|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
45-462 |
8.45e-162 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 464.62 E-value: 8.45e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 45 SFAELGVSQPLCDACQRLGWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSLLD----HPQAffcLVLTP 120
Cdd:COG0513 3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPsrprAPQA---LILAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 121 TRELAFQIGQQFEALGSGIGLIAAVIVGGVDMAAQAMALARRPHIIVATPGRLVDHLENtKGFNLKALKFLIMDEADRIL 200
Cdd:COG0513 80 TRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIER-GALDLSGVETLVLDEADRML 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 201 NMDFEVELDKILKVIPRERRTYLFSATMTKKVSKLERASLRDPARVSVSSRYKTVDNLKQHYIFVPNKYKETYLVYLLNE 280
Cdd:COG0513 159 DMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 281 HAGNSAIVFCATCATTMQIAVMLRQLGMQAVPLHGQMSQEKRLGSLNKFKSKAREILVCTDVAARGLDIPHVDMVINYDM 360
Cdd:COG0513 239 EDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 361 PSQSKDYVHRVGRTARAGRSGIAITVVTQYDVEAYQKIEANLGKKLDEYKCVENEvmvlvERTQEATENARIEMKEMDEK 440
Cdd:COG0513 319 PEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFE-----PVEEKRLERLKPKIKEKLKG 393
|
410 420
....*....|....*....|..
gi 17555296 441 KKSGKKRRQNDDFGDTEESGGR 462
Cdd:COG0513 394 KKAGRGGRPGPKGERKARRGKR 415
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
45-247 |
1.63e-148 |
|
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: 422.11 E-value: 1.63e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 45 SFAELGVSQPLCDACQRLGWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSLLDHPQAFFCLVLTPTREL 124
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 125 AFQIGQQFEALGSGIGLIAAVIVGGVDMAAQAMALARRPHIIVATPGRLVDHLENTKGFNLKALKFLIMDEADRILNMDF 204
Cdd:cd17954 81 AQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKGFSLKSLKFLVMDEADRLLNMDF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17555296 205 EVELDKILKVIPRERRTYLFSATMTKKVSKLERASLRDPARVS 247
Cdd:cd17954 161 EPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKIE 203
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
44-407 |
2.68e-104 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 319.05 E-value: 2.68e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 44 KSFAELGVSQPLCDACQRLGW--MKPskIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSLldHPQAFFC--LVLT 119
Cdd:PRK11776 4 TAFSTLPLPPALLANLNELGYteMTP--IQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL--DVKRFRVqaLVLC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 120 PTRELAFQIGQQFEALGSGIGLIAAV-IVGGVDMAAQAMALARRPHIIVATPGRLVDHLEntKG-FNLKALKFLIMDEAD 197
Cdd:PRK11776 80 PTRELADQVAKEIRRLARFIPNIKVLtLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLR--KGtLDLDALNTLVLDEAD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 198 RILNMDFEVELDKILKVIPRERRTYLFSATMTKKVSKLERASLRDPARVSVSSRYKTvDNLKQHYIFVPNKYKETYLVYL 277
Cdd:PRK11776 158 RMLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDL-PAIEQRFYEVSPDERLPALQRL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 278 LNEHAGNSAIVFCATCATTMQIAVMLRQLGMQAVPLHGQMSQEKRLGSLNKFKSKAREILVCTDVAARGLDIPHVDMVIN 357
Cdd:PRK11776 237 LLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVIN 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 17555296 358 YDMPSQSKDYVHRVGRTARAGRSGIAITVVTQYDVEAYQKIEANLGKKLD 407
Cdd:PRK11776 317 YELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLN 366
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
46-451 |
9.41e-96 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 296.08 E-value: 9.41e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 46 FAELGVSQPLCDACQRLGWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSLLDHPQAF----FCLVLTPT 121
Cdd:PRK11192 3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRKsgppRILILTPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 122 RELAFQIGQQFEALGSGIGLIAAVIVGGVDMAAQAMALARRPHIIVATPGRLVDHLENTKgFNLKALKFLIMDEADRILN 201
Cdd:PRK11192 83 RELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEEN-FDCRAVETLILDEADRMLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 202 MDFEVELDKILKVIPRERRTYLFSATMT-KKVSKLERASLRDPARVSV-SSR---------YKTVDNLKqhyifvpnkYK 270
Cdd:PRK11192 162 MGFAQDIETIAAETRWRKQTLLFSATLEgDAVQDFAERLLNDPVEVEAePSRrerkkihqwYYRADDLE---------HK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 271 ETYLVYLLNEHAGNSAIVFCATCATTMQIAVMLRQLGMQAVPLHGQMSQEKRLGSLNKFKSKAREILVCTDVAARGLDIP 350
Cdd:PRK11192 233 TALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDID 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 351 HVDMVINYDMPSQSKDYVHRVGRTARAGRSGIAITVVTQYDVEAYQKIEANLGKKL-----DEYKCVENEVMVLVERTQE 425
Cdd:PRK11192 313 DVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLkarviDELRPKTKAPSEKKTGKPS 392
|
410 420
....*....|....*....|....*.
gi 17555296 426 ATENARIEMKEMDEKKKSGKKRRQND 451
Cdd:PRK11192 393 KKVLAKRAEKKEKEKEKPKVKKRHRD 418
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
46-243 |
1.00e-92 |
|
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: 280.26 E-value: 1.00e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 46 FAELGVSQPLCDACQRLGWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSLLDHPQAFFCLVLTPTRELA 125
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 126 FQIGQQFEALGSGIGLIAAVIVGGVDMAAQAMALARRPHIIVATPGRLVDHLENTKG--FNLKALKFLIMDEADRILNMD 203
Cdd:cd17955 81 YQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDttKVLSRVKFLVLDEADRLLTGS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17555296 204 FEVELDKILKVIPRERRTYLFSATMTKKVSKLERASLRDP 243
Cdd:cd17955 161 FEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
45-454 |
4.24e-88 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 280.12 E-value: 4.24e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 45 SFAELGVSQPLCDACQRLGWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVL-----QSLLDHPQAFFCLVLT 119
Cdd:PTZ00110 131 SFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIvhinaQPLLRYGDGPIVLVLA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 120 PTRELAFQIGQQFEALGSGIGLIAAVIVGGVDMAAQAMALARRPHIIVATPGRLVDHLENTKGfNLKALKFLIMDEADRI 199
Cdd:PTZ00110 211 PTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVT-NLRRVTYLVLDEADRM 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 200 LNMDFEVELDKILKVIPRERRTYLFSATMTKKVSKLERASLRD-PARVSVSS-RYKTVDNLKQhYIFVPNKY-KETYLVY 276
Cdd:PTZ00110 290 LDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSlDLTACHNIKQ-EVFVVEEHeKRGKLKM 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 277 LLNE--HAGNSAIVFCATCATTMQIAVMLRQLGMQAVPLHGQMSQEKRLGSLNKFKSKAREILVCTDVAARGLDIPHVDM 354
Cdd:PTZ00110 369 LLQRimRDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKY 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 355 VINYDMPSQSKDYVHRVGRTARAGRSGIAITVVTQydveayqkieanlgkklDEYKCVENEVMVLVERTQEATEnariEM 434
Cdd:PTZ00110 449 VINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTP-----------------DKYRLARDLVKVLREAKQPVPP----EL 507
|
410 420
....*....|....*....|
gi 17555296 435 KEMDEKKKSGKKRRQNDDFG 454
Cdd:PTZ00110 508 EKLSNERSNGTERRRWGGYG 527
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
43-399 |
6.82e-88 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 281.74 E-value: 6.82e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 43 EKSFAELGVSQPLCDACQRLGWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSL---LDHPQAffcLVLT 119
Cdd:PRK11634 5 ETTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLdpeLKAPQI---LVLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 120 PTRELAFQIGQ---QFEALGSGIGLIAavIVGGVDMAAQAMALARRPHIIVATPGRLVDHLENTKgFNLKALKFLIMDEA 196
Cdd:PRK11634 82 PTRELAVQVAEamtDFSKHMRGVNVVA--LYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGT-LDLSKLSGLVLDEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 197 DRILNMDFEVELDKILKVIPRERRTYLFSATMTKKVSKLERASLRDPARVSVSSRYKTVDNLKQHYIFVPNKYKETYLVY 276
Cdd:PRK11634 159 DEMLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 277 LLNEHAGNSAIVFCATCATTMQIAVMLRQLGMQAVPLHGQMSQEKRLGSLNKFKSKAREILVCTDVAARGLDIPHVDMVI 356
Cdd:PRK11634 239 FLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVV 318
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 17555296 357 NYDMPSQSKDYVHRVGRTARAGRSGIAITVVTQYDVEAYQKIE 399
Cdd:PRK11634 319 NYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIE 361
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
55-247 |
3.99e-85 |
|
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: 260.45 E-value: 3.99e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 55 LCDACQRLGWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSLLDHPQAFF----CLVLTPTRELAFQIGQ 130
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGrgpqALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 131 QFEALGSGIGLIAAVIVGGVDMAAQAMALARRPHIIVATPGRLVDHLENTKgFNLKALKFLIMDEADRILNMDFEVELDK 210
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGK-LDLSNVKYLVLDEADRMLDMGFEEDVEK 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 17555296 211 ILKVIPRERRTYLFSATMTKKVSKLERASLRDPARVS 247
Cdd:cd00268 160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
45-387 |
4.34e-78 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 251.27 E-value: 4.34e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 45 SFAELGVSQPLCDACQRLGWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSLLDHPQA------FFCLVL 118
Cdd:PRK10590 2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHakgrrpVRALIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 119 TPTRELAFQIGQQFEALGSGIGLIAAVIVGGVDMAAQAMALARRPHIIVATPGRLVDhLENTKGFNLKALKFLIMDEADR 198
Cdd:PRK10590 82 TPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLD-LEHQNAVKLDQVEILVLDEADR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 199 ILNMDFEVELDKILKVIPRERRTYLFSATMTKKVSKLERASLRDPARVSVSSRYKTVDNLKQHYIFVPNKYKETYLVYLL 278
Cdd:PRK10590 161 MLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 279 NEHAGNSAIVFCATCATTMQIAVMLRQLGMQAVPLHGQMSQEKRLGSLNKFKSKAREILVCTDVAARGLDIPHVDMVINY 358
Cdd:PRK10590 241 GKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNY 320
|
330 340
....*....|....*....|....*....
gi 17555296 359 DMPSQSKDYVHRVGRTARAGRSGIAITVV 387
Cdd:PRK10590 321 ELPNVPEDYVHRIGRTGRAAATGEALSLV 349
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
46-407 |
9.39e-76 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 245.59 E-value: 9.39e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 46 FAELGVSQPLCDACQRLGWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSLLDHP---QAFF----CLVL 118
Cdd:PRK01297 89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPppkERYMgeprALII 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 119 TPTRELAFQIGQQFEALGSGIGLIAAVIVGGVDMAAQAMAL-ARRPHIIVATPGRLVDHLENtKGFNLKALKFLIMDEAD 197
Cdd:PRK01297 169 APTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLeARFCDILVATPGRLLDFNQR-GEVHLDMVEVMVLDEAD 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 198 RILNMDFEVELDKILKVIPR--ERRTYLFSATMTKKVSKLERASLRDPARVSVSSRYKTVDNLKQHYIFVPNKYKETYLV 275
Cdd:PRK01297 248 RMLDMGFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDKYKLLY 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 276 YLLNEHAGNSAIVFCATCATTMQIAVMLRQLGMQAVPLHGQMSQEKRLGSLNKFKSKAREILVCTDVAARGLDIPHVDMV 355
Cdd:PRK01297 328 NLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHV 407
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 17555296 356 INYDMPSQSKDYVHRVGRTARAGRSGIAITVVTQYDVEAYQKIEANLGKKLD 407
Cdd:PRK01297 408 INFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKIS 459
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
45-398 |
5.49e-74 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 243.70 E-value: 5.49e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 45 SFAELGVSQPLCDACQRLGWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSLLDHP-------QAFFCLV 117
Cdd:PRK04537 10 TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPaladrkpEDPRALI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 118 LTPTRELAFQIGQQFEALGSGIGLIAAVIVGGVDMAAQAMALARRPHIIVATPGRLVDHLENTKGFNLKALKFLIMDEAD 197
Cdd:PRK04537 90 LAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVVSLHACEICVLDEAD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 198 RILNMDFEVELDKILKVIPRE--RRTYLFSATMTKKVSKLERASLRDPARVSVSSRYKTVDNLKQHYIFVPNKYKETYLV 275
Cdd:PRK04537 170 RMFDLGFIKDIRFLLRRMPERgtRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADEEKQTLLL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 276 YLLNEHAGNSAIVFCATCATTMQIAVMLRQLGMQAVPLHGQMSQEKRLGSLNKFKSKAREILVCTDVAARGLDIPHVDMV 355
Cdd:PRK04537 250 GLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYV 329
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 17555296 356 INYDMPSQSKDYVHRVGRTARAGRSGIAITVVTQY------DVEAY--QKI 398
Cdd:PRK04537 330 YNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERyamslpDIEAYieQKI 380
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
58-247 |
8.24e-71 |
|
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: 223.67 E-value: 8.24e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 58 ACQRLGWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSLLDHPQAFF---CLVLTPTRELAFQIGQQFEA 134
Cdd:cd17947 4 ALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAatrVLVLVPTRELAMQCFSVLQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 135 LGSGIGLIAAVIVGGVDMAAQAMALARRPHIIVATPGRLVDHLENTKGFNLKALKFLIMDEADRILNMDFEVELDKILKV 214
Cdd:cd17947 84 LAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSFDLDSIEILVLDEADRMLEEGFADELKEILRL 163
|
170 180 190
....*....|....*....|....*....|...
gi 17555296 215 IPRERRTYLFSATMTKKVSKLERASLRDPARVS 247
Cdd:cd17947 164 CPRTRQTMLFSATMTDEVKDLAKLSLNKPVRVF 196
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
45-408 |
3.02e-67 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 221.24 E-value: 3.02e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 45 SFAELGVSQPLCDACQRLGWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSLLDHPQAFFCLVLTPTREL 124
Cdd:PTZ00424 29 SFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTREL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 125 AFQIGQQFEALGSGIGLIAAVIVGGVDMAAQAMALARRPHIIVATPGRLVDHLENtKGFNLKALKFLIMDEADRILNMDF 204
Cdd:PTZ00424 109 AQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDK-RHLRVDDLKLFILDEADEMLSRGF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 205 EVELDKILKVIPRERRTYLFSATMTKKVSKLERASLRDPARVSVSSRYKTVDNLKQHYIFV-PNKYKETYLVYLLNEHAG 283
Cdd:PTZ00424 188 KGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVeKEEWKFDTLCDLYETLTI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 284 NSAIVFCATCATTMQIAVMLRQLGMQAVPLHGQMSQEKRLGSLNKFKSKAREILVCTDVAARGLDIPHVDMVINYDMPSQ 363
Cdd:PTZ00424 268 TQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPAS 347
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 17555296 364 SKDYVHRVGRTARAGRSGIAITVVTQYDVEAYQKIEANLGKKLDE 408
Cdd:PTZ00424 348 PENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEE 392
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
43-394 |
9.96e-67 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 220.61 E-value: 9.96e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 43 EKSFAELGVSQPLCDACQRLGWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSLLDHPQAFF-------C 115
Cdd:PRK04837 7 EQKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDrkvnqprA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 116 LVLTPTRELAFQIGQQFEALGSGIGLIAAVIVGGVDMAAQAMALARRPHIIVATPGRLVDHLENtKGFNLKALKFLIMDE 195
Cdd:PRK04837 87 LIMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQ-NHINLGAIQVVVLDE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 196 ADRILNMDFEVELDKILKVIP--RERRTYLFSATMTKKVSKLERASLRDPARVSVSSRYKTVDNLKQHyIFVP-NKYKET 272
Cdd:PRK04837 166 ADRMFDLGFIKDIRWLFRRMPpaNQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEE-LFYPsNEEKMR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 273 YLVYLLNEHAGNSAIVFCATCATTMQIAVMLRQLGMQAVPLHGQMSQEKRLGSLNKFKSKAREILVCTDVAARGLDIPHV 352
Cdd:PRK04837 245 LLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAV 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17555296 353 DMVINYDMPSQSKDYVHRVGRTARAGRSGIAITV---------------------VTQYDVEA 394
Cdd:PRK04837 325 THVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLaceeyalnlpaietyighsipVSKYDSDA 387
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
63-248 |
2.36e-61 |
|
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: 199.05 E-value: 2.36e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 63 GWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSL-------LDhpqAFFCLVLTPTRELAFQIGQQFEAL 135
Cdd:cd17941 9 GFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLyrerwtpED---GLGALIISPTRELAMQIFEVLRKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 136 GSGIGLIAAVIVGGVDMAAQAMALARRpHIIVATPGRLVDHLENTKGFNLKALKFLIMDEADRILNMDFEVELDKILKVI 215
Cdd:cd17941 86 GKYHSFSAGLIIGGKDVKEEKERINRM-NILVCTPGRLLQHMDETPGFDTSNLQMLVLDEADRILDMGFKETLDAIVENL 164
|
170 180 190
....*....|....*....|....*....|...
gi 17555296 216 PRERRTYLFSATMTKKVSKLERASLRDPARVSV 248
Cdd:cd17941 165 PKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
68-235 |
1.35e-60 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 195.92 E-value: 1.35e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 68 SKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSLLDHPQAFFCLVLTPTRELAFQIGQQFEALGSGIGLIAAVIV 147
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 148 GGVDMAAQAMALaRRPHIIVATPGRLVDHLENTKgfNLKALKFLIMDEADRILNMDFEVELDKILKVIPRERRTYLFSAT 227
Cdd:pfam00270 81 GGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK--LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSAT 157
|
....*...
gi 17555296 228 MTKKVSKL 235
Cdd:pfam00270 158 LPRNLEDL 165
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
258-387 |
5.60e-60 |
|
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: 193.11 E-value: 5.60e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 258 LKQHYIFVPNKYKETYL-VYLLNEHAGNSAIVFCATCATTMQIAVMLRQLGMQAVPLHGQMSQEKRLGSLNKFKSKAREI 336
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 17555296 337 LVCTDVAARGLDIPHVDMVINYDMPSQSKDYVHRVGRTARAGRSGIAITVV 387
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
45-246 |
5.47e-58 |
|
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: 190.59 E-value: 5.47e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 45 SFAELGVSQPLCDACQRLGWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSLLDHPQAF--FCLVLTPTR 122
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVgaRALILSPTR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 123 ELAFQIGQQFEALGSGIGLIAAVIVGGVDMAAQAMALARRPHIIVATPGRLVDHLENTkGFNLKALKFLIMDEADRILNM 202
Cdd:cd17959 82 ELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEM-NLKLSSVEYVVFDEADRLFEM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 17555296 203 DFEVELDKILKVIPRERRTYLFSATMTKKVSKLERASLRDPARV 246
Cdd:cd17959 161 GFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
55-247 |
9.52e-58 |
|
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: 190.61 E-value: 9.52e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 55 LCDACQRLGWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSLL-----------DHPQAffcLVLTPTRE 123
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISrlppldeetkdDGPYA---LILAPTRE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 124 LAFQIGQQFEALGSGIGLIAAVIVGGVDMAAQAMALARRPHIIVATPGRLVDHLENtKGFNLKALKFLIMDEADRILNMD 203
Cdd:cd17945 78 LAQQIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLER-RLLVLNQCTYVVLDEADRMIDMG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17555296 204 FEVELDKILKVIP--------------------RERRTYLFSATMTKKVSKLERASLRDPARVS 247
Cdd:cd17945 157 FEPQVTKILDAMPvsnkkpdteeaeklaasgkhRYRQTMMFTATMPPAVEKIAKGYLRRPVVVT 220
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
51-241 |
2.45e-54 |
|
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350722 [Multi-domain] Cd Length: 211 Bit Score: 181.24 E-value: 2.45e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 51 VSQPLCDACQRLGWMKPSKIQQAALPHALQ-GKDVIGLAETGSGKTGAFAIPVLQSLLDHPQAF-----FCLVLTPTREL 124
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGrrsgvSALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 125 AFQIGQQFEALGSGI-GLIAAVIVGGVDMAAQAMALAR-RPHIIVATPGRLVDHLENTKGFN-LKALKFLIMDEADRILN 201
Cdd:cd17964 81 ALQIAAEAKKLLQGLrKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLENPGVAKaFTDLDYLVLDEADRLLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 17555296 202 MDFEVELDKILKVIP----RERRTYLFSATMTKKVSKLERASLR 241
Cdd:cd17964 161 MGFRPDLEQILRHLPeknaDPRQTLLFSATVPDEVQQIARLTLK 204
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
61-247 |
3.02e-54 |
|
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: 180.64 E-value: 3.02e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 61 RLGWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVL-----QSLLDHPQAFFCLVLTPTRELAFQIGQQFEAL 135
Cdd:cd17966 7 RQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIvhinaQPPLERGDGPIVLVLAPTRELAQQIQQEANKF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 136 GSGIGLIAAVIVGGVDMAAQAMALARRPHIIVATPGRLVDHLENTKGfNLKALKFLIMDEADRILNMDFEVELDKILKVI 215
Cdd:cd17966 87 GGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKT-NLRRVTYLVLDEADRMLDMGFEPQIRKIVDQI 165
|
170 180 190
....*....|....*....|....*....|..
gi 17555296 216 PRERRTYLFSATMTKKVSKLERASLRDPARVS 247
Cdd:cd17966 166 RPDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
58-244 |
6.58e-54 |
|
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: 180.09 E-value: 6.58e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 58 ACQRLGWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSLLDH------PQAFFCLVLTPTRELAFQIGQQ 131
Cdd:cd17961 8 AIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAkaesgeEQGTRALILVPTRELAQQVSKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 132 FEALGSGIG-LIAAV-IVGGVDMAAQAMALARRPHIIVATPGRLVDHLENTKGFNLKALKFLIMDEADRILNMDFEVELD 209
Cdd:cd17961 88 LEQLTAYCRkDVRVVnLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLLSTLKYLVIDEADLVLSYGYEEDLK 167
|
170 180 190
....*....|....*....|....*....|....*
gi 17555296 210 KILKVIPRERRTYLFSATMTKKVSKLERASLRDPA 244
Cdd:cd17961 168 SLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
58-230 |
1.19e-53 |
|
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: 180.13 E-value: 1.19e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 58 ACQRLGWMKPSKIQQAALPHAL-QGKDVIGLAETGSGKTGAFAIPVLQSLLDHPQ---------AFFCLVLTPTRELAFQ 127
Cdd:cd17946 4 ALADLGFSEPTPIQALALPAAIrDGKDVIGAAETGSGKTLAFGIPILERLLSQKSsngvggkqkPLRALILTPTRELAVQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 128 IGQQFEALGSGIGLIAAVIVGGVDMAAQAMALARRPHIIVATPGRLVDHLENTKGF--NLKALKFLIMDEADRIL-NMDF 204
Cdd:cd17946 84 VKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHlaNLKSLRFLVLDEADRMLeKGHF 163
|
170 180 190
....*....|....*....|....*....|...
gi 17555296 205 EvELDKILKVIPRE-------RRTYLFSATMTK 230
Cdd:cd17946 164 A-ELEKILELLNKDragkkrkRQTFVFSATLTL 195
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
58-243 |
2.06e-53 |
|
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: 178.32 E-value: 2.06e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 58 ACQRLGWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSLldHPQAFF------CLVLTPTRELAFQIgqq 131
Cdd:cd17942 4 AIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELL--YKLKFKprngtgVIIISPTRELALQI--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 132 feaLGSGIGLIA------AVIVGGVDMAAQAMALARRPHIIVATPGRLVDHLENTKGFNLKALKFLIMDEADRILNMDFE 205
Cdd:cd17942 79 ---YGVAKELLKyhsqtfGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKNLQCLIIDEADRILEIGFE 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 17555296 206 VELDKILKVIPRERRTYLFSATMTKKVSKLERASLRDP 243
Cdd:cd17942 156 EEMRQIIKLLPKRRQTMLFSATQTRKVEDLARISLKKK 193
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
45-242 |
3.80e-53 |
|
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: 178.45 E-value: 3.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 45 SFAELGVSQPLCDACQRLGWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSLLDHPQAF----------F 114
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSvgrgrrkaypS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 115 CLVLTPTRELAFQI---GQQFeALGSGIGliAAVIVGGVDMAAQAMALARRPHIIVATPGRLVDHLENTKgFNLKALKFL 191
Cdd:cd17967 81 ALILAPTRELAIQIyeeARKF-SYRSGVR--SVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGR-ISLSSIKFL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17555296 192 IMDEADRILNMDFEVELDKILK----VIPRERRTYLFSATMTKKVSKLERASLRD 242
Cdd:cd17967 157 VLDEADRMLDMGFEPQIRKIVEhpdmPPKGERQTLMFSATFPREIQRLAADFLKN 211
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
60-247 |
7.20e-53 |
|
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: 177.39 E-value: 7.20e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 60 QRLGWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSLLDHPQAF------FCLVLTPTRELAFQIGQQFE 133
Cdd:cd17949 7 SKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVdrsdgtLALVLVPTRELALQIYEVLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 134 ALGSG-IGLIAAVIVGGVDMAAQAMALARRPHIIVATPGRLVDHLENTKGFNLKALKFLIMDEADRILNMDFEVELDKIL 212
Cdd:cd17949 87 KLLKPfHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQSFDVSNLRWLVLDEADRLLDMGFEKDITKIL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 17555296 213 KVI-------------PRERRTYLFSATMTKKVSKLERASLRDPARVS 247
Cdd:cd17949 167 ELLddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
57-247 |
2.32e-52 |
|
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: 175.84 E-value: 2.32e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 57 DACQRLGWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSLLDH-----PQAFFCLVLTPTRELAFQIgqq 131
Cdd:cd17960 3 DVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRkanlkKGQVGALIISPTRELATQI--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 132 FEALGS-----GIGLIAAVIVGGVDMAAQ-AMALARRPHIIVATPGRLVDHLENTKG-FNLKALKFLIMDEADRILNMDF 204
Cdd:cd17960 80 YEVLQSflehhLPKLKCQLLIGGTNVEEDvKKFKRNGPNILVGTPGRLEELLSRKADkVKVKSLEVLVLDEADRLLDLGF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17555296 205 EVELDKILKVIPRERRTYLFSATMTKKVSKLERASLRDPARVS 247
Cdd:cd17960 160 EADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRVV 202
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
44-243 |
4.77e-51 |
|
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: 172.95 E-value: 4.77e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 44 KSFAELGVSQPLCDACQRLGWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSLLDHP-----QAFFCLVL 118
Cdd:cd17953 12 QKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRpvkpgEGPIGLIM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 119 TPTRELAFQIGQQFEALGSGIGLIAAVIVGGVDMAAQAMALARRPHIIVATPGRLVDHL--ENTKGFNLKALKFLIMDEA 196
Cdd:cd17953 92 APTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtaNNGRVTNLRRVTYVVLDEA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17555296 197 DRILNMDFEVELDKILKVIPRERRTYLFSATMTKKVSKLERASLRDP 243
Cdd:cd17953 172 DRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKP 218
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
61-261 |
4.01e-50 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 169.98 E-value: 4.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 61 RLGWMKPSKIQQAALPHALQG-KDVIGLAETGSGKTGAFAIPVLQSLLDHPqAFFCLVLTPTRELAFQIGQQFEALGSGI 139
Cdd:smart00487 3 KFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGK-GGRVLVLVPTRELAEQWAEELKKLGPSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 140 GLIAAVIVGGVDMAAQAMALAR-RPHIIVATPGRLVDHLENtKGFNLKALKFLIMDEADRILNMDFEVELDKILKVIPRE 218
Cdd:smart00487 82 GLKVVGLYGGDSKREQLRKLESgKTDILVTTPGRLLDLLEN-DKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPKN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17555296 219 RRTYLFSATMTKKVSKLERASLRDPARVSVSSRykTVDNLKQH 261
Cdd:smart00487 161 VQLLLLSATPPEEIENLLELFLNDPVFIDVGFT--PLEPIEQF 201
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
45-391 |
1.69e-49 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 177.29 E-value: 1.69e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 45 SFAELGVSQPLCDACQRLGWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSL----LDHP---QAFFCLV 117
Cdd:PLN00206 122 SFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCctirSGHPseqRNPLAMV 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 118 LTPTRELAFQIGQQFEALGSGIGLIAAVIVGGVDMAAQAMALARRPHIIVATPGRLVDHLeNTKGFNLKALKFLIMDEAD 197
Cdd:PLN00206 202 LTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLL-SKHDIELDNVSVLVLDEVD 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 198 RILNMDFEVELDKILKVIPRERrTYLFSATMTKKVSKLERASLRDPARVSVSSRYKTVDNLKQHYIFVPNKYKETYLVYL 277
Cdd:PLN00206 281 CMLERGFRDQVMQIFQALSQPQ-VLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQKLFDI 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 278 L--NEHAGNSAIVFCATCATTMQIAVMLRQL-GMQAVPLHGQMSQEKRLGSLNKFKSKAREILVCTDVAARGLDIPHVDM 354
Cdd:PLN00206 360 LksKQHFKPPAVVFVSSRLGADLLANAITVVtGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQ 439
|
330 340 350
....*....|....*....|....*....|....*..
gi 17555296 355 VINYDMPSQSKDYVHRVGRTARAGRSGIAITVVTQYD 391
Cdd:PLN00206 440 VIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEED 476
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
55-243 |
3.32e-47 |
|
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: 163.19 E-value: 3.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 55 LCDACQRLGWMKPSKIQQAALPHALQG---------KDVIGLAETGSGKTGAFAIPVLQSLLD--HPQaFFCLVLTPTRE 123
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKrvVPR-LRALIVVPTKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 124 LAFQIGQQFEALGSGIGLIAAVIVGGVDMAAQAMALAR--------RPHIIVATPGRLVDHLENTKGFNLKALKFLIMDE 195
Cdd:cd17956 80 LVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVdtsgrylsRVDILVATPGRLVDHLNSTPGFTLKHLRFLVIDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17555296 196 ADRILNMDFEVELDKILKVIPRERRT--------------------YLFSATMTKKVSKLERASLRDP 243
Cdd:cd17956 160 ADRLLNQSFQDWLETVMKALGRPTAPdlgsfgdanllersvrplqkLLFSATLTRDPEKLSSLKLHRP 227
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
61-248 |
8.39e-47 |
|
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: 160.83 E-value: 8.39e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 61 RLGWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSLLDHPQA--FFCLVLTPTRELAFQIGQQFEALGSG 138
Cdd:cd17957 7 ESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKkgLRALILAPTRELASQIYRELLKLSKG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 139 IGLIAAVIVGG-VDMAAQAMALARRPHIIVATPGRLVDHLENTKgFNLKALKFLIMDEADRILNMDFEVELDKILKVI-- 215
Cdd:cd17957 87 TGLRIVLLSKSlEAKAKDGPKSITKYDILVSTPLRLVFLLKQGP-IDLSSVEYLVLDEADKLFEPGFREQTDEILAACtn 165
|
170 180 190
....*....|....*....|....*....|...
gi 17555296 216 PRERRTyLFSATMTKKVSKLERASLRDPARVSV 248
Cdd:cd17957 166 PNLQRS-LFSATIPSEVEELARSVMKDPIRIIV 197
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
55-247 |
1.25e-46 |
|
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: 160.66 E-value: 1.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 55 LCDACQRLGWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSLLDHPQ-----AFFCLVLTPTRELAFQIG 129
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRElekgeGPIAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 130 QQFEALGSGIGLIAAVIVGGVDMAAQAMALARRPHIIVATPGRLVDHLEnTKGFNLKALKFLIMDEADRILNMDFEVELD 209
Cdd:cd17952 81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVK-KKATNLQRVTYLVLDEADRMFDMGFEYQVR 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 17555296 210 KILKVIPRERRTYLFSATMTKKVSKLERASLRDPARVS 247
Cdd:cd17952 160 SIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRVV 197
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
46-243 |
3.03e-46 |
|
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: 159.77 E-value: 3.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 46 FAELGVSQPLCDACQRLGWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSL---LDHPQAffcLVLTPTR 122
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIdpkKDVIQA---LILVPTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 123 ELAFQIGQQFEALGSGIGLIAAVIVGGVDMAAQAMALARRPHIIVATPGRLVDhLENTKGFNLKALKFLIMDEADRILNM 202
Cdd:cd17940 78 ELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILD-LAKKGVADLSHCKTLVLDEADKLLSQ 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 17555296 203 DFEVELDKILKVIPRERRTYLFSATMTKKVSKLERASLRDP 243
Cdd:cd17940 157 DFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNP 197
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
48-246 |
2.07e-45 |
|
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: 157.49 E-value: 2.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 48 ELGVSQPLCDACQRLGWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSL---LDHPQAffcLVLTPTREL 124
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIdttVRETQA---LVLAPTREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 125 AFQIGQQFEALGSGIGLIAAVIVGGVDMAAQAMALARRPHIIVATPGRLVDHLeNTKGFNLKALKFLIMDEADRILNMDF 204
Cdd:cd17939 78 AQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDML-QRRSLRTDKIKMFVLDEADEMLSRGF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17555296 205 EVELDKILKVIPRERRTYLFSATMTKKVSKLERASLRDPARV 246
Cdd:cd17939 157 KDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
45-265 |
5.52e-45 |
|
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: 158.21 E-value: 5.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 45 SFAELGVSQPLCDACQRLGWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSLLDH---------PQAFFC 115
Cdd:cd18052 44 TFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEgltassfseVQEPQA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 116 LVLTPTRELAFQIGQQFEALGSGIGLIAAVIVGGVDMAAQAMALARRPHIIVATPGRLVDHLENTKgFNLKALKFLIMDE 195
Cdd:cd18052 124 LIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGK-ISLSKLKYLILDE 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17555296 196 ADRILNMDFEVELDKILKV--IPR--ERRTYLFSATMTKKVSKLERaslrdparvsvssryktvDNLKQHYIFV 265
Cdd:cd18052 203 ADRMLDMGFGPEIRKLVSEpgMPSkeDRQTLMFSATFPEEIQRLAA------------------EFLKEDYLFL 258
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
66-246 |
2.71e-42 |
|
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: 149.41 E-value: 2.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 66 KPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSLLD--------HPQAFFCLVLTPTRELAFQ----IGQQFE 133
Cdd:cd17951 12 KPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEqekklpfiKGEGPYGLIVCPSRELARQthevIEYYCK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 134 AL--GSGIGLIAAVIVGGVDMAAQAMALARRPHIIVATPGRLVDHLeNTKGFNLKALKFLIMDEADRILNMDFEVELDKI 211
Cdd:cd17951 92 ALqeGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDML-NKKKINLDICRYLCLDEADRMIDMGFEEDIRTI 170
|
170 180 190
....*....|....*....|....*....|....*
gi 17555296 212 LKVIPRERRTYLFSATMTKKVSKLERASLRDPARV 246
Cdd:cd17951 171 FSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
46-250 |
4.50e-42 |
|
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: 149.77 E-value: 4.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 46 FAELGVSQPLCDACQRLGWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVL-----QSLLDHPQAFFCLVLTP 120
Cdd:cd18049 26 FYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIvhinhQPFLERGDGPICLVLAP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 121 TRELAFQIGQQFEALGSGIGLIAAVIVGGVDMAAQAMALARRPHIIVATPGRLVDHLENTKGfNLKALKFLIMDEADRIL 200
Cdd:cd18049 106 TRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKT-NLRRCTYLVLDEADRML 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17555296 201 NMDFEVELDKILKVIPRERRTYLFSATMTKKVSKLERASLRDPARVSVSS 250
Cdd:cd18049 185 DMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGA 234
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
46-235 |
1.74e-41 |
|
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: 147.08 E-value: 1.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 46 FAELGVSQPLCDACQRLGWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSLLdhpqaffCLVLTPTRELA 125
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIVV-------ALILEPSRELA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 126 FQIGQQFEALGSGI---GLIAAVIVGGVDMAAQAMALARRPHIIVATPGRLVDHLENTKgFNLKALKFLIMDEADRILNM 202
Cdd:cd17938 74 EQTYNCIENFKKYLdnpKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGK-LDLSSVRFFVLDEADRLLSQ 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17555296 203 DFEVELDKILKVIP----RERR--TYLFSATM-TKKVSKL 235
Cdd:cd17938 153 GNLETINRIYNRIPkitsDGKRlqVIVCSATLhSFEVKKL 192
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
60-246 |
2.13e-39 |
|
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis antigen 13 or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 is also called cancer/testis antigen 26 or DEAD-Box Protein CAGE. Both DDX46 and DDX53 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350716 [Multi-domain] Cd Length: 197 Bit Score: 141.45 E-value: 2.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 60 QRLGWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSLLDHPQAF------FCLVLTPTRELAFQIGQQFE 133
Cdd:cd17958 6 KKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPReqrngpGVLVLTPTRELALQIEAECS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 134 ALgSGIGLIAAVIVGGVDMAAQAMALARRPHIIVATPGRLVDhLENTKGFNLKALKFLIMDEADRILNMDFEVELDKILK 213
Cdd:cd17958 86 KY-SYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLND-LQMNNVINLKSITYLVLDEADRMLDMGFEPQIRKILL 163
|
170 180 190
....*....|....*....|....*....|...
gi 17555296 214 VIPRERRTYLFSATMTKKVSKLERASLRDPARV 246
Cdd:cd17958 164 DIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
63-247 |
3.48e-39 |
|
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: 140.76 E-value: 3.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 63 GWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSLLDHPQAFFCLVLTPTRELAFQIGQQFEALGSGI-GL 141
Cdd:cd17962 9 GYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKELMKGLpPM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 142 IAAVIVGGVDMAAQAMALARRPHIIVATPGRLVDHLeNTKGFNLKALKFLIMDEADRILNMDFEVELDKILKVIPRERRT 221
Cdd:cd17962 89 KTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDIL-KQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILENISHDHQT 167
|
170 180
....*....|....*....|....*.
gi 17555296 222 YLFSATMTKKVSKLERASLRDPARVS 247
Cdd:cd17962 168 ILVSATIPRGIEQLAGQLLQNPVRIT 193
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
63-246 |
4.24e-39 |
|
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: 140.66 E-value: 4.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 63 GWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSL---LDHPQAffcLVLTPTRELAFQIGQQFEALGSGI 139
Cdd:cd18046 18 GFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIdtsLKATQA---LVLAPTRELAQQIQKVVMALGDYM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 140 GLIAAVIVGGVDMAAQAMALARRPHIIVATPGRLVDHLeNTKGFNLKALKFLIMDEADRILNMDFEVELDKILKVIPRER 219
Cdd:cd18046 95 GIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMI-NRRYLRTDYIKMFVLDEADEMLSRGFKDQIYDIFQKLPPDT 173
|
170 180
....*....|....*....|....*..
gi 17555296 220 RTYLFSATMTKKVSKLERASLRDPARV 246
Cdd:cd18046 174 QVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
45-248 |
4.74e-39 |
|
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: 142.84 E-value: 4.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 45 SFAELGVSQPLCDACQRLGWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVL-----QSLLDHPQAFFCLVLT 119
Cdd:cd18050 63 AFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIvhinhQPYLERGDGPICLVLA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 120 PTRELAFQIGQQFEALGSGIGLIAAVIVGGVDMAAQAMALARRPHIIVATPGRLVDHLENTKGfNLKALKFLIMDEADRI 199
Cdd:cd18050 143 PTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKT-NLRRCTYLVLDEADRM 221
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17555296 200 LNMDFEVELDKILKVIPRERRTYLFSATMTKKVSKLERASLRDPARVSV 248
Cdd:cd18050 222 LDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINI 270
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
64-242 |
3.29e-38 |
|
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: 139.79 E-value: 3.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 64 WMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSLLD-------------------HPQAffcLVLTPTREL 124
Cdd:cd18051 41 YTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEqgpgeslpsesgyygrrkqYPLA---LVLAPTREL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 125 AFQIGQQFEALGSGIGLIAAVIVGGVDMAAQAMALARRPHIIVATPGRLVDHLENTKgFNLKALKFLIMDEADRILNMDF 204
Cdd:cd18051 118 ASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGK-IGLDYCKYLVLDEADRMLDMGF 196
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17555296 205 EVELDKILK--VIPR--ERRTYLFSATMTKKVSKLERASLRD 242
Cdd:cd18051 197 EPQIRRIVEqdTMPPtgERQTLMFSATFPKEIQMLARDFLDN 238
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
63-248 |
1.70e-37 |
|
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: 136.71 E-value: 1.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 63 GWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSLLDHPQAFFCLVLTPTRELAFQIGQQFEALGSGI-GL 141
Cdd:cd17950 21 GFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRELAFQISNEYERFSKYMpNV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 142 IAAVIVGGVDMAAQAMALARR-PHIIVATPGRLVDHLENtKGFNLKALKFLIMDEADRIL-NMDFEVELDKILKVIPRER 219
Cdd:cd17950 101 KTAVFFGGVPIKKDIEVLKNKcPHIVVGTPGRILALVRE-KKLKLSHVKHFVLDECDKMLeQLDMRRDVQEIFRATPHDK 179
|
170 180
....*....|....*....|....*....
gi 17555296 220 RTYLFSATMTKKVSKLERASLRDPARVSV 248
Cdd:cd17950 180 QVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
270-378 |
6.58e-35 |
|
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: 126.17 E-value: 6.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 270 KETYLVYLLNEHAGNSAIVFCATCATtMQIAVMLRQLGMQAVPLHGQMSQEKRLGSLNKFKSKAREILVCTDVAARGLDI 349
Cdd:pfam00271 2 KLEALLELLKKERGGKVLIFSQTKKT-LEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDL 80
|
90 100
....*....|....*....|....*....
gi 17555296 350 PHVDMVINYDMPSQSKDYVHRVGRTARAG 378
Cdd:pfam00271 81 PDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
57-247 |
2.56e-34 |
|
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, Component Of Gems 3, Gemin-3, and SMN-Interacting Protein) interacts directly with SMN (survival of motor neurons), the spinal muscular atrophy gene product, and may play a catalytic role in the function of the SMN complex on ribonucleoproteins. Diseases associated with DDX20 include spinal muscular atrophy and muscular atrophy. DDX20 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350701 [Multi-domain] Cd Length: 192 Bit Score: 127.38 E-value: 2.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 57 DACQRLGWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSLL---DHPQAffcLVLTPTRELAFQIGQQFE 133
Cdd:cd17943 3 EGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDlerRHPQV---LILAPTREIAVQIHDVFK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 134 ALGSGI-GLIAAVIVGGVDMaAQAMALARRPHIIVATPGRLVdHLENTKGFNLKALKFLIMDEADRILNMDFEVELDKIL 212
Cdd:cd17943 80 KIGKKLeGLKCEVFIGGTPV-KEDKKKLKGCHIAVGTPGRIK-QLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIF 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 17555296 213 KVIPRERRTYLFSATMTKKV-SKLERAsLRDPARVS 247
Cdd:cd17943 158 SSLPKNKQVIAFSATYPKNLdNLLARY-MRKPVLVR 192
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
54-237 |
3.41e-34 |
|
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called DEAD box RNA helicase DEAD5) and DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH)) are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350721 [Multi-domain] Cd Length: 196 Bit Score: 127.31 E-value: 3.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 54 PLCDACQRLGWMKPSKIQQAALPHALQG--KDVIGLAETGSGKTGAFAIPVLQSL---LDHPQaffCLVLTPTRELAFQI 128
Cdd:cd17963 4 ELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVdptLKSPQ---ALCLAPTRELARQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 129 GQQFEALGSGIGLIAAVIVGGVDMAAQAMALArrpHIIVATPGRLVDHLEnTKGFNLKALKFLIMDEADRILNMD-FEVE 207
Cdd:cd17963 81 GEVVEKMGKFTGVKVALAVPGNDVPRGKKITA---QIVIGTPGTVLDWLK-KRQLDLKKIKILVLDEADVMLDTQgHGDQ 156
|
170 180 190
....*....|....*....|....*....|
gi 17555296 208 LDKILKVIPRERRTYLFSATMTKKVSKLER 237
Cdd:cd17963 157 SIRIKRMLPRNCQILLFSATFPDSVRKFAE 186
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
46-246 |
2.89e-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: 2.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 46 FAELGVSQPLCDACQRLGWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSL---LDHPQAffcLVLTPTR 122
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLdiqVRETQA---LILSPTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 123 ELAFQIGQQFEALGSGIGLIAAVIVGGVDMAAQAMALARRPHIIVATPGRLVDHLENtKGFNLKALKFLIMDEADRILNM 202
Cdd:cd18045 78 ELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRR-RSLRTRHIKMLVLDEADEMLNK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 17555296 203 DFEVELDKILKVIPRERRTYLFSATMTKKVSKLERASLRDPARV 246
Cdd:cd18045 157 GFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
55-269 |
4.10e-29 |
|
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350706 [Multi-domain] Cd Length: 231 Bit Score: 114.39 E-value: 4.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 55 LCDACQRLGWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSLLD----------HPQAffcLVLTPTREL 124
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRykllaegpfnAPRG---LVITPSREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 125 AFQIGQQFEALGSGIGLIAAVIVGGVDMaaQAMALARRPH--IIVATPGRLVDhLENTKGFNLKALKFLIMDEADRILNM 202
Cdd:cd17948 78 AEQIGSVAQSLTEGLGLKVKVITGGRTK--RQIRNPHFEEvdILVATPGALSK-LLTSRIYSLEQLRHLVLDEADTLLDD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 203 DFEVELDKILK-----------VIPRERRTYLF--SATMTKKVSK-LERAslrdparVSVSSrYKTVDNLKQHYIF--VP 266
Cdd:cd17948 155 SFNEKLSHFLRrfplasrrsenTDGLDPGTQLVlvSATMPSGVGEvLSKV-------IDVDS-IETVTSDKLHRLMphVK 226
|
...
gi 17555296 267 NKY 269
Cdd:cd17948 227 QKF 229
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
298-378 |
1.11e-27 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 105.37 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 298 QIAVMLRQLGMQAVPLHGQMSQEKRLGSLNKFKSKAREILVCTDVAARGLDIPHVDMVINYDMPSQSKDYVHRVGRTARA 377
Cdd:smart00490 2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRA 81
|
.
gi 17555296 378 G 378
Cdd:smart00490 82 G 82
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
70-256 |
1.14e-25 |
|
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and nucleolar RNA helicase 2) is an RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II. It promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) and binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs. DDX50 (also called Gu-Beta, Nucleolar Protein Gu2, and malignant cell derived RNA helicase). DDX21 and DDX50 have similar genomic structures and are in tandem orientation on chromosome 10, suggesting that the two genes arose by gene duplication in evolution. Diseases associated with DDX21 include stomach disease and cerebral creatine deficiency syndrome 3. Diseases associated with DDX50 include rectal disease. Both are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. Their name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.
Pssm-ID: 350702 [Multi-domain] Cd Length: 202 Bit Score: 104.16 E-value: 1.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 70 IQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSLLDHPQ------AFFCLVLTPTRELAFQIGQQFEALGSgiGLIA 143
Cdd:cd17944 16 IQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQprkrgrAPKVLVLAPTRELANQVTKDFKDITR--KLSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 144 AVIVGGVDMAAQAMALARRPHIIVATPGRLVDHLENTKgFNLKALKFLIMDEADRILNMDFEVELDKILKVIPRER---- 219
Cdd:cd17944 94 ACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGR-LDLTKLKHVVLDEVDQMLDMGFAEQVEEILSVSYKKDsedn 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 17555296 220 -RTYLFSATMTKKVSKLERASLRdparvsvsSRYKTVD 256
Cdd:cd17944 173 pQTLLFSATCPDWVYNVAKKYMK--------SQYEQVD 202
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
44-243 |
8.27e-24 |
|
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH) is a testis-specific protein essential for completion of spermatogenesis. DDX25 is also a novel negative regulator of IFN pathway and facilitates RNA virus infection. Diseases associated with DDX25 include hydrolethalus syndrome, an autosomal recessive lethal malformation syndrome characterized by multiple developmental defects of fetus.. DDX25 (also called gonadotropin-regulated testicular RNA helicase) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350806 [Multi-domain] Cd Length: 229 Bit Score: 99.71 E-value: 8.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 44 KSFAELGVSQPLCDACQRLGWMKPSKIQQAALPHALQG--KDVIGLAETGSGKTGAFAIPVLQ---SLLDHPQaffCLVL 118
Cdd:cd18048 18 KSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSrvdALKLYPQ---CLCL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 119 TPTRELAFQIGQQFEALG---SGIGLIAAV----IVGGVDMAAQamalarrphIIVATPGRLVDHLENTKGFNLKALKFL 191
Cdd:cd18048 95 SPTFELALQTGKVVEEMGkfcVGIQVIYAIrgnrPGKGTDIEAQ---------IVIGTPGTVLDWCFKLRLIDVTNISVF 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17555296 192 IMDEADRILNMD-FEVELDKILKVIPRERRTYLFSATMTKKVSKLERASLRDP 243
Cdd:cd18048 166 VLDEADVMINVQgHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDP 218
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
81-227 |
8.72e-22 |
|
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: 91.31 E-value: 8.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 81 GKDVIGLAETGSGKTGAFAIPVLQSLLdhPQAFFCLVLTPTRELAFQIGQQFEALGSgIGLIAAVIVGGVDMAAQAMALA 160
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLL--KKGKKVLVLVPTKALALQTAERLRELFG-PGIRVAVLVGGSSAEEREKNKL 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17555296 161 RRPHIIVATPGRLVDHLENTKGFNLKALKFLIMDEADRIL-NMDFEVELD-KILKVIPRERRTYLFSAT 227
Cdd:cd00046 78 GDADIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALLiDSRGALILDlAVRKAGLKNAQVILLSAT 146
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
44-243 |
1.30e-19 |
|
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: 87.08 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 44 KSFAELGVSQPLCDACQRLGWMKPSKIQQAALPHALQG--KDVIGLAETGSGKTGAFAIPVLQSLLDHPQAFFCLVLTPT 121
Cdd:cd18047 1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 122 RELAFQIGQQFEALGSGIGLIA-AVIVGGVDMaaqAMALARRPHIIVATPGRLVDHLENTKGFNLKALKFLIMDEAD-RI 199
Cdd:cd18047 81 YELALQTGKVIEQMGKFYPELKlAYAVRGNKL---ERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADvMI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 17555296 200 LNMDFEVELDKILKVIPRERRTYLFSATMTKKVSKLERASLRDP 243
Cdd:cd18047 158 ATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
90-392 |
1.13e-18 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 88.93 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 90 TGSGKT--GAFAIpvlQSLLDHPQAffcLVLTPTRELAFQIGQQFEALgsgigLIAAVIVGGVDmaaqamalARRPHIIV 167
Cdd:COG1061 109 TGTGKTvlALALA---AELLRGKRV---LVLVPRRELLEQWAEELRRF-----LGDPLAGGGKK--------DSDAPITV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 168 ATPGRLV--DHLENTKgfnlKALKFLIMDEADRILNMDFEveldKILKVIPRERRtYLFSAT------MTKKVSKLE--- 236
Cdd:COG1061 170 ATYQSLArrAHLDELG----DRFGLVIIDEAHHAGAPSYR----RILEAFPAAYR-LGLTATpfrsdgREILLFLFDgiv 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 237 -RASLRD-------------PARVSVSSRYKTVDNLKQHY---IFVPNKYKETYLVYLLNEHAGNS-AIVFCATCATTMQ 298
Cdd:COG1061 241 yEYSLKEaiedgylappeyyGIRVDLTDERAEYDALSERLreaLAADAERKDKILRELLREHPDDRkTLVFCSSVDHAEA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 299 IAVMLRQLGMQAVPLHGQMSQEKRLGSLNKFKSKAREILVCTDVAARGLDIPHVDMVInYDMPSQSK-DYVHRVGRTARA 377
Cdd:COG1061 321 LAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI-LLRPTGSPrEFIQRLGRGLRP 399
|
330
....*....|....*
gi 17555296 378 GRSGiaiTVVTQYDV 392
Cdd:COG1061 400 APGK---EDALVYDF 411
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
278-460 |
4.70e-16 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 80.93 E-value: 4.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 278 LNEHAGNSAIVFCATCATTMQIAVMLRQLGMQAVPLHGQ--------MSQEKRLGSLNKFKSKAREILVCTDVAARGLDI 349
Cdd:COG1111 348 LGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQaskegdkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDI 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 350 PHVDMVINYD-MPSQSKdYVHRVGRTARaGRSGIAITVVTQYDV-EAYQKIEANLGKKldeykcvenevMVLVERTQEAt 427
Cdd:COG1111 428 PEVDLVIFYEpVPSEIR-SIQRKGRTGR-KREGRVVVLIAKGTRdEAYYWSSRRKEKK-----------MKSILKKLKK- 493
|
170 180 190
....*....|....*....|....*....|...
gi 17555296 428 enariEMKEMDEKKKSGKKRRQNDDFGDTEESG 460
Cdd:COG1111 494 -----LLDKQEKEKLKESAQATLDEFESIKELA 521
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
42-196 |
2.38e-15 |
|
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: 78.72 E-value: 2.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 42 KEKSFAEL--GVSQPLCDACQRLGWMKPSKIQQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSLLDHPQAFFcLVLT 119
Cdd:COG1205 30 REARYAPWpdWLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPGATA-LYLY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 120 PTRELAF-Q---IGQQFEALGSGIGliAAVIVGGVDMAAQAMALaRRPHIIVATPgrlvD--H---LENTKGF--NLKAL 188
Cdd:COG1205 109 PTKALARdQlrrLRELAEALGLGVR--VATYDGDTPPEERRWIR-EHPDIVLTNP----DmlHyglLPHHTRWarFFRNL 181
|
....*...
gi 17555296 189 KFLIMDEA 196
Cdd:COG1205 182 RYVVIDEA 189
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
71-381 |
1.55e-13 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 72.48 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 71 QQAALPHALQGKDVIGLAETGSGKTGAFAIPVLqsLLDHPqaffCLVLTPTreLAFQIGQQFEALGSGIGliAAVIVGGV 150
Cdd:COG0514 22 QEEIIEAVLAGRDALVVMPTGGGKSLCYQLPAL--LLPGL----TLVVSPL--IALMKDQVDALRAAGIR--AAFLNSSL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 151 DMAAQAMALAR----RPHIIVATPGRLvdhleNTKGFnLKALK-----FLIMDEA-------DrilnmDFEVE---LDKI 211
Cdd:COG0514 92 SAEERREVLRAlragELKLLYVAPERL-----LNPRF-LELLRrlkisLFAIDEAhcisqwgH-----DFRPDyrrLGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 212 LKVIPReRRTYLFSATMTKKVSK--LERASLRDPaRVSVSS--RyktvDNLkqHYIFVP--NKYKETYLVYLLNEHAGNS 285
Cdd:COG0514 161 RERLPN-VPVLALTATATPRVRAdiAEQLGLEDP-RVFVGSfdR----PNL--RLEVVPkpPDDKLAQLLDFLKEHPGGS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 286 AIVFCATCATTMQIAVMLRQLGMQAVPLHGQMSQEKRLGSLNKFKSKAREILVCTdVA-ARGLDIPHVDMVINYDMPSQS 364
Cdd:COG0514 233 GIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLPKSI 311
|
330
....*....|....*..
gi 17555296 365 KDYVHRVGrtaRAGRSG 381
Cdd:COG0514 312 EAYYQEIG---RAGRDG 325
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
66-234 |
4.28e-13 |
|
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: 68.94 E-value: 4.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 66 KPSKIQQAALPHALQ----------GKDVIGL------AETGSGKTGAFAIPVLQSLLDHPQAFF--------------- 114
Cdd:cd17965 30 KPSPIQTLAIKKLLKtlmrkvtkqtSNEEPKLevfllaAETGSGKTLAYLAPLLDYLKRQEQEPFeeaeeeyesakdtgr 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 115 --CLVLTPTRELAFQIGQQFEALGSGIGLIAAVIVGGVDMAAQAMALA--RRPHIIVATPGRLVDhLENTKGFNLKALKF 190
Cdd:cd17965 110 prSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGPSYQRLQLAfkGRIDILVTTPGKLAS-LAKSRPKILSRVTH 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 17555296 191 LIMDEADRILNMDFEVELDKILKVIPRERRTYLFSATMTKKVSK 234
Cdd:cd17965 189 LVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDK 232
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
278-458 |
7.74e-13 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 71.06 E-value: 7.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 278 LNEHAGNSAIVFCATCATTMQIAVMLRQLGMQAVPLHGQ--------MSQEKRLGSLNKFKSKAREILVCTDVAARGLDI 349
Cdd:PRK13766 360 LGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGQaskdgdkgMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDI 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 350 PHVDMVINYD-MPSQSKdYVHRVGRTARaGRSGIAITVVTQ--YDvEAYQKIEANLGKK----LDEYKCVENEVMVLVER 422
Cdd:PRK13766 440 PSVDLVIFYEpVPSEIR-SIQRKGRTGR-QEEGRVVVLIAKgtRD-EAYYWSSRRKEKKmkeeLKNLKGILNKKLQELDE 516
|
170 180 190
....*....|....*....|....*....|....*.
gi 17555296 423 TQEATENARIEMKEMDEKKKSGKKRRQNDDFGDTEE 458
Cdd:PRK13766 517 EQKGEEEEKDEQLSLDDFVKSKGKEEEEEEEKEEKD 552
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
71-196 |
2.12e-12 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 65.68 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 71 QQAALPHALQGKDVIGLAETGSGKTGAFAIPVLQSLLDHPQAFFcLVLTPTRELAfqigQ-QFEAL-----GSGIGLIAA 144
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDPGSRA-LYLYPTKALA----QdQLRSLrelleQLGLGIRVA 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 17555296 145 VIVGGVDMAAQAMALARRPHIIVATPGRL---VDHLENTKGFNLKALKFLIMDEA 196
Cdd:cd17923 80 TYDGDTPREERRAIIRNPPRILLTNPDMLhyaLLPHHDRWARFLRNLRYVVLDEA 134
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
81-238 |
4.16e-12 |
|
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: 64.14 E-value: 4.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 81 GKDVIGLAETGSGKTGAFAIPVLQSLLDHP-QAFFCLVLTPTRELAFQIGQQFEALGSGIGLIAAVIV--GGVDMAAQAM 157
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPeKGVQVLYISPLKALINDQERRLEEPLDEIDLEIPVAVrhGDTSQSEKAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 158 ALARRPHIIVATPGRLVDHLENTKGFN-LKALKFLIMDEADRILN----MDFEVELDKILKVIPRERRTYLFSATmtkkV 232
Cdd:cd17922 81 QLKNPPGILITTPESLELLLVNKKLRElFAGLRYVVVDEIHALLGskrgVQLELLLERLRKLTGRPLRRIGLSAT----L 156
|
....*.
gi 17555296 233 SKLERA 238
Cdd:cd17922 157 GNLEEA 162
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
71-399 |
1.03e-11 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 66.84 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 71 QQAALPHAL-QGKDVIGLAETGSGKT--GAFAIpvLQSLLDHPQAFFclvLTPTRELAFQIGQQFEALGSGIGLIAAVIV 147
Cdd:COG1204 27 QAEALEAGLlEGKNLVVSAPTASGKTliAELAI--LKALLNGGKALY---IVPLRALASEKYREFKRDFEELGIKVGVST 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 148 GGVDMAAqamALARRPHIIVATPGRLvDHLENTKGFNLKALKFLIMDEA------DR--ILnmdfEVELDKILKVIPrER 219
Cdd:COG1204 102 GDYDSDD---EWLGRYDILVATPEKL-DSLLRNGPSWLRDVDLVVVDEAhliddeSRgpTL----EVLLARLRRLNP-EA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 220 RTYLFSATM--TKKVSKLERASLrdparvsVSSRYKTVDN----LKQHYIFVPNKYKET--YLVYLLNEHAGN--SAIVF 289
Cdd:COG1204 173 QIVALSATIgnAEEIAEWLDAEL-------VKSDWRPVPLnegvLYDGVLRFDDGSRRSkdPTLALALDLLEEggQVLVF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 290 CATCATTMQIAVMLRQ-LGMQAVPL------------------------------------HGQMSQEKRLGSLNKFKSK 332
Cdd:COG1204 246 VSSRRDAESLAKKLADeLKRRLTPEereeleelaeellevseethtnekladclekgvafhHAGLPSELRRLVEDAFREG 325
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17555296 333 AREILVCTDVAARGLDIPhVDMVI--------NYDMPSQskDYVHRVGRTARAGR--SGIAItVVTQYDVEAYQKIE 399
Cdd:COG1204 326 LIKVLVATPTLAAGVNLP-ARRVIirdtkrggMVPIPVL--EFKQMAGRAGRPGYdpYGEAI-LVAKSSDEADELFE 398
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
256-381 |
2.55e-11 |
|
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: 61.07 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 256 DNLKQHYIFVPNKYKE-TYLVYLLNEHAGNSAIVFCATCATTMQIAVMLRQLGMQAVPLHGQMSQEKRLGSLNKFKSKAR 334
Cdd:cd18794 2 PNLFYSVRPKDKKDEKlDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKI 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 17555296 335 EILVCTDVAARGLDIPHVDMVINYDMPSQSKDYVHRVGrtaRAGRSG 381
Cdd:cd18794 82 QVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESG---RAGRDG 125
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
335-387 |
1.66e-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: 1.66e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 17555296 335 EILVCTDVAARGLDIPHVDMVINYDMPSQSKDYVHRVGRTARAG-RSGIAITVV 387
Cdd:cd18785 24 EILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGkDEGEVILFV 77
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
274-374 |
1.98e-10 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 63.32 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 274 LVYLLNEH--AGNSAIVFCATCATTMQIAVMLRQLGMQAVPLHGQMSQEKRLGSLNKFKSK--AREILVCTDVAARGLDI 349
Cdd:COG0553 538 LLELLEELlaEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGpeAPVFLISLKAGGEGLNL 617
|
90 100 110
....*....|....*....|....*....|.
gi 17555296 350 PHVDMVINYDMP------SQSKDYVHRVGRT 374
Cdd:COG0553 618 TAADHVIHYDLWwnpaveEQAIDRAHRIGQT 648
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
270-372 |
1.15e-09 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 56.33 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 270 KETYLVYLLNE--HAGNSAIVFCATCATTMQIAVMLRQLGMQAVPLHGQMSQEKRLGSLNKFK--SKAREILVCTDVAAR 345
Cdd:cd18793 12 KLEALLELLEElrEPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNedPDIRVFLLSTKAGGV 91
|
90 100 110
....*....|....*....|....*....|...
gi 17555296 346 GLDIPHVDMVINYDMP------SQSKDYVHRVG 372
Cdd:cd18793 92 GLNLTAANRVILYDPWwnpaveEQAIDRAHRIG 124
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
71-391 |
1.43e-09 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 60.50 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 71 QQAALPHALQGKDVIGLAETGSGKTGAFAIPVLqsLLDHpqafFCLVLTPTRELAFQIGQQFEALGsgiglIAAVIVGGV 150
Cdd:PRK11057 30 QQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPAL--VLDG----LTLVVSPLISLMKDQVDQLLANG-----VAAACLNST 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 151 DMAAQAMALARRPH-----IIVATPGRLV--DHLENTKGFNLKalkFLIMDEADRI--LNMDFEVELDKILKVipRERRT 221
Cdd:PRK11057 99 QTREQQLEVMAGCRtgqikLLYIAPERLMmdNFLEHLAHWNPA---LLAVDEAHCIsqWGHDFRPEYAALGQL--RQRFP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 222 YL----FSATM--TKKVSKLERASLRDPaRVSVSS------RYKTVDnlkqhyifvpnKYKET-YLVYLLNEHAGNSAIV 288
Cdd:PRK11057 174 TLpfmaLTATAddTTRQDIVRLLGLNDP-LIQISSfdrpniRYTLVE-----------KFKPLdQLMRYVQEQRGKSGII 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 289 FCATCATTMQIAVMLRQLGMQAVPLHGQMSQEKRLGSLNKFKSKAREILVCTDVAARGLDIPHVDMVINYDMPSQSKDYV 368
Cdd:PRK11057 242 YCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYY 321
|
330 340
....*....|....*....|...
gi 17555296 369 HrvgRTARAGRSGIAITVVTQYD 391
Cdd:PRK11057 322 Q---ETGRAGRDGLPAEAMLFYD 341
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
317-381 |
2.27e-09 |
|
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: 55.82 E-value: 2.27e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17555296 317 MSQEKRLGSLNKFKSKAREILVCTDVAARGLDIPHVDMVINYDMPSQSKDYVHRVGRTARaGRSG 381
Cdd:cd18801 74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR-KRQG 137
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
274-377 |
1.36e-08 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350189 [Multi-domain] Cd Length: 142 Bit Score: 53.36 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 274 LVYLLNEHAGNS----AIVFCATCATTMQIAVMLRQLGMQAVPLHGQ---------------MSQEKRLGSLNKFKSKAR 334
Cdd:cd18802 12 LIEILREYFPKTpdfrGIIFVERRATAVVLSRLLKEHPSTLAFIRCGfligrgnssqrkrslMTQRKQKETLDKFRDGEL 91
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 17555296 335 EILVCTDVAARGLDIPHVDMVINYDMPSQSKDYVHRVGRtARA 377
Cdd:cd18802 92 NLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARA 133
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
65-196 |
1.59e-08 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 54.58 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 65 MKPSKIQQAALPHALQgKDVIGLAETGSGKTgAFAIPVLQSLLDHPQAF-----FCLVLTPTRELAFqigQQFEALGSGI 139
Cdd:cd18034 1 FTPRSYQLELFEAALK-RNTIVVLPTGSGKT-LIAVMLIKEMGELNRKEknpkkRAVFLVPTVPLVA---QQAEAIRSHT 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17555296 140 GLIAAVIVG--GVDMAAQAMALA--RRPHIIVATPGRLVDHLENTKgFNLKALKFLIMDEA 196
Cdd:cd18034 76 DLKVGEYSGemGVDKWTKERWKEelEKYDVLVMTAQILLDALRHGF-LSLSDINLLIFDEC 135
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
64-381 |
9.42e-08 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 54.72 E-value: 9.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 64 WMKPSKIQQAALPHALQGKDVIGLAETGSGKT-GAFaIPVLQSLLDHPQAFF------CLVLTPTRELAFQIGQQFEALG 136
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPRPGElpdglrVLYISPLKALANDIERNLRAPL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 137 SGIGLIAAVIVGGVDMAA----------QAMaLARRPHIIVATPgrlvdhlE------NTKGF--NLKALKFLIMDE--- 195
Cdd:COG1201 101 EEIGEAAGLPLPEIRVGVrtgdtpaserQRQ-RRRPPHILITTP-------EslalllTSPDAreLLRGVRTVIVDEiha 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 196 -AD------------RilnmdfeveLDKILkviPRE-RRTYLfSATmtkkVSKLERA--------SLRDPARVSVSSRyK 253
Cdd:COG1201 173 lAGskrgvhlalsleR---------LRALA---PRPlQRIGL-SAT----VGPLEEVarflvgyeDPRPVTIVDAGAG-K 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 254 TVDnLKqhyIFVP--------------NKYKETYLVYLLNEHagNSAIVFCATCATTMQIAVMLRQL-GMQAVPL---HG 315
Cdd:COG1201 235 KPD-LE---VLVPvedlierfpwaghlWPHLYPRVLDLIEAH--RTTLVFTNTRSQAERLFQRLNELnPEDALPIaahHG 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17555296 316 QMSQEKRL--------GSLnkfksKAreiLVCT---DVaarGLDIPHVDMVINYDMPsqskdyvHRVGRTA-RAGRSG 381
Cdd:COG1201 309 SLSREQRLeveealkaGEL-----RA---VVATsslEL---GIDIGDVDLVIQVGSP-------KSVARLLqRIGRAG 368
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
69-196 |
1.91e-07 |
|
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: 51.11 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 69 KIQQAALPHALQ-GKDVIGLAETGSGKT--GAFAIpvLQSLLDHPQAffCLVLTPTRELAFQIGQQF-EALGSGIGLIAA 144
Cdd:cd17921 4 PIQREALRALYLsGDSVLVSAPTSSGKTliAELAI--LRALATSGGK--AVYIAPTRALVNQKEADLrERFGPLGKNVGL 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 17555296 145 VIvGGVDMAAQAMAlarRPHIIVATPGRLVDHLENTKGFNLKALKFLIMDEA 196
Cdd:cd17921 80 LT-GDPSVNKLLLA---EADILVATPEKLDLLLRNGGERLIQDVRLVVVDEA 127
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
281-387 |
2.06e-07 |
|
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: 50.34 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 281 HAGNSAIVFCATCATTMQIAVMLRQLGMQAVPL------HGQMSQEKRLGSLNKFKSKAREILVCTDVAARGLDIPHVDM 354
Cdd:cd18796 36 ERHKSTLVFTNTRSQAERLAQRLRELCPDRVPPdfialhHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDL 115
|
90 100 110
....*....|....*....|....*....|...
gi 17555296 355 VINYDMPSQSKDYVHRVGRTARAGRSGIAITVV 387
Cdd:cd18796 116 VIQIGSPKSVARLLQRLGRSGHRPGAASKGRLV 148
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
285-376 |
8.01e-07 |
|
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: 47.94 E-value: 8.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 285 SAIVFCATCATTMQIAVMLRQLGMQAVPLHGQMSQEKRLGS---LNKFKSKAREILVCTDVAARGLDIPHVDMVInYDMP 361
Cdd:cd18799 8 KTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDEaliLLFFGELKPPILVTVDLLTTGVDIPEVDNVV-FLRP 86
|
90
....*....|....*.
gi 17555296 362 SQSKD-YVHRVGRTAR 376
Cdd:cd18799 87 TESRTlFLQMLGRGLR 102
|
|
| mfd |
TIGR00580 |
transcription-repair coupling factor (mfd); All proteins in this family for which functions ... |
91-383 |
1.23e-05 |
|
transcription-repair coupling factor (mfd); All proteins in this family for which functions are known are DNA-dependent ATPases that function in the process of transcription-coupled DNA repair in which the repair of the transcribed strand of actively transcribed genes is repaired at a higher rate than the repair of non-transcribed regions of the genome and than the non-transcribed strand of the same gene. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). This family is closely related to the RecG and UvrB families. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273152 [Multi-domain] Cd Length: 926 Bit Score: 48.12 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 91 GSGKTGAFAIPVLQSLLDHPQAffcLVLTPTRELAFQ----IGQQFEALGSGIGLIAAVIvggvDMAAQAMALARRPH-- 164
Cdd:TIGR00580 482 GFGKTEVAMRAAFKAVLDGKQV---AVLVPTTLLAQQhfetFKERFANFPVTIELLSRFR----SAKEQNEILKELASgk 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 165 --IIVATpgrlvdHLENTKGFNLKALKFLIMDEADRilnmdFEVELDKILKviprERRTYLFSATMTK---------KVS 233
Cdd:TIGR00580 555 idILIGT------HKLLQKDVKFKDLGLLIIDEEQR-----FGVKQKEKLK----ELRTSVDVLTLSAtpiprtlhmSMS 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 234 KLERASL-------RDPARVSVSSryktvdnlkqhyiFVPNKYKETylvyLLNEHAGNSAIVFCATCATTMQ-IAVMLRQ 305
Cdd:TIGR00580 620 GIRDLSIiatppedRLPVRTFVME-------------YDPELVREA----IRRELLRGGQVFYVHNRIESIEkLATQLRE 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 306 LgmqaVP------LHGQMSQEKRLGSLNKFKSKAREILVCTDVAARGLDIPHVDMVI--NYDMPSQSKDYVHRvGRTARA 377
Cdd:TIGR00580 683 L----VPeariaiAHGQMTENELEEVMLEFYKGEFQVLVCTTIIETGIDIPNANTIIieRADKFGLAQLYQLR-GRVGRS 757
|
....*.
gi 17555296 378 GRSGIA 383
Cdd:TIGR00580 758 KKKAYA 763
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
281-399 |
6.13e-05 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 45.66 E-value: 6.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 281 HAGNSAIVFCATCATTMQIAVMLRQLGMQAVPLHGQMSQEKRlGSLNKFKSKAREILVCTDVA-ARGLDIPHVDMVINYD 359
Cdd:PLN03137 678 HFDECGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQR-AFVQKQWSKDEINIICATVAfGMGINKPDVRFVIHHS 756
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 17555296 360 MPSQSKDYVHRVGrtaRAGRSGIAITVVTQYDVEAYQKIE 399
Cdd:PLN03137 757 LPKSIEGYHQECG---RAGRDGQRSSCVLYYSYSDYIRVK 793
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
299-383 |
9.46e-05 |
|
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: 42.72 E-value: 9.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 299 IAVMLRQLGMQA--VPLHGQMSQEKRLGSLNKFKSKAREILVCTDVAARGLDIPHVDMVI--NYDMPSQSKDYVHRvGRT 374
Cdd:cd18810 41 LATQLRQLVPEAriAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIieRADKFGLAQLYQLR-GRV 119
|
....*....
gi 17555296 375 ARAGRSGIA 383
Cdd:cd18810 120 GRSKERAYA 128
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
250-381 |
9.93e-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: 42.62 E-value: 9.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 250 SRYKTVDNL-KQHYIFVPNKYKETYLVYLLNEHA-GNSAIVFCATCATTMQIA-VMLRQLgmqavpLHGQMSQEKRLGSL 326
Cdd:cd18789 14 REYLGLGAHrKRRLLAAMNPNKLRALEELLKRHEqGDKIIVFTDNVEALYRYAkRLLKPF------ITGETPQSEREEIL 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 17555296 327 NKFKSKAREILVCTDVAARGLDIPH--VDMVINYDMPSQsKDYVHRVGRTARAGRSG 381
Cdd:cd18789 88 QNFREGEYNTLVVSKVGDEGIDLPEanVAIQISGHGGSR-RQEAQRLGRILRPKKGG 143
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
313-357 |
1.80e-04 |
|
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: 41.87 E-value: 1.80e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 17555296 313 LHGQMSQEKRLGSLNKFKSKAREILVCTDVAARGLDIPHVD-MVIN 357
Cdd:cd18792 66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANtMIIE 111
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
79-227 |
2.67e-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: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 79 LQGKDVIGLAETGSGKTGAFAIPVLQSLLDHPQAFFclvLTPTRELAFQIGQQFEALgSGIGLIAAVIVGGVDMAAQAMA 158
Cdd:cd18028 15 LKGENLLISIPTASGKTLIAEMAMVNTLLEGGKALY---LVPLRALASEKYEEFKKL-EEIGLKVGISTGDYDEDDEWLG 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17555296 159 LArrpHIIVATPGRLvDHLENTKGFNLKALKFLIMDEADRILNMD----FEVELDKILKVIPRERRTYLfSAT 227
Cdd:cd18028 91 DY---DIIVATYEKF-DSLLRHSPSWLRDVGVVVVDEIHLISDEErgptLESIVARLRRLNPNTQIIGL-SAT 158
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
313-356 |
1.68e-03 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 39.25 E-value: 1.68e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 17555296 313 LHGQMSQEKRLGSLNKFKSKAREILVCTDVAARGLDIPHVD-MVI 356
Cdd:cd18811 67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATvMVI 111
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
282-428 |
2.59e-03 |
|
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: 40.11 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 282 AGNSAIVFCATCATTMQIAVMLRQLGMQA-VPL-HGQMSQ----EKRLGSLNKFKSKAREILVCTDVAARGLDIpHVDMV 355
Cdd:cd09639 217 KGGSVAIIVNTVDRAQEFYQQLKEKGPEEeIMLiHSRFTEkdraKKEAELLLEFKKSEKFVIVATQVIEASLDI-SVDVM 295
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17555296 356 INYDMPSQSkdYVHRVGRTARAGRSGIAITVVTqydveayqkieanlgKKLDEYKCVENEVMVLVERTQEATE 428
Cdd:cd09639 296 ITELAPIDS--LIQRLGRLHRYGEKNGEEVYII---------------TDAPDGKGQKPYPYDLVERTIELLE 351
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
71-198 |
4.13e-03 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 38.26 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 71 QQAALPHALQGKDVIgLAETGSGKTgAFAIPVLQSLLDHPQAFfCLVLTPTRELAFQIGQQFEALGSGIGLIAAvIVGGV 150
Cdd:cd18035 7 QVLIAAVALNGNTLI-VLPTGLGKT-IIAILVAADRLTKKGGK-VLILAPSRPLVEQHAENLKRVLNIPDKITS-LTGEV 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 17555296 151 DMAAQAmALARRPHIIVATPGRLVDHLENTKgFNLKALKFLIMDEADR 198
Cdd:cd18035 83 KPEERA-ERWDASKIIVATPQVIENDLLAGR-ITLDDVSLLIFDEAHH 128
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
90-227 |
4.88e-03 |
|
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: 37.67 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555296 90 TGSGKTG-AFAIPVLQSlldhpqAFFCLVLTPTRELAFQIGQQFEALGSG--IGLIaavivGGVDMAAQAMALarrphII 166
Cdd:cd17926 27 TGSGKTLtALALIAYLK------ELRTLIVVPTDALLDQWKERFEDFLGDssIGLI-----GGGKKKDFDDAN-----VV 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17555296 167 VATPGRLVDHLENTKGFNLKALkFLIMDEADRILNMDFEveldkilKVIPRERRTYL--FSAT 227
Cdd:cd17926 91 VATYQSLSNLAEEEKDLFDQFG-LLIVDEAHHLPAKTFS-------EILKELNAKYRlgLTAT 145
|
|
| |
