEFNVLVSTSVAEEGLDIPSVDLVIFY-----EPVPSEIRSIQRKGRTGRqeEGR 471
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
8-153 |
1.26e-05 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 49.13 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 8 AGGGGREYHDDRSNRDHRHGNGGSDAGQRRREdhnssyqsyRRPDGRQDSYGGGHQGNHGNSYGRREDDRSHSRDNHGGS 87
Cdd:PRK12678 146 GEGGEQPATEARADAAERTEEEERDERRRRGD---------REDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRRE 216
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392921583 88 RYGERDDRGNNGRSADNRYSQSNYNYDSNRGGQHYQRDNHGSKDDRGPMNQYNDHGSNHNSNSRND 153
Cdd:PRK12678 217 ERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDRDRRGRRGGDGGNE 282
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
635-754 |
2.03e-05 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 45.33 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 635 EILKQNVNGKtlKTIIFVQKKDQCDACAAKLtsgGMLAQTL---------HGDRSQDMREKLINDFKSNRVNLLVTTDLL 705
Cdd:cd18796 30 EVIFLLERHK--STLVFTNTRSQAERLAQRL---RELCPDRvppdfialhHGSLSRELREEVEAALKRGDLKVVVATSSL 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 392921583 706 SRGIDVSDLDRVINFDLPdgdpdQGADTFIHRAGRTG-RTGRKENGLCVS 754
Cdd:cd18796 105 ELGIDIGDVDLVIQIGSP-----KSVARLLQRLGRSGhRPGAASKGRLVP 149
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
646-747 |
2.65e-05 |
|
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: 44.94 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 646 LKTIIFVQKKDQCD--ACAAK--LTSGGMLAQTLHGDRS---QDMREKLINDFKSNRVNLLVTTDLLSRGIDVSDLDRVI 718
Cdd:cd18797 36 VKTIVFCRSRKLAEllLRYLKarLVEEGPLASKVASYRAgylAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVV 115
|
90 100
....*....|....*....|....*....
gi 392921583 719 NfdlpDGDPDQGAdTFIHRAGRTGRTGRK 747
Cdd:cd18797 116 L----AGYPGSLA-SLWQQAGRAGRRGKD 139
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
615-746 |
4.84e-05 |
|
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: 44.12 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 615 RVNLEFFECKGLAEKNAKLR-EILKQNVNGKTlkTIIFVQKKDQCDACAAKLTSGGMLAQTLHGDRSQDMREKLINDFKS 693
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDLlKRIKVEHLGGS--GIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLR 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 392921583 694 NRVNLLVTTDLLSRGIDVSDLDRVINFDLPdgdpdQGADTFIHRAGRTGRTGR 746
Cdd:cd18794 79 DKIQVIVATVAFGMGIDKPDVRFVIHYSLP-----KSMESYYQESGRAGRDGL 126
|
|
| Nucleoporin_FG |
pfam13634 |
Nucleoporin FG repeat region; This family includes a number of FG repeats that are found in ... |
867-950 |
8.46e-05 |
|
Nucleoporin FG repeat region; This family includes a number of FG repeats that are found in nucleoporin proteins. This family includes the yeast nucleoporins Nup116, Nup100, Nup49, Nup57 and Nup 145.
Pssm-ID: 463941 [Multi-domain] Cd Length: 90 Bit Score: 42.22 E-value: 8.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 867 PSGFGGsrNNAEPTSSGGGFGAPKAPTGFPSDNN---DASEDAPAAGGFGFSTKAAQdakkaeesATLGSSTFGTANNAD 943
Cdd:pfam13634 11 GGLFGN--TSTTAASGGGLFGAASTATATTSGGGlfgNSSSNAPSGGLFGATNTTTQ--------TATGGGLFGNNAATT 80
|
....*..
gi 392921583 944 EEPTETG 950
Cdd:pfam13634 81 TSTTGGG 87
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
622-723 |
9.13e-05 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 46.37 E-value: 9.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 622 ECKGLAEKNAK---LREILKQNV-NGKtlKTIIFVQKKDQCDACAAKLTSGGMLAQTLHGDRSQDMREKLINDFKSN--- 694
Cdd:COG0553 524 EGAELSGRSAKleaLLELLEELLaEGE--KVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGpea 601
|
90 100
....*....|....*....|....*....
gi 392921583 695 RVnLLVTTDLLSRGIDVSDLDRVINFDLP 723
Cdd:COG0553 602 PV-FLISLKAGGEGLNLTAADHVIHYDLW 629
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
624-759 |
1.46e-04 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 45.52 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 624 KGLAEKNAKLREILKQNVNGKTlktIIFVQKKDQCDACAAKLTSGGMLAQTLHGDRSQDMREKLINDFKSNRVNLLVTTD 703
Cdd:COG0514 212 KPPDDKLAQLLDFLKEHPGGSG---IVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATI 288
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392921583 704 LLSRGIDVSDLDRVINFDLPD---------GdpdqgadtfihRAGRTGrtgrkENGLCVSFVDPQ 759
Cdd:COG0514 289 AFGMGIDKPDVRFVIHYDLPKsieayyqeiG-----------RAGRDG-----LPAEALLLYGPE 337
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
644-718 |
6.11e-04 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350186 [Multi-domain] Cd Length: 116 Bit Score: 40.24 E-value: 6.11e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392921583 644 KTLKTIIFVQKKDQCDACAAKLTSGGMLAQTLHGDRSQDMR--EKLINDFKSN-RVNLLVTTDLLSRGIDVSDLDRVI 718
Cdd:cd18799 5 VEIKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERgdEALILLFFGElKPPILVTVDLLTTGVDIPEVDNVV 82
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
6-104 |
6.25e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 43.74 E-value: 6.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 6 NNAGGGGREYHDDRSNRDHRHGNGGSDAGQRRREDhnssyqsyRRPDGRQDSYGGGHQGNHGNSYGRREDDRSHSRDNHG 85
Cdd:PRK12678 191 GRREERGRDGDDRDRRDRREQGDRREERGRRDGGD--------RRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRR 262
|
90
....*....|....*....
gi 392921583 86 GSRYGERDDRGNNGRSADN 104
Cdd:PRK12678 263 GRRFRDRDRRGRRGGDGGN 281
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
414-541 |
1.19e-03 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 41.09 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 414 VLDGHDVLGQAETSAGKTAAFGLPIIDKILRMdeetrnkarqddGPLALILAPTRELAAQIHEALRTYCQNTDIIVLLSY 493
Cdd:cd17921 14 YLSGDSVLVSAPTSSGKTLIAELAILRALATS------------GGKAVYIAPTRALVNQKEADLRERFGPLGKNVGLLT 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 392921583 494 GqsDRARSLNEIRNgCDILIGTcGRIMDFTVK--SHISLLHLRFLVFDEA 541
Cdd:cd17921 82 G--DPSVNKLLLAE-ADILVAT-PEKLDLLLRngGERLIQDVRLVVVDEA 127
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
8-167 |
1.36e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 42.58 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 8 AGGGGREYHDDRSNRDHRHGNGGSDAGQRRREDHNSSYQSYRRPDGRQDSYGGGHQGNHGNSYGRREDDRshsRDNHGGS 87
Cdd:PRK12678 124 AAQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRR---EERGRDG 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 88 RYGERDDRGNNGRSADNRYSQSNYNYDSNRGGQHY-QRDNHGSKDDRGPMNQYNDHGSNHNSNSRNDQYRQGSYQGDGHS 166
Cdd:PRK12678 201 DDRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRrDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDRDRRGRRGGDGG 280
|
.
gi 392921583 167 G 167
Cdd:PRK12678 281 N 281
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
7-116 |
2.08e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 41.81 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 7 NAGGGGREYHDDRSNRDHRhGNGGSDAGQRRREDHNSSYQSYRRPDGRQDSYGGGHQGNhgnsyGRREDDRSHSRDNHGG 86
Cdd:PRK12678 180 DRQAEAERGERGRREERGR-DGDDRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRRD-----ARGDDNREDRGDRDGD 253
|
90 100 110
....*....|....*....|....*....|
gi 392921583 87 SRYGERDDRGNNGRSADNRYSQSNYNYDSN 116
Cdd:PRK12678 254 DGEGRGGRRGRRFRDRDRRGRRGGDGGNER 283
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
462-582 |
2.18e-03 |
|
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350682 [Multi-domain] Cd Length: 189 Bit Score: 40.39 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 462 LILAPTRELAAQIHEALRTYCQNTD--IIVLLSYG---QSDRARSLNEIRNG-CDILIGTCGrimdFTVKSHISLLHLRF 535
Cdd:cd17924 64 YLIFPTKSLVKQAYERLSKYAEKAGveVKILVYHSrlkKKEKEELLEKIEKGdFDILVTTNQ----FLSKNFDLLSNKKF 139
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 392921583 536 -LVF-DEADRLLQDMKkdplgHLGAIIKDAGFmesaatRQTIMTSATFN 582
Cdd:cd17924 140 dFVFvDDVDAVLKSSK-----NIDRLLKLLGF------GQLVVSSATGR 177
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
462-543 |
2.31e-03 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 40.19 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 462 LILAPTRELAAQIHEALRTYCQNTDIIVLLSYGQSDRARSlnEIRNGCDILIGTCGRIMDFTVKSHISLLHLRFLVFDEA 541
Cdd:cd18035 49 LILAPSRPLVEQHAENLKRVLNIPDKITSLTGEVKPEERA--ERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEA 126
|
..
gi 392921583 542 DR 543
Cdd:cd18035 127 HH 128
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
461-515 |
3.38e-03 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 41.29 E-value: 3.38e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 392921583 461 ALILAPTRELAAQIHEALRTYCQNTDI-IVLLSYGQSDRARS--LNEIRNG-CDILIGT 515
Cdd:PRK10917 313 AALMAPTEILAEQHYENLKKLLEPLGIrVALLTGSLKGKERReiLEAIASGeADIVIGT 371
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
17-224 |
3.47e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 41.04 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 17 DDRSNRDHRHGNGGSDAGQRRREDHNSSYQSYRRPDGRQDSYGGGHQGNHGNSYGRREDDRSHSRDNHGGSRyGERDDRG 96
Cdd:PRK12678 107 AARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDR-EDRQAEA 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 97 NNGRSADNRysqsnynyDSNRGGQHYQRDNHGSKDDRGpmnqyNDHGSNHNSNSRNDQYRQGSYQGDGHSGYRRDDDRRR 176
Cdd:PRK12678 186 ERGERGRRE--------ERGRDGDDRDRRDRREQGDRR-----EERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDG 252
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 392921583 177 NDNDQARPYQSNRDSDRNSPRDhhnynsqsspRSHQGGQDRYSAPKED 224
Cdd:PRK12678 253 DDGEGRGGRRGRRFRDRDRRGR----------RGGDGGNEREPELRED 290
|
|
| DEXHc_RecG |
cd17992 |
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in ... |
463-515 |
5.02e-03 |
|
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. It is a member 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: 350750 [Multi-domain] Cd Length: 225 Bit Score: 39.44 E-value: 5.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 392921583 463 ILAPTRELAAQIHEALRTYCQNTDI-IVLL--SYGQSDRARSLNEIRNG-CDILIGT 515
Cdd:cd17992 99 LMAPTEILAEQHYDSLKKLLEPLGIrVALLtgSTKAKEKREILEKIASGeIDIVIGT 155
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
385-478 |
5.90e-03 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 40.64 E-value: 5.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 385 SGLHPTILETLKRiKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKT-AAFgLPIIDKILRMDEEtrNKArqDDGPLALI 463
Cdd:PRK13767 16 DLLRPYVREWFKE-KFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAF-LAIIDELFRLGRE--GEL--EDKVYCLY 89
|
90
....*....|....*
gi 392921583 464 LAPTRELAAQIHEAL 478
Cdd:PRK13767 90 VSPLRALNNDIHRNL 104
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
12-315 |
6.80e-03 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 40.28 E-value: 6.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 12 GREYHDDRSNRDhRHGNGGSDAGQRRREDHNSSYQSYRRPDGRQDSYGGGHQGNHGNSYGRREDDRSHSRDNHGGSRYGE 91
Cdd:NF033609 566 GSDSGSDSSNSD-SGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSDS 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 92 RDDRGNNGRSADNRYSQSNYNYDSNRGG-----QHYQRDNHGSKDDRGPMNQYNDHGSNHNSNSRNDQYRQGSYQGDGHS 166
Cdd:NF033609 645 DSDSDSDSDSDSDSDSDSDSDSDSDSDSdsdsdSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 167 GYRRDDDRRRNDNDQA-RPYQSNRDSDRNSPRDHHNYNSQSSPRSHQGGQDRYSAPKEDNQRRYDNHQGGhDSYRGQNSG 245
Cdd:NF033609 725 DSDSDSDSDSDSDSDSdSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS-DSDSDSDSD 803
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921583 246 GYSGNNSgEYRNDYRSQQDSRDHRSGGNNSSSGFKNDGGFGGNDNRGFGNNGGGSFGNPNNSYRGNSNNI 315
Cdd:NF033609 804 SDSDSDS-DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSESGSNNNV 872
|
|
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
461-515 |
9.51e-03 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 39.65 E-value: 9.51e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 392921583 461 ALILAPTRELAAQIHEALRTYCQNTDI-IVLL--SYGQSDRARSLNEIRNG-CDILIGT 515
Cdd:COG1200 311 AALMAPTEILAEQHYRSLSKLLEPLGIrVALLtgSTKAKERREILAALASGeADIVVGT 369
|
|
| |
