|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
6-421 |
9.14e-150 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 432.26 E-value: 9.14e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 6 FEHFNLDENLIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQLIESDIQ-EPQAIVVAPTREL 84
Cdd:COG0513 4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPrAPQALILAPTREL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 85 AQQLYQVAMHLVKFKkGINVKLFIGGTDLEKDKQRCNHQPQLIIGTPTRINDLAHSGYLHAHLASYLIIDEADLMIDLGL 164
Cdd:COG0513 84 ALQVAEELRKLAKYL-GLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 165 IEDVDHIAARLDnENAHLAVFSATIPKSLQPFLNKYLSQPEFVVVDGKAHNKENIEFYLIPTKGSAKVDKTLELIDILNP 244
Cdd:COG0513 163 IEDIERILKLLP-KERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDEDP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 245 YLCIIFCNSRENADELADTLNKEGIKIGMIHGGLTPRERKQQMKRIRNLDFQFVIASDLASRGIDIEGVSHVINFDVPND 324
Cdd:COG0513 242 ERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPED 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 325 IDFFTHRVGRTGRGNYKGVAITLYGPDEESNITLIEDK-GYKFKNVDIKNGElkPIKAHNMRKSRQRKDDHLTNEVKHKV 403
Cdd:COG0513 322 PEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLiGQKIEEEELPGFE--PVEEKRLERLKPKIKEKLKGKKAGRG 399
|
410
....*....|....*...
gi 488377159 404 RSKSKRKVKPGYKKKFKQ 421
Cdd:COG0513 400 GRPGPKGERKARRGKRRR 417
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
15-207 |
4.07e-75 |
|
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: 233.49 E-value: 4.07e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 15 LIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQLIESDIQ----EPQAIVVAPTRELAQQLYQ 90
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKkkgrGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 91 VAMHLVKFKkGINVKLFIGGTDLEKDKQRCNHQPQLIIGTPTRINDLAHSGYLHAHLASYLIIDEADLMIDLGLIEDVDH 170
Cdd:cd00268 81 VARKLGKGT-GLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 488377159 171 IAARLdNENAHLAVFSATIPKSLQPFLNKYLSQPEFV 207
Cdd:cd00268 160 ILSAL-PKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
1-383 |
3.67e-70 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 229.30 E-value: 3.67e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 1 MSKHPFEHFNLDENLIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQLIESDIQEPQAIVVAP 80
Cdd:PRK11776 1 MSMTAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 81 TRELAQQlyqVAMHLVKFKKGI-NVKLFI--GGT-------DLEkdkqrcnHQPQLIIGTPTRINDLAHSGYLHAHLASY 150
Cdd:PRK11776 81 TRELADQ---VAKEIRRLARFIpNIKVLTlcGGVpmgpqidSLE-------HGAHIIVGTPGRILDHLRKGTLDLDALNT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 151 LIIDEADLMIDLGLIEDVDHIAARLDNENAHLaVFSATIPKSLQPFLNKYLSQPEFVVVDGkAHNKENIE--FYLIPTKg 228
Cdd:PRK11776 151 LVLDEADRMLDMGFQDAIDAIIRQAPARRQTL-LFSATYPEGIAAISQRFQRDPVEVKVES-THDLPAIEqrFYEVSPD- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 229 sakvDKTLELIDILN---PYLCIIFCNSRENADELADTLNKEGIKIGMIHGGLTPRERKQQMKRIRNLDFQFVIASDLAS 305
Cdd:PRK11776 228 ----ERLPALQRLLLhhqPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAA 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488377159 306 RGIDIEGVSHVINFDVPNDIDFFTHRVGRTGRGNYKGVAITLYGPDEESNITLIEDkgykFKNVDIKNGELKPIKAHN 383
Cdd:PRK11776 304 RGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIED----YLGRKLNWEPLPSLSPLS 377
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
6-360 |
3.16e-68 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 222.78 E-value: 3.16e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 6 FEHFNLDENLIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQLIESDIQEPQAIVVAPTRELA 85
Cdd:PTZ00424 30 FDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTRELA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 86 QQLYQVAMHLVKFKKgINVKLFIGGTDLEKDKQRCNHQPQLIIGTPTRINDLAHSGYLHAHLASYLIIDEADLMIDLGLI 165
Cdd:PTZ00424 110 QQIQKVVLALGDYLK-VRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 166 EDVDHIAARLDnENAHLAVFSATIPKSLQPFLNKYLSQPEFVVVDGKAHNKENI-EFYLIPTKGSAKVDKTLELIDILNP 244
Cdd:PTZ00424 189 GQIYDVFKKLP-PDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIrQFYVAVEKEEWKFDTLCDLYETLTI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 245 YLCIIFCNSRENADELADTLNKEGIKIGMIHGGLTPRERKQQMKRIRNLDFQFVIASDLASRGIDIEGVSHVINFDVPND 324
Cdd:PTZ00424 268 TQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPAS 347
|
330 340 350
....*....|....*....|....*....|....*.
gi 488377159 325 IDFFTHRVGRTGRGNYKGVAITLYGPDEESNITLIE 360
Cdd:PTZ00424 348 PENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIE 383
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
3-379 |
3.44e-66 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 219.40 E-value: 3.44e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 3 KHPFEHFNLDENLIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLI-QLIESDIQ------EPQA 75
Cdd:PRK01297 86 KTRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIInQLLQTPPPkerymgEPRA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 76 IVVAPTRELAQQLYQVAMHLVKFKkGINVKLFIGGTDLEKDKQRCNHQ-PQLIIGTPTRINDLAHSGYLHAHLASYLIID 154
Cdd:PRK01297 166 LIIAPTRELVVQIAKDAAALTKYT-GLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQRGEVHLDMVEVMVLD 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 155 EADLMIDLGLIEDVDHIAARLD-NENAHLAVFSATIPKSLQPFLNKYLSQPEFVVVDGKAHNKENIEFYLIPTKGSakvD 233
Cdd:PRK01297 245 EADRMLDMGFIPQVRQIIRQTPrKEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGS---D 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 234 KTLELIDIL--NPY-LCIIFCNSRENADELADTLNKEGIKIGMIHGGLTPRERKQQMKRIRNLDFQFVIASDLASRGIDI 310
Cdd:PRK01297 322 KYKLLYNLVtqNPWeRVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHI 401
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 311 EGVSHVINFDVPNDIDFFTHRVGRTGRGNYKGVAITLYGPDEESNITLIEDK-GYKFKNVDIKNGELKPI 379
Cdd:PRK01297 402 DGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELlGRKISCEMPPAELLKPV 471
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
6-418 |
3.57e-64 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 212.88 E-value: 3.57e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 6 FEHFNLDENLIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQ-LIESDIQEPQA---IVVAPT 81
Cdd:PRK11192 3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQhLLDFPRRKSGPpriLILTPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 82 RELAQQLYQVAMHLVKFkKGINVKLFIGGTDLEKDKQRCNHQPQLIIGTPTRINDLAHSGYLHAHLASYLIIDEADLMID 161
Cdd:PRK11192 83 RELAMQVADQARELAKH-THLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 162 LGLIEDVDHIAARLDNENAHLaVFSATIP-KSLQPFLNKYLSQPEFVVVDGKAHNKENI-EFYLIPTKGSAKVDKTLELI 239
Cdd:PRK11192 162 MGFAQDIETIAAETRWRKQTL-LFSATLEgDAVQDFAERLLNDPVEVEAEPSRRERKKIhQWYYRADDLEHKTALLCHLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 240 DILNPYLCIIFCNSRENADELADTLNKEGIKIGMIHGGLTPRERKQQMKRIRNLDFQFVIASDLASRGIDIEGVSHVINF 319
Cdd:PRK11192 241 KQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 320 DVPNDIDFFTHRVGRTGRGNYKGVAITLYgpdeESNITLIEDKGYKFKNVDIKN---GELKPI-KAHNMRKSRQRKDDHL 395
Cdd:PRK11192 321 DMPRSADTYLHRIGRTGRAGRKGTAISLV----EAHDHLLLGKIERYIEEPLKArviDELRPKtKAPSEKKTGKPSKKVL 396
|
410 420
....*....|....*....|...
gi 488377159 396 TNEVKHKVRSKSKRKVKPGYKKK 418
Cdd:PRK11192 397 AKRAEKKEKEKEKPKVKKRHRDT 419
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
6-345 |
7.85e-64 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 217.02 E-value: 7.85e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 6 FEHFNLDENLIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQLIESDIQEPQAIVVAPTRELA 85
Cdd:PRK11634 8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTRELA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 86 QQLYQVAMHLVKFKKGINVKLFIGGTDLEKDKQRCNHQPQLIIGTPTRINDLAHSGYLHAHLASYLIIDEADLMIDLGLI 165
Cdd:PRK11634 88 VQVAEAMTDFSKHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 166 EDVDHIAARLDNENaHLAVFSATIPKSLQPFLNKYLSQPEFVVVDGKAHNKENIEFYLIPTKGSAKVDKTLELIDILNPY 245
Cdd:PRK11634 168 EDVETIMAQIPEGH-QTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVRFLEAEDFD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 246 LCIIFCNSRENADELADTLNKEGIKIGMIHGGLTPRERKQQMKRIRNLDFQFVIASDLASRGIDIEGVSHVINFDVPNDI 325
Cdd:PRK11634 247 AAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDS 326
|
330 340
....*....|....*....|
gi 488377159 326 DFFTHRVGRTGRGNYKGVAI 345
Cdd:PRK11634 327 ESYVHRIGRTGRAGRAGRAL 346
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
1-361 |
8.77e-55 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 187.87 E-value: 8.77e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 1 MSKHPFEHFNLDENLIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLL---------PLIQliESDIQ 71
Cdd:PRK04837 5 LTEQKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTatfhyllshPAPE--DRKVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 72 EPQAIVVAPTRELAQQLYQVAMHLVKfKKGINVKLFIGGTDLEKDKQRCNHQPQLIIGTPTRINDLAHSGYLHAHLASYL 151
Cdd:PRK04837 83 QPRALIMAPTRELAVQIHADAEPLAQ-ATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 152 IIDEADLMIDLGLIEDVDHIAARLDNENAHLA-VFSATIPKSLQPFLNKYLSQPEFVVVDGK---AHN-KENIeFYliPT 226
Cdd:PRK04837 162 VLDEADRMFDLGFIKDIRWLFRRMPPANQRLNmLFSATLSYRVRELAFEHMNNPEYVEVEPEqktGHRiKEEL-FY--PS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 227 KGsakvDKTLELIDILN---PYLCIIFCNSRENADELADTLNKEGIKIGMIHGGLTprerkqQMKRIRNLDfQF------ 297
Cdd:PRK04837 239 NE----EKMRLLQTLIEeewPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVA------QKKRLRILE-EFtrgdld 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488377159 298 -VIASDLASRGIDIEGVSHVINFDVPNDIDFFTHRVGRTGRGNYKGVAITLYGPDEESNITLIED 361
Cdd:PRK04837 308 iLVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIET 372
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
6-360 |
1.40e-51 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 180.39 E-value: 1.40e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 6 FEHFNLDENLIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQLIESDIQEPQ------AIVVA 79
Cdd:PRK10590 3 FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKgrrpvrALILT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 80 PTRELAQQlyqVAMHLVKFKKGINVKLFI--GGTDLEKDKQRCNHQPQLIIGTPTRINDLAHSGYLHAHLASYLIIDEAD 157
Cdd:PRK10590 83 PTRELAAQ---IGENVRDYSKYLNIRSLVvfGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 158 LMIDLGLIEDVDHIAARLDNENAHLaVFSATIPKSLQPFLNKYLSQPEFVVVDGKAHNKENIEFYLIPTKGSAKVDKTLE 237
Cdd:PRK10590 160 RMLDMGFIHDIRRVLAKLPAKRQNL-LFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 238 LIDILNPYLCIIFCNSRENADELADTLNKEGIKIGMIHGGltprerKQQMKRIRNL-DFQ-----FVIASDLASRGIDIE 311
Cdd:PRK10590 239 MIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGN------KSQGARTRALaDFKsgdirVLVATDIAARGLDIE 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 488377159 312 GVSHVINFDVPNDIDFFTHRVGRTGRGNYKGVAITLYGPDEESNITLIE 360
Cdd:PRK10590 313 ELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIE 361
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
1-356 |
3.05e-51 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 182.07 E-value: 3.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 1 MSKHP-----FEHFNLDENLIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQ-------LIES 68
Cdd:PRK04537 1 MSDKPltdltFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNrllsrpaLADR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 69 DIQEPQAIVVAPTRELAQQLYQVAmhlVKFKK--GINVKLFIGGTDLEKDKQRCNHQPQLIIGTPTRIND-LAHSGYLHA 145
Cdd:PRK04537 81 KPEDPRALILAPTRELAIQIHKDA---VKFGAdlGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDyVKQHKVVSL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 146 HLASYLIIDEADLMIDLGLIEDVDHIAARL-DNENAHLAVFSATIPKSLQPFLNKYLSQPEFVVVDGK----AHNKENIE 220
Cdd:PRK04537 158 HACEICVLDEADRMFDLGFIKDIRFLLRRMpERGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETEtitaARVRQRIY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 221 FyliPTKgSAKVDKTLELIDILNPYLCIIFCNSRENADELADTLNKEGIKIGMIHGGLTPRERKQQMKRIRNLDFQFVIA 300
Cdd:PRK04537 238 F---PAD-EEKQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVA 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488377159 301 SDLASRGIDIEGVSHVINFDVPNDIDFFTHRVGRTGRGNYKGVAITL----YG---PDEESNI 356
Cdd:PRK04537 314 TDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFacerYAmslPDIEAYI 376
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
219-348 |
1.16e-49 |
|
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: 164.99 E-value: 1.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 219 IEFYLIPTKGSAKVDKTL-ELIDILNPYLCIIFCNSRENADELADTLNKEGIKIGMIHGGLTPRERKQQMKRIRNLDFQF 297
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLlLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 488377159 298 VIASDLASRGIDIEGVSHVINFDVPNDIDFFTHRVGRTGRGNYKGVAITLY 348
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
6-352 |
8.19e-48 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 172.27 E-value: 8.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 6 FEHFNLDENLIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQLIESDI-----QEPQAIVVAP 80
Cdd:PTZ00110 132 FEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPllrygDGPIVLVLAP 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 81 TRELAQQLYQVAMHLVKFKKgINVKLFIGGTDLEKDKQRCNHQPQLIIGTPTRINDLAHSGYLHAHLASYLIIDEADLMI 160
Cdd:PTZ00110 212 TRELAEQIREQCNKFGASSK-IRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRML 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 161 DLGLIEDVDHIAARLDNENAHLaVFSATIPKSLQPfLNKYLSQPEFVVV-----DGKA-HNKENIEFYLIPTKGSAKVDK 234
Cdd:PTZ00110 291 DMGFEPQIRKIVSQIRPDRQTL-MWSATWPKEVQS-LARDLCKEEPVHVnvgslDLTAcHNIKQEVFVVEEHEKRGKLKM 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 235 TLELIDILNPYLcIIFCNSRENADELADTLNKEGIKIGMIHGGLTPRERKQQMKRIRNLDFQFVIASDLASRGIDIEGVS 314
Cdd:PTZ00110 369 LLQRIMRDGDKI-LIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVK 447
|
330 340 350
....*....|....*....|....*....|....*...
gi 488377159 315 HVINFDVPNDIDFFTHRVGRTGRGNYKGVAITLYGPDE 352
Cdd:PTZ00110 448 YVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDK 485
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
15-207 |
7.62e-45 |
|
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: 154.73 E-value: 7.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 15 LIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQLIESDIQEPQAIVVAPTRELAQQLYQVAMH 94
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 95 LVKFKKGINVKLFIGGTDLEKDKQRCNhQPQLIIGTPTRINDLAHSGYLHAHLASYLIIDEADLMIDLGLIEDVDHIAAR 174
Cdd:cd17943 81 IGKKLEGLKCEVFIGGTPVKEDKKKLK-GCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSS 159
|
170 180 190
....*....|....*....|....*....|...
gi 488377159 175 LDNeNAHLAVFSATIPKSLQPFLNKYLSQPEFV 207
Cdd:cd17943 160 LPK-NKQVIAFSATYPKNLDNLLARYMRKPVLV 191
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
28-194 |
7.50e-43 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 148.54 E-value: 7.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 28 TEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQLIESDIQEPQAIVVAPTRELAQQLYQVAMHLVKFkKGINVKLF 107
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKG-LGLKVASL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 108 IGGTDLEKDKQRcNHQPQLIIGTPTRIND-LAHSGYLHAhlASYLIIDEADLMIDLGLIEDVDHIAARLdNENAHLAVFS 186
Cdd:pfam00270 80 LGGDSRKEQLEK-LKGPDILVGTPGRLLDlLQERKLLKN--LKLLVLDEAHRLLDMGFGPDLEEILRRL-PKKRQILLLS 155
|
....*...
gi 488377159 187 ATIPKSLQ 194
Cdd:pfam00270 156 ATLPRNLE 163
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
10-204 |
8.02e-43 |
|
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: 149.78 E-value: 8.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 10 NLDENLIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQLIESDIQEPQAIVVAPTRELAQQLY 89
Cdd:cd17939 3 GLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQIQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 90 QVAMHLVKFkKGINVKLFIGGTDLEKDKQRCNHQPQLIIGTPTRINDLAHSGYLHAHLASYLIIDEADLMIDLGLIEDVD 169
Cdd:cd17939 83 KVVKALGDY-MGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQIY 161
|
170 180 190
....*....|....*....|....*....|....*
gi 488377159 170 HIAARLDNEnAHLAVFSATIPKSLQPFLNKYLSQP 204
Cdd:cd17939 162 DIFQFLPPE-TQVVLFSATMPHEVLEVTKKFMRDP 195
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
6-345 |
1.12e-42 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 157.64 E-value: 1.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 6 FEHFNLDENLIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQ---LIE----SDIQEPQAIVV 78
Cdd:PLN00206 123 FSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISrccTIRsghpSEQRNPLAMVL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 79 APTRELAQQlyqVAMHLVKFKKGINVK--LFIGGTDLEKDKQRCNHQPQLIIGTPTRINDLAHSGYLHAHLASYLIIDEA 156
Cdd:PLN00206 203 TPTRELCVQ---VEDQAKVLGKGLPFKtaLVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEV 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 157 DLMIDLGLIEDVDHIAARLdnENAHLAVFSATIPKSLQPFLNKYLSQPEFVVVdGKAhNKENIEFYLIPTKGSAKvDKTL 236
Cdd:PLN00206 280 DCMLERGFRDQVMQIFQAL--SQPQVLLFSATVSPEVEKFASSLAKDIILISI-GNP-NRPNKAVKQLAIWVETK-QKKQ 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 237 ELIDIL---NPYL--CIIFCNSRENADELADTLNK-EGIKIGMIHGGLTPRERKQQMKRIRNLDFQFVIASDLASRGIDI 310
Cdd:PLN00206 355 KLFDILkskQHFKppAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDL 434
|
330 340 350
....*....|....*....|....*....|....*
gi 488377159 311 EGVSHVINFDVPNDIDFFTHRVGRTGRGNYKGVAI 345
Cdd:PLN00206 435 LRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAI 469
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
6-204 |
1.48e-42 |
|
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: 149.13 E-value: 1.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 6 FEHFNLDENLIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQLIESDIQEPQAIVVAPTRELA 85
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 86 QQLYQVAMHLVKFkKGINVKLFIGGTDLEKDKQRCNHQPQLIIGTPTRINDLAHSGYLHAHLASYLIIDEADLMIDLGLI 165
Cdd:cd18046 81 QQIQKVVMALGDY-MGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFK 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 488377159 166 EDVDHIAARLdNENAHLAVFSATIPKSLQPFLNKYLSQP 204
Cdd:cd18046 160 DQIYDIFQKL-PPDTQVVLLSATMPNDVLEVTTKFMRDP 197
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
15-207 |
2.56e-40 |
|
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and PRP28 homolog) is involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation. Diseases associated with DDX23 include distal hereditary motor neuropathy, type II. DDX23 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350703 [Multi-domain] Cd Length: 220 Bit Score: 143.61 E-value: 2.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 15 LIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQLI--------ESDIQEPQAIVVAPTRELAQ 86
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYIsrlppldeETKDDGPYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 87 QLYQVAmhlVKF--KKGINVKLFIGGTDLEKDKQRCNHQPQLIIGTPTRINDLAHSGYLHAHLASYLIIDEADLMIDLGL 164
Cdd:cd17945 81 QIEEET---QKFakPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488377159 165 IEDVDHIAARL-------DNENAHLAV------------FSATIPKSLQPFLNKYLSQPEFV 207
Cdd:cd17945 158 EPQVTKILDAMpvsnkkpDTEEAEKLAasgkhryrqtmmFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
11-210 |
9.91e-40 |
|
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: 141.95 E-value: 9.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 11 LDENLIEAVKNLNFEKPTEIQNRIIPRIL-KGTNLIGQSQTGTGKSHAFLLPLIQ-LIESDIQEPQ----AIVVAPTREL 84
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPAIQsLLNTKPAGRRsgvsALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 85 AQQLYQVAMHLVKFKKGINVKLFIGGTDleKDKQRCNHQ---PQLIIGTPTRINDLAHSGYLHAHLAS--YLIIDEADLM 159
Cdd:cd17964 81 ALQIAAEAKKLLQGLRKLRVQSAVGGTS--RRAELNRLRrgrPDILVATPGRLIDHLENPGVAKAFTDldYLVLDEADRL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488377159 160 IDLGLIEDVDHIAARLDNENAHL---AVFSATIPKSLQPFLNKYLsQPEFVVVD 210
Cdd:cd17964 159 LDMGFRPDLEQILRHLPEKNADPrqtLLFSATVPDEVQQIARLTL-KKDYKFID 211
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
6-209 |
1.86e-39 |
|
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: 141.47 E-value: 1.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 6 FEHFNLDENLIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQ-LIESDI---------QEPQA 75
Cdd:cd17967 2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISkLLEDGPpsvgrgrrkAYPSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 76 IVVAPTRELAQQLYQVAmhlVKFKKGINVKLFI--GGTD----LEKDKQRCNhqpqLIIGTPTRINDLAHSGYLHAHLAS 149
Cdd:cd17967 82 LILAPTRELAIQIYEEA---RKFSYRSGVRSVVvyGGADvvhqQLQLLRGCD----ILVATPGRLVDFIERGRISLSSIK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488377159 150 YLIIDEADLMIDLGLIEDVDHIAARLD---NENAHLAVFSATIPKSLQ----PFLNKYLsqpeFVVV 209
Cdd:cd17967 155 FLVLDEADRMLDMGFEPQIRKIVEHPDmppKGERQTLMFSATFPREIQrlaaDFLKNYI----FLTV 217
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
6-204 |
3.16e-39 |
|
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: 140.13 E-value: 3.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 6 FEHFNLDENLIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQLIESDIQEPQAIVVAPTRELA 85
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 86 QQLYQVAMHLVKFKKGINVKLFiGGTDLEKDKQRCNHQPQLIIGTPTRINDLAHSGylHAHLA--SYLIIDEADLMIDLG 163
Cdd:cd17940 81 LQTSQVCKELGKHMGVKVMVTT-GGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKG--VADLShcKTLVLDEADKLLSQD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488377159 164 LIEDVDHIAARLDNENAHLaVFSATIPKSLQPFLNKYLSQP 204
Cdd:cd17940 158 FQPIIEKILNFLPKERQIL-LFSATFPLTVKNFMDRHMHNP 197
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
6-209 |
6.54e-39 |
|
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: 139.40 E-value: 6.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 6 FEHFNLDENLIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQLIESDIQEPQAIVVAPTRELA 85
Cdd:cd17950 4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRELA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 86 QQLYQVAMHLVKFKKGINVKLFIGGTDLEKDKQRC-NHQPQLIIGTPTRINDLAHSGYLHAHLASYLIIDEADLMI-DLG 163
Cdd:cd17950 84 FQISNEYERFSKYMPNVKTAVFFGGVPIKKDIEVLkNKCPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLeQLD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488377159 164 LIEDVDHI--AARLDNEnahLAVFSATIPKSLQPFLNKYLSQPEFVVV 209
Cdd:cd17950 164 MRRDVQEIfrATPHDKQ---VMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
6-209 |
1.81e-38 |
|
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: 140.10 E-value: 1.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 6 FEHFNLDENLIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQ-LIE--------SDIQEPQAI 76
Cdd:cd18052 45 FEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTgMMKegltassfSEVQEPQAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 77 VVAPTRELAQQLYQVAmhlVKFKKGINVKLFI--GGT-------DLEKDkqrCNhqpqLIIGTPTRINDLAHSGYLHAHL 147
Cdd:cd18052 125 IVAPTRELANQIFLEA---RKFSYGTCIRPVVvyGGVsvghqirQIEKG---CH----ILVATPGRLLDFIGRGKISLSK 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 148 ASYLIIDEADLMIDLGLIEDVDHIAARLD---NENAHLAVFSATIPKSLQ----PFLNK-YLsqpeFVVV 209
Cdd:cd18052 195 LKYLILDEADRMLDMGFGPEIRKLVSEPGmpsKEDRQTLMFSATFPEEIQrlaaEFLKEdYL----FLTV 260
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
6-207 |
3.31e-38 |
|
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: 137.44 E-value: 3.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 6 FEHFNLDENLIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQLIE--SDIQEPQAIVVAPTRE 83
Cdd:cd17959 3 FQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKahSPTVGARALILSPTRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 84 LAQQLYQVAMHLVKFkKGINVKLFIGGTDLEKDKQRCNHQPQLIIGTPTRINDLAHSGYLHAHLASYLIIDEADLMIDLG 163
Cdd:cd17959 83 LALQTLKVTKELGKF-TDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488377159 164 LIEDVDHIAARLDnENAHLAVFSATIPKSLQPFLNKYLSQPEFV 207
Cdd:cd17959 162 FAEQLHEILSRLP-ENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
15-194 |
5.59e-38 |
|
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: 136.94 E-value: 5.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 15 LIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQLI---ESDIQEPQ--AIVVAPTRELAQQLY 89
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrKANLKKGQvgALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 90 QVAMHLVKF-KKGINVKLFIGGTDLEKD-KQRCNHQPQLIIGTPTRINDLAHSGYLHAHLAS--YLIIDEADLMIDLGLI 165
Cdd:cd17960 81 EVLQSFLEHhLPKLKCQLLIGGTNVEEDvKKFKRNGPNILVGTPGRLEELLSRKADKVKVKSleVLVLDEADRLLDLGFE 160
|
170 180
....*....|....*....|....*....
gi 488377159 166 EDVDHIAARLDnENAHLAVFSATIPKSLQ 194
Cdd:cd17960 161 ADLNRILSKLP-KQRRTGLFSATQTDAVE 188
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
6-204 |
9.28e-38 |
|
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: 136.44 E-value: 9.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 6 FEHFNLDENLIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQLIESDIQEPQAIVVAPTRELA 85
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 86 QQLYQVAMHLVKFkKGINVKLFIGGTDLEKDKQRCNHQPQLIIGTPTRINDLAHSGYLHAHLASYLIIDEADLMIDLGLI 165
Cdd:cd18045 81 VQIQKVLLALGDY-MNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFK 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 488377159 166 EDVDHIAARLDNeNAHLAVFSATIPKSLQPFLNKYLSQP 204
Cdd:cd18045 160 EQIYDVYRYLPP-ATQVVLVSATLPQDILEMTNKFMTDP 197
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
19-222 |
3.60e-37 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 134.93 E-value: 3.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 19 VKNLNFEKPTEIQNRIIPRILKGT-NLIGQSQTGTGKSHAFLLPLIQLIESDiQEPQAIVVAPTRELAQQLYQVAMHLVK 97
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEALKRG-KGGRVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 98 FKKGINVkLFIGGTDLEKDKQRC-NHQPQLIIGTPTRINDLAHSGYLHAHLASYLIIDEADLMIDLGLIEDVDHIAARLd 176
Cdd:smart00487 80 SLGLKVV-GLYGGDSKREQLRKLeSGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLL- 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488377159 177 NENAHLAVFSATIPKSLQPFLNKYLSQPEFVVVDGKAHnkENIEFY 222
Cdd:smart00487 158 PKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFTPL--EPIEQF 201
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
6-206 |
5.98e-37 |
|
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: 134.27 E-value: 5.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 6 FEHFNLDENLIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQLIESDIQEPQAIVVAPTRELA 85
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 86 qqlYQVAMHLVKFKKGINVK--LFIGGTDLEKDKQRCNHQPQLIIGTPTRINDLAHSGYLHA---HLASYLIIDEADLMI 160
Cdd:cd17955 81 ---YQIAEQFRALGAPLGLRccVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDTTkvlSRVKFLVLDEADRLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488377159 161 DLGLIEDVDHIAARLDNENAHLaVFSATIPKSLQPFLNKYLSQPEF 206
Cdd:cd17955 158 TGSFEDDLATILSALPPKRQTL-LFSATLTDALKALKELFGNKPFF 202
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
11-204 |
2.79e-36 |
|
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: 132.31 E-value: 2.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 11 LDENLIEAVKNLNFEKPTEIQNRIIPRILKGT--NLIGQSQTGTGKSHAFLLPLIQLIESDIQEPQAIVVAPTRELAQQL 88
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDPpeNLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 89 YQVAMHLVKFkKGINVKLFIGGTDLEKDKqrcNHQPQLIIGTPTRINDLAHSGYLHAHLASYLIIDEADLMIDL-GLIED 167
Cdd:cd17963 81 GEVVEKMGKF-TGVKVALAVPGNDVPRGK---KITAQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGHGDQ 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 488377159 168 VDHIaARLDNENAHLAVFSATIPKSLQPFLNKYLSQP 204
Cdd:cd17963 157 SIRI-KRMLPRNCQILLFSATFPDSVRKFAEKIAPNA 192
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
15-209 |
1.04e-35 |
|
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: 130.79 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 15 LIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQLIESDIQE--PQAIVVAPTRELAQQLYqva 92
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKkgLRALILAPTRELASQIY--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 93 MHLVKFKKGINVK---LFIGGTDLEKDKQRCNHQPQLIIGTPTRINDLAHSGYLHAHLASYLIIDEADLMIDLGLIEDVD 169
Cdd:cd17957 78 RELLKLSKGTGLRivlLSKSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488377159 170 HIAARLDNENAHLAVFSATIPKSLQPFLNKYLSQPEFVVV 209
Cdd:cd17957 158 EILAACTNPNLQRSLFSATIPSEVEELARSVMKDPIRIIV 197
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
6-204 |
1.77e-34 |
|
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: 127.43 E-value: 1.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 6 FEHFNLDENLIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQLIESDIQEPQAIVVAPTRELA 85
Cdd:cd17954 2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTRELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 86 qqlYQVAMHLVKFKKGINVK--LFIGGTDLEKDKQRCNHQPQLIIGTPTRINDlahsgylhaHLAS----------YLII 153
Cdd:cd17954 82 ---QQISEQFEALGSSIGLKsaVLVGGMDMMAQAIALAKKPHVIVATPGRLVD---------HLENtkgfslkslkFLVM 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488377159 154 DEADLMIDLGLIEDVDHIAARLDNENAHLaVFSATIPKSLQPFLNKYLSQP 204
Cdd:cd17954 150 DEADRLLNMDFEPEIDKILKVIPRERTTY-LFSATMTTKVAKLQRASLKNP 199
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
15-204 |
2.48e-34 |
|
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: 126.99 E-value: 2.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 15 LIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQ-LIESDIQEP--QAIVVAPTRELAQQLYQV 91
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILErLLYRPKKKAatRVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 92 AMHLVKFkKGINVKLFIGGTDLEKDKQRCNHQPQLIIGTPTRINDLAH-SGYLHAHLASYLIIDEADLMIDLGLIEDVDH 170
Cdd:cd17947 81 LQQLAQF-TDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRnSPSFDLDSIEILVLDEADRMLEEGFADELKE 159
|
170 180 190
....*....|....*....|....*....|....
gi 488377159 171 IaARLDNENAHLAVFSATIPKSLQPFLNKYLSQP 204
Cdd:cd17947 160 I-LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKP 192
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
18-209 |
4.20e-34 |
|
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: 126.25 E-value: 4.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 18 AVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQLIESDIQEPQ----AIVVAPTRELAQQLYQVam 93
Cdd:cd17941 4 GLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTPEdglgALIISPTRELAMQIFEV-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 94 hLVKFKKGINVK--LFIGGTDLEKDKQRCnHQPQLIIGTPTRIndLAH---SGYLHAHLASYLIIDEADLMIDLGLIEDV 168
Cdd:cd17941 82 -LRKVGKYHSFSagLIIGGKDVKEEKERI-NRMNILVCTPGRL--LQHmdeTPGFDTSNLQMLVLDEADRILDMGFKETL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488377159 169 DHIAARLDNENAHLaVFSATIPKSLQPFLNKYLSQPEFVVV 209
Cdd:cd17941 158 DAIVENLPKSRQTL-LFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
11-204 |
7.98e-34 |
|
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of infectious West Nile virus particles. New research suggests that DDX56 relocalizes to the site of virus assembly during WNV infection and that its interaction with WNV capsid in the cytoplasm may occur transiently during virion morphogenesis. DDX56 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350719 [Multi-domain] Cd Length: 206 Bit Score: 125.77 E-value: 7.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 11 LDENLIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQLI------ESDIQEPQAIVVAPTREL 84
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlkakaeSGEEQGTRALILVPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 85 AQQLYQVAMHLVKF-KKGINVKLFIGGTDLEKDKQRCNHQPQLIIGTPTRINDLAHSGYLH--AHLaSYLIIDEADLMID 161
Cdd:cd17961 81 AQQVSKVLEQLTAYcRKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLllSTL-KYLVIDEADLVLS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488377159 162 LGLIEDVDHIAARLDNeNAHLAVFSATIPKSLQPFLNKYLSQP 204
Cdd:cd17961 160 YGYEEDLKSLLSYLPK-NYQTFLMSATLSEDVEALKKLVLHNP 201
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
6-189 |
8.54e-33 |
|
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350696 [Multi-domain] Cd Length: 204 Bit Score: 123.20 E-value: 8.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 6 FEHFNLDENLIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQLIesdiqepQAIVVAPTRELA 85
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV-------VALILEPSRELA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 86 QQLYQVAMHLVKFKKG--INVKLFIGGTDLEKDKQRCNHQPQLIIGTPTRINDLAHSGYLHAHLASYLIIDEADLMIDLG 163
Cdd:cd17938 74 EQTYNCIENFKKYLDNpkLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQG 153
|
170 180 190
....*....|....*....|....*....|.
gi 488377159 164 LIEDVDHIAARL-----DNENAHLAVFSATI 189
Cdd:cd17938 154 NLETINRIYNRIpkitsDGKRLQVIVCSATL 184
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
15-208 |
2.53e-32 |
|
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: 121.42 E-value: 2.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 15 LIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLP-LIQLIESDIQE-----PQAIVVAPTRELAQql 88
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPgFIHLDLQPIPReqrngPGVLVLTPTRELAL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 89 yQVAMHLVKFK-KGINVKLFIGGTDLEKDKQRCNHQPQLIIGTPTRINDLAHSGYLHAHLASYLIIDEADLMIDLGLIED 167
Cdd:cd17958 79 -QIEAECSKYSyKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQ 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488377159 168 VDHIA--ARLDNenaHLAVFSATIPKSLQPFLNKYLSQPEFVV 208
Cdd:cd17958 158 IRKILldIRPDR---QTIMTSATWPDGVRRLAQSYLKDPMIVY 197
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
11-204 |
5.00e-32 |
|
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: 121.72 E-value: 5.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 11 LDENLIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLI-----QLIESDIQEPQAIVVAPTRELA 85
Cdd:cd17953 19 LSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFrhikdQRPVKPGEGPIGLIMAPTRELA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 86 QQLYQvamHLVKFKK--GINVKLFIGGTDLEKDKQRCNHQPQLIIGTPTRINDL--AHSGYL-HAHLASYLIIDEADLMI 160
Cdd:cd17953 99 LQIYV---ECKKFSKalGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDIltANNGRVtNLRRVTYVVLDEADRMF 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488377159 161 DLGLIEDVDHI--AARLDNEnahLAVFSATIPKSLQPFLNKYLSQP 204
Cdd:cd17953 176 DMGFEPQIMKIvnNIRPDRQ---TVLFSATFPRKVEALARKVLHKP 218
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
15-208 |
1.38e-31 |
|
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: 119.44 E-value: 1.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 15 LIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQLIeSDIQE------PQAIVVAPTRELAQQL 88
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHI-MDQRElekgegPIAVIVAPTRELAQQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 89 YQVAMhlvKFKK--GINVKLFIGGTDLEKDKQRCNHQPQLIIGTPTRINDLAHSGYLHAHLASYLIIDEADLMIDLGLIE 166
Cdd:cd17952 80 YLEAK---KFGKayNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEY 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488377159 167 DVDHIAARLDNENAHLaVFSATIPKSLQPFLNKYLSQPEFVV 208
Cdd:cd17952 157 QVRSIVGHVRPDRQTL-LFSATFKKKIEQLARDILSDPIRVV 197
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
19-208 |
1.49e-31 |
|
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: 120.00 E-value: 1.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 19 VKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQLI---ESDIQEPQ---AIVVAPTRELAQQLYQVA 92
Cdd:cd17949 6 KSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLlslEPRVDRSDgtlALVLVPTRELALQIYEVL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 93 MHLVKFKKGINVKLFIGGTDLEKDKQR----CNhqpqLIIGTPTRINDlahsgylhaHLAS----------YLIIDEADL 158
Cdd:cd17949 86 EKLLKPFHWIVPGYLIGGEKRKSEKARlrkgVN----ILIATPGRLLD---------HLKNtqsfdvsnlrWLVLDEADR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488377159 159 MIDLGLIEDVDHIAARLDNENAHLAVF------------SATIPKSLQPFLNKYLSQPEFVV 208
Cdd:cd17949 153 LLDMGFEKDITKILELLDDKRSKAGGEkskpsrrqtvlvSATLTDGVKRLAGLSLKDPVYID 214
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
15-194 |
8.40e-31 |
|
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: 118.50 E-value: 8.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 15 LIEAVKNLNFEKPTEIQNRIIPRILK-GTNLIGQSQTGTGKSHAFLLPLIQLIESDIQE---------PQAIVVAPTREL 84
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLLSQKSSngvggkqkpLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 85 AQqlyQVAMHLVKFKKGINVKL--FIGGTDLEKDKQRCNHQPQLIIGTPTRINDLAHSGYLHA---HLASYLIIDEADLM 159
Cdd:cd17946 81 AV---QVKDHLKAIAKYTNIKIasIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLanlKSLRFLVLDEADRM 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488377159 160 IDLGLIEDVDHIAARLDNENAHLA------VFSATIPKSLQ 194
Cdd:cd17946 158 LEKGHFAELEKILELLNKDRAGKKrkrqtfVFSATLTLDHQ 198
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
15-207 |
3.09e-30 |
|
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: 116.28 E-value: 3.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 15 LIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLI-QLIESDI-------QEPQAIVVAPTRELAQ 86
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLImFALEQEKklpfikgEGPYGLIVCPSRELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 87 QLYQVAMHLVK-FKKG----INVKLFIGGTDLEKDKQRCNHQPQLIIGTPTRINDLAHSGYLHAHLASYLIIDEADLMID 161
Cdd:cd17951 81 QTHEVIEYYCKaLQEGgypqLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488377159 162 LGLIEDVDHIAARLDNENAHLaVFSATIPKSLQPFLNKYLSQPEFV 207
Cdd:cd17951 161 MGFEEDIRTIFSYFKGQRQTL-LFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
15-208 |
1.09e-29 |
|
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350724 [Multi-domain] Cd Length: 197 Bit Score: 114.39 E-value: 1.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 15 LIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLI------QLIESDiQEPQAIVVAPTRELAQQL 88
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIvhinaqPPLERG-DGPIVLVLAPTRELAQQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 89 YQVAmhlVKFKKGINVK--LFIGGTDLEKDKQRCNHQPQLIIGTPTRINDLAHSGYLHAHLASYLIIDEADLMIDLGLIE 166
Cdd:cd17966 80 QQEA---NKFGGSSRLRntCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488377159 167 DVDHIAARLdNENAHLAVFSATIPKSLQPFLNKYLSQPEFVV 208
Cdd:cd17966 157 QIRKIVDQI-RPDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
230-339 |
1.80e-28 |
|
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: 108.07 E-value: 1.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 230 AKVDKTLELIDILNPYLCIIFCNSRENADElADTLNKEGIKIGMIHGGLTPRERKQQMKRIRNLDFQFVIASDLASRGID 309
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 488377159 310 IEGVSHVINFDVPNDIDFFTHRVGRTGRGN 339
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
18-188 |
9.81e-28 |
|
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: 108.99 E-value: 9.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 18 AVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQLIESDIQEPQ----AIVVAPTRELAQQLYQVAM 93
Cdd:cd17942 4 AIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRngtgVIIISPTRELALQIYGVAK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 94 HLVKFKKgINVKLFIGGTDLEKDKQRCNHQPQLIIGTPTRINDlaH----SGYLHAHLASyLIIDEADLMIDLGLIEDVD 169
Cdd:cd17942 84 ELLKYHS-QTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLD--HlqntKGFLYKNLQC-LIIDEADRILEIGFEEEMR 159
|
170
....*....|....*....
gi 488377159 170 HIAARLDNENAHLaVFSAT 188
Cdd:cd17942 160 QIIKLLPKRRQTM-LFSAT 177
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
6-201 |
1.04e-27 |
|
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: 110.51 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 6 FEHFNLDENLIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQLI------ESDIQE------- 72
Cdd:cd18051 23 FSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIyeqgpgESLPSEsgyygrr 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 73 ---PQAIVVAPTRELAQQLYQVAMhlvKF--KKGINVKLFIGGTDLE---KDKQRCNHqpqLIIGTPTRINDLAHSGYLH 144
Cdd:cd18051 103 kqyPLALVLAPTRELASQIYDEAR---KFayRSRVRPCVVYGGADIGqqmRDLERGCH---LLVATPGRLVDMLERGKIG 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488377159 145 AHLASYLIIDEADLMIDLGLIEDVDHIAARLD---NENAHLAVFSATIPKSLQ----PFLNKYL 201
Cdd:cd18051 177 LDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTmppTGERQTLMFSATFPKEIQmlarDFLDNYI 240
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
15-204 |
3.38e-27 |
|
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: 107.63 E-value: 3.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 15 LIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQLIESDIQEPQAIVVAPTRELAQQLYQVAMH 94
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 95 LVKFKKGINVKLFIGGTDLEKDKQRCNHQPQLIIGTPTRINDLAHSGYLHAHLASYLIIDEADLMIDLGLIEDVDHIAAR 174
Cdd:cd17962 81 LMKGLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILEN 160
|
170 180 190
....*....|....*....|....*....|
gi 488377159 175 LDNENAHLaVFSATIPKSLQPFLNKYLSQP 204
Cdd:cd17962 161 ISHDHQTI-LVSATIPRGIEQLAGQLLQNP 189
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
6-201 |
8.44e-27 |
|
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, G17P1, or HUMP68) is involved in pathways that include the alteration of RNA structures, plays a role as a coregulator of transcription, a regulator of splicing, and in the processing of small noncoding RNAs. It synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. Dysregulation of this gene may play a role in cancer development. DDX5 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350807 [Multi-domain] Cd Length: 234 Bit Score: 107.79 E-value: 8.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 6 FEHFNLDENLIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQLIESD--IQE---PQAIVVAP 80
Cdd:cd18049 26 FYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQpfLERgdgPICLVLAP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 81 TRELAQQLYQVAMHLVKFKKgINVKLFIGGT-------DLEKDKQRCnhqpqliIGTPTRINDLAHSGYLHAHLASYLII 153
Cdd:cd18049 106 TRELAQQVQQVAAEYGRACR-LKSTCIYGGApkgpqirDLERGVEIC-------IATPGRLIDFLEAGKTNLRRCTYLVL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488377159 154 DEADLMIDLGLIEDVDHIAARLDNENAHLaVFSATIPKSL----QPFLNKYL 201
Cdd:cd18049 178 DEADRMLDMGFEPQIRKIVDQIRPDRQTL-MWSATWPKEVrqlaEDFLKDYI 228
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
30-210 |
2.04e-26 |
|
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: 105.70 E-value: 2.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 30 IQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQLIESDIQE------PQAIVVAPTRELAQQlyqVAMHLVKFKKGIN 103
Cdd:cd17944 16 IQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPrkrgraPKVLVLAPTRELANQ---VTKDFKDITRKLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 104 VKLFIGGTDLEKDKQRCNHQPQLIIGTPTRINDLAHSGYLHAHLASYLIIDEADLMIDLGL---IEDVDHIAARLDNE-N 179
Cdd:cd17944 93 VACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFaeqVEEILSVSYKKDSEdN 172
|
170 180 190
....*....|....*....|....*....|.
gi 488377159 180 AHLAVFSATIPKSLQPFLNKYLsQPEFVVVD 210
Cdd:cd17944 173 PQTLLFSATCPDWVYNVAKKYM-KSQYEQVD 202
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
15-199 |
4.49e-25 |
|
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: 102.83 E-value: 4.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 15 LIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQ-------LIESDIQEPQAIVVAPTRELAQQ 87
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQrllryklLAEGPFNAPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 88 LYQVAMHLVKfKKGINVKLFIGGTDLEKDKQRCNHQPQLIIGTPTRINDLAHSGYLHAHLASYLIIDEADLMIDLGLIED 167
Cdd:cd17948 81 IGSVAQSLTE-GLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488377159 168 VDHIAAR---------LDNEN---AHLAVFSATIPKSLQPFLNK 199
Cdd:cd17948 160 LSHFLRRfplasrrseNTDGLdpgTQLVLVSATMPSGVGEVLSK 203
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
258-339 |
5.38e-25 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 97.67 E-value: 5.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 258 DELADTLNKEGIKIGMIHGGLTPRERKQQMKRIRNLDFQFVIASDLASRGIDIEGVSHVINFDVPNDIDFFTHRVGRTGR 337
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 488377159 338 GN 339
Cdd:smart00490 81 AG 82
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
6-201 |
6.88e-25 |
|
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: 103.17 E-value: 6.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 6 FEHFNLDENLIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQLIESDI-----QEPQAIVVAP 80
Cdd:cd18050 64 FHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPylergDGPICLVLAP 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 81 TRELAQQLYQVAMHLVKFKKgINVKLFIGGT-------DLEKDKQRCnhqpqliIGTPTRINDLAHSGYLHAHLASYLII 153
Cdd:cd18050 144 TRELAQQVQQVADDYGKSSR-LKSTCIYGGApkgpqirDLERGVEIC-------IATPGRLIDFLEAGKTNLRRCTYLVL 215
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488377159 154 DEADLMIDLGLIEDVDHIAARLDNENAHLaVFSATIPKSLQPFLNKYL 201
Cdd:cd18050 216 DEADRMLDMGFEPQIRKIVDQIRPDRQTL-MWSATWPKEVRQLAEDFL 262
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
6-207 |
7.71e-25 |
|
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH) is a testis-specific protein essential for completion of spermatogenesis. DDX25 is also a novel negative regulator of IFN pathway and facilitates RNA virus infection. Diseases associated with DDX25 include hydrolethalus syndrome, an autosomal recessive lethal malformation syndrome characterized by multiple developmental defects of fetus.. DDX25 (also called gonadotropin-regulated testicular RNA helicase) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350806 [Multi-domain] Cd Length: 229 Bit Score: 102.02 E-value: 7.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 6 FEHFNLDENLIEAVKNLNFEKPTEIQNRIIPRILKG--TNLIGQSQTGTGKSHAFLLPLIQLIESDIQEPQAIVVAPTRE 83
Cdd:cd18048 20 FEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLSPTFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 84 LAQQLYQVAMHLVKFKKGINVKLFIGGTDLEKDKQRcnhQPQLIIGTPTRINDLAHSGYL-HAHLASYLIIDEADLMIDL 162
Cdd:cd18048 100 LALQTGKVVEEMGKFCVGIQVIYAIRGNRPGKGTDI---EAQIVIGTPGTVLDWCFKLRLiDVTNISVFVLDEADVMINV 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488377159 163 GLIEDVDHIAARLDNENAHLAVFSATIPKSLQPFLNKYLSQPEFV 207
Cdd:cd18048 177 QGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNII 221
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
6-207 |
2.18e-20 |
|
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: 89.01 E-value: 2.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 6 FEHFNLDENLIEAVKNLNFEKPTEIQNRIIPRILKG--TNLIGQSQTGTGKSHAFLLPLIQLIESDIQEPQAIVVAPTRE 83
Cdd:cd18047 3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 84 LAQQLYQVAMHLVKFKKGINVKLFIGGTDLEKDKQRcnhQPQLIIGTPTRINDLA-HSGYLHAHLASYLIIDEADLMIDL 162
Cdd:cd18047 83 LALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKI---SEQIVIGTPGTVLDWCsKLKFIDPKKIKVFVLDEADVMIAT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488377159 163 GLIEDVDHIAARLDNENAHLAVFSATIPKSLQPFLNKYLSQPEFV 207
Cdd:cd18047 160 QGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVI 204
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
10-351 |
1.47e-19 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 91.44 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 10 NLDENLIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQLIESDiQEPQAIVVAPTRELAQ-QL 88
Cdd:COG1205 40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLED-PGATALYLYPTKALARdQL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 89 YQVAMHLVKFKKGINVKLFIGGTDLEkDKQRCNHQPQLIIGTPtrinDLAHSGYLHAH------LAS--YLIIDEAdlmi 160
Cdd:COG1205 119 RRLRELAEALGLGVRVATYDGDTPPE-ERRWIREHPDIVLTNP----DMLHYGLLPHHtrwarfFRNlrYVVIDEA---- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 161 dlgliedvdH-------------------IAARLDNEnahlAVF---SATI--PKSlqpFLNKyLSQPEFVVV--DGKAH 214
Cdd:COG1205 190 ---------HtyrgvfgshvanvlrrlrrICRHYGSD----PQFilaSATIgnPAE---HAER-LTGRPVTVVdeDGSPR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 215 NKENIEFYLIP-TKGSAKVDKTLELIDIL-----NPYLCIIFCNSRENADELADTLNKE------GIKIGMIHGGLTPRE 282
Cdd:COG1205 253 GERTFVLWNPPlVDDGIRRSALAEAARLLadlvrEGLRTLVFTRSRRGAELLARYARRAlrepdlADRVAAYRAGYLPEE 332
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488377159 283 RKQQMKRIRNLDFQFVIAS---DLasrGIDIEGVSHVINFDVPNDIDFFTHRVGRTGRGNYKGVAITLYGPD 351
Cdd:COG1205 333 RREIERGLRSGELLGVVSTnalEL---GIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVLVAGDD 401
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
50-317 |
1.79e-19 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 90.85 E-value: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 50 TGTGKSHAFLLpliqLIESDIQEPQAIVVAPTRELAQQLYQvamhlvKFKKGINVKLFIGGtdlEKDKQRcnhqpQLIIG 129
Cdd:COG1061 109 TGTGKTVLALA----LAAELLRGKRVLVLVPRRELLEQWAE------ELRRFLGDPLAGGG---KKDSDA-----PITVA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 130 TPTRINDLAHSGYLHAHlASYLIIDEADLMIDLGLIEDVDHIAA-----------RLDNENAHLA-----VFSATIPKSL 193
Cdd:COG1061 171 TYQSLARRAHLDELGDR-FGLVIIDEAHHAGAPSYRRILEAFPAayrlgltatpfRSDGREILLFlfdgiVYEYSLKEAI 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 194 QpflNKYLSQPEFVVVDGK--------AHNKENIEFYLIPtkGSAKVDKTLEliDILNPYL----CIIFCNSRENADELA 261
Cdd:COG1061 250 E---DGYLAPPEYYGIRVDltderaeyDALSERLREALAA--DAERKDKILR--ELLREHPddrkTLVFCSSVDHAEALA 322
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 488377159 262 DTLNKEGIKIGMIHGGLTPRERKQQMKRIRNLDFQFVIASDLASRGIDIEGVSHVI 317
Cdd:COG1061 323 ELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI 378
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
15-208 |
2.43e-18 |
|
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: 83.84 E-value: 2.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 15 LIEAVKNLNFEKPTEIQNRIIPRILKGTNLIGQSQ---------TGTGKSHAFLLPLIQLIeSDIQEPQ--AIVVAPTRE 83
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSSKSTPPYRpgdlcvsapTGSGKTLAYVLPIVQAL-SKRVVPRlrALIVVPTKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 84 LAQQLYQVAMHLVKfKKGINVKLFIGGTDLEKDKQRCNHQ--------PQLIIGTPTRIndLAH----SGYLHAHLaSYL 151
Cdd:cd17956 80 LVQQVYKVFESLCK-GTGLKVVSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRL--VDHlnstPGFTLKHL-RFL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488377159 152 IIDEADLMIDLGLIEDVDHIAARLDNE-------------------NAHLAVFSATI---PKSLQpFLNkyLSQPEFVV 208
Cdd:cd17956 156 VIDEADRLLNQSFQDWLETVMKALGRPtapdlgsfgdanllersvrPLQKLLFSATLtrdPEKLS-SLK--LHRPRLFT 231
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
41-188 |
3.51e-16 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 75.13 E-value: 3.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 41 GTNLIGQSQTGTGKSHAFLLPLIQLIESdiQEPQAIVVAPTRELAQQLYQVAMHLvkFKKGINVKLFIGGTDLEKDKQRC 120
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLK--KGKKVLVLVPTKALALQTAERLREL--FGPGIRVAVLVGGSSAEEREKNK 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488377159 121 NHQPQLIIGTPTRI-NDLAHSGYLHAHLASYLIIDEADLMIDLG---LIEDVDHIAARLDneNAHLAVFSAT 188
Cdd:cd00046 77 LGDADIIIATPDMLlNLLLREDRLFLKDLKLIIVDEAHALLIDSrgaLILDLAVRKAGLK--NAQVILLSAT 146
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
11-199 |
4.27e-16 |
|
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 (MRH4) plays an essential role during the late stages of mitochondrial ribosome or mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions. MRH4 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350723 [Multi-domain] Cd Length: 251 Bit Score: 77.80 E-value: 4.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 11 LDENLIEAVKNLNFEKPTEIQNRIIPRILKgtNLIGQ------------------SQTGTGKSHAFLLPLIQ-LIESDIQ 71
Cdd:cd17965 15 IKEILKGSNKTDEEIKPSPIQTLAIKKLLK--TLMRKvtkqtsneepklevfllaAETGSGKTLAYLAPLLDyLKRQEQE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 72 E----------------PQAIVVAPTRELAQQLYQVAM---HLVKFkkGINVkLFIGGTDLEKDKQRCNHQP-QLIIGTP 131
Cdd:cd17965 93 PfeeaeeeyesakdtgrPRSVILVPTHELVEQVYSVLKklsHTVKL--GIKT-FSSGFGPSYQRLQLAFKGRiDILVTTP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488377159 132 TRINDLAHSGYLHAHLASYLIIDEADLMIDLGLIEDVDHIAARLDNENaHLAVFSATIPKSLQPFLNK 199
Cdd:cd17965 170 GKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLK-HLILCSATIPKEFDKTLRK 236
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
217-348 |
4.04e-14 |
|
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: 69.16 E-value: 4.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 217 ENIEFYLIPTKGSAKVDKTLELIDILNPYLC-IIFCNSRENADELADTLNKEGIKIGMIHGGLTPRERKQQMKRIRNLDF 295
Cdd:cd18794 2 PNLFYSVRPKDKKDEKLDLLKRIKVEHLGGSgIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKI 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 488377159 296 QFVIASDLASRGIDIEGVSHVINFDVPNDIDFFTHRVGRTGRGNYKGVAITLY 348
Cdd:cd18794 82 QVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
248-350 |
2.98e-12 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 68.59 E-value: 2.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 248 IIFCNSRENADELADTLNKEGIKIGMIHGGLTPRERKQQMKRIRNLDFQFVIASDLASRGIDIEGVSHVINFDVPNDIDF 327
Cdd:PRK11057 240 IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIES 319
|
90 100
....*....|....*....|...
gi 488377159 328 FTHRVGRTGRGNYKGVAITLYGP 350
Cdd:PRK11057 320 YYQETGRAGRDGLPAEAMLFYDP 342
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
231-339 |
3.57e-12 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 68.60 E-value: 3.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 231 KVDKTLELID-ILNPYL---CIIFCNSRENADELADTLNKEGIKIGMIHG--------GLTPRERKQQMKRIRNLDFQFV 298
Cdd:COG1111 336 KLSKLREILKeQLGTNPdsrIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGqaskegdkGLTQKEQIEILERFRAGEFNVL 415
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 488377159 299 IASDLASRGIDIEGVSHVINFD-VPNDIDFFtHRVGRTGRGN 339
Cdd:COG1111 416 VATSVAEEGLDIPEVDLVIFYEpVPSEIRSI-QRKGRTGRKR 456
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
229-322 |
7.58e-12 |
|
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: 62.49 E-value: 7.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 229 SAKVDKTLELIDIL--NPYLCIIFCNSRENADELADTLNKEGIKIGMIHGGLTPRERKQQMKRIRNLD--FQFVIASDLA 304
Cdd:cd18793 10 SGKLEALLELLEELrePGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdiRVFLLSTKAG 89
|
90
....*....|....*...
gi 488377159 305 SRGIDIEGVSHVINFDVP 322
Cdd:cd18793 90 GVGLNLTAANRVILYDPW 107
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
31-156 |
2.01e-11 |
|
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: 62.60 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 31 QNRIIPRILKGTNLIGQSQTGTGKSHAFLLPLIQLIESDiQEPQAIVVAPTRELAQ-QLYQVAMHLVKFKKGINVKLFIG 109
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRD-PGSRALYLYPTKALAQdQLRSLRELLEQLGLGIRVATYDG 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 488377159 110 GTDLEKDKQRCNHQPQLIIGTPtrinDLAHSGYLHAHLAS--------YLIIDEA 156
Cdd:cd17923 84 DTPREERRAIIRNPPRILLTNP----DMLHYALLPHHDRWarflrnlrYVVLDEA 134
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
164-322 |
3.83e-11 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 65.25 E-value: 3.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 164 LIEDVDHIAARLDNENAHLAVFSATIpkslqpflnkYLSQpefvVVDGKAHNKENIEFYLIPtkgSAKVDKTLELID--I 241
Cdd:COG0553 484 VLEYLRRELEGAEGIRRRGLILAALT----------RLRQ----ICSHPALLLEEGAELSGR---SAKLEALLELLEelL 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 242 LNPYLCIIFCNSRENADELADTLNKEGIKIGMIHGGLTPRERKQQMKRIRNLD--FQFVIASDLASRGIDIEGVSHVINF 319
Cdd:COG0553 547 AEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGGEGLNLTAADHVIHY 626
|
...
gi 488377159 320 DVP 322
Cdd:COG0553 627 DLW 629
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
215-351 |
6.19e-11 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 64.01 E-value: 6.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 215 NKENIEFYLIPTKGSAKVDKTLELIDILNPYLCIIFCNSRENADELADTLNKEGIKIGMIHGGLTPRERKQQMKRIRNLD 294
Cdd:COG0514 201 DRPNLRLEVVPKPPDDKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDE 280
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 488377159 295 FQFVIAsdlasrGIDIEGVSHVINFDVPNDIDFFTHRVGRTGRGNYKGVAITLYGPD 351
Cdd:COG0514 281 VDVIVAtiafgmGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPE 337
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
44-370 |
9.35e-11 |
|
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: 63.22 E-value: 9.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 44 LIGQSQTGTGKSHAFLLPLIQLIESDIqEPQAIVVAPTRELAQQLYQVAMHLVK-------FKKGINVKLFIGGTDLEKD 116
Cdd:cd09639 2 LVIEAPTGYGKTEAALLWALHSLKSQK-ADRVIIALPTRATINAMYRRAKEAFGetglyhsSILSSRIKEMGDSEEFEHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 117 KQRCNHQPQLIIGTPTRINDLAH---------SGYLHAHLA---SYLIIDEADLMID--LGLIEDVDHIAARLDnenAHL 182
Cdd:cd09639 81 FPLYIHSNDTLFLDPITVCTIDQvlksvfgefGHYEFTLASianSLLIFDEVHFYDEytLALILAVLEVLKDND---VPI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 183 AVFSATIPKSLQPFLNKYLsqpefVVVDGKAHNKENIEFYLIPTKGSAKVDKTLELIDILNPYL----CIIFCNSRENAD 258
Cdd:cd09639 158 LLMSATLPKFLKEYAEKIG-----YVEENEPLDLKPNERAPFIKIESDKVGEISSLERLLEFIKkggsVAIIVNTVDRAQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 259 ELADTLNKEG--IKIGMIHGGLTP--RERKQQMKRIRNLDFQ--FVIASDLASRGIDiegvshvINFDV----PNDIDFF 328
Cdd:cd09639 233 EFYQQLKEKGpeEEIMLIHSRFTEkdRAKKEAELLLEFKKSEkfVIVATQVIEASLD-------ISVDVmiteLAPIDSL 305
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 488377159 329 THRVGRTGRGNYKgvaitlYGPDEESNITLIEDKGYKFKNVD 370
Cdd:cd09639 306 IQRLGRLHRYGEK------NGEEVYIITDAPDGKGQKPYPYD 341
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
247-348 |
2.54e-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: 56.56 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 247 CIIFCNSRENADELADTLnkegikigmihggltprerkqqmkrirnldfQFVIASDLASRGIDIEGVSHVINFDVPNDID 326
Cdd:cd18785 6 IIVFTNSIEHAEEIASSL-------------------------------EILVATNVLGEGIDVPSLDTVIFFDPPSSAA 54
|
90 100
....*....|....*....|..
gi 488377159 327 FFTHRVGRTGRGNYKGVAITLY 348
Cdd:cd18785 55 SYIQRVGRAGRGGKDEGEVILF 76
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
12-193 |
1.63e-09 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 57.04 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 12 DENLIEA-VKNLNFeKPTEIQNRIIPRILKG------TNLIGQSQTGTGKSHAFLLPLIQLIESDiqePQAIVVAPTREL 84
Cdd:cd17918 1 DRALIQElCKSLPF-SLTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAALLAYKNG---KQVAILVPTEIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 85 AQQLYQVAmhlVKFKKGINVKLFIGGTDlEKDKQrcnhQPQLIIGTPTRINDLAHSgylhaHLASYLIIDEADLMidlgl 164
Cdd:cd17918 77 AHQHYEEA---RKFLPFINVELVTGGTK-AQILS----GISLLVGTHALLHLDVKF-----KNLDLVIVDEQHRF----- 138
|
170 180 190
....*....|....*....|....*....|
gi 488377159 165 ieDVDHIAARLDNENAHLAVFSAT-IPKSL 193
Cdd:cd17918 139 --GVAQREALYNLGATHFLEATATpIPRTL 166
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
231-340 |
3.16e-09 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 59.12 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 231 KVDKTLELI-DIL--NP-YLCIIFCNSRENADELADTLNKEGIKIGMIHG--------GLTPRERKQQMKRIRNLDFQFV 298
Cdd:PRK13766 348 KLEKLREIVkEQLgkNPdSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGqaskdgdkGMSQKEQIEILDKFRAGEFNVL 427
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 488377159 299 IASDLASRGIDIEGVSHVINFD-VPNDIDFFtHRVGRTGRGNY 340
Cdd:PRK13766 428 VSTSVAEEGLDIPSVDLVIFYEpVPSEIRSI-QRKGRTGRQEE 469
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
220-334 |
1.07e-07 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350189 [Multi-domain] Cd Length: 142 Bit Score: 50.67 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 220 EFYLIPtkgsakvdKTLELIDILNPYL-------CIIFCNSRENADELADTLNKEGIK---------IGMIHG------G 277
Cdd:cd18802 2 EIVVIP--------KLQKLIEILREYFpktpdfrGIIFVERRATAVVLSRLLKEHPSTlafircgflIGRGNSsqrkrsL 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 488377159 278 LTPRERKQQMKRIRNLDFQFVIASDLASRGIDIEGVSHVINFDVPNDIDFFTHRVGR 334
Cdd:cd18802 74 MTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR 130
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
247-310 |
1.19e-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: 49.87 E-value: 1.19e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488377159 247 CIIFCNSRENADELADTLNKEGIKIGMIHGGLTPRERKQQMKRI---RNLDFQFVIASDLASRGIDI 310
Cdd:cd18799 9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDEALILlffGELKPPILVTVDLLTTGVDI 75
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
248-339 |
9.55e-07 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350188 [Multi-domain] Cd Length: 143 Bit Score: 48.12 E-value: 9.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 248 IIFCNSRENADELADTLNK--EGIK----IGMIHG----GLTPRERKQQMKRIRNLDFQFVIASDLASRGIDIEGVSHVI 317
Cdd:cd18801 34 IIFSEFRDSAEEIVNFLSKirPGIRatrfIGQASGksskGMSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLII 113
|
90 100
....*....|....*....|...
gi 488377159 318 NFD-VPNDIDFFtHRVGRTGRGN 339
Cdd:cd18801 114 CYDaSPSPIRMI-QRMGRTGRKR 135
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
247-337 |
1.01e-06 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 48.03 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 247 CIIFCNSRENADELADTLNK------EGIKIGMIHGGLTPRERKQQMKRIRNLDFQFVIAS---DLasrGIDIEGVSHVI 317
Cdd:cd18796 41 TLVFTNTRSQAERLAQRLRElcpdrvPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATsslEL---GIDIGDVDLVI 117
|
90 100
....*....|....*....|
gi 488377159 318 NFDVPNDIDFFTHRVGRTGR 337
Cdd:cd18796 118 QIGSPKSVARLLQRLGRSGH 137
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
28-161 |
1.71e-06 |
|
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: 48.03 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 28 TEIQNRIIPRI-LKGTNLIGQSQTGTGKSHAFLLPLIQLIESdiQEPQAIVVAPTRELAQQLYQvamhlvKFKK-----G 101
Cdd:cd17921 3 NPIQREALRALyLSGDSVLVSAPTSSGKTLIAELAILRALAT--SGGKAVYIAPTRALVNQKEA------DLRErfgplG 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488377159 102 INVKLFIGGTDLEKDKQRcnhQPQLIIGTPTRINDLA-HSGYLHAHLASYLIIDEADLMID 161
Cdd:cd17921 75 KNVGLLTGDPSVNKLLLA---EADILVATPEKLDLLLrNGGERLIQDVRLVVVDEAHLIGD 132
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
247-345 |
1.92e-06 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 47.25 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 247 CIIFCNSRENAD----ELADTLNKEGIKIGMI---HGGLTPRERKQQMKRIRNLDFQFVIASDLASRGIDIEGVSHVINF 319
Cdd:cd18797 38 TIVFCRSRKLAElllrYLKARLVEEGPLASKVasyRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLA 117
|
90 100
....*....|....*....|....*.
gi 488377159 320 DVPNDIDFFTHRVGRTGRGNYKGVAI 345
Cdd:cd18797 118 GYPGSLASLWQQAGRAGRRGKDSLVI 143
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
38-190 |
2.63e-05 |
|
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: 44.63 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 38 ILKGTNLIGQSQTGTGKShafLLPLIQLIESDIQEPQAIVVAPTRELAQQLYQvamhlvKFKK----GINVKLFIGGTDl 113
Cdd:cd18028 14 LLKGENLLISIPTASGKT---LIAEMAMVNTLLEGGKALYLVPLRALASEKYE------EFKKleeiGLKVGISTGDYD- 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488377159 114 EKDKQRcnHQPQLIIGTPTRINDLAHSGYLHAHLASYLIIDEADLMIDL--GLIEDVDHIAARLDNENAHLAVFSATIP 190
Cdd:cd18028 84 EDDEWL--GDYDIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEerGPTLESIVARLRRLNPNTQIIGLSATIG 160
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
50-188 |
8.22e-05 |
|
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: 42.68 E-value: 8.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 50 TGTGKShaflLPLIQLIEsDIQEPQAIVVAPTRELAQQLYQvamHLVKFKKGINVKLFigGTDLEKDKQRCNhqpqLIIG 129
Cdd:cd17926 27 TGSGKT----LTALALIA-YLKELRTLIVVPTDALLDQWKE---RFEDFLGDSSIGLI--GGGKKKDFDDAN----VVVA 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488377159 130 TPTRINDLAHSGYLHAHLASYLIIDEAdlmidlgliedvDHIAAR-----LDNENAHLAV-FSAT 188
Cdd:cd17926 93 TYQSLSNLAEEEKDLFDQFGLLIVDEA------------HHLPAKtfseiLKELNAKYRLgLTAT 145
|
|
| SF2_C_viral |
cd18806 |
C-terminal helicase domain of viral helicase; Viral helicases in this family here are ... |
248-338 |
1.18e-04 |
|
C-terminal helicase domain of viral helicase; Viral helicases in this family here 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: 350193 [Multi-domain] Cd Length: 145 Bit Score: 42.25 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 248 IIFCNSRENADELADTLNKEGIKIGMIHGGLTPRErkqqMKRIRNLDFQFVIASDL--------ASRGIDI-EGVSHVIN 318
Cdd:cd18806 28 VWFVHSKKKGNEIAACLSGLGKNVIQLYRKLDDTE----YPKIKTIDWDFVVTTDIsemganfdADRVIDCrTCVKPTIL 103
|
90 100 110
....*....|....*....|....*....|
gi 488377159 319 FD----------VPNDIDFFTHRVGRTGRG 338
Cdd:cd18806 104 FSgdfrviltgpVPQTAASAAQRRGRTGRN 133
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
205-284 |
1.30e-04 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350182 [Multi-domain] Cd Length: 154 Bit Score: 42.15 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 205 EFVVVDGKAHNKENIEFYLIPtkgsAKVDKTLELIDILNPYL-CIIFCNSRENADELADTLnkegIKIGMIHGGLTPRER 283
Cdd:cd18795 7 EYVLGFNGLGIKLRVDVMNKF----DSDIIVLLKIETVSEGKpVLVFCSSRKECEKTAKDL----AGIAFHHAGLTREDR 78
|
.
gi 488377159 284 K 284
Cdd:cd18795 79 E 79
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
208-349 |
1.86e-04 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 44.12 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 208 VVDGKAHNKENIEFYLIPtkgsaKVDKTLELID--ILNPYL--C-IIFCNSRENADELADTLNKEGIKIGMIHGGLTPRE 282
Cdd:PLN03137 644 VVFRQSFNRPNLWYSVVP-----KTKKCLEDIDkfIKENHFdeCgIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQ 718
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488377159 283 RKQQMKRIRNLDFQFVIASDLASRGIDIEGVSHVINFDVPNDIDFFTHRVGRTGRGNYKGVAITLYG 349
Cdd:PLN03137 719 RAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGRAGRDGQRSSCVLYYS 785
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
1-309 |
6.16e-04 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 41.99 E-value: 6.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 1 MSKHPFEHFNLD--ENLIEAVKNLNFEKP---TEIQNRIIPRILKGTNL-IGQSQTGTGKSHAFLLPLIQLIEsDIQEPQ 74
Cdd:COG1203 101 MARQALDHLLAErlERLLPKKSKPRTPINplqNEALELALEAAEEEPGLfILTAPTGGGKTEAALLFALRLAA-KHGGRR 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 75 AIVVAPTRELAQQLYQVAM-----------HLVKFKKGINVKLFIGGTDLEKDKQRcNHQPQLIIGTP--------TRIN 135
Cdd:COG1203 180 IIYALPFTSIINQTYDRLRdlfgedvllhhSLADLDLLEEEEEYESEARWLKLLKE-LWDAPVVVTTIdqlfeslfSNRK 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 136 dlaHSGYLHAHLA-SYLIIDEADlMID---LGLIEDVDHIAARLdneNAHLAVFSATIPKSLQPFLNKYL----SQPEFV 207
Cdd:COG1203 259 ---GQERRLHNLAnSVIILDEVQ-AYPpymLALLLRLLEWLKNL---GGSVILMTATLPPLLREELLEAYelipDEPEEL 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 208 VVDGKAHNKENIEFYLIPTKGSAKVDKTLELIDILNPYLCIifCNSRENADELADTLNKEGIKIGMI--HGGLTPRERKQ 285
Cdd:COG1203 332 PEYFRAFVRKRVELKEGPLSDEELAELILEALHKGKSVLVI--VNTVKDAQELYEALKEKLPDEEVYllHSRFCPADRSE 409
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 488377159 286 QMKRIRN---------------------LDFQFVIaSDLAsrGID 309
Cdd:COG1203 410 IEKEIKErlergkpcilvstqvveagvdIDFDVVI-RDLA--PLD 451
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
3-350 |
6.30e-04 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 42.06 E-value: 6.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 3 KHPFEHFNLDENLIEA-VKNLNFEkPTEIQNRIIPRILKGTN-------LIgQSQTGTGKSHAFLLPLIQLIESDIQepq 74
Cdd:PRK10917 238 SKKAGPLPYDGELLKKfLASLPFE-LTGAQKRVVAEILADLAspkpmnrLL-QGDVGSGKTVVAALAALAAIEAGYQ--- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 75 AIVVAPTRELAQQLYQVAMHLvkFKK-GINVKLFIGGTdleKDKQRC-------NHQPQLIIGTptrindlahsgylHAh 146
Cdd:PRK10917 313 AALMAPTEILAEQHYENLKKL--LEPlGIRVALLTGSL---KGKERReileaiaSGEADIVIGT-------------HA- 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 147 lasyLIIDE---ADL---MID----------LGLIEdvdhiaarlDNENAHLAVFSAT-IPKSLQpfLNKY--LsqpEFV 207
Cdd:PRK10917 374 ----LIQDDvefHNLglvIIDeqhrfgveqrLALRE---------KGENPHVLVMTATpIPRTLA--MTAYgdL---DVS 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 208 VVDGKAHNKENIEFYLIPtkgSAKVDKTLELID--ILNPYLCIIFC---NSRE-----NADELADTLNKE--GIKIGMIH 275
Cdd:PRK10917 436 VIDELPPGRKPITTVVIP---DSRRDEVYERIReeIAKGRQAYVVCpliEESEkldlqSAEETYEELQEAfpELRVGLLH 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 276 GGLTPRERKQQMKRIRNldfqfviasdlasRGID-------IE-GVshvinfDVPN-------DIDFF----TH--RvGR 334
Cdd:PRK10917 513 GRMKPAEKDAVMAAFKA-------------GEIDilvattvIEvGV------DVPNatvmvieNAERFglaqLHqlR-GR 572
|
410
....*....|....*.
gi 488377159 335 TGRGNYKGVAITLYGP 350
Cdd:PRK10917 573 VGRGAAQSYCVLLYKD 588
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
28-155 |
9.02e-04 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350781 [Multi-domain] Cd Length: 206 Bit Score: 40.42 E-value: 9.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 28 TEIQNRIIPRILKGT-NLIGQSQTGTGKSHAFLLPLIQLI----ESDIQEPQAIVVAPTRELAQQLYQVAMHlvKFKK-G 101
Cdd:cd18023 3 NRIQSEVFPDLLYSDkNFVVSAPTGSGKTVLFELAILRLLkernPLPWGNRKVVYIAPIKALCSEKYDDWKE--KFGPlG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 102 INVKLFIGGTDLEKDK--QRCNhqpqLIIGTPTRINDL----AHSGYLHAHLASYLiIDE 155
Cdd:cd18023 81 LSCAELTGDTEMDDTFeiQDAD----IILTTPEKWDSMtrrwRDNGNLVQLVALVL-IDE 135
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
39-285 |
1.21e-03 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 41.42 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 39 LKGTNLIGQSQTGTGKS-----------------HAFLLPLiqliesdiqepqaivVAptreLAQQLYQVAMHlvKFKKG 101
Cdd:COG1202 223 LEGKDQLVVSATATGKTligelagiknalegkgkMLFLVPL---------------VA----LANQKYEDFKD--RYGDG 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 102 INVKLFIGGTDLEKDKQRCNHQPQLIIGTPTRINDLAHSGylhahlaSYL------IIDEADLMIDL-------GLIedv 168
Cdd:COG1202 282 LDVSIRVGASRIRDDGTRFDPNADIIVGTYEGIDHALRTG-------RDLgdigtvVIDEVHMLEDPerghrldGLI--- 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 169 dhiaARLDN--ENAHLAVFSATI--PKSLQPFLNKYLSQPEFVVVDgkahnkenIEFYLIPTKGSAKVDKTLELI----D 240
Cdd:COG1202 352 ----ARLKYycPGAQWIYLSATVgnPEELAKKLGAKLVEYEERPVP--------LERHLTFADGREKIRIINKLVkrefD 419
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 488377159 241 ILNPY----LCIIFCNSRENADELADTLnkeGIKIGMIHGGLTPRERKQ 285
Cdd:COG1202 420 TKSSKgyrgQTIIFTNSRRRCHEIARAL---GYKAAPYHAGLDYGERKK 465
|
|
| DEXHc_RecG |
cd17992 |
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in ... |
2-193 |
2.21e-03 |
|
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. It is a member of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350750 [Multi-domain] Cd Length: 225 Bit Score: 39.44 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 2 SKHPFEHFNLDENLIEAVKNLNFEkPTEIQNRIIPRI---LKGTN----LIgQSQTGTGKSHAFLLPLIQLIESDIQepq 74
Cdd:cd17992 22 ELKGIILEISGELLKKFLEALPFE-LTGAQKRVIDEIlrdLASEKpmnrLL-QGDVGSGKTVVAALAMLAAVENGYQ--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 75 AIVVAPTRELAQQLYQVAMHLVKfKKGINVKLFIGGTdleKDKQR-------CNHQPQLIIGTptrindlahsgylHAhl 147
Cdd:cd17992 97 VALMAPTEILAEQHYDSLKKLLE-PLGIRVALLTGST---KAKEKreilekiASGEIDIVIGT-------------HA-- 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488377159 148 asyLIIDEADLMiDLGL-IEDVDH-------IAARLDNENAHLAVFSAT-IPKSL 193
Cdd:cd17992 158 ---LIQEDVEFH-NLGLvIIDEQHrfgveqrLKLREKGETPHVLVMTATpIPRTL 208
|
|
| SF2_C_suv3 |
cd18805 |
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene ... |
233-302 |
3.20e-03 |
|
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene encodes a DNA and RNA helicase, which is localized in mitochondria and is a subunit of the degradosome complex involved in regulation of RNA surveillance and turnover. SUV3 exhibits DNA and RNA-dependent ATPase, DNA and RNA-binding and DNA and RNA unwinding activities. SUV3 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: 350192 [Multi-domain] Cd Length: 135 Bit Score: 37.54 E-value: 3.20e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488377159 233 DKTLELIDILNPYLCIIfCNSRENADELADTLNKE-GIKIGMIHGGLTPRERKQQMKRIR--NLDFQFVIASD 302
Cdd:cd18805 7 SKPLGSLRNLRPGDCVV-AFSRKDIFSLKREIEKRtGLKCAVIYGALPPETRRQQARLFNdpESGYDVLVASD 78
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
31-264 |
6.75e-03 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 38.71 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 31 QNRIIPRILKGTNLIGQSQTGTGKShafLLPLIQLIESDIQEPQAIVVAPTRELAQQLYQVAMHLVKFkkGINVKLFIGG 110
Cdd:PRK01172 27 QRMAIEQLRKGENVIVSVPTAAGKT---LIAYSAIYETFLAGLKSIYIVPLRSLAMEKYEELSRLRSL--GMRVKISIGD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 111 TDLEKDKQRCNhqpQLIIGTPTRINDLAHSGYLHAHLASYLIIDEADLMIDLGLIEDVDHIA--ARLDNENAHLAVFSAT 188
Cdd:PRK01172 102 YDDPPDFIKRY---DVVILTSEKADSLIHHDPYIINDVGLIVADEIHIIGDEDRGPTLETVLssARYVNPDARILALSAT 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488377159 189 IPKS--LQPFLNKYLSQPEFVVVDGKAHNKENIEFYLiPTKGSAKVDKTLELIDILNPY-LCIIFCNSRENADELADTL 264
Cdd:PRK01172 179 VSNAneLAQWLNASLIKSNFRPVPLKLGILYRKRLIL-DGYERSQVDINSLIKETVNDGgQVLVFVSSRKNAEDYAEML 256
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
255-355 |
7.33e-03 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350179 [Multi-domain] Cd Length: 160 Bit Score: 37.25 E-value: 7.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 255 ENADELADTLNKE--GIKIGMIHGGLTPRERKQQMKRIRNLDFQFVIASDLASRGIDIEGVshviNFDVPNDIDFF---- 328
Cdd:cd18792 45 KSIEALAEELKELvpEARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNA----NTMIIEDADRFglsq 120
|
90 100
....*....|....*....|....*...
gi 488377159 329 THRV-GRTGRGNYKGVAITLYGPDEESN 355
Cdd:cd18792 121 LHQLrGRVGRGKHQSYCYLLYPDPKKLT 148
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
270-352 |
9.78e-03 |
|
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: 36.55 E-value: 9.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377159 270 KIGMIHGGLTPRERKQQMKRIRNLDFQFVIASDLASRGIDIEGVSHVInfdvPNDIDFF----THRV-GRTGRGNYKGVA 344
Cdd:cd18810 53 RIAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTII----IERADKFglaqLYQLrGRVGRSKERAYA 128
|
....*...
gi 488377159 345 ITLYGPDE 352
Cdd:cd18810 129 YFLYPDQK 136
|
|
| |
