|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
156-587 |
3.89e-176 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 505.84 E-value: 3.89e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 156 FSSPPLDELLMENIKLASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFTELFrsgpspvpekaqsfYSRK 235
Cdd:COG0513 4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLD--------------PSRP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 236 GYPSALVLAPTRELATQIFEEARKFTYRSWVRPCVVYGGAPIGNQMREVDRGCDLLVATPGRLNDLLERGKVSLANIKYL 315
Cdd:COG0513 70 RAPQALILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 316 VLDEADRMLDMGFEPQIRHIVEECDmpsvENRQTLMFSATFPVDIQHLARDFLDNYIFLSVGRVGSTSENITQRILYVDD 395
Cdd:COG0513 150 VLDEADRMLDMGFIEDIERILKLLP----KERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 396 MDKKSALLDLLSAEHKGLTLIFVETKRMADQLTDFLIMQNFKATAIHGDRTQAERERALSAFKANVADILVATAVAARGL 475
Cdd:COG0513 226 RDKLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 476 DIPNVTHVINYDLPSDIDDYVHRIGRTGRAGNTGVATSFFNSNNQNIVKGLMEILNE--ANQEVPTFLSDLSRQNSRGGR 553
Cdd:COG0513 306 DIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQkiEEEELPGFEPVEEKRLERLKP 385
|
410 420 430
....*....|....*....|....*....|....
gi 768886153 554 TRGGGGFFNSRNNGSRDYRKHGGSGSFGSTRPRN 587
Cdd:COG0513 386 KIKEKLKGKKAGRGGRPGPKGERKARRGKRRRRK 419
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
156-380 |
2.22e-160 |
|
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: 457.72 E-value: 2.22e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 156 FSSPPLDELLMENIKLASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFTELFRSGPSPVPekaqsFYSRK 235
Cdd:cd17967 2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVG-----RGRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 236 GYPSALVLAPTRELATQIFEEARKFTYRSWVRPCVVYGGAPIGNQMREVDRGCDLLVATPGRLNDLLERGKVSLANIKYL 315
Cdd:cd17967 77 AYPSALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768886153 316 VLDEADRMLDMGFEPQIRHIVEECDMPSVENRQTLMFSATFPVDIQHLARDFLDNYIFLSVGRVG 380
Cdd:cd17967 157 VLDEADRMLDMGFEPQIRKIVEHPDMPPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVGRVG 221
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
134-381 |
7.31e-159 |
|
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: 455.27 E-value: 7.31e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 134 FDNYDDIPVDASGKDVPEPILDFSSPPLDELLMENIKLASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLF 213
Cdd:cd18051 1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 214 TELFRSGPSPVPEKAQSFY-SRKGYPSALVLAPTRELATQIFEEARKFTYRSWVRPCVVYGGAPIGNQMREVDRGCDLLV 292
Cdd:cd18051 81 SQIYEQGPGESLPSESGYYgRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 293 ATPGRLNDLLERGKVSLANIKYLVLDEADRMLDMGFEPQIRHIVEECDMPSVENRQTLMFSATFPVDIQHLARDFLDNYI 372
Cdd:cd18051 161 ATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFLDNYI 240
|
....*....
gi 768886153 373 FLSVGRVGS 381
Cdd:cd18051 241 FLAVGRVGS 249
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
115-380 |
3.39e-143 |
|
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: 415.91 E-value: 3.39e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 115 EAELFGVhddpdYHSsGIKFDNYDDIPVDASGKDVPEPILDFSSPPLDELLMENIKLASFTKPTPVQKYSIPIVTKGRDL 194
Cdd:cd18052 10 EDEIFAT-----IQT-GINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 195 MACAQTGSGKTGGFLFPLFTELFRSGPSPvpekaqSFYSRKGYPSALVLAPTRELATQIFEEARKFTYRSWVRPCVVYGG 274
Cdd:cd18052 84 MACAQTGSGKTAAFLLPVLTGMMKEGLTA------SSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 275 APIGNQMREVDRGCDLLVATPGRLNDLLERGKVSLANIKYLVLDEADRMLDMGFEPQIRHIVEECDMPSVENRQTLMFSA 354
Cdd:cd18052 158 VSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQTLMFSA 237
|
250 260
....*....|....*....|....*..
gi 768886153 355 TFPVDIQHLARDFL-DNYIFLSVGRVG 380
Cdd:cd18052 238 TFPEEIQRLAAEFLkEDYLFLTVGRVG 264
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
54-592 |
1.37e-125 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 381.43 E-value: 1.37e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 54 GDFFRRAGRQTGNNGGFFGFSKERNGGTSANYNRGGSSNYKSS--GNR-----WVNGKHIPGPKNAKLEaelfgvHDDpd 126
Cdd:PTZ00110 28 PDSSNPYGNYQANHQDNYGGFRPGYGNYSGGYGGFGMNSYGSStlGKRlqpidWKSINLVPFEKNFYKE------HPE-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 127 yhSSGIKFDNYDDIPVD-----ASGKDVPEPILDFSSPPLDELLMENIKLASFTKPTPVQKYSIPIVTKGRDLMACAQTG 201
Cdd:PTZ00110 100 --VSALSSKEVDEIRKEkeitiIAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 202 SGKTGGFLFPLFTELfrsgpspvpeKAQSFYSRKGYPSALVLAPTRELATQIFEEARKFTYRSWVRPCVVYGGAPIGNQM 281
Cdd:PTZ00110 178 SGKTLAFLLPAIVHI----------NAQPLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 282 REVDRGCDLLVATPGRLNDLLERGKVSLANIKYLVLDEADRMLDMGFEPQIRHIVEECDmpsvENRQTLMFSATFPVDIQ 361
Cdd:PTZ00110 248 YALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIR----PDRQTLMWSATWPKEVQ 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 362 HLARDFL-DNYIFLSVGRVG-STSENITQRILYVDDMDKKSALLDLLSA--EHKGLTLIFVETKRMADQLTDFLIMQNFK 437
Cdd:PTZ00110 324 SLARDLCkEEPVHVNVGSLDlTACHNIKQEVFVVEEHEKRGKLKMLLQRimRDGDKILIFVETKKGADFLTKELRLDGWP 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 438 ATAIHGDRTQAERERALSAFKANVADILVATAVAARGLDIPNVTHVINYDLPSDIDDYVHRIGRTGRAGNTGVATSFFNS 517
Cdd:PTZ00110 404 ALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTP 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768886153 518 NNQNIVKGLMEILNEANQEVPTFLSDLSrqnsrggrtrggggffNSRNNGSRDYRKHGGSGSFGSTRPRNTGTSN 592
Cdd:PTZ00110 484 DKYRLARDLVKVLREAKQPVPPELEKLS----------------NERSNGTERRRWGGYGRFSNNVNNIPLGGSN 542
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
155-516 |
5.95e-100 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 312.12 E-value: 5.95e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 155 DFSSPPLDELLMENIKLASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFTELfrsgpspvpeKAQSFYsr 234
Cdd:PRK11776 5 AFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL----------DVKRFR-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 235 kgyPSALVLAPTRELATQIFEEARK---FTYRswVRPCVVYGGAPIGNQMREVDRGCDLLVATPGRLNDLLERGKVSLAN 311
Cdd:PRK11776 73 ---VQALVLCPTRELADQVAKEIRRlarFIPN--IKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 312 IKYLVLDEADRMLDMGFEPQIRHIVEECDmpsvENRQTLMFSATFPVDIQHLARDFLDNYIFLSVGRVGSTSEnITQRIL 391
Cdd:PRK11776 148 LNTLVLDEADRMLDMGFQDAIDAIIRQAP----ARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPA-IEQRFY 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 392 YVDDMDKKSALLDLLSAEHKGLTLIFVETKRMADQLTDFLIMQNFKATAIHGDRTQAERERALSAFkAN-VADILVATAV 470
Cdd:PRK11776 223 EVSPDERLPALQRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRF-ANrSCSVLVATDV 301
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 768886153 471 AARGLDIPNVTHVINYDLPSDIDDYVHRIGRTGRAGNTGVATSFFN 516
Cdd:PRK11776 302 AARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVA 347
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
154-513 |
2.39e-95 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 300.19 E-value: 2.39e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 154 LDFSSPPLDELLMENIKLASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFTELFRSGPSPvpekaqsfys 233
Cdd:PRK10590 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHA---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 234 rKGYP--SALVLAPTRELATQIFEEARKFTYRSWVRPCVVYGGAPIGNQMREVDRGCDLLVATPGRLNDLLERGKVSLAN 311
Cdd:PRK10590 71 -KGRRpvRALILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 312 IKYLVLDEADRMLDMGFEPQIRHIVEEcdMPSveNRQTLMFSATFPVDIQHLARDFLDNYIFLSVGRVGSTSENITQRIL 391
Cdd:PRK10590 150 VEILVLDEADRMLDMGFIHDIRRVLAK--LPA--KRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVH 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 392 YVDDMDKKSALLDLLSAEHKGLTLIFVETKRMADQLTDFLIMQNFKATAIHGDRTQAERERALSAFKANVADILVATAVA 471
Cdd:PRK10590 226 FVDKKRKRELLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIA 305
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 768886153 472 ARGLDIPNVTHVINYDLPSDIDDYVHRIGRTGRAGNTGVATS 513
Cdd:PRK10590 306 ARGLDIEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALS 347
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
155-514 |
1.75e-91 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 289.15 E-value: 1.75e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 155 DFSSPPLDELLMENIKLASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFTELfrsgpspvpekaQSFYSR 234
Cdd:PRK11192 2 TFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHL------------LDFPRR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 235 K-GYPSALVLAPTRELATQIFEEARKFTYRSWVRPCVVYGGAPIGNQMREVDRGCDLLVATPGRLNDLLERGKVSLANIK 313
Cdd:PRK11192 70 KsGPPRILILTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 314 YLVLDEADRMLDMGFEPQIRHIVEECdmpsVENRQTLMFSATFPVD-IQHLARDFLDNYIFLSVGrvGSTSE--NITQRI 390
Cdd:PRK11192 150 TLILDEADRMLDMGFAQDIETIAAET----RWRKQTLLFSATLEGDaVQDFAERLLNDPVEVEAE--PSRRErkKIHQWY 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 391 LYVDDMDKKSALL-DLLSAEHKGLTLIFVETKRMADQLTDFLIMQNFKATAIHGDRTQAERERALSAFKANVADILVATA 469
Cdd:PRK11192 224 YRADDLEHKTALLcHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATD 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 768886153 470 VAARGLDIPNVTHVINYDLPSDIDDYVHRIGRTGRAGNTGVATSF 514
Cdd:PRK11192 304 VAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
106-538 |
5.14e-91 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 290.92 E-value: 5.14e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 106 IPGPKNAKLEAELFGVHDdpdyhsSGIKFDNYDD--------IPVDASGKDVPEPILDFSSPPLDELLMENIKLASFTKP 177
Cdd:PLN00206 71 APKPKRLPATDECFYVRD------PGSTSGLSSSqaellrrkLEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFP 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 178 TPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFTE--LFRSGPSPVPEKaqsfysrkgyPSALVLAPTRELATQIFE 255
Cdd:PLN00206 145 TPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRccTIRSGHPSEQRN----------PLAMVLTPTRELCVQVED 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 256 EARKFTYRSWVRPCVVYGGAPIGNQMREVDRGCDLLVATPGRLNDLLERGKVSLANIKYLVLDEADRMLDMGFEPQIRHI 335
Cdd:PLN00206 215 QAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQI 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 336 VEECDMPsvenrQTLMFSATFPVDIQHLARDFLDNYIFLSVGRVGSTSENITQRILYVDDMDKKSALLDLL-SAEH-KGL 413
Cdd:PLN00206 295 FQALSQP-----QVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQKLFDILkSKQHfKPP 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 414 TLIFVETKRMADQLTDFL-IMQNFKATAIHGDRTQAERERALSAFKANVADILVATAVAARGLDIPNVTHVINYDLPSDI 492
Cdd:PLN00206 370 AVVFVSSRLGADLLANAItVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTI 449
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 768886153 493 DDYVHRIGRTGRAGNTGVATSFFNSNNQNIVKGLMEILNEANQEVP 538
Cdd:PLN00206 450 KEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKSSGAAIP 495
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
161-514 |
1.86e-89 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 285.27 E-value: 1.86e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 161 LDELLMENIKLASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFTELFRSgpsPVPEKaqsfySRKGYPSA 240
Cdd:PRK01297 94 LAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQT---PPPKE-----RYMGEPRA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 241 LVLAPTRELATQIFEEARKFTYRSWVRPCVVYGGAPIGNQMREVD-RGCDLLVATPGRLNDLLERGKVSLANIKYLVLDE 319
Cdd:PRK01297 166 LIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 320 ADRMLDMGFEPQIRHIVEECdmPSVENRQTLMFSATFPVDIQHLARDFLDNYIFLSVGRVGSTSENITQRILYVDDMDKK 399
Cdd:PRK01297 246 ADRMLDMGFIPQVRQIIRQT--PRKEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDKY 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 400 SALLDLLSAEHKGLTLIFVETKRMADQLTDFLIMQNFKATAIHGDRTQAERERALSAFKANVADILVATAVAARGLDIPN 479
Cdd:PRK01297 324 KLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDG 403
|
330 340 350
....*....|....*....|....*....|....*
gi 768886153 480 VTHVINYDLPSDIDDYVHRIGRTGRAGNTGVATSF 514
Cdd:PRK01297 404 ISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISF 438
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
156-514 |
1.64e-88 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 281.09 E-value: 1.64e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 156 FSSPPLDELLMENIKLASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFTELFRSgpsPVPEKAQsfysrK 235
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSH---PAPEDRK-----V 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 236 GYPSALVLAPTRELATQIFEEARKFTYRSWVRPCVVYGGAPIGNQMREVDRGCDLLVATPGRLNDLLERGKVSLANIKYL 315
Cdd:PRK04837 82 NQPRALIMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 316 VLDEADRMLDMGFEPQIRHIVEEcdMPSVENRQTLMFSATFPVDIQHLARDFLDNYIFLSVGRVGSTSENITQRILYVDD 395
Cdd:PRK04837 162 VLDEADRMFDLGFIKDIRWLFRR--MPPANQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYPSN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 396 MDKKSALLDLLSAEHKGLTLIFVETKRMADQLTDFLIMQNFKATAIHGDRTQAERERALSAFKANVADILVATAVAARGL 475
Cdd:PRK04837 240 EEKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGL 319
|
330 340 350
....*....|....*....|....*....|....*....
gi 768886153 476 DIPNVTHVINYDLPSDIDDYVHRIGRTGRAGNTGVATSF 514
Cdd:PRK04837 320 HIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
165-375 |
1.80e-88 |
|
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350669 [Multi-domain] Cd Length: 196 Bit Score: 272.78 E-value: 1.80e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 165 LMENIKLASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFTELfrsgpspvpeKAQSFYSRKGyPSALVLA 244
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKL----------LPEPKKKGRG-PQALVLA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 245 PTRELATQIFEEARKFTYRSWVRPCVVYGGAPIGNQMREVDRGCDLLVATPGRLNDLLERGKVSLANIKYLVLDEADRML 324
Cdd:cd00268 70 PTRELAMQIAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRML 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 768886153 325 DMGFEPQIRHIVEECDmpsvENRQTLMFSATFPVDIQHLARDFLDNYIFLS 375
Cdd:cd00268 150 DMGFEEDVEKILSALP----KDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
148-514 |
6.01e-81 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 266.05 E-value: 6.01e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 148 DVPEPILDFSSPPLDELLMENIKLASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFTELFrSGPSPVPEK 227
Cdd:PRK04537 3 DKPLTDLTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLL-SRPALADRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 228 AQSfysrkgyPSALVLAPTRELATQIFEEARKFTYRSWVRPCVVYGGAPIGNQMREVDRGCDLLVATPGRLNDLLERGKV 307
Cdd:PRK04537 82 PED-------PRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 308 -SLANIKYLVLDEADRMLDMGFEPQIRHIVEEcdMPSVENRQTLMFSATFPVDIQHLARDFLDNYIFLSVGRVGSTSENI 386
Cdd:PRK04537 155 vSLHACEICVLDEADRMFDLGFIKDIRFLLRR--MPERGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 387 TQRILYVDDMDKKSALLDLLSAEHKGLTLIFVETKRMADQLTDFLIMQNFKATAIHGDRTQAERERALSAFKANVADILV 466
Cdd:PRK04537 233 RQRIYFPADEEKQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILV 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 768886153 467 ATAVAARGLDIPNVTHVINYDLPSDIDDYVHRIGRTGRAGNTGVATSF 514
Cdd:PRK04537 313 ATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISF 360
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
165-375 |
7.71e-80 |
|
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: 250.36 E-value: 7.71e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 165 LMENIKLASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPlftelfrsgpSPVPEKAQSFYSRKGYPSALVLA 244
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLP----------AIVHINAQPPLERGDGPIVLVLA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 245 PTRELATQIFEEARKFTYRSWVRPCVVYGGAPIGNQMREVDRGCDLLVATPGRLNDLLERGKVSLANIKYLVLDEADRML 324
Cdd:cd17966 71 PTRELAQQIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRML 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 768886153 325 DMGFEPQIRHIVEECDmpsvENRQTLMFSATFPVDIQHLARDFLDNYIFLS 375
Cdd:cd17966 151 DMGFEPQIRKIVDQIR----PDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
174-514 |
5.27e-73 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 246.30 E-value: 5.27e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 174 FTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFTELfrsgpspVPE-KAqsfysrkgyPSALVLAPTRELATQ 252
Cdd:PRK11634 26 YEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNL-------DPElKA---------PQILVLAPTRELAVQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 253 IFEEARKFT-YRSWVRPCVVYGGAPIGNQMREVDRGCDLLVATPGRLNDLLERGKVSLANIKYLVLDEADRMLDMGFEPQ 331
Cdd:PRK11634 90 VAEAMTDFSkHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFIED 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 332 IRHIVEEcdMPsvENRQTLMFSATFPVDIQHLARDFLDNYIFLSVGRVGSTSENITQRILYVDDMDKKSALLDLLSAEHK 411
Cdd:PRK11634 170 VETIMAQ--IP--EGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVRFLEAEDF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 412 GLTLIFVETKRMADQLTDFLIMQNFKATAIHGDRTQAERERALSAFKANVADILVATAVAARGLDIPNVTHVINYDLPSD 491
Cdd:PRK11634 246 DAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMD 325
|
330 340
....*....|....*....|...
gi 768886153 492 IDDYVHRIGRTGRAGNTGVATSF 514
Cdd:PRK11634 326 SESYVHRIGRTGRAGRAGRALLF 348
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
144-372 |
1.34e-68 |
|
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: 222.25 E-value: 1.34e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 144 ASGKDVPEPILDFSSPPLDELLMENIKLASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFTELfrsgpsp 223
Cdd:cd17953 2 VRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHI------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 224 vpeKAQSFYSRKGYPSALVLAPTRELATQIFEEARKFTYRSWVRPCVVYGGAPIGNQMREVDRGCDLLVATPGRLNDLL- 302
Cdd:cd17953 75 ---KDQRPVKPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILt 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768886153 303 -ERGKV-SLANIKYLVLDEADRMLDMGFEPQIRHIVEECDmpsvENRQTLMFSATFPVDIQHLARDFLDNYI 372
Cdd:cd17953 152 aNNGRVtNLRRVTYVVLDEADRMFDMGFEPQIMKIVNNIR----PDRQTVLFSATFPRKVEALARKVLHKPI 219
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
142-377 |
4.54e-68 |
|
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, G17P1, or HUMP68) is involved in pathways that include the alteration of RNA structures, plays a role as a coregulator of transcription, a regulator of splicing, and in the processing of small noncoding RNAs. It synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. Dysregulation of this gene may play a role in cancer development. DDX5 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350807 [Multi-domain] Cd Length: 234 Bit Score: 221.42 E-value: 4.54e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 142 VDASGKDVPEPILDFSSPPLDELLMENIKLASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFTELfrsgp 221
Cdd:cd18049 12 ITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHI----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 222 spvpeKAQSFYSRKGYPSALVLAPTRELATQIFEEARKFTYRSWVRPCVVYGGAPIGNQMREVDRGCDLLVATPGRLNDL 301
Cdd:cd18049 87 -----NHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDF 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768886153 302 LERGKVSLANIKYLVLDEADRMLDMGFEPQIRHIVEECDmpsvENRQTLMFSATFPVDIQHLARDFLDNYIFLSVG 377
Cdd:cd18049 162 LEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIR----PDRQTLMWSATWPKEVRQLAEDFLKDYIHINIG 233
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
386-515 |
8.27e-64 |
|
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: 206.20 E-value: 8.27e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 386 ITQRILYVDDMDKKSALLDLLSAEHK-GLTLIFVETKRMADQLTDFLIMQNFKATAIHGDRTQAERERALSAFKANVADI 464
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLLLLEKLKpGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 768886153 465 LVATAVAARGLDIPNVTHVINYDLPSDIDDYVHRIGRTGRAGNTGVATSFF 515
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
165-372 |
1.19e-63 |
|
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: 208.04 E-value: 1.19e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 165 LMENIKLASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFTELFrsgpspvpekAQSFYSRKGYPSALVLA 244
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIM----------DQRELEKGEGPIAVIVA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 245 PTRELATQIFEEARKFTYRSWVRPCVVYGGAPIGNQMREVDRGCDLLVATPGRLNDLLERGKVSLANIKYLVLDEADRML 324
Cdd:cd17952 71 PTRELAQQIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMF 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 768886153 325 DMGFEPQIRHIVEECDmpsvENRQTLMFSATFPVDIQHLARDFLDNYI 372
Cdd:cd17952 151 DMGFEYQVRSIVGHVR----PDRQTLLFSATFKKKIEQLARDILSDPI 194
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
165-377 |
2.41e-63 |
|
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: 207.44 E-value: 2.41e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 165 LMENIKLASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFTELFRSGpspvpekaqsfysRKGYPSALVLA 244
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPR-------------KKKGLRALILA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 245 PTRELATQIFEEARKFTYRSWVRPCVVYGG-APIGNQMREVDRGCDLLVATPGRLNDLLERGKVSLANIKYLVLDEADRM 323
Cdd:cd17957 68 PTRELASQIYRELLKLSKGTGLRIVLLSKSlEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 768886153 324 LDMGFEPQIRHIVEECDMPSVenrQTLMFSATFPVDIQHLARDFLDNYIFLSVG 377
Cdd:cd17957 148 FEPGFREQTDEILAACTNPNL---QRSLFSATIPSEVEELARSVMKDPIRIIVG 198
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
161-375 |
2.85e-63 |
|
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: 207.82 E-value: 2.85e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 161 LDELLMENIKLASFTKPTPVQKYSI-PIVTKGRDLMACAQTGSGKTGGFLFPLFTELFRSGPSPVPEKAqsfysrkgypS 239
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLkPILSTGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGV----------S 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 240 ALVLAPTRELATQIFEEARKFTYRSW-VRPCVVYGGAPIGNQMREVDR-GCDLLVATPGRLNDLLE--RGKVSLANIKYL 315
Cdd:cd17964 71 ALIISPTRELALQIAAEAKKLLQGLRkLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLEnpGVAKAFTDLDYL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768886153 316 VLDEADRMLDMGFEPQIRHIVEECDMPSVENRQTLMFSATFPVDIQHLARDFLD-NYIFLS 375
Cdd:cd17964 151 VLDEADRLLDMGFRPDLEQILRHLPEKNADPRQTLLFSATVPDEVQQIARLTLKkDYKFID 211
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
146-377 |
7.06e-63 |
|
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: 209.10 E-value: 7.06e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 146 GKDVPEPILDFSSPPLDELLMENIKLASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFTELfrsgpspvp 225
Cdd:cd18050 54 GVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHI--------- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 226 eKAQSFYSRKGYPSALVLAPTRELATQIFEEARKFTYRSWVRPCVVYGGAPIGNQMREVDRGCDLLVATPGRLNDLLERG 305
Cdd:cd18050 125 -NHQPYLERGDGPICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAG 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768886153 306 KVSLANIKYLVLDEADRMLDMGFEPQIRHIVEECDmpsvENRQTLMFSATFPVDIQHLARDFLDNYIFLSVG 377
Cdd:cd18050 204 KTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIR----PDRQTLMWSATWPKEVRQLAEDFLRDYVQINIG 271
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
165-375 |
2.39e-62 |
|
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: 205.63 E-value: 2.39e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 165 LMENIKLASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFTELFRSGPSPVPEKAQSfysrkgyPSALVLA 244
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDEETKDDG-------PYALILA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 245 PTRELATQIFEEARKFTYRSWVRPCVVYGGAPIGNQMREVDRGCDLLVATPGRLNDLLERGKVSLANIKYLVLDEADRML 324
Cdd:cd17945 74 PTRELAQQIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768886153 325 DMGFEPQIRHIVEEcdMPSVEN------------------RQTLMFSATFPVDIQHLARDFLDNYIFLS 375
Cdd:cd17945 154 DMGFEPQVTKILDA--MPVSNKkpdteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVVT 220
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
136-544 |
1.31e-61 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 209.68 E-value: 1.31e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 136 NYDDIpVDAsgkdvpepildFSSPPLDELLMENIKLASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFplfTE 215
Cdd:PTZ00424 22 NYDEI-VDS-----------FDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVI---AA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 216 LFRSGPSPVPEKAqsfysrkgypsaLVLAPTRELATQIFEEARKFTYRSWVRPCVVYGGAPIGNQMREVDRGCDLLVATP 295
Cdd:PTZ00424 87 LQLIDYDLNACQA------------LILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 296 GRLNDLLERGKVSLANIKYLVLDEADRMLDMGFEPQIRHIVEEcdMPSveNRQTLMFSATFPVDIQHLARDFLDNYIFLS 375
Cdd:PTZ00424 155 GRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFKGQIYDVFKK--LPP--DVQVALFSATMPNEILELTTKFMRDPKRIL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 376 VGRVGSTSENITQRILYVDDMDKK-SALLDLLSAEHKGLTLIFVETKRMADQLTDFLIMQNFKATAIHGDRTQAERERAL 454
Cdd:PTZ00424 231 VKKDELTLEGIRQFYVAVEKEEWKfDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 455 SAFKANVADILVATAVAARGLDIPNVTHVINYDLPSDIDDYVHRIGRTGRAGNTGVATSFFNSNNQNIVKGLMEILNEAN 534
Cdd:PTZ00424 311 REFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQI 390
|
410
....*....|
gi 768886153 535 QEVPTFLSDL 544
Cdd:PTZ00424 391 EEMPMEVADY 400
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
165-370 |
2.17e-60 |
|
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis antigen 13 or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 is also called cancer/testis antigen 26 or DEAD-Box Protein CAGE. Both DDX46 and DDX53 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350716 [Multi-domain] Cd Length: 197 Bit Score: 199.61 E-value: 2.17e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 165 LMENIKLASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFTELfRSGPSPvpekaqsfYSRKGYPSALVLA 244
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHL-DLQPIP--------REQRNGPGVLVLT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 245 PTRELATQIFEEARKFTYRSWVRPCVvYGGAPIGNQMREVDRGCDLLVATPGRLNDLLERGKVSLANIKYLVLDEADRML 324
Cdd:cd17958 72 PTRELALQIEAECSKYSYKGLKSVCV-YGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRML 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 768886153 325 DMGFEPQIRHIVEECDmpsvENRQTLMFSATFPVDIQHLARDFLDN 370
Cdd:cd17958 151 DMGFEPQIRKILLDIR----PDRQTIMTSATWPDGVRRLAQSYLKD 192
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
173-370 |
4.83e-57 |
|
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: 190.54 E-value: 4.83e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 173 SFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFTELFRSgpspvpeKAQSFYSRkgypsALVLAPTRELATQ 252
Cdd:cd17947 9 GFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYR-------PKKKAATR-----VLVLVPTRELAMQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 253 IFEEARKFTYRSWVRPCVVYGGAPIGNQMREVDRGCDLLVATPGRLNDLLERGK-VSLANIKYLVLDEADRMLDMGFEPQ 331
Cdd:cd17947 77 CFSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGFADE 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 768886153 332 IRHIVEECDmpsvENRQTLMFSATFPVDIQHLARDFLDN 370
Cdd:cd17947 157 LKEILRLCP----RTRQTMLFSATMTDEVKDLAKLSLNK 191
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
178-363 |
8.39e-57 |
|
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: 188.99 E-value: 8.39e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 178 TPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFtelfrsgpspvpekaQSFYSRKGYPSALVLAPTRELATQIFEEA 257
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPAL---------------EALDKLDNGPQALVLAPTRELAEQIYEEL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 258 RKFTYRSWVRPCVVYGGAPIGNQMREVdRGCDLLVATPGRLNDLLERgKVSLANIKYLVLDEADRMLDMGFEPQIRHIVE 337
Cdd:pfam00270 66 KKLGKGLGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQE-RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILR 143
|
170 180
....*....|....*....|....*.
gi 768886153 338 ECDmpsvENRQTLMFSATFPVDIQHL 363
Cdd:pfam00270 144 RLP----KKRQILLLSATLPRNLEDL 165
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
169-389 |
1.59e-55 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 186.93 E-value: 1.59e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 169 IKLASFTKPTPVQKYSIPIVTKG-RDLMACAQTGSGKTGGFLFPLFTELFRsgpspvpekaqsfysrKGYPSALVLAPTR 247
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKR----------------GKGGRVLVLVPTR 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 248 ELATQIFEEARKFTYRSWVRPCVVYGGAPIGNQMREVDRGC-DLLVATPGRLNDLLERGKVSLANIKYLVLDEADRMLDM 326
Cdd:smart00487 65 ELAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768886153 327 GFEPQIRHIVEECDmpsvENRQTLMFSATFPVDIQHLARDFLDNYIFLSVGRvgSTSENITQR 389
Cdd:smart00487 145 GFGDQLEKLLKLLP----KNVQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
156-370 |
4.87e-52 |
|
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can shuttle between the nucleus and the cytoplasm, and has an RNA-independent ATPase activity. DX47 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350712 [Multi-domain] Cd Length: 203 Bit Score: 177.51 E-value: 4.87e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 156 FSSPPLDELLMENIKLASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFTELFrsgpspvpEKAQSFYsrk 235
Cdd:cd17954 2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALL--------ENPQRFF--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 236 gypsALVLAPTRELATQIFEEARKFTYRSWVRPCVVYGGAPIGNQMREVDRGCDLLVATPGRLNDLLERGK-VSLANIKY 314
Cdd:cd17954 71 ----ALVLAPTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLKF 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 768886153 315 LVLDEADRMLDMGFEPQIRHIVEEcdMPSveNRQTLMFSATFPVDIQHLARDFLDN 370
Cdd:cd17954 147 LVMDEADRLLNMDFEPEIDKILKV--IPR--ERTTYLFSATMTTKVAKLQRASLKN 198
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
156-374 |
3.17e-50 |
|
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: 172.87 E-value: 3.17e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 156 FSSPPLDELLMENIKLASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFtelfrsgpspvpEKAQSFYSRK 235
Cdd:cd17959 3 FQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMI------------EKLKAHSPTV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 236 GYpSALVLAPTRELATQIFEEARKFTYRSWVRPCVVYGGAPIGNQMREVDRGCDLLVATPGRLNDLLERGKVSLANIKYL 315
Cdd:cd17959 71 GA-RALILSPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 768886153 316 VLDEADRMLDMGFEPQIRHIVEEcdMPsvENRQTLMFSATFPVDIQHLARDFLDNYIFL 374
Cdd:cd17959 150 VFDEADRLFEMGFAEQLHEILSR--LP--ENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
176-368 |
2.99e-49 |
|
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: 170.21 E-value: 2.99e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 176 KPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFTELFRSgpspvpEKAQSFYSRKGyPSALVLAPTRELATQIFE 255
Cdd:cd17951 12 KPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQ------EKKLPFIKGEG-PYGLIVCPSRELARQTHE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 256 EARKFTYR------SWVRPCVVYGGAPIGNQMREVDRGCDLLVATPGRLNDLLERGKVSLANIKYLVLDEADRMLDMGFE 329
Cdd:cd17951 85 VIEYYCKAlqeggyPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMIDMGFE 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 768886153 330 PQIRHIVEECDMPsvenRQTLMFSATFPVDIQHLARDFL 368
Cdd:cd17951 165 EDIRTIFSYFKGQ----RQTLLFSATMPKKIQNFAKSAL 199
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
165-375 |
4.23e-49 |
|
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: 170.07 E-value: 4.23e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 165 LMENIKlasFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFTELfrsgpspvpEKAQSFYSRKGYPSALVLA 244
Cdd:cd17949 5 LKSKMG---IEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRL---------LSLEPRVDRSDGTLALVLV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 245 PTRELATQIFEEARKFT-YRSWVRPCVVYGGApigNQMREVDR---GCDLLVATPGRLNDLLERGKV-SLANIKYLVLDE 319
Cdd:cd17949 73 PTRELALQIYEVLEKLLkPFHWIVPGYLIGGE---KRKSEKARlrkGVNILIATPGRLLDHLKNTQSfDVSNLRWLVLDE 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768886153 320 ADRMLDMGFEPQIRHIVE---------ECDMPSVENRQTLMFSATFPVDIQHLARDFLDNYIFLS 375
Cdd:cd17949 150 ADRLLDMGFEKDITKILEllddkrskaGGEKSKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
156-375 |
9.16e-49 |
|
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: 168.94 E-value: 9.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 156 FSSPPLDELLMENIKLASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFTELfrsgpspvpekaqsfySRK 235
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRL----------------SED 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 236 GY-PSALVLAPTRELATQIFEEARKFTYRSWVRPCVVYGGAPIGNQMREVDRGCDLLVATPGRLNDLLE---RGKVSLAN 311
Cdd:cd17955 65 PYgIFALVLTPTRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768886153 312 IKYLVLDEADRMLDMGFEPQIRHIVEECdmPSveNRQTLMFSATFPVDIQHLARDFLDNYIFLS 375
Cdd:cd17955 145 VKFLVLDEADRLLTGSFEDDLATILSAL--PP--KRQTLLFSATLTDALKALKELFGNKPFFWE 204
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
172-376 |
1.85e-45 |
|
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin gene, NUP98, by inversion 11 (p15q22) chromosome translocation is found in the patients with de novo or therapy-related myeloid malignancies. Diseases associated with DDX10 (also known as DDX10-NUP98 Fusion Protein Type 2) include myelodysplastic syndrome and leukemia, acute myeloid. DDX10 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350699 [Multi-domain] Cd Length: 198 Bit Score: 159.76 E-value: 1.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 172 ASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFTELFRSGpspvpekaqsfYSRKGYPSALVLAPTRELAT 251
Cdd:cd17941 8 AGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRER-----------WTPEDGLGALIISPTRELAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 252 QIFEEARKFTYRSWVRPCVVYGGAPIGNQMREVDRgCDLLVATPGR-LNDLLERGKVSLANIKYLVLDEADRMLDMGFEP 330
Cdd:cd17941 77 QIFEVLRKVGKYHSFSAGLIIGGKDVKEEKERINR-MNILVCTPGRlLQHMDETPGFDTSNLQMLVLDEADRILDMGFKE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 768886153 331 QIRHIVEEcdMPSVenRQTLMFSATFPVDIQHLARDFLDNYIFLSV 376
Cdd:cd17941 156 TLDAIVEN--LPKS--RQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
165-370 |
3.34e-45 |
|
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: 159.28 E-value: 3.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 165 LMENIKLASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFTELFRSGPSPvpekaqsfysRKGYPSALVLA 244
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANL----------KKGQVGALIIS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 245 PTRELATQIFEEARKFTYRSW--VRPCVVYGGAPIGNQMREVDR-GCDLLVATPGRLNDLLER--GKVSLANIKYLVLDE 319
Cdd:cd17960 71 PTRELATQIYEVLQSFLEHHLpkLKCQLLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLSRkaDKVKVKSLEVLVLDE 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 768886153 320 ADRMLDMGFEPQIRHIVEEcdMPsvENRQTLMFSATFPVDIQHLARDFLDN 370
Cdd:cd17960 151 ADRLLDLGFEADLNRILSK--LP--KQRRTGLFSATQTDAVEELIKAGLRN 197
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
165-375 |
6.73e-44 |
|
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: 155.40 E-value: 6.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 165 LMENIKLASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFTELFrsgpspvpekaqsFYSRKgyPSALVLA 244
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCL-------------TEHRN--PSALILT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 245 PTRELATQIFEEARKFTY-RSWVRPCVVYGGAPIGNQMREVDRGCDLLVATPGRLNDLLERGKVSLANIKYLVLDEADRM 323
Cdd:cd17962 66 PTRELAVQIEDQAKELMKgLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTM 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 768886153 324 LDMGFEPQIRHIVEECDmpsvENRQTLMFSATFPVDIQHLARDFLDNYIFLS 375
Cdd:cd17962 146 LKMGFQQQVLDILENIS----HDHQTILVSATIPRGIEQLAGQLLQNPVRIT 193
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
163-370 |
6.76e-44 |
|
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: 155.53 E-value: 6.76e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 163 ELLMeNIKLASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFtelfrsgpspvpekaQSFYSRKGYPSALV 242
Cdd:cd17940 9 ELLM-GIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPIL---------------EKIDPKKDVIQALI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 243 LAPTRELATQIFEEARKFTYRSWVRPCVVYGGAPIGNQMREVDRGCDLLVATPGRLNDLLERGKVSLANIKYLVLDEADR 322
Cdd:cd17940 73 LVPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADK 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 768886153 323 MLDMGFEPQIRHIVEECDmpsvENRQTLMFSATFPVDIQHLARDFLDN 370
Cdd:cd17940 153 LLSQDFQPIIEKILNFLP----KERQILLFSATFPLTVKNFMDRHMHN 196
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
173-361 |
1.87e-41 |
|
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: 150.08 E-value: 1.87e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 173 SFTKPTPVQKYSIP-IVTKGRDLMACAQTGSGKTGGFLFPLFTELFRSgpspvpEKAQSFYSRKGYPSALVLAPTRELAT 251
Cdd:cd17946 9 GFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERLLSQ------KSSNGVGGKQKPLRALILTPTRELAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 252 QI---FEEARKFTYrswVRPCVVYGGAPIGNQMREVDRGCDLLVATPGRLNDLLERGK---VSLANIKYLVLDEADRMLD 325
Cdd:cd17946 83 QVkdhLKAIAKYTN---IKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNehlANLKSLRFLVLDEADRMLE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 768886153 326 MG-FEpQIRHIVE---ECDMPSVENRQTLMFSATFPVDIQ 361
Cdd:cd17946 160 KGhFA-ELEKILEllnKDRAGKKRKRQTFVFSATLTLDHQ 198
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
397-506 |
9.11e-40 |
|
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: 140.81 E-value: 9.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 397 DKKSALLDLLSAEHKGLTLIFVETKRMADqLTDFLIMQNFKATAIHGDRTQAERERALSAFKANVADILVATAVAARGLD 476
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 768886153 477 IPNVTHVINYDLPSDIDDYVHRIGRTGRAG 506
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
166-365 |
1.37e-38 |
|
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: 140.96 E-value: 1.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 166 MENIKLASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFTELFRSGpspvpekaqsFYSRKGyPSALVLAP 245
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLK----------FKPRNG-TGVIIISP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 246 TRELATQIFEEARKF-TYRSWVRPCVVyGGApigNQMREVDR---GCDLLVATPGRLNDLLERGKVSL-ANIKYLVLDEA 320
Cdd:cd17942 71 TRELALQIYGVAKELlKYHSQTFGIVI-GGA---NRKAEAEKlgkGVNILVATPGRLLDHLQNTKGFLyKNLQCLIIDEA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 768886153 321 DRMLDMGFEPQIRHIVEEcdMPSveNRQTLMFSATFPVDIQHLAR 365
Cdd:cd17942 147 DRILEIGFEEEMRQIIKL--LPK--RRQTMLFSATQTRKVEDLAR 187
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
179-368 |
1.15e-37 |
|
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: 138.44 E-value: 1.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 179 PVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFTELfrsgpspvpEKAQSFYSRKGYPSALVLAPTRELATQIFEEAR 258
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKL---------QEDQQPRKRGRAPKVLVLAPTRELANQVTKDFK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 259 KFTYRSWVrpCVVYGGAPIGNQMREVDRGCDLLVATPGRLNDLLERGKVSLANIKYLVLDEADRMLDMGFEPQIRHIVEE 338
Cdd:cd17944 86 DITRKLSV--ACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSV 163
|
170 180 190
....*....|....*....|....*....|.
gi 768886153 339 C-DMPSVENRQTLMFSATFPVDIQHLARDFL 368
Cdd:cd17944 164 SyKKDSEDNPQTLLFSATCPDWVYNVAKKYM 194
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
165-364 |
1.31e-37 |
|
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: 138.61 E-value: 1.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 165 LMENIKLASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFtELFRsgpspvpekaqsfysrkgypsALVLA 244
Cdd:cd17938 10 LIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL-QIVV---------------------ALILE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 245 PTRELATQIFEEARKFTY---RSWVRPCVVYGGAPIGNQMREVDRGCDLLVATPGRLNDLLERGKVSLANIKYLVLDEAD 321
Cdd:cd17938 68 PSRELAEQTYNCIENFKKyldNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEAD 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 768886153 322 RMLDMGFEPQIRHIVEEcdMPSVENR----QTLMFSATF-PVDIQHLA 364
Cdd:cd17938 148 RLLSQGNLETINRIYNR--IPKITSDgkrlQVIVCSATLhSFEVKKLA 193
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
165-357 |
4.34e-36 |
|
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350706 [Multi-domain] Cd Length: 231 Bit Score: 135.19 E-value: 4.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 165 LMENIKLASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFTELFRSGPSP-VPEKAqsfysrkgyPSALVL 243
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAeGPFNA---------PRGLVI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 244 APTRELATQIFEEARKFTYRSWVRPCVVYGGAPIGNQMREVDRGCDLLVATPGRLNDLLERGKVSLANIKYLVLDEADRM 323
Cdd:cd17948 72 TPSRELAEQIGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 768886153 324 LDMGFEPQIRHIVEECDMPSVENR---------QTLMFSATFP 357
Cdd:cd17948 152 LDDSFNEKLSHFLRRFPLASRRSEntdgldpgtQLVLVSATMP 194
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
161-370 |
6.73e-36 |
|
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: 133.86 E-value: 6.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 161 LDELLMENIKLASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFTELFRsgpspvpEKAQSfySRKGYPSA 240
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILK-------AKAES--GEEQGTRA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 241 LVLAPTRELATQIFEEARKFTY--RSWVRpCVvyggaPIGNQMREVDRGC------DLLVATPGRLNDLLERG-KVSLAN 311
Cdd:cd17961 72 LILVPTRELAQQVSKVLEQLTAycRKDVR-VV-----NLSASSSDSVQRAllaekpDIVVSTPARLLSHLESGsLLLLST 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 768886153 312 IKYLVLDEADRMLDMGFEPQIRHIVEEcdMPSveNRQTLMFSATFPVDIQHLARDFLDN 370
Cdd:cd17961 146 LKYLVIDEADLVLSYGYEEDLKSLLSY--LPK--NYQTFLMSATLSEDVEALKKLVLHN 200
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
161-370 |
2.17e-35 |
|
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and is required for the export of mRNA out of the nucleus. DDX39B is an essential splicing factor required for association of U2 small nuclear ribonucleoprotein with pre-mRNA, and it also plays an important role in mRNA export from the nucleus to the cytoplasm. Diseases associated with DDX39A (also called UAP56-Related Helicase, 49 kDa) include gastrointestinal stromal tumor and inflammatory bowel disease 6, while diseases associated with DDX39B (also called 56 kDa U2AF65-Associated Protein) include Plasmodium vivax malaria. DDX39 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350708 [Multi-domain] Cd Length: 208 Bit Score: 132.47 E-value: 2.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 161 LDELLMENIKLASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFTELfrsgpSPVPekaqsfysrkGYPSA 240
Cdd:cd17950 9 LKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQL-----EPVD----------GQVSV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 241 LVLAPTRELATQIFEEARKFT-YRSWVRPCVVYGGAPIGNQMREV-DRGCDLLVATPGRLNDLLERGKVSLANIKYLVLD 318
Cdd:cd17950 74 LVICHTRELAFQISNEYERFSkYMPNVKTAVFFGGVPIKKDIEVLkNKCPHIVVGTPGRILALVREKKLKLSHVKHFVLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 768886153 319 EADRM---LDMgfepqiRHIVEECDMPSVENRQTLMFSATFPVDIQHLARDFLDN 370
Cdd:cd17950 154 ECDKMleqLDM------RRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQD 202
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
156-372 |
9.20e-35 |
|
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: 130.64 E-value: 9.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 156 FSSPPLDELLMENIKLASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFTELFRSGPSPvpekaqsfysrk 235
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKAT------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 236 gypSALVLAPTRELATQIFE--EARKFTYRSWVRPCVvyGGAPIGNQMREVDRGCDLLVATPGRLNDLLERGKVSLANIK 313
Cdd:cd18046 69 ---QALVLAPTRELAQQIQKvvMALGDYMGIKCHACI--GGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIK 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 768886153 314 YLVLDEADRMLDMGFEPQIRHIVEEcdMPsvENRQTLMFSATFPVDIQHLARDFLDNYI 372
Cdd:cd18046 144 MFVLDEADEMLSRGFKDQIYDIFQK--LP--PDTQVVLLSATMPNDVLEVTTKFMRDPI 198
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
160-370 |
1.07e-34 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation factor-4A (eIF4A) family consists of 3 proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA. EIF4A proteins are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350697 [Multi-domain] Cd Length: 199 Bit Score: 130.14 E-value: 1.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 160 PLDELLMENIKLASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFTELFRSGPSPvpekaqsfysrkgypS 239
Cdd:cd17939 3 GLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRET---------------Q 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 240 ALVLAPTRELATQIFE--EARKFTYRSWVRPCVvyGGAPIGNQMREVDRGCDLLVATPGRLNDLLERGKVSLANIKYLVL 317
Cdd:cd17939 68 ALVLAPTRELAQQIQKvvKALGDYMGVKVHACI--GGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 768886153 318 DEADRMLDMGFEPQIRHIVEEcdMPSveNRQTLMFSATFPVDIQHLARDFLDN 370
Cdd:cd17939 146 DEADEMLSRGFKDQIYDIFQF--LPP--ETQVVLFSATMPHEVLEVTKKFMRD 194
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
161-374 |
2.82e-33 |
|
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: 126.15 E-value: 2.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 161 LDELLMENIKLASFTKPTPVQKYSIPIVTKG--RDLMACAQTGSGKTGGFLFplfTELFRSGPspvpekaqsfysRKGYP 238
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVL---AMLSRVDP------------TLKSP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 239 SALVLAPTRELATQIFEEARKF------TYRSWVRPCVVYGGAPIGNQmrevdrgcdLLVATPGRLNDLLERGKVSLANI 312
Cdd:cd17963 66 QALCLAPTRELARQIGEVVEKMgkftgvKVALAVPGNDVPRGKKITAQ---------IVIGTPGTVLDWLKKRQLDLKKI 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768886153 313 KYLVLDEADRMLDM-GFEPQIRHIVEecDMPSveNRQTLMFSATFPVDIQHLARDFLDNYIFL 374
Cdd:cd17963 137 KILVLDEADVMLDTqGHGDQSIRIKR--MLPR--NCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
165-375 |
1.48e-32 |
|
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: 123.91 E-value: 1.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 165 LMENIKLASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFtelfrsgpspvpekaQSFYSRKGYPSALVLA 244
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIAL---------------ESLDLERRHPQVLILA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 245 PTRELATQIFEEARKF-TYRSWVRPCVVYGGAPIgNQMREVDRGCDLLVATPGRLNDLLERGKVSLANIKYLVLDEADRM 323
Cdd:cd17943 66 PTREIAVQIHDVFKKIgKKLEGLKCEVFIGGTPV-KEDKKKLKGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKL 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 768886153 324 LDMGFEPQIRHIVEEcdMPsvENRQTLMFSATFPVDIQHLARDFLDNYIFLS 375
Cdd:cd17943 145 MEGSFQKDVNWIFSS--LP--KNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
425-506 |
1.73e-31 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 116.93 E-value: 1.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 425 DQLTDFLIMQNFKATAIHGDRTQAERERALSAFKANVADILVATAVAARGLDIPNVTHVINYDLPSDIDDYVHRIGRTGR 504
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 768886153 505 AG 506
Cdd:smart00490 81 AG 82
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
156-370 |
7.02e-30 |
|
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: 116.80 E-value: 7.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 156 FSSPPLDELLMENIKLASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFtelfrsgpspvpekaQSFYSRK 235
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVL---------------QCLDIQV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 236 GYPSALVLAPTRELATQIFEEARKFTYRSWVRPCVVYGGAPIGNQMREVDRGCDLLVATPGRLNDLLERGKVSLANIKYL 315
Cdd:cd18045 66 RETQALILSPTRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKML 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 768886153 316 VLDEADRMLDMGFEPQIRHIVEEcdMPSveNRQTLMFSATFPVDIQHLARDFLDN 370
Cdd:cd18045 146 VLDEADEMLNKGFKEQIYDVYRY--LPP--ATQVVLVSATLPQDILEMTNKFMTD 196
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
165-365 |
3.87e-25 |
|
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350714 [Multi-domain] Cd Length: 231 Bit Score: 104.25 E-value: 3.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 165 LMENIKLASFTKPTPVQKYSIPIVTKG---------RDLMACAQTGSGKTGGFLFPLFTELFRSgpsPVPEKaqsfysrk 235
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKR---VVPRL-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 236 gypSALVLAPTRELATQIFEEARKFTYRSWVRPCVVYGGAPIGNQMREVDRGC--------DLLVATPGRLNDLLERGK- 306
Cdd:cd17956 70 ---RALIVVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTsgrylsrvDILVATPGRLVDHLNSTPg 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768886153 307 VSLANIKYLVLDEADRMLDMGFEPQIRHIVEECD----------------MPSVENRQTLMFSATFPVDIQHLAR 365
Cdd:cd17956 147 FTLKHLRFLVIDEADRLLNQSFQDWLETVMKALGrptapdlgsfgdanllERSVRPLQKLLFSATLTRDPEKLSS 221
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
281-528 |
6.71e-23 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 102.14 E-value: 6.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 281 MREVDRG-CDLLVATPGRLN-----DLLERGKVSLanikyLVLDEA--------DrmldmgFEP---QIRHIVEECDmps 343
Cdd:COG0514 100 LRALRAGeLKLLYVAPERLLnprflELLRRLKISL-----FAIDEAhcisqwghD------FRPdyrRLGELRERLP--- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 344 veNRQTLMFSATF--PV--DI-QHLARDflDNYIFL-SVGRvgstsENITQRILYVDDMDKKSALLDLLSAEHKGLTLIF 417
Cdd:COG0514 166 --NVPVLALTATAtpRVraDIaEQLGLE--DPRVFVgSFDR-----PNLRLEVVPKPPDDKLAQLLDFLKEHPGGSGIVY 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 418 VETKRMADQLTDFLIMQNFKATAIHGDRTQAERERALSAFKANVADILVATaVA-ARGLDIPNVTHVINYDLPSDIDDYV 496
Cdd:COG0514 237 CLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLPKSIEAYY 315
|
250 260 270
....*....|....*....|....*....|..
gi 768886153 497 HRIGRTGRAGNTGVATSFFNSNNQNIVKGLME 528
Cdd:COG0514 316 QEIGRAGRDGLPAEALLLYGPEDVAIQRFFIE 347
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
151-484 |
9.68e-23 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 102.41 E-value: 9.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 151 EPILDFSSPPLDELLMENIKLASFTKPTP-------VQKYSIPIVTKGRDLMACAQTGSGKTGGFLFpLFTELFRSGPsp 223
Cdd:COG1061 53 LPEEDTERELAEAEALEAGDEASGTSFELrpyqqeaLEALLAALERGGGRGLVVAPTGTGKTVLALA-LAAELLRGKR-- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 224 vpekaqsfysrkgypsALVLAPTRELATQIFEEARKFTYRSwvrpcVVYGGapignqmrEVDRGCDLLVATPGRLNDLLE 303
Cdd:COG1061 130 ----------------VLVLVPRRELLEQWAEELRRFLGDP-----LAGGG--------KKDSDAPITVATYQSLARRAH 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 304 RGKVSlANIKYLVLDEA--------DRMLDMgFEPQIRhiveecdmpsvenrqtLMFSAT------------------FP 357
Cdd:COG1061 181 LDELG-DRFGLVIIDEAhhagapsyRRILEA-FPAAYR----------------LGLTATpfrsdgreillflfdgivYE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 358 VDIQHLARD-FLDNYIFLSV--------GRVGSTSENITQRILYVDDMdKKSALLDLLSAEHKGL-TLIFVETKRMADQL 427
Cdd:COG1061 243 YSLKEAIEDgYLAPPEYYGIrvdltderAEYDALSERLREALAADAER-KDKILRELLREHPDDRkTLVFCSSVDHAEAL 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 768886153 428 TDFLIMQNFKATAIHGDRTQAERERALSAFKANVADILVATAVAARGLDIPNVTHVI 484
Cdd:COG1061 322 AELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI 378
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
159-357 |
2.27e-20 |
|
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: 90.90 E-value: 2.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 159 PPLDELLMENIKLASFT-----KPTPVQKYSIPIVTKGR----------------DLMACAQTGSGKTGGFLFPLFTELF 217
Cdd:cd17965 8 PSVREAIIKEILKGSNKtdeeiKPSPIQTLAIKKLLKTLmrkvtkqtsneepkleVFLLAAETGSGKTLAYLAPLLDYLK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 218 RSGPSPVPEKAQSFYSRK--GYPSALVLAPTRELATQIFEEARKFTYRSWVRPCVV-YGGAPIGNQMREVDRG-CDLLVA 293
Cdd:cd17965 88 RQEQEPFEEAEEEYESAKdtGRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFsSGFGPSYQRLQLAFKGrIDILVT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768886153 294 TPGRLNDLLERGKVSLANIKYLVLDEADRMLDMGFEPQIRHIVEEcdMPSVenRQTLMFSATFP 357
Cdd:cd17965 168 TPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKR--APKL--KHLILCSATIP 227
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
414-506 |
1.23e-16 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 83.63 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 414 TLIFVETKRMADQLTDFLIMQNFKAT------AIHGDR--TQAERERALSAFKANVADILVATAVAARGLDIPNVTHVIN 485
Cdd:COG1111 356 IIVFTQYRDTAEMIVEFLSEPGIKAGrfvgqaSKEGDKglTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIF 435
|
90 100
....*....|....*....|..
gi 768886153 486 YDL-PSDIdDYVHRIGRTGRAG 506
Cdd:COG1111 436 YEPvPSEI-RSIQRKGRTGRKR 456
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
142-364 |
1.27e-16 |
|
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH) is a testis-specific protein essential for completion of spermatogenesis. DDX25 is also a novel negative regulator of IFN pathway and facilitates RNA virus infection. Diseases associated with DDX25 include hydrolethalus syndrome, an autosomal recessive lethal malformation syndrome characterized by multiple developmental defects of fetus.. DDX25 (also called gonadotropin-regulated testicular RNA helicase) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350806 [Multi-domain] Cd Length: 229 Bit Score: 79.29 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 142 VDASGKDVPEPILD---FSSPPLDELLMENIKLASFTKPTPVQKYSIPIVTKG--RDLMACAQTGSGKTGGFLFPLFTEL 216
Cdd:cd18048 3 VEVLQRDPTSPLFSvksFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 217 frsgpspvpekaqsfYSRKGYPSALVLAPTRELATQ---IFEEARKFTyrswVRPCVVYggAPIGNQM-REVDRGCDLLV 292
Cdd:cd18048 83 ---------------DALKLYPQCLCLSPTFELALQtgkVVEEMGKFC----VGIQVIY--AIRGNRPgKGTDIEAQIVI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768886153 293 ATPGRLNDLLERGK-VSLANIKYLVLDEADRMLDM-GFEPQI----RHIVEECDMpsvenrqtLMFSATFPVDIQHLA 364
Cdd:cd18048 142 GTPGTVLDWCFKLRlIDVTNISVFVLDEADVMINVqGHSDHSvrvkRSMPKECQM--------LLFSATFEDSVWAFA 211
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
383-506 |
7.80e-15 |
|
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: 71.47 E-value: 7.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 383 SENITQRILYVDDMDKKSALLDLLSAEHK-GLTLIFVETKRMADQLTDFLIMQNFKATAIHGDRTQAERERALSAFKANV 461
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDLLKRIKVEHLgGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 768886153 462 ADILVATAVAARGLDIPNVTHVINYDLPSDIDDYVHRIGRTGRAG 506
Cdd:cd18794 81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDG 125
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
402-500 |
1.76e-13 |
|
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: 67.50 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 402 LLDLLSAEHKglTLIFVETKRMADQLTDFLIMQNFKATAIHGDRTQAERERALSAFKAN--VADILVATAVAARGLDIPN 479
Cdd:cd18793 20 LEELREPGEK--VLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDpdIRVFLLSTKAGGVGLNLTA 97
|
90 100
....*....|....*....|....*..
gi 768886153 480 VTHVINYDL---PSDID---DYVHRIG 500
Cdd:cd18793 98 ANRVILYDPwwnPAVEEqaiDRAHRIG 124
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
395-507 |
1.59e-12 |
|
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: 65.31 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 395 DMDKKSALLDLLSAEHKGL----TLIFVETKRMADQLTDFL-----IMQNFKATAI--HGDRTQAER--------ERALS 455
Cdd:cd18802 5 VIPKLQKLIEILREYFPKTpdfrGIIFVERRATAVVLSRLLkehpsTLAFIRCGFLigRGNSSQRKRslmtqrkqKETLD 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 768886153 456 AFKANVADILVATAVAARGLDIPNVTHVINYDLPSDIDDYVHRIGRtGRAGN 507
Cdd:cd18802 85 KFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARAPN 135
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
415-538 |
1.93e-11 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 67.21 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 415 LIFVETKRMADQLTDFLIMQNFKATAIHG--DR------TQAERERALSAFKANVADILVATAVAARGLDIPNVTHVINY 486
Cdd:PRK13766 369 IVFTQYRDTAEKIVDLLEKEGIKAVRFVGqaSKdgdkgmSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFY 448
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768886153 487 D-LPSDIdDYVHRIGRTGRaGNTG-----VA------TSFFNSNN-----QNIVKGLMEILNEANQEVP 538
Cdd:PRK13766 449 EpVPSEI-RSIQRKGRTGR-QEEGrvvvlIAkgtrdeAYYWSSRRkekkmKEELKNLKGILNKKLQELD 515
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
191-355 |
2.80e-11 |
|
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: 61.65 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 191 GRDLMACAQTGSGKTGGFLFPLFtELFRSGPSPVpekaqsfysrkgypsaLVLAPTRELATQIFEEARKftYRSWVRPC- 269
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAAL-LLLLKKGKKV----------------LVLVPTKALALQTAERLRE--LFGPGIRVa 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 270 VVYGGAPIGNQMREVDRGCDLLVATPGRLNDLLER-GKVSLANIKYLVLDEADRMLDMGFEPQIRHIVEECDMPSVEnrQ 348
Cdd:cd00046 62 VLVGGSSAEEREKNKLGDADIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNA--Q 139
|
....*..
gi 768886153 349 TLMFSAT 355
Cdd:cd00046 140 VILLSAT 146
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
402-502 |
7.02e-11 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 65.25 E-value: 7.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 402 LLDLLSAEHKglTLIFVETKRMADQLTDFLIMQNFKATAIHGDRTQAERERALSAFKAN--VADILVATAVAARGLDIPN 479
Cdd:COG0553 542 LEELLAEGEK--VLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGpeAPVFLISLKAGGEGLNLTA 619
|
90 100
....*....|....*....|....*....
gi 768886153 480 VTHVINYDL---PSDID---DYVHRIGRT 502
Cdd:COG0553 620 ADHVIHYDLwwnPAVEEqaiDRAHRIGQT 648
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
414-510 |
2.27e-10 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 56.94 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 414 TLIFVETKRMADQLTDFLImqnfkataihgdrtqaereralsafkanvadILVATAVAARGLDIPNVTHVINYDLPSDID 493
Cdd:cd18785 6 IIVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDPPSSAA 54
|
90
....*....|....*..
gi 768886153 494 DYVHRIGRTGRAGNTGV 510
Cdd:cd18785 55 SYIQRVGRAGRGGKDEG 71
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
178-506 |
2.11e-09 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 60.29 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 178 TPVQKYSIP-IVTKGRDLMACAQTGSGKTggflfpLFTELFrsgpspvpekAQSFYSRKGypSALVLAPTRELATQIFEE 256
Cdd:COG1204 24 YPPQAEALEaGLLEGKNLVVSAPTASGKT------LIAELA----------ILKALLNGG--KALYIVPLRALASEKYRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 257 ARKFtYRSW-VRPCVVYGGAPIGNqmREVDRgCDLLVATPGRLnDLLERGKVS-LANIKYLVLDEAdrmldmgfepqirH 334
Cdd:COG1204 86 FKRD-FEELgIKVGVSTGDYDSDD--EWLGR-YDILVATPEKL-DSLLRNGPSwLRDVDLVVVDEA-------------H 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 335 IVEEcdmpsvENRqtlmfSATFPVDIQHLARDFLD-NYIFLS--------VGR------VGST------SENI-TQRILY 392
Cdd:COG1204 148 LIDD------ESR-----GPTLEVLLARLRRLNPEaQIVALSatignaeeIAEwldaelVKSDwrpvplNEGVlYDGVLR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 393 VDDMDKKS------ALLDLLSAEhkGLTLIFVETKR--------MADQLTDFLIMQNFKATAI----------------- 441
Cdd:COG1204 217 FDDGSRRSkdptlaLALDLLEEG--GQVLVFVSSRRdaeslakkLADELKRRLTPEEREELEElaeellevseethtnek 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 442 ------------HGDRTQAERERALSAFKANVADILVATAVAARGLDIPnVTHVI--------NYDLPsdIDDYVHRIGR 501
Cdd:COG1204 295 ladclekgvafhHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLP-ARRVIirdtkrggMVPIP--VLEFKQMAGR 371
|
....*
gi 768886153 502 TGRAG 506
Cdd:COG1204 372 AGRPG 376
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
156-356 |
2.30e-09 |
|
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: 57.81 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 156 FSSPPLDELLMENIKLASFTKPTPVQKYSIPIV--TKGRDLMACAQTGSGKTGGFLFPLFTELfrsgpSPVPEKAQsfys 233
Cdd:cd18047 3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMlaEPPQNLIAQSQSGTGKTAAFVLAMLSQV-----EPANKYPQ---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 234 rkgypsALVLAPTRELATQ---IFEEARKFTyrswvrPCVVYGGAPIGNQMREVDRGCD-LLVATPGRLNDLLERGK-VS 308
Cdd:cd18047 74 ------CLCLSPTYELALQtgkVIEQMGKFY------PELKLAYAVRGNKLERGQKISEqIVIGTPGTVLDWCSKLKfID 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 768886153 309 LANIKYLVLDEADRML-DMGFEPQI----RHIVEECDMpsvenrqtLMFSATF 356
Cdd:cd18047 142 PKKIKVFVLDEADVMIaTQGHQDQSiriqRMLPRNCQM--------LLFSATF 186
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
159-511 |
1.79e-08 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 57.54 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 159 PPLDELLMENIKLASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKTGGFLFPLFTELfRSGPSpvpekaqsfysrkgyP 238
Cdd:COG1205 39 DWLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEAL-LEDPG---------------A 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 239 SALVLAPT-----------RELATQIFEEARKFTY--------RSWVRpcvvyggapignqmrevdRGCDLLVATPgrln 299
Cdd:COG1205 103 TALYLYPTkalardqlrrlRELAEALGLGVRVATYdgdtppeeRRWIR------------------EHPDIVLTNP---- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 300 DLLERG------KVS--LANIKYLVLDEA---------------DRML----DMGFEPQIrhiveecdmpsvenrqtLMF 352
Cdd:COG1205 161 DMLHYGllphhtRWArfFRNLRYVVIDEAhtyrgvfgshvanvlRRLRricrHYGSDPQF-----------------ILA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 353 SAT-----------FPVDIQHLARD----------FLDNYIFLSVGRVGSTSEniTQRIlyvddmdkksaLLDLLSAEHK 411
Cdd:COG1205 224 SATignpaehaerlTGRPVTVVDEDgsprgertfvLWNPPLVDDGIRRSALAE--AARL-----------LADLVREGLR 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 412 glTLIFVETKRMADQLTdfLIMQNFKATAIHGDRTQA--------EReRAL-SAFKANVADILVAT-AVAArGLDIPNVT 481
Cdd:COG1205 291 --TLVFTRSRRGAELLA--RYARRALREPDLADRVAAyragylpeER-REIeRGLRSGELLGVVSTnALEL-GIDIGGLD 364
|
410 420 430
....*....|....*....|....*....|
gi 768886153 482 HVINYDLPSDIDDYVHRIGRTGRAGNTGVA 511
Cdd:COG1205 365 AVVLAGYPGTRASFWQQAGRAGRRGQDSLV 394
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
415-504 |
2.41e-08 |
|
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: 53.13 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 415 LIFVETKRMADQLTDFL--IMQNFKATAIHGDR--------TQAERERALSAFKANVADILVATAVAARGLDIPNVTHVI 484
Cdd:cd18801 34 IIFSEFRDSAEEIVNFLskIRPGIRATRFIGQAsgksskgmSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLII 113
|
90 100
....*....|....*....|.
gi 768886153 485 NYD-LPSDIdDYVHRIGRTGR 504
Cdd:cd18801 114 CYDaSPSPI-RMIQRMGRTGR 133
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
182-355 |
2.60e-08 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 54.36 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 182 KYSIPIV---TKGRDLMACAQTGSGKTggFLFPLFTE-LFRSGPSpvpekaqsfySRKGYpsALVLAPTRELATQIFEEA 257
Cdd:cd17927 5 NYQLELAqpaLKGKNTIICLPTGSGKT--FVAVLICEhHLKKFPA----------GRKGK--VVFLANKVPLVEQQKEVF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 258 RKFTYRSWVRPCVVYGGAPIGNQMREVDRGCDLLVATPGRL-NDLLERGKVSLANIKYLVLDEADRMLDMGFEPQIRHIV 336
Cdd:cd17927 71 RKHFERPGYKVTGLSGDTSENVSVEQIVESSDVIIVTPQILvNDLKSGTIVSLSDFSLLVFDECHNTTKNHPYNEIMFRY 150
|
170 180
....*....|....*....|
gi 768886153 337 EECDMPSV-ENRQTLMFSAT 355
Cdd:cd17927 151 LDQKLGSSgPLPQILGLTAS 170
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
400-507 |
3.73e-08 |
|
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: 52.65 E-value: 3.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 400 SALLDLLSAeHKGlTLIFVETKRMADQLTD---FLIMQNFKATAI---HGDRTQAERERALSAFKANVADILVATAVAAR 473
Cdd:cd18796 29 AEVIFLLER-HKS-TLVFTNTRSQAERLAQrlrELCPDRVPPDFIalhHGSLSRELREEVEAALKRGDLKVVVATSSLEL 106
|
90 100 110
....*....|....*....|....*....|....
gi 768886153 474 GLDIPNVTHVINYDLPSDIDDYVHRIGRTGRAGN 507
Cdd:cd18796 107 GIDIGDVDLVIQIGSPKSVARLLQRLGRSGHRPG 140
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
187-320 |
5.19e-08 |
|
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: 53.03 E-value: 5.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 187 IVTKGRDLMACAQTGSGKTGGFLFPLFTELFRSGPSpvpekaqsfysrkgypsALVLAPTRELATQIFEEARKFTYRSWV 266
Cdd:cd17921 13 LYLSGDSVLVSAPTSSGKTLIAELAILRALATSGGK-----------------AVYIAPTRALVNQKEADLRERFGPLGK 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 768886153 267 RPCVVYGGAPIGNQMrevDRGCDLLVATPGRLNDLLERGKV-SLANIKYLVLDEA 320
Cdd:cd17921 76 NVGLLTGDPSVNKLL---LAEADILVATPEKLDLLLRNGGErLIQDVRLVVVDEA 127
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
414-504 |
1.19e-07 |
|
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350177 [Multi-domain] Cd Length: 171 Bit Score: 51.86 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 414 TLIFVETKRMADQLTDFLIMQNFKATAIHGDRTQAERERALSAFKANVADILVATAVAARGLDIPNVTHVINYDlpSDID 493
Cdd:cd18790 30 VLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILD--ADKE 107
|
90
....*....|....*...
gi 768886153 494 DY-------VHRIGRTGR 504
Cdd:cd18790 108 GFlrsetslIQTIGRAAR 125
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
400-515 |
1.29e-07 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 51.58 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 400 SALLDLLSA--EHKGLTLIFvetkrmadqltdfliMQNFKATAIHGDRTQAERERALSAFKANVADILVATAVAARGLDI 477
Cdd:cd18811 39 SEKLDLKAAvaMYEYLKERF---------------RPELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDV 103
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 768886153 478 PNVTHVINYDlpsdiddyVHRIGRT------GRAGNTGVATSFF 515
Cdd:cd18811 104 PNATVMVIED--------AERFGLSqlhqlrGRVGRGDHQSYCL 139
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
191-320 |
2.44e-07 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 51.05 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 191 GRDLMACAQTGSGKTGGFLFPLFTELfrsgpspvpekaqsfYSRKGyPSALVLAPTRELATQIFEEARKFT--YRSWVRP 268
Cdd:cd17923 15 GRSVVVTTGTASGKSLCYQLPILEAL---------------LRDPG-SRALYLYPTKALAQDQLRSLRELLeqLGLGIRV 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 768886153 269 CVVYGGAPIGNQMREVDRGCDLLVATPGRLNDLL----ERGKVSLANIKYLVLDEA 320
Cdd:cd17923 79 ATYDGDTPREERRAIIRNPPRILLTNPDMLHYALlphhDRWARFLRNLRYVVLDEA 134
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
422-487 |
4.93e-07 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350179 [Multi-domain] Cd Length: 160 Bit Score: 49.96 E-value: 4.93e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768886153 422 RMADQLTDflIMQNFKATAIHGDRTQAERERALSAFKANVADILVATAVAARGLDIPNVTHVINYD 487
Cdd:cd18792 49 ALAEELKE--LVPEARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIED 112
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
386-516 |
2.51e-06 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 50.48 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 386 ITQRILYVDDMDKKSALldllsaehkgltlIFVETKRMADQLTDFLIMQNFKATAIHGDRTQAERERALSAFKANVADIL 465
Cdd:PRK11057 224 LDQLMRYVQEQRGKSGI-------------IYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIV 290
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 768886153 466 VATAVAARGLDIPNVTHVINYDLPSDIDDYVHRIGRTGRAGNTGVATSFFN 516
Cdd:PRK11057 291 VATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYD 341
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
385-504 |
2.75e-06 |
|
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350185 [Multi-domain] Cd Length: 174 Bit Score: 48.07 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 385 NITQriLYVDDMDKKSALLDLLSAEHKGlTLIFVET---KRMADQLTDFLIMQNFKATAIHgdrtqAERERALSAFKANV 461
Cdd:cd18798 1 NIVD--VYIEDSDSLEKLLELVKKLGDG-GLIFVSIdygKEYAEELKEFLERHGIKAELAL-----SSTEKNLEKFEEGE 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 768886153 462 ADILVATA----VAARGLDIPN-VTHVINYDLPsdIDDYVHRIGRTGR 504
Cdd:cd18798 73 IDVLIGVAsyygVLVRGIDLPErIKYAIFYGVP--VTTYIQASGRTSR 118
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
191-319 |
7.12e-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: 46.42 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 191 GRDLMACAQTGSGKTGGFLFPLFTELFRSGPSPVpekaqsfysrkgypSALVLAPTRELATQIFE------EARKFTYRS 264
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGV--------------QVLYISPLKALINDQERrleeplDEIDLEIPV 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 768886153 265 WVRpcvvYGGAPIGNQMREVDRGCDLLVATPGRLNDLL--ERGKVSLANIKYLVLDE 319
Cdd:cd17922 67 AVR----HGDTSQSEKAKQLKNPPGILITTPESLELLLvnKKLRELFAGLRYVVVDE 119
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
172-227 |
1.28e-05 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 48.56 E-value: 1.28e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 768886153 172 ASFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKT-GGFLFPLfTELFRSGPSPVPEK 227
Cdd:COG1201 20 ARFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAFLPAL-DELARRPRPGELPD 75
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
402-515 |
1.86e-05 |
|
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: 44.93 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 402 LLDLLSAEHKglTLIFVETKrmaDQLTDflIMQNFKATAIHGDRTQAERERALSAFKANVADILVATAVAARGLDIP--N 479
Cdd:cd18789 42 LLKRHEQGDK--IIVFTDNV---EALYR--YAKRLLKPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPeaN 114
|
90 100 110
....*....|....*....|....*....|....*.
gi 768886153 480 VTHVINYDLPSDiDDYVHRIGRTGRAGNTGVATSFF 515
Cdd:cd18789 115 VAIQISGHGGSR-RQEAQRLGRILRPKKGGGKNAFF 149
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
151-205 |
2.47e-05 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 47.57 E-value: 2.47e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 768886153 151 EPILDFSSPPLDELLMEniklaSFTKPTPVQKYSIPIVTKGRDLMACAQTGSGKT 205
Cdd:PRK13767 12 EEILDLLRPYVREWFKE-----KFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKT 61
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
192-320 |
9.77e-05 |
|
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: 43.79 E-value: 9.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 192 RDLMACAQTGSGKTggFLFPL----FTELFRSGPSPvpEKAQSFysrkgypsalvLAPTRELATQIFEEARKFTYRSwVR 267
Cdd:cd18034 17 RNTIVVLPTGSGKT--LIAVMlikeMGELNRKEKNP--KKRAVF-----------LVPTVPLVAQQAEAIRSHTDLK-VG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 768886153 268 PCVVYGGAPIGNQMR--EVDRGCDLLVATPGRLNDLLERGKVSLANIKYLVLDEA 320
Cdd:cd18034 81 EYSGEMGVDKWTKERwkEELEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
414-484 |
9.97e-05 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350186 [Multi-domain] Cd Length: 116 Bit Score: 42.16 E-value: 9.97e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768886153 414 TLIFVETKRMADQLTDFLIMQNFKATAIHGDRTQAERERA---LSAFKANVADILVATAVAARGLDIPNVTHVI 484
Cdd:cd18799 9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDEaliLLFFGELKPPILVTVDLLTTGVDIPEVDNVV 82
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
308-506 |
1.95e-04 |
|
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
Pssm-ID: 187770 [Multi-domain] Cd Length: 353 Bit Score: 43.96 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 308 SLANIKY--LVLDEADrmldmGFEPQIRHIVEECDMPSVENRQTLM-FSATFPvdiqhlarDFLDNYiFLSVGRVG---- 380
Cdd:cd09639 118 TLASIANslLIFDEVH-----FYDEYTLALILAVLEVLKDNDVPILlMSATLP--------KFLKEY-AEKIGYVEenep 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 381 -STSENITQRI-LYVDDMDKKSALLDLLSAEHK--GLTLIFVETKRMADQLTDFLIMQN--FKATAIHGDRTQAERERA- 453
Cdd:cd09639 184 lDLKPNERAPFiKIESDKVGEISSLERLLEFIKkgGSVAIIVNTVDRAQEFYQQLKEKGpeEEIMLIHSRFTEKDRAKKe 263
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 454 ---LSAFKANVADILVATAVAARGLDipnvthvINYDL----PSDIDDYVHRIGRTGRAG 506
Cdd:cd09639 264 aelLLEFKKSEKFVIVATQVIEASLD-------ISVDVmiteLAPIDSLIQRLGRLHRYG 316
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
441-511 |
2.31e-04 |
|
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350197 [Multi-domain] Cd Length: 151 Bit Score: 41.95 E-value: 2.31e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768886153 441 IHGDRTQAERERALSAFKANVADILVATAVAARGLDIPNV-THVINydlpsDIDDY----VHRI-GRTGRAGNTGVA 511
Cdd:cd18810 57 AHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNAnTIIIE-----RADKFglaqLYQLrGRVGRSKERAYA 128
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
179-357 |
3.51e-04 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 41.94 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 179 PVQKYSI-PIVTKGRDLMACAQTGSGKTggflfpLFTELfrsgpspvpeKAQSFYSRKGypSALVLAPTRELATQIFEEA 257
Cdd:cd18028 4 PPQAEAVrAGLLKGENLLISIPTASGKT------LIAEM----------AMVNTLLEGG--KALYLVPLRALASEKYEEF 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 258 RKFtYRSWVRPcvvygGAPIGNqMREVDRG---CDLLVATPGRLNDLLERGKVSLANIKYLVLDEADRMLDMGFEPQIRH 334
Cdd:cd18028 66 KKL-EEIGLKV-----GISTGD-YDEDDEWlgdYDIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPTLES 138
|
170 180
....*....|....*....|...
gi 768886153 335 IVEECDMpSVENRQTLMFSATFP 357
Cdd:cd18028 139 IVARLRR-LNPNTQIIGLSATIG 160
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
241-322 |
4.77e-04 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 41.35 E-value: 4.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 241 LVLAPTRELATQIFEEARKFTyrSWVRPCVVYGGAPIGNQMREVDRGCDLLVATPGRL-NDLLErGKVSLANIKYLVLDE 319
Cdd:cd18035 49 LILAPSRPLVEQHAENLKRVL--NIPDKITSLTGEVKPEERAERWDASKIIVATPQVIeNDLLA-GRITLDDVSLLIFDE 125
|
...
gi 768886153 320 ADR 322
Cdd:cd18035 126 AHH 128
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
241-356 |
7.40e-04 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 40.37 E-value: 7.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 241 LVLAPTRELATQIFEEARKFTYRSWVrpCVVYGGApignqmREVDRGCDLLVATPGRLNDLLERGKVSLANIKYLVLDEA 320
Cdd:cd17926 48 LIVVPTDALLDQWKERFEDFLGDSSI--GLIGGGK------KKDFDDANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEA 119
|
90 100 110
....*....|....*....|....*....|....*.
gi 768886153 321 DRmldmGFEPQIRHIVEECDMPSVenrqtLMFSATF 356
Cdd:cd17926 120 HH----LPAKTFSEILKELNAKYR-----LGLTATP 146
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
441-481 |
9.54e-04 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 42.06 E-value: 9.54e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 768886153 441 IHGDRTQAERERALSAFKANVADILVATAVAARGLDIPNVT 481
Cdd:PRK10917 511 LHGRMKPAEKDAVMAAFKAGEIDILVATTVIEVGVDVPNAT 551
|
|
| PLN03142 |
PLN03142 |
Probable chromatin-remodeling complex ATPase chain; Provisional |
399-502 |
1.11e-03 |
|
Probable chromatin-remodeling complex ATPase chain; Provisional
Pssm-ID: 215601 [Multi-domain] Cd Length: 1033 Bit Score: 42.10 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 399 KSALLDLLSA---EHKGLTLIFVETKRMADQLTDFLIMQNFKATAIHGDRTQAERERALSAFKANVAD---ILVATAVAA 472
Cdd:PLN03142 472 KMVLLDKLLPklkERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEkfvFLLSTRAGG 551
|
90 100 110
....*....|....*....|....*....|....*...
gi 768886153 473 RGLDIPNVTHVINYDlpSD----ID----DYVHRIGRT 502
Cdd:PLN03142 552 LGINLATADIVILYD--SDwnpqVDlqaqDRAHRIGQK 587
|
|
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
400-481 |
1.23e-03 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 41.96 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 400 SALLDLLSAEhkgltlifvetkRMADQLTDFLimQNFKATAIHGDRTQAERERALSAFKANVADILVATAVAARGLDIPN 479
Cdd:COG1200 482 SEKLDLQAAE------------ETYEELREAF--PGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTVIEVGVDVPN 547
|
..
gi 768886153 480 VT 481
Cdd:COG1200 548 AT 549
|
|
| PRK05580 |
PRK05580 |
primosome assembly protein PriA; Validated |
451-509 |
1.24e-03 |
|
primosome assembly protein PriA; Validated
Pssm-ID: 235514 [Multi-domain] Cd Length: 679 Bit Score: 41.68 E-value: 1.24e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768886153 451 ERALSAFKANVADILVATAVAARGLDIPNVT--HVINYDLPSDIDDYvhR------------IGRTGRAGNTG 509
Cdd:PRK05580 470 EQLLAQFARGEADILIGTQMLAKGHDFPNVTlvGVLDADLGLFSPDF--RasertfqlltqvAGRAGRAEKPG 540
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
308-506 |
1.31e-03 |
|
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.
Pssm-ID: 273707 [Multi-domain] Cd Length: 359 Bit Score: 41.29 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 308 SLANIKY--LVLDEADrmldmGFEPQIRHIVEECDMPSVENRQTLM-FSATFPVDIQHLARDfLDNYIFLS--VGRVGST 382
Cdd:TIGR01587 119 TLASIANslLIFDEVH-----FYDEYTLALILAVLEVLKDNDVPILlMSATLPKFLKEYAEK-IGYVEFNEplDLKEERR 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 383 SENitQRI-LYVDDMDKKSALLDLLSAEHK--GLTLIFVETKRMADQLTDFL--IMQNFKATAIHG-----DRTQAERER 452
Cdd:TIGR01587 193 FEN--HRFiLIESDKVGEISSLERLLEFIKkgGSIAIIVNTVDRAQEFYQQLkeKAPEEEIILYHSrftekDRAKKEAEL 270
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 768886153 453 ALSAFKANVADILVATAVAARGLDipnvthvINYDL----PSDIDDYVHRIGRTGRAG 506
Cdd:TIGR01587 271 LREMKKSNEKFVIVATQVIEASLD-------ISADVmiteLAPIDSLIQRLGRLHRYG 321
|
|
| SF2_C_priA |
cd18804 |
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ... |
445-509 |
1.41e-03 |
|
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350191 [Multi-domain] Cd Length: 238 Bit Score: 40.69 E-value: 1.41e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768886153 445 RTQAERERALSAFKANVADILVATAVAARGLDIPNVTHV--INYDLPSDIDDY---------VHRI-GRTGRAGNTG 509
Cdd:cd18804 128 RKKGALEKLLDQFERGEIDILIGTQMIAKGLDFPNVTLVgiLNADSGLNSPDFraserafqlLTQVsGRAGRGDKPG 204
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
437-506 |
2.53e-03 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 41.03 E-value: 2.53e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 437 KATAIHGDRTQAERERALSAFKANVADILVATAVAARGLDIPNVTHVINYDLPSDIDDYVHRIGRTGRAG 506
Cdd:PLN03137 706 KAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGRAGRDG 775
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
176-323 |
4.31e-03 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 38.55 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 176 KPTPVQKYSIPIVTKG------RDLMACAQTGSGKTGGFLFPlftelfrsgpspvpekaqSFYSRKGYPSALVLAPTREL 249
Cdd:cd17918 15 SLTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGA------------------ALLAYKNGKQVAILVPTEIL 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768886153 250 ATQIFEEARKFTyrSWVRPCVVYGGapignQMREVDRGCDLLVATpgrlNDLLERgKVSLANIKYLVLDEADRM 323
Cdd:cd17918 77 AHQHYEEARKFL--PFINVELVTGG-----TKAQILSGISLLVGT----HALLHL-DVKFKNLDLVIVDEQHRF 138
|
|
| PriA |
COG1198 |
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, ... |
451-481 |
4.81e-03 |
|
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440811 [Multi-domain] Cd Length: 728 Bit Score: 40.10 E-value: 4.81e-03
10 20 30
....*....|....*....|....*....|.
gi 768886153 451 ERALSAFKANVADILVATAVAARGLDIPNVT 481
Cdd:COG1198 521 EKLLEAFARGEADILVGTQMLAKGHDFPNVT 551
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
200-357 |
5.02e-03 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 38.04 E-value: 5.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 200 TGSGKTGGFLFpLFTELFRSGPspvpekaqsfysrkgYPSALVLAPTRELATQIFEEARKFTYRSWVRPCVVYGgapiGN 279
Cdd:pfam04851 32 TGSGKTLTAAK-LIARLFKKGP---------------IKKVLFLVPRKDLLEQALEEFKKFLPNYVEIGEIISG----DK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 280 QMREVDrGCDLLVATPGRLNDLLERGKVSLA--NIKYLVLDEADRmldmGFEPQIRHIVEecdmpSVENRQTLMFSATFP 357
Cdd:pfam04851 92 KDESVD-DNKIVVTTIQSLYKALELASLELLpdFFDVIIIDEAHR----SGASSYRNILE-----YFKPAFLLGLTATPE 161
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
356-509 |
6.69e-03 |
|
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family members 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: 350178 [Multi-domain] Cd Length: 171 Bit Score: 37.90 E-value: 6.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 356 FPVDIQhlardFLDNYIFLSVGRVGSTSENITQRILyvddmdkkSALLDLLSAEHKGLTLIFV----ETKRMADQLTDFL 431
Cdd:cd18791 1 FPVEVY-----YLEDILELLGISSEKEDPDYVDAAV--------RLILQIHRTEEPGDILVFLpgqeEIERLCELLREEL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768886153 432 IMQNFKATAI---HGDRTQAERERALSAFKANVADILVATAVAARGLDIPNVTHVI--------NYDlpsdiddyvHRIG 500
Cdd:cd18791 68 LSPDLGKLLVlplHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVYVIdsglvkekVYD---------PRTG 138
|
170 180
....*....|....*....|....*
gi 768886153 501 ----------------RTGRAGNTG 509
Cdd:cd18791 139 lsslvtvwiskasaeqRAGRAGRTR 163
|
|
| |
