|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
77-538 |
0e+00 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 606.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 77 LRDVDWSAENLTPIEKDFYHENAAVSRREQYEIDQWVSANQVT-LEGRGVPRPVFEFNEAPLPGQIHELLYGK-FQKPTV 154
Cdd:PTZ00110 76 LQPIDWKSINLVPFEKNFYKEHPEVSALSSKEVDEIRKEKEITiIAGENVPKPVVSFEYTSFPDYILKSLKNAgFTEPTP 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 155 IQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHITKQAHRQRGEGPAVLVLLPTRELAQQVQEVSIDFCHSLGLKMT 234
Cdd:PTZ00110 156 IQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNT 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 235 CLFGGASKGPQARDLERGVDIVVATPGRLLDFLDNGTTNMKKCSYLVLDEADRMLDMGFEPQIKKIIGQIRPDRQTLMFS 314
Cdd:PTZ00110 236 VAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWS 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 315 ATWPKEVRALASDFQKDAAF-LNVGSLELAANHNITQVVDILEEHAKQAKLMELLNHIMNQKEcKTIIFVETKRKADELT 393
Cdd:PTZ00110 316 ATWPKEVQSLARDLCKEEPVhVNVGSLDLTACHNIKQEVFVVEEHEKRGKLKMLLQRIMRDGD-KILIFVETKKGADFLT 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 394 RAMRRDGWPTLCIHGDKNQGERDWVLQEFKAGKTPIMLATDVAARGLDVDDIKFVINYDYPNNSEDYVHRIGRTGRSDKK 473
Cdd:PTZ00110 395 KELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAK 474
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3877954 474 GTAYTFFTHTNASKAKDLLKVLDEAKQTVPQALRDMANRSYGGsNSRGRYGGGGfqkRGYGGNDN 538
Cdd:PTZ00110 475 GASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSNERSNG-TERRRWGGYG---RFSNNVNN 535
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
149-504 |
9.81e-155 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 449.21 E-value: 9.81e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 149 FQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHITKQAHRQrgegPAVLVLLPTRELAQQVQEVSIDFCHS 228
Cdd:COG0513 22 YTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRA----PQALILAPTRELALQVAEELRKLAKY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 229 LGLKMTCLFGGASKGPQARDLERGVDIVVATPGRLLDFLDNGTTNMKKCSYLVLDEADRMLDMGFEPQIKKIIGQIRPDR 308
Cdd:COG0513 98 LGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGFIEDIERILKLLPKER 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 309 QTLMFSATWPKEVRALASDFQKDAAFLNVGSLELAANhNITQVVDILEEHAKqaklMELLNHIMNQKEC-KTIIFVETKR 387
Cdd:COG0513 178 QTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAE-TIEQRYYLVDKRDK----LELLRRLLRDEDPeRAIVFCNTKR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 388 KADELTRAMRRDGWPTLCIHGDKNQGERDWVLQEFKAGKTPIMLATDVAARGLDVDDIKFVINYDYPNNSEDYVHRIGRT 467
Cdd:COG0513 253 GADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRT 332
|
330 340 350
....*....|....*....|....*....|....*..
gi 3877954 468 GRSDKKGTAYTFFTHTNASKAKDLLKVLdeaKQTVPQ 504
Cdd:COG0513 333 GRAGAEGTAISLVTPDERRLLRAIEKLI---GQKIEE 366
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
141-336 |
4.41e-133 |
|
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: 385.57 E-value: 4.41e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 141 IHELLYGK-FQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHITKQAHRQRGEGPAVLVLLPTRELAQQVQ 219
Cdd:cd17966 1 VMDELKRQgFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGDGPIVLVLAPTRELAQQIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 220 EVSIDFCHSLGLKMTCLFGGASKGPQARDLERGVDIVVATPGRLLDFLDNGTTNMKKCSYLVLDEADRMLDMGFEPQIKK 299
Cdd:cd17966 81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 3877954 300 IIGQIRPDRQTLMFSATWPKEVRALASDFQKDAAFLN 336
Cdd:cd17966 161 IVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
77-338 |
1.61e-116 |
|
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: 346.23 E-value: 1.61e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 77 LRDVDWSAENLTPIEKDFYHENAAVSRREQYEIDQWVSANQVTLEGRGVPRPVFEFNEAPLPGQIHELLYGK-FQKPTVI 155
Cdd:cd18050 9 LRKKKWDLSELPKFEKNFYVEHPEVARMTQYDVEELRRKKEITIRGVGCPKPVFAFHQANFPQYVMDVLLDQnFKEPTPI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 156 QSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHITKQAHRQRGEGPAVLVLLPTRELAQQVQEVSIDFCHSLGLKMTC 235
Cdd:cd18050 89 QCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQVQQVADDYGKSSRLKSTC 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 236 LFGGASKGPQARDLERGVDIVVATPGRLLDFLDNGTTNMKKCSYLVLDEADRMLDMGFEPQIKKIIGQIRPDRQTLMFSA 315
Cdd:cd18050 169 IYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSA 248
|
250 260
....*....|....*....|...
gi 3877954 316 TWPKEVRALASDFQKDAAFLNVG 338
Cdd:cd18050 249 TWPKEVRQLAEDFLRDYVQINIG 271
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
108-339 |
4.82e-112 |
|
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: 333.13 E-value: 4.82e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 108 EIDQWVSANQVTLEGRGVPRPVFEFNEAPLPGQIHELLYGK-FQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLP 186
Cdd:cd18049 2 EVEQYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQnFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 187 ALVHITKQAHRQRGEGPAVLVLLPTRELAQQVQEVSIDFCHSLGLKMTCLFGGASKGPQARDLERGVDIVVATPGRLLDF 266
Cdd:cd18049 82 AIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDF 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3877954 267 LDNGTTNMKKCSYLVLDEADRMLDMGFEPQIKKIIGQIRPDRQTLMFSATWPKEVRALASDFQKDAAFLNVGS 339
Cdd:cd18049 162 LEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGA 234
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
131-491 |
4.06e-102 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 315.97 E-value: 4.06e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 131 EFNEAPL-PGQIHELLYGKFQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHItkQAHRQRgegPAVLVLL 209
Cdd:PRK11776 5 AFSTLPLpPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL--DVKRFR---VQALVLC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 210 PTRELAQQV-QEV-----SIDfchslGLKMTCLFGGASKGPQARDLERGVDIVVATPGRLLDFLDNGTTNMKKCSYLVLD 283
Cdd:PRK11776 80 PTRELADQVaKEIrrlarFIP-----NIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 284 EADRMLDMGFEPQIKKIIGQIRPDRQTLMFSATWPKEVRALASDFQKDAAFLNVGSLElaANHNITQVVDILEEHAKQAK 363
Cdd:PRK11776 155 EADRMLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTH--DLPAIEQRFYEVSPDERLPA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 364 LMELLNHimNQKEcKTIIFVETKRKADELTRAMRRDGWPTLCIHGDKNQGERDWVLQEFKAGKTPIMLATDVAARGLDVD 443
Cdd:PRK11776 233 LQRLLLH--HQPE-SCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIK 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 3877954 444 DIKFVINYDYPNNSEDYVHRIGRTGRSDKKGTAYTFFTHTNASKAKDL 491
Cdd:PRK11776 310 ALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAI 357
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
149-335 |
6.19e-98 |
|
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: 295.51 E-value: 6.19e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 149 FQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHITKQAhRQRGEGPAVLVLLPTRELAQQVQEVSIDFCHS 228
Cdd:cd00268 10 FEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEP-KKKGRGPQALVLAPTRELAMQIAEVARKLGKG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 229 LGLKMTCLFGGASKGPQARDLERGVDIVVATPGRLLDFLDNGTTNMKKCSYLVLDEADRMLDMGFEPQIKKIIGQIRPDR 308
Cdd:cd00268 89 TGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKILSALPKDR 168
|
170 180
....*....|....*....|....*..
gi 3877954 309 QTLMFSATWPKEVRALASDFQKDAAFL 335
Cdd:cd00268 169 QTLLFSATLPEEVKELAKKFLKNPVRI 195
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
149-476 |
2.85e-89 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 281.83 E-value: 2.85e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 149 FQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHItkQAHRQRGEGPA-VLVLLPTRELAQQVQEVSIDFCH 227
Cdd:PRK11192 21 YTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHL--LDFPRRKSGPPrILILTPTRELAMQVADQARELAK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 228 SLGLKMTCLFGGASKGPQARDLERGVDIVVATPGRLLDFLDNGTTNMKKCSYLVLDEADRMLDMGFEPQIKKIIGQIRPD 307
Cdd:PRK11192 99 HTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAAETRWR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 308 RQTLMFSATWPKE-VRALASDFQKDAAFLNVGS--LELAANHNITQVVDILeEHaKQAklmeLLNHIMNQKEC-KTIIFV 383
Cdd:PRK11192 179 KQTLLFSATLEGDaVQDFAERLLNDPVEVEAEPsrRERKKIHQWYYRADDL-EH-KTA----LLCHLLKQPEVtRSIVFV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 384 ETKRKADELTRAMRRDGWPTLCIHGDKNQGERDWVLQEFKAGKTPIMLATDVAARGLDVDDIKFVINYDYPNNSEDYVHR 463
Cdd:PRK11192 253 RTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHR 332
|
330
....*....|...
gi 3877954 464 IGRTGRSDKKGTA 476
Cdd:PRK11192 333 IGRTGRAGRKGTA 345
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
149-543 |
8.34e-88 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 278.62 E-value: 8.34e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 149 FQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHITKQAHRQRGEGPA-VLVLLPTRELAQQVQEVSIDFCH 227
Cdd:PRK10590 21 YREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVrALILTPTRELAAQIGENVRDYSK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 228 SLGLKMTCLFGGASKGPQARDLERGVDIVVATPGRLLDFLDNGTTNMKKCSYLVLDEADRMLDMGFEPQIKKIIGQIRPD 307
Cdd:PRK10590 101 YLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFIHDIRRVLAKLPAK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 308 RQTLMFSATWPKEVRALASDFQKDAAflnvgSLELA----ANHNITQVVDILEEHAKQaklmELLNHIMNQKECKTI-IF 382
Cdd:PRK10590 181 RQNLLFSATFSDDIKALAEKLLHNPL-----EIEVArrntASEQVTQHVHFVDKKRKR----ELLSQMIGKGNWQQVlVF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 383 VETKRKADELTRAMRRDGWPTLCIHGDKNQGERDWVLQEFKAGKTPIMLATDVAARGLDVDDIKFVINYDYPNNSEDYVH 462
Cdd:PRK10590 252 TRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPEDYVH 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 463 RIGRTGRSDKKGTAYTFFTHTNASKAKDLLKVLdeaKQTVPQalrdMANRSYGGS---------NSRGRYGGGGFQKRGY 533
Cdd:PRK10590 332 RIGRTGRAAATGEALSLVCVDEHKLLRDIEKLL---KKEIPR----IAIPGYEPDpsikaepiqNGRQQRGGGGRGQGGG 404
|
410
....*....|
gi 3877954 534 GGNDNFAPKR 543
Cdd:PRK10590 405 RGQQQGQPRR 414
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
119-325 |
2.49e-85 |
|
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: 264.24 E-value: 2.49e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 119 TLEGRGVPRPVFEFNEAPLPGQIHELLYG-KFQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHITKQAHR 197
Cdd:cd17953 1 KVRGKDCPKPIQKWSQCGLSEKVLDLIKKlGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 198 QRGEGPAVLVLLPTRELAQQVQEVSIDFCHSLGLKMTCLFGGASKGPQARDLERGVDIVVATPGRLLDFL--DNG-TTNM 274
Cdd:cd17953 81 KPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtaNNGrVTNL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 3877954 275 KKCSYLVLDEADRMLDMGFEPQIKKIIGQIRPDRQTLMFSATWPKEVRALA 325
Cdd:cd17953 161 RRVTYVVLDEADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALA 211
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
132-338 |
1.45e-83 |
|
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: 259.34 E-value: 1.45e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 132 FNEAPLPGQIHE-LLYGKFQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHITKQ-----AHRQRGEGPAV 205
Cdd:cd17967 2 FEEAGLRELLLEnIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDgppsvGRGRRKAYPSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 206 LVLLPTRELAQQVQEVSIDFCHSLGLKMTCLFGGASKGPQARDLERGVDIVVATPGRLLDFLDNGTTNMKKCSYLVLDEA 285
Cdd:cd17967 82 LILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDEA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 3877954 286 DRMLDMGFEPQIKKIIGQ----IRPDRQTLMFSATWPKEVRALASDFQKDAAFLNVG 338
Cdd:cd17967 162 DRMLDMGFEPQIRKIVEHpdmpPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVG 218
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
141-331 |
1.54e-83 |
|
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: 258.50 E-value: 1.54e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 141 IHELLYGKFQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHITKQAHRQRGEGPAVLVLLPTRELAQQVQE 220
Cdd:cd17952 2 LNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGEGPIAVIVAPTRELAQQIYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 221 VSIDFCHSLGLKMTCLFGGASKGPQARDLERGVDIVVATPGRLLDFLDNGTTNMKKCSYLVLDEADRMLDMGFEPQIKKI 300
Cdd:cd17952 82 EAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRSI 161
|
170 180 190
....*....|....*....|....*....|.
gi 3877954 301 IGQIRPDRQTLMFSATWPKEVRALASDFQKD 331
Cdd:cd17952 162 VGHVRPDRQTLLFSATFKKKIEQLARDILSD 192
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
135-479 |
6.78e-80 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 263.25 E-value: 6.78e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 135 APLPGQIHELLYgkfQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHITKQAhrqrgEGPAVLVLLPTREL 214
Cdd:PRK11634 15 APILEALNDLGY---EKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPEL-----KAPQILVLAPTREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 215 AQQVQEVSIDFC-HSLGLKMTCLFGGASKGPQARDLERGVDIVVATPGRLLDFLDNGTTNMKKCSYLVLDEADRMLDMGF 293
Cdd:PRK11634 87 AVQVAEAMTDFSkHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 294 EPQIKKIIGQIRPDRQTLMFSATWPKEVRALASDFQKDAAFLNVGSlELAANHNITQVVDILEEHAKQAKLMELLNhimN 373
Cdd:PRK11634 167 IEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQS-SVTTRPDISQSYWTVWGMRKNEALVRFLE---A 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 374 QKECKTIIFVETKRKADELTRAMRRDGWPTLCIHGDKNQGERDWVLQEFKAGKTPIMLATDVAARGLDVDDIKFVINYDY 453
Cdd:PRK11634 243 EDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDI 322
|
330 340
....*....|....*....|....*.
gi 3877954 454 PNNSEDYVHRIGRTGRSDKKGTAYTF 479
Cdd:PRK11634 323 PMDSESYVHRIGRTGRAGRAGRALLF 348
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
148-332 |
2.66e-76 |
|
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: 240.06 E-value: 2.66e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 148 KFQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHITKQ-AHRQRGEGPAVLVLLPTRELAQQVQEVSIDFC 226
Cdd:cd17958 9 GFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQpIPREQRNGPGVLVLTPTRELALQIEAECSKYS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 227 HSlGLKMTCLFGGASKGPQARDLERGVDIVVATPGRLLDFLDNGTTNMKKCSYLVLDEADRMLDMGFEPQIKKIIGQIRP 306
Cdd:cd17958 89 YK-GLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIRKILLDIRP 167
|
170 180
....*....|....*....|....*.
gi 3877954 307 DRQTLMFSATWPKEVRALASDFQKDA 332
Cdd:cd17958 168 DRQTIMTSATWPDGVRRLAQSYLKDP 193
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
130-545 |
6.30e-76 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 251.02 E-value: 6.30e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 130 FEFNEAPLPGqiheLLYGKFQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFML---------PALVHitkqahrQRG 200
Cdd:PRK04537 14 FDLHPALLAG----LESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVavmnrllsrPALAD-------RKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 201 EGPAVLVLLPTRELAQQVQEVSIDFCHSLGLKMTCLFGGASKGPQARDLERGVDIVVATPGRLLDFL-DNGTTNMKKCSY 279
Cdd:PRK04537 83 EDPRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVkQHKVVSLHACEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 280 LVLDEADRMLDMGFEPQIKKIIGQI--RPDRQTLMFSATWPKEVRALASDFQKDAAFLnVGSLELAANHNITQVVDILEE 357
Cdd:PRK04537 163 CVLDEADRMFDLGFIKDIRFLLRRMpeRGTRQTLLFSATLSHRVLELAYEHMNEPEKL-VVETETITAARVRQRIYFPAD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 358 HAKQAKLMELLNHimnQKECKTIIFVETKRKADELTRAMRRDGWPTLCIHGDKNQGERDWVLQEFKAGKTPIMLATDVAA 437
Cdd:PRK04537 242 EEKQTLLLGLLSR---SEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 438 RGLDVDDIKFVINYDYPNNSEDYVHRIGRTGRSDKKGTAYTFFTHTNASKAKD-----------------LLKVL----- 495
Cdd:PRK04537 319 RGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDieayieqkipvepvtaeLLTPLprppr 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3877954 496 ---------DEAKQTVPQALRDM------------ANRSYGGSNSRGRYGGGGFQKRGYGGNDNfaPKRPR 545
Cdd:PRK04537 399 vpvegeeadDEAGDSVGTIFREAreqraaeeqrrgGGRSGPGGGSRSGSVGGGGRRDGAGADGK--PRPRR 467
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
117-524 |
7.98e-75 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 246.62 E-value: 7.98e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 117 QVTLEGRGVPRPVFEFNEAPLPGQI-HELLYGKFQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHITK-- 193
Cdd:PLN00206 108 EIHVKGEAVPPPILSFSSCGLPPKLlLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTir 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 194 QAHRQRGEGPAVLVLLPTRELAQQVQEVSIDFCHSLGLKMTCLFGGASKGPQARDLERGVDIVVATPGRLLDFLDNGTTN 273
Cdd:PLN00206 188 SGHPSEQRNPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIE 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 274 MKKCSYLVLDEADRMLDMGFEPQIKKIIgQIRPDRQTLMFSATWPKEVRALASDFQKDAAFLNVGSLElAANHNITQVVD 353
Cdd:PLN00206 268 LDNVSVLVLDEVDCMLERGFRDQVMQIF-QALSQPQVLLFSATVSPEVEKFASSLAKDIILISIGNPN-RPNKAVKQLAI 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 354 ILEEHAKQAKLMELL---NHIMNqkecKTIIFVETKRKADELTRAMRR-DGWPTLCIHGDKNQGERDWVLQEFKAGKTPI 429
Cdd:PLN00206 346 WVETKQKKQKLFDILkskQHFKP----PAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERREVMKSFLVGEVPV 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 430 MLATDVAARGLDVDDIKFVINYDYPNNSEDYVHRIGRTGRSDKKGTAYTFFTHTNASKAKDLLKVLDEAKQTVPQALRDM 509
Cdd:PLN00206 422 IVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKSSGAAIPRELANS 501
|
410
....*....|....*.
gi 3877954 510 ANRSYG-GSNSRGRYG 524
Cdd:PLN00206 502 RYLGSGrKRKKKRRYG 517
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
131-479 |
2.34e-73 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 241.74 E-value: 2.34e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 131 EFNEAP-LPGQIHELlygKFQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPA---LVHITKQAHRQRGEgPAVL 206
Cdd:PRK01297 91 DFNLAPeLMHAIHDL---GFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIinqLLQTPPPKERYMGE-PRAL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 207 VLLPTRELAQQVQEVSIDFCHSLGLKMTCLFGGASKGPQARDLE-RGVDIVVATPGRLLDFLDNGTTNMKKCSYLVLDEA 285
Cdd:PRK01297 167 IIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 286 DRMLDMGFEPQIKKIIGQIRP--DRQTLMFSATWPKEVRALASDFQKDAAFLNVGSlELAANHNITQVVDILeehAKQAK 363
Cdd:PRK01297 247 DRMLDMGFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEP-ENVASDTVEQHVYAV---AGSDK 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 364 LMELLNHIMNQKECKTIIFVETKRKADELTRAMRRDGWPTLCIHGDKNQGERDWVLQEFKAGKTPIMLATDVAARGLDVD 443
Cdd:PRK01297 323 YKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHID 402
|
330 340 350
....*....|....*....|....*....|....*.
gi 3877954 444 DIKFVINYDYPNNSEDYVHRIGRTGRSDKKGTAYTF 479
Cdd:PRK01297 403 GISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISF 438
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
118-338 |
2.83e-73 |
|
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: 234.48 E-value: 2.83e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 118 VTLEGRGVPRPVFEFNEAPLPGQIHE-LLYGKFQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHITKQAH 196
Cdd:cd18052 31 VEVTGRNPPPAILTFEEANLCETLLKnIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEGL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 197 R----QRGEGPAVLVLLPTRELAQQVQEVSIDFCHSLGLKMTCLFGGASKGPQARDLERGVDIVVATPGRLLDFLDNGTT 272
Cdd:cd18052 111 TassfSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKI 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3877954 273 NMKKCSYLVLDEADRMLDMGFEPQIKKIIGQI----RPDRQTLMFSATWPKEVRALASDFQK-DAAFLNVG 338
Cdd:cd18052 191 SLSKLKYLILDEADRMLDMGFGPEIRKLVSEPgmpsKEDRQTLMFSATFPEEIQRLAAEFLKeDYLFLTVG 261
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
132-479 |
1.62e-72 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 237.95 E-value: 1.62e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 132 FNEAPLPGQIHELLYGK-FQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFmLPALVH--ITKQAHRQR-GEGPAVLV 207
Cdd:PRK04837 10 FSDFALHPQVVEALEKKgFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAF-LTATFHylLSHPAPEDRkVNQPRALI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 208 LLPTRELAQQVQEVSIDFCHSLGLKMTCLFGGASKGPQARDLERGVDIVVATPGRLLDFLDNGTTNMKKCSYLVLDEADR 287
Cdd:PRK04837 89 MAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 288 MLDMGFepqIKKIIGQIR--PD---RQTLMFSATWPKEVRALASDFQKDAAFLNVGSLElAANHNITqvvdilEE---HA 359
Cdd:PRK04837 169 MFDLGF---IKDIRWLFRrmPPanqRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQ-KTGHRIK------EElfyPS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 360 KQAKLMELLNHIMNQKECKTIIFVETKRKADELTRAMRRDGWPTLCIHGDKNQGERDWVLQEFKAGKTPIMLATDVAARG 439
Cdd:PRK04837 239 NEEKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARG 318
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 3877954 440 LDVDDIKFVINYDYPNNSEDYVHRIGRTGRSDKKGTAYTF 479
Cdd:PRK04837 319 LHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
149-335 |
2.51e-70 |
|
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: 225.28 E-value: 2.51e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 149 FQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHITKQAHRQ---RGEGPAVLVLLPTRELAQQVQEVSIDF 225
Cdd:cd17945 10 YKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDeetKDDGPYALILAPTRELAQQIEEETQKF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 226 CHSLGLKMTCLFGGASKGPQARDLERGVDIVVATPGRLLDFLDNGTTNMKKCSYLVLDEADRMLDMGFEPQIKKIIGQI- 304
Cdd:cd17945 90 AKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQVTKILDAMp 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 3877954 305 ----RPD---------------RQTLMFSATWPKEVRALASDFQKDAAFL 335
Cdd:cd17945 170 vsnkKPDteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
146-491 |
3.46e-69 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 228.56 E-value: 3.46e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 146 YGkFQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHITKQAHRQRgegpaVLVLLPTRELAQQVQEVSIDF 225
Cdd:PTZ00424 46 YG-FEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQ-----ALILAPTRELAQQIQKVVLAL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 226 CHSLGLKMTCLFGGASKGPQARDLERGVDIVVATPGRLLDFLDNGTTNMKKCSYLVLDEADRMLDMGFEPQIKKIIGQIR 305
Cdd:PTZ00424 120 GDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFKGQIYDVFKKLP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 306 PDRQTLMFSATWPKEVRALASDFQKDAAFLNVGSLELAAnHNITQV-VDILEEHAKQAKLMELLNHIMnqkECKTIIFVE 384
Cdd:PTZ00424 200 PDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTL-EGIRQFyVAVEKEEWKFDTLCDLYETLT---ITQAIIYCN 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 385 TKRKADELTRAMRRDGWPTLCIHGDKNQGERDWVLQEFKAGKTPIMLATDVAARGLDVDDIKFVINYDYPNNSEDYVHRI 464
Cdd:PTZ00424 276 TRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRI 355
|
330 340
....*....|....*....|....*..
gi 3877954 465 GRTGRSDKKGTAYTFFTHTNASKAKDL 491
Cdd:PTZ00424 356 GRSGRFGRKGVAINFVTPDDIEQLKEI 382
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
122-338 |
3.51e-69 |
|
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: 223.38 E-value: 3.51e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 122 GRGVPRPVFEFNEAPLPGQIHE-LLYGKFQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHITKQAH---- 196
Cdd:cd18051 13 GENCPPHIETFSDLDLGEIIRNnIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQGPgesl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 197 -------RQRGEGPAVLVLLPTRELAQQVQEVSIDFCHSLGLKMTCLFGGASKGPQARDLERGVDIVVATPGRLLDFLDN 269
Cdd:cd18051 93 psesgyyGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLER 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3877954 270 GTTNMKKCSYLVLDEADRMLDMGFEPQIKKIIGQI----RPDRQTLMFSATWPKEVRALASDFQKDAAFLNVG 338
Cdd:cd18051 173 GKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDtmppTGERQTLMFSATFPKEIQMLARDFLDNYIFLAVG 245
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
153-324 |
8.38e-64 |
|
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: 205.94 E-value: 8.38e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 153 TVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHItkqahRQRGEGPAVLVLLPTRELAQQVQEVSIDFCHSLGLK 232
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAL-----DKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 233 MTCLFGGASKGPQARDLeRGVDIVVATPGRLLDFLDNgTTNMKKCSYLVLDEADRMLDMGFEPQIKKIIGQIRPDRQTLM 312
Cdd:pfam00270 76 VASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQE-RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILL 153
|
170
....*....|..
gi 3877954 313 FSATWPKEVRAL 324
Cdd:pfam00270 154 LSATLPRNLEDL 165
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
148-325 |
2.53e-58 |
|
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: 193.32 E-value: 2.53e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 148 KFQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHITKQAHR---QRGEGPAVLVLLPTRELAQQVQEVSID 224
Cdd:cd17951 9 GIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEKKlpfIKGEGPYGLIVCPSRELARQTHEVIEY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 225 FCHSL------GLKMTCLFGGASKGPQARDLERGVDIVVATPGRLLDFLDNGTTNMKKCSYLVLDEADRMLDMGFEPQIK 298
Cdd:cd17951 89 YCKALqeggypQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMIDMGFEEDIR 168
|
170 180
....*....|....*....|....*..
gi 3877954 299 KIIGQIRPDRQTLMFSATWPKEVRALA 325
Cdd:cd17951 169 TIFSYFKGQRQTLLFSATMPKKIQNFA 195
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
348-480 |
1.09e-56 |
|
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: 186.17 E-value: 1.09e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 348 ITQVVDILEEHAKQAKLMELLNHIMNQKecKTIIFVETKRKADELTRAMRRDGWPTLCIHGDKNQGERDWVLQEFKAGKT 427
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLLLLEKLKPG--KAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKV 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 3877954 428 PIMLATDVAARGLDVDDIKFVINYDYPNNSEDYVHRIGRTGRSDKKGTAYTFF 480
Cdd:cd18787 79 RVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
148-326 |
3.38e-56 |
|
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: 187.79 E-value: 3.38e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 148 KFQKPTVIQSISW-PIAMSGRDIISIAKTGSGKTLAFMLPALVHITKQAHRQRGEGPAVLVLLPTRELAQQVQEVSIDFC 226
Cdd:cd17964 13 GFETMTPVQQKTLkPILSTGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGVSALIISPTRELALQIAAEAKKLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 227 HSL-GLKMTCLFGGASKGPQARDLER-GVDIVVATPGRLLDFLDN--GTTNMKKCSYLVLDEADRMLDMGFEPQIKKIIG 302
Cdd:cd17964 93 QGLrKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLENpgVAKAFTDLDYLVLDEADRLLDMGFRPDLEQILR 172
|
170 180
....*....|....*....|....*...
gi 3877954 303 QIRP----DRQTLMFSATWPKEVRALAS 326
Cdd:cd17964 173 HLPEknadPRQTLLFSATVPDEVQQIAR 200
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
148-351 |
2.00e-54 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 182.69 E-value: 2.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 148 KFQKPTVIQSISWPIAMSG-RDIISIAKTGSGKTLAFMLPALVHItkqahrQRGEGPAVLVLLPTRELAQQVQEVSIDFC 226
Cdd:smart00487 5 GFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAL------KRGKGGRVLVLVPTRELAEQWAEELKKLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 227 HSLGLKMTCLFGGASKGPQARDLERGV-DIVVATPGRLLDFLDNGTTNMKKCSYLVLDEADRMLDMGFEPQIKKIIGQIR 305
Cdd:smart00487 79 PSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 3877954 306 PDRQTLMFSATWPKEVRALASDFQKDAAFLNVGSLelaANHNITQV 351
Cdd:smart00487 159 KNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFT---PLEPIEQF 201
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
149-324 |
2.23e-54 |
|
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: 182.90 E-value: 2.23e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 149 FQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHITKQAHRQrgegpAVLVLLPTRELAQQVQEVSIDFCHS 228
Cdd:cd17954 20 WKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRF-----FALVLAPTRELAQQISEQFEALGSS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 229 LGLKMTCLFGGASKGPQARDLERGVDIVVATPGRLLDFLDNgtT---NMKKCSYLVLDEADRMLDMGFEPQIKKIIGQIR 305
Cdd:cd17954 95 IGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLEN--TkgfSLKSLKFLVMDEADRLLNMDFEPEIDKILKVIP 172
|
170
....*....|....*....
gi 3877954 306 PDRQTLMFSATWPKEVRAL 324
Cdd:cd17954 173 RERTTYLFSATMTTKVAKL 191
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
149-326 |
7.79e-54 |
|
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: 180.91 E-value: 7.79e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 149 FQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPA---LVHITKQAHRQRgegpaVLVLLPTRELAQQVQEVSIDF 225
Cdd:cd17947 10 FTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPIlerLLYRPKKKAATR-----VLVLVPTRELAMQCFSVLQQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 226 CHSLGLKMTCLFGGASKGPQARDLERGVDIVVATPGRLLDFLDNGTT-NMKKCSYLVLDEADRMLDMGFEPQIKKIIGQI 304
Cdd:cd17947 85 AQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSfDLDSIEILVLDEADRMLEEGFADELKEILRLC 164
|
170 180
....*....|....*....|..
gi 3877954 305 RPDRQTLMFSATWPKEVRALAS 326
Cdd:cd17947 165 PRTRQTMLFSATMTDEVKDLAK 186
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
148-325 |
1.51e-52 |
|
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: 177.55 E-value: 1.51e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 148 KFQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHITKQAHRQRgEGPAVLVLLPTRELAQQVQEVSIDFC- 226
Cdd:cd17942 9 GFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPR-NGTGVIIISPTRELALQIYGVAKELLk 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 227 ---HSLGLKMtclfGGASKGPQARDLERGVDIVVATPGRLLDFLDNGTTNM-KKCSYLVLDEADRMLDMGFEPQIKKIIG 302
Cdd:cd17942 88 yhsQTFGIVI----GGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLyKNLQCLIIDEADRILEIGFEEEMRQIIK 163
|
170 180
....*....|....*....|...
gi 3877954 303 QIRPDRQTLMFSATWPKEVRALA 325
Cdd:cd17942 164 LLPKRRQTMLFSATQTRKVEDLA 186
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
148-334 |
4.46e-52 |
|
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: 176.65 E-value: 4.46e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 148 KFQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHITKQAHrqrgeGPAVLVLLPTRELAQQVQEVSIDFCH 227
Cdd:cd17955 18 GIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPY-----GIFALVLTPTRELAYQIAEQFRALGA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 228 SLGLKMTCLFGGASKGPQARDLERGVDIVVATPGRLLDFL---DNGTTNMKKCSYLVLDEADRMLDMGFEPQIKKIIGQI 304
Cdd:cd17955 93 PLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLrssDDTTKVLSRVKFLVLDEADRLLTGSFEDDLATILSAL 172
|
170 180 190
....*....|....*....|....*....|
gi 3877954 305 RPDRQTLMFSATWPKEVRALASDFQKDAAF 334
Cdd:cd17955 173 PPKRQTLLFSATLTDALKALKELFGNKPFF 202
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
148-335 |
8.70e-52 |
|
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: 176.24 E-value: 8.70e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 148 KFQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHITKQAHR-QRGEGPAVLVLLPTRELAQQVQEVsidfC 226
Cdd:cd17949 10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRvDRSDGTLALVLVPTRELALQIYEV----L 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 227 HSLGLKMT-----CLFGGASKGPQ-ARdLERGVDIVVATPGRLLDFLDNgTTNMK--KCSYLVLDEADRMLDMGFEPQIK 298
Cdd:cd17949 86 EKLLKPFHwivpgYLIGGEKRKSEkAR-LRKGVNILIATPGRLLDHLKN-TQSFDvsNLRWLVLDEADRLLDMGFEKDIT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 3877954 299 KIIGQIR-------------PDRQTLMFSATWPKEVRALASDFQKDAAFL 335
Cdd:cd17949 164 KILELLDdkrskaggekskpSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
148-325 |
5.90e-49 |
|
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: 168.14 E-value: 5.90e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 148 KFQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHITKQAHRQRGEGPAVLVLLPTRELAQQVQEVSIDFCH 227
Cdd:cd17960 9 GFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKKGQVGALIISPTRELATQIYEVLQSFLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 228 SLGLKMTCLF--GGASKGPQARDLER-GVDIVVATPGRLLDFLDNGTT--NMKKCSYLVLDEADRMLDMGFEPQIKKIIG 302
Cdd:cd17960 89 HHLPKLKCQLliGGTNVEEDVKKFKRnGPNILVGTPGRLEELLSRKADkvKVKSLEVLVLDEADRLLDLGFEADLNRILS 168
|
170 180
....*....|....*....|...
gi 3877954 303 QIRPDRQTLMFSATWPKEVRALA 325
Cdd:cd17960 169 KLPKQRRTGLFSATQTDAVEELI 191
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
148-316 |
6.47e-49 |
|
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: 169.34 E-value: 6.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 148 KFQKPTVIQSISWPIAMS-GRDIISIAKTGSGKTLAFMLPALVHITKQAHRQRGE----GPAVLVLLPTRELAQQVQEVS 222
Cdd:cd17946 9 GFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLLSQKSSNGVGgkqkPLRALILTPTRELAVQVKDHL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 223 IDFCHSLGLKMTCLFGGASKGPQARDLERGVDIVVATPGRLLDFLDNG---TTNMKKCSYLVLDEADRMLDMG-FEpQIK 298
Cdd:cd17946 89 KAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGnehLANLKSLRFLVLDEADRMLEKGhFA-ELE 167
|
170 180
....*....|....*....|....*
gi 3877954 299 KIIGQI-------RPDRQTLMFSAT 316
Cdd:cd17946 168 KILELLnkdragkKRKRQTFVFSAT 192
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
144-337 |
8.03e-49 |
|
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: 167.85 E-value: 8.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 144 LLYGKFQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHItkqaHRQR---GEGPAVLVLLPTRELAQQVQE 220
Cdd:cd17941 5 LKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKL----YRERwtpEDGLGALIISPTRELAMQIFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 221 V--SIDFCHSL--GLkmtcLFGGaskgpqaRDLER------GVDIVVATPGRLLDFLDN----GTTNMKkcsYLVLDEAD 286
Cdd:cd17941 81 VlrKVGKYHSFsaGL----IIGG-------KDVKEekerinRMNILVCTPGRLLQHMDEtpgfDTSNLQ---MLVLDEAD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 3877954 287 RMLDMGFEPQIKKIIGQIRPDRQTLMFSATWPKEVRALASDFQKDAAFLNV 337
Cdd:cd17941 147 RILDMGFKETLDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
148-338 |
9.36e-49 |
|
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: 167.77 E-value: 9.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 148 KFQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHItkQAHRQRGeGPAVLVLLPTRELAQQVQEVSIDFCH 227
Cdd:cd17957 9 GYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKL--GKPRKKK-GLRALILAPTRELASQIYRELLKLSK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 228 SLGLKmTCLF--GGASKGPQARDLERGVDIVVATPGRLLDFLDNGTTNMKKCSYLVLDEADRMLDMGFEPQIKKIIGQIR 305
Cdd:cd17957 86 GTGLR-IVLLskSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEILAACT 164
|
170 180 190
....*....|....*....|....*....|....
gi 3877954 306 -PDRQTLMFSATWPKEVRALASDFQKDAAFLNVG 338
Cdd:cd17957 165 nPNLQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
143-325 |
1.40e-48 |
|
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: 167.47 E-value: 1.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 143 ELLYGKFQK----PTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHI-TKQAHRQrgegpaVLVLLPTRELAQQ 217
Cdd:cd17940 9 ELLMGIFEKgfekPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIdPKKDVIQ------ALILVPTRELALQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 218 VQEVSIDFCHSLGLKMTCLFGGASkgpqARD----LERGVDIVVATPGRLLDFLDNGTTNMKKCSYLVLDEADRMLDMGF 293
Cdd:cd17940 83 TSQVCKELGKHMGVKVMVTTGGTS----LRDdimrLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDF 158
|
170 180 190
....*....|....*....|....*....|..
gi 3877954 294 EPQIKKIIGQIRPDRQTLMFSATWPKEVRALA 325
Cdd:cd17940 159 QPIIEKILNFLPKERQILLFSATFPLTVKNFM 190
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
149-319 |
6.45e-48 |
|
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: 165.56 E-value: 6.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 149 FQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHItkQAHRQRGeGPAVLVLLPTRELAQQVQEVSIDFCHS 228
Cdd:cd17959 21 YKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKL--KAHSPTV-GARALILSPTRELALQTLKVTKELGKF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 229 LGLKMTCLFGGASKGPQARDLERGVDIVVATPGRLLDFLDNGTTNMKKCSYLVLDEADRMLDMGFEPQIKKIIGQIRPDR 308
Cdd:cd17959 98 TDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMGFAEQLHEILSRLPENR 177
|
170
....*....|.
gi 3877954 309 QTLMFSATWPK 319
Cdd:cd17959 178 QTLLFSATLPK 188
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
148-335 |
2.90e-42 |
|
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: 150.43 E-value: 2.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 148 KFQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHITKQAHRQRGE-GPAVLVLLPTRELAQQVQEVSIDFC 226
Cdd:cd17961 13 GWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGEEqGTRALILVPTRELAQQVSKVLEQLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 227 HSLGLKMTC--LFGGASKGPQARDLERGVDIVVATPGRLLDFLDNGTT-NMKKCSYLVLDEADRMLDMGFEPQIKKIIGQ 303
Cdd:cd17961 93 AYCRKDVRVvnLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLlLLSTLKYLVIDEADLVLSYGYEEDLKSLLSY 172
|
170 180 190
....*....|....*....|....*....|..
gi 3877954 304 IRPDRQTLMFSATWPKEVRALASDFQKDAAFL 335
Cdd:cd17961 173 LPKNYQTFLMSATLSEDVEALKKLVLHNPAIL 204
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
146-331 |
3.79e-41 |
|
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: 147.09 E-value: 3.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 146 YGkFQKPTVIQ--SISwPIaMSGRDIISIAKTGSGKTLAFMLPALVHITKQAHRqrgegPAVLVLLPTRELAQQVQEVSI 223
Cdd:cd17939 15 YG-FEKPSAIQqrAIV-PI-IKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRE-----TQALVLAPTRELAQQIQKVVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 224 DFCHSLGLKMTCLFGGASKGPQARDLERGVDIVVATPGRLLDFLDNGTTNMKKCSYLVLDEADRMLDMGFEPQIKKIIGQ 303
Cdd:cd17939 87 ALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQIYDIFQF 166
|
170 180
....*....|....*....|....*...
gi 3877954 304 IRPDRQTLMFSATWPKEVRALASDFQKD 331
Cdd:cd17939 167 LPPETQVVLFSATMPHEVLEVTKKFMRD 194
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
149-331 |
1.66e-40 |
|
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: 145.38 E-value: 1.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 149 FQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHITKQAhrqrgEGPAVLVLLPTRELAQQVQEVSIDFCHS 228
Cdd:cd17962 10 YEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEH-----RNPSALILTPTRELAVQIEDQAKELMKG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 229 L-GLKMTCLFGGASKGPQARDLERGVDIVVATPGRLLDFLDNGTTNMKKCSYLVLDEADRMLDMGFEPQIKKIIGQIRPD 307
Cdd:cd17962 85 LpPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILENISHD 164
|
170 180
....*....|....*....|....
gi 3877954 308 RQTLMFSATWPKEVRALASDFQKD 331
Cdd:cd17962 165 HQTILVSATIPRGIEQLAGQLLQN 188
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
155-330 |
1.11e-38 |
|
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: 140.75 E-value: 1.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 155 IQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHITK-QAHRQRGEGPAVLVLLPTRELAQQVQEVSIDFCHSLglKM 233
Cdd:cd17944 16 IQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEdQQPRKRGRAPKVLVLAPTRELANQVTKDFKDITRKL--SV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 234 TCLFGGASKGPQARDLERGVDIVVATPGRLLDFLDNGTTNMKKCSYLVLDEADRMLDMGFEPQIKKIIG-QIRPDR---- 308
Cdd:cd17944 94 ACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSvSYKKDSednp 173
|
170 180
....*....|....*....|..
gi 3877954 309 QTLMFSATWPKEVRALASDFQK 330
Cdd:cd17944 174 QTLLFSATCPDWVYNVAKKYMK 195
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
147-330 |
4.33e-38 |
|
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: 138.55 E-value: 4.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 147 GKFQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHITKQAHRqrgegPAVLVLLPTRELAQQVQEVSIDFC 226
Cdd:cd17943 8 AGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRH-----PQVLILAPTREIAVQIHDVFKKIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 227 HSL-GLKmTCLFGGASkgPQARDLER--GVDIVVATPGRLLDFLDNGTTNMKKCSYLVLDEADRMLDMGFEPQIKKIIGQ 303
Cdd:cd17943 83 KKLeGLK-CEVFIGGT--PVKEDKKKlkGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSS 159
|
170 180
....*....|....*....|....*..
gi 3877954 304 IRPDRQTLMFSATWPKevrALASDFQK 330
Cdd:cd17943 160 LPKNKQVIAFSATYPK---NLDNLLAR 183
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
143-332 |
3.48e-37 |
|
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: 136.17 E-value: 3.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 143 ELLYG----KFQKPTVIQSISWPIAMSG--RDIISIAKTGSGKTLAFMLPAL--VHITKQAhrqrgegPAVLVLLPTREL 214
Cdd:cd17963 4 ELLKGlyamGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLsrVDPTLKS-------PQALCLAPTREL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 215 AQQVQEVSIDFCHSLGLKMTClfggASKGPQARDLERGVD-IVVATPGRLLDFLDNGTTNMKKCSYLVLDEADRMLDM-G 292
Cdd:cd17963 77 ARQIGEVVEKMGKFTGVKVAL----AVPGNDVPRGKKITAqIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqG 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 3877954 293 FEPQIKKIIGQIRPDRQTLMFSATWPKEVRALASDFQKDA 332
Cdd:cd17963 153 HGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNA 192
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
146-331 |
6.17e-35 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation factor 4A-I (DDX2A) and eukaryotic initiation factor 4A-II (DDX2B) are involved in cap recognition and are required for mRNA binding to ribosome. They are DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350804 [Multi-domain] Cd Length: 201 Bit Score: 130.26 E-value: 6.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 146 YGkFQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHITKQAhrqrgEGPAVLVLLPTRELAQQVQEVSIDF 225
Cdd:cd18046 17 YG-FEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSL-----KATQALVLAPTRELAQQIQKVVMAL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 226 CHSLGLKMTCLFGGASKGPQARDLERGVDIVVATPGRLLDFLDNGTTNMKKCSYLVLDEADRMLDMGFEPQIKKIIGQIR 305
Cdd:cd18046 91 GDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKDQIYDIFQKLP 170
|
170 180
....*....|....*....|....*.
gi 3877954 306 PDRQTLMFSATWPKEVRALASDFQKD 331
Cdd:cd18046 171 PDTQVVLLSATMPNDVLEVTTKFMRD 196
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
362-469 |
9.49e-35 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 126.56 E-value: 9.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 362 AKLMELLNHIMNQKECKTIIFVETKRKADElTRAMRRDGWPTLCIHGDKNQGERDWVLQEFKAGKTPIMLATDVAARGLD 441
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100
....*....|....*....|....*...
gi 3877954 442 VDDIKFVINYDYPNNSEDYVHRIGRTGR 469
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGR 107
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
151-327 |
2.22e-34 |
|
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: 129.79 E-value: 2.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 151 KPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHITKQAHRQRGE--GPAVLVLLPTRELAQQVQEVSIDFCHS 228
Cdd:cd17948 12 KPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPfnAPRGLVITPSRELAEQIGSVAQSLTEG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 229 LGLKMTCLFGGASKGpQARDLERG-VDIVVATPGRLLDFLDNGTTNMKKCSYLVLDEADRMLDMGFEPQIKKI-----IG 302
Cdd:cd17948 92 LGLKVKVITGGRTKR-QIRNPHFEeVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKLSHFlrrfpLA 170
|
170 180 190
....*....|....*....|....*....|...
gi 3877954 303 QIRPDR--------QTLMFSATWPKEVRALASD 327
Cdd:cd17948 171 SRRSENtdgldpgtQLVLVSATMPSGVGEVLSK 203
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
152-325 |
1.25e-33 |
|
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350696 [Multi-domain] Cd Length: 204 Bit Score: 127.05 E-value: 1.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 152 PTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALvHITKqahrqrgegpaVLVLLPTRELAQQVQEVSIDFCHSLG- 230
Cdd:cd17938 22 PTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL-QIVV-----------ALILEPSRELAEQTYNCIENFKKYLDn 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 231 --LKMTCLFGGASKGPQARDLERGVDIVVATPGRLLDFLDNGTTNMKKCSYLVLDEADRMLDMGFEPQIKKIIGQI---- 304
Cdd:cd17938 90 pkLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQGNLETINRIYNRIpkit 169
|
170 180
....*....|....*....|....
gi 3877954 305 -RPDR-QTLMFSATWPK-EVRALA 325
Cdd:cd17938 170 sDGKRlQVIVCSATLHSfEVKKLA 193
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
143-331 |
2.00e-31 |
|
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: 120.65 E-value: 2.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 143 ELLYG----KFQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHITKQAHRqrgegPAVLVLLPTRELAQQV 218
Cdd:cd18045 9 DLLRGiyayGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRE-----TQALILSPTRELAVQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 219 QEVSIDFCHSLGLKMTCLFGGASKGPQARDLERGVDIVVATPGRLLDFLDNGTTNMKKCSYLVLDEADRMLDMGFEPQIK 298
Cdd:cd18045 84 QKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKEQIY 163
|
170 180 190
....*....|....*....|....*....|...
gi 3877954 299 KIIGQIRPDRQTLMFSATWPKEVRALASDFQKD 331
Cdd:cd18045 164 DVYRYLPPATQVVLVSATLPQDILEMTNKFMTD 196
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
149-331 |
1.05e-30 |
|
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: 118.99 E-value: 1.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 149 FQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHITKQAhrqrgEGPAVLVLLPTRELAQQVQEVSIDFCHS 228
Cdd:cd17950 22 FEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVD-----GQVSVLVICHTRELAFQISNEYERFSKY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 229 L-GLKMTCLFGGASKGPQARDLERGV-DIVVATPGRLLDFLDNGTTNMKKCSYLVLDEADRML-DMGFEPQIKKIIGQIR 305
Cdd:cd17950 97 MpNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLeQLDMRRDVQEIFRATP 176
|
170 180
....*....|....*....|....*.
gi 3877954 306 PDRQTLMFSATWPKEVRALASDFQKD 331
Cdd:cd17950 177 HDKQVMMFSATLSKEIRPVCKKFMQD 202
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
152-316 |
8.43e-29 |
|
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: 114.27 E-value: 8.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 152 PTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHITKQAHRQ-RgegpaVLVLLPTRELAQQVQEVSIDFCHSLG 230
Cdd:cd17956 22 PWLLPSSKSTPPYRPGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPRlR-----ALIVVPTKELVQQVYKVFESLCKGTG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 231 LKmTCLFGGASKGPQ---------ARDLERGVDIVVATPGRLLDFLDNGTT-NMKKCSYLVLDEADRMLDMGFE------ 294
Cdd:cd17956 97 LK-VVSLSGQKSFKKeqklllvdtSGRYLSRVDILVATPGRLVDHLNSTPGfTLKHLRFLVIDEADRLLNQSFQdwletv 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 3877954 295 ------------PQIKKIIGQIRPDR--QTLMFSAT 316
Cdd:cd17956 176 mkalgrptapdlGSFGDANLLERSVRplQKLLFSAT 211
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
390-469 |
3.69e-28 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 107.30 E-value: 3.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 390 DELTRAMRRDGWPTLCIHGDKNQGERDWVLQEFKAGKTPIMLATDVAARGLDVDDIKFVINYDYPNNSEDYVHRIGRTGR 469
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
151-328 |
3.63e-25 |
|
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: 104.38 E-value: 3.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 151 KPTVIQSISWP---------------IAMSGRDIISIA-KTGSGKTLAFMLPALVHITKQ------------AHRQRGEG 202
Cdd:cd17965 30 KPSPIQTLAIKkllktlmrkvtkqtsNEEPKLEVFLLAaETGSGKTLAYLAPLLDYLKRQeqepfeeaeeeyESAKDTGR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 203 PAVLVLLPTRELAQQVQEVSIDFCHSLGLKMTCLfgGASKGPQARDLER----GVDIVVATPGRLLDFLDNGTTNMKKCS 278
Cdd:cd17965 110 PRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTF--SSGFGPSYQRLQLafkgRIDILVTTPGKLASLAKSRPKILSRVT 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 3877954 279 YLVLDEADRMLDMGFEPQIKKIIGQIRPDRQTLMFSATWPKEV-RALASDF 328
Cdd:cd17965 188 HLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFdKTLRKLF 238
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
154-480 |
3.84e-22 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 99.83 E-value: 3.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 154 VIQSIswpiaMSGRDIISIAKTGSGKTLAFMLPALVhitkqahrqrGEGPAVLV--LLptrELAQ-QVQEVsidfcHSLG 230
Cdd:COG0514 25 IIEAV-----LAGRDALVVMPTGGGKSLCYQLPALL----------LPGLTLVVspLI---ALMKdQVDAL-----RAAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 231 LKMTCLFGGASKGPQA---RDLERG-VDIVVATPGRL-----LDFLDNGttnmkKCSYLVLDEA--------DrmldmgF 293
Cdd:COG0514 82 IRAAFLNSSLSAEERRevlRALRAGeLKLLYVAPERLlnprfLELLRRL-----KISLFAIDEAhcisqwghD------F 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 294 EP---QIKKIIGQIrPDRQTLMFSATWPKEVRA-LASDFQKDAAFLNVGSLelaANHNIT-QVVDILEEHAKQaklmELL 368
Cdd:COG0514 151 RPdyrRLGELRERL-PNVPVLALTATATPRVRAdIAEQLGLEDPRVFVGSF---DRPNLRlEVVPKPPDDKLA----QLL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 369 NHIMNQKECKTIIFVETKRKADELTRAMRRDGWPTLCIHGDKNQGERDWVLQEFKAGKTPIMLATdvAARGLDVD--DIK 446
Cdd:COG0514 223 DFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT--IAFGMGIDkpDVR 300
|
330 340 350
....*....|....*....|....*....|....
gi 3877954 447 FVINYDYPNNSEDYVHRIGRTGRSDKKGTAYTFF 480
Cdd:COG0514 301 FVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLY 334
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
172-482 |
7.67e-19 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 90.08 E-value: 7.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 172 IAKTGSGKTLAFMLPAlvhitkqahRQRGEGPAVLVLLPTRELAQQVQEvsiDFCHSLGLKmtcLFGGASKGPQArdler 251
Cdd:COG1061 106 VAPTGTGKTVLALALA---------AELLRGKRVLVLVPRRELLEQWAE---ELRRFLGDP---LAGGGKKDSDA----- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 252 gvDIVVATPGRL-----LDFLDNgttnmkKCSYLVLDEADRmldmGFEPQIKKIIGQIRPDRqTLMFSAT-------WPK 319
Cdd:COG1061 166 --PITVATYQSLarrahLDELGD------RFGLVIIDEAHH----AGAPSYRRILEAFPAAY-RLGLTATpfrsdgrEIL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 320 EVR------------ALASDFQKDAAFLNVG---SLELAANHNITQVVD---ILEEHAKQAKLMELLNHIMNQKecKTII 381
Cdd:COG1061 233 LFLfdgivyeyslkeAIEDGYLAPPEYYGIRvdlTDERAEYDALSERLRealAADAERKDKILRELLREHPDDR--KTLV 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 382 FVETKRKADELTRAMRRDGWPTLCIHGDKNQGERDWVLQEFKAGKTPIMLATDVAARGLDVDDIKFVInYDYPNNSE-DY 460
Cdd:COG1061 311 FCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI-LLRPTGSPrEF 389
|
330 340
....*....|....*....|..
gi 3877954 461 VHRIGRTGRSDKKGTAYTFFTH 482
Cdd:COG1061 390 IQRLGRGLRPAPGKEDALVYDF 411
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
173-316 |
1.29e-16 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 77.06 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 173 AKTGSGKTLAFMLPALVHITKQahrqrgeGPAVLVLLPTRELAQQVQEvSIDFCHSLGLKMTCLFGGASKGPQARDLERG 252
Cdd:cd00046 8 APTGSGKTLAALLAALLLLLKK-------GKKVLVLVPTKALALQTAE-RLRELFGPGIRVAVLVGGSSAEEREKNKLGD 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3877954 253 VDIVVATPGRLL-DFLDNGTTNMKKCSYLVLDEADRMLDMGFEPQIKKIIGQ--IRPDRQTLMFSAT 316
Cdd:cd00046 80 ADIIIATPDMLLnLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRkaGLKNAQVILLSAT 146
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
143-342 |
1.83e-15 |
|
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: 75.83 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 143 ELLYG----KFQKPTVIQSISWPIAMSG--RDIISIAKTGSGKTLAFMLPALVHITKQAHRqrgegPAVLVLLPTRELAQ 216
Cdd:cd18048 28 ELLRGiyamGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLY-----PQCLCLSPTFELAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 217 Q---VQEVSIDFChsLGLKMTCLFGGaSKGPQARDLERgvDIVVATPGRLLDF-LDNGTTNMKKCSYLVLDEADRMLDM- 291
Cdd:cd18048 103 QtgkVVEEMGKFC--VGIQVIYAIRG-NRPGKGTDIEA--QIVIGTPGTVLDWcFKLRLIDVTNISVFVLDEADVMINVq 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 3877954 292 GFEPQIKKIIGQIRPDRQTLMFSATWPKEVRALASDFQKDAAFLNVGSLEL 342
Cdd:cd18048 178 GHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEEL 228
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
336-473 |
1.35e-13 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 73.61 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 336 NVGSLELAANHNITQVVDILE----EHAKQAKLMELLNHIMN-QKECKTIIFVETKRKADELTRAMRRDGWPTL------ 404
Cdd:COG1111 308 SKASKRLVSDPRFRKAMRLAEeadiEHPKLSKLREILKEQLGtNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGrfvgqa 387
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3877954 405 CIHGDK--NQGERDWVLQEFKAGKTPIMLATDVAARGLDVDDIKFVINYDyPNNSE-DYVHRIGRTGRSDKK 473
Cdd:COG1111 388 SKEGDKglTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYE-PVPSEiRSIQRKGRTGRKREG 458
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
379-480 |
3.39e-13 |
|
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: 66.85 E-value: 3.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 379 TIIFVETKRKADELTRAMRRDGWPTLCIHGDKNQGERDWVLQEFKAGKTPIMLATDVAARGLDVDDIKFVINYDYPNNSE 458
Cdd:cd18794 33 GIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSME 112
|
90 100
....*....|....*....|..
gi 3877954 459 DYVHRIGRTGRSDKKGTAYTFF 480
Cdd:cd18794 113 SYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
154-323 |
9.44e-12 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 64.48 E-value: 9.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 154 VIQSIswpiaMSGRDIISIAKTGSGKTLAFMLPALVhitkqahrqrgEGPAVLVLLPTRELAQ-QVQEvsidfCHSLGLK 232
Cdd:cd17920 20 AINAV-----LAGRDVLVVMPTGGGKSLCYQLPALL-----------LDGVTLVVSPLISLMQdQVDR-----LQQLGIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 233 MTCLFGGASKGPQARDLER----GVDIVVATPGRLL--DFLD--NGTTNMKKCSYLVLDEADRMLDMG--FEPQIKKiIG 302
Cdd:cd17920 79 AAALNSTLSPEEKREVLLRikngQYKLLYVTPERLLspDFLEllQRLPERKRLALIVVDEAHCVSQWGhdFRPDYLR-LG 157
|
170 180
....*....|....*....|....
gi 3877954 303 QIR---PDRQTLMFSATWPKEVRA 323
Cdd:cd17920 158 RLRralPGVPILALTATATPEVRE 181
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
132-325 |
9.98e-12 |
|
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: 64.36 E-value: 9.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 132 FNEAPLPGQIHELLYGK-FQKPTVIQSISWPIAMSG--RDIISIAKTGSGKTLAFMLPALVHITKQAHRQRgegpaVLVL 208
Cdd:cd18047 3 FEELRLKPQLLQGVYAMgFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQ-----CLCL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 209 LPTRELAQQVQEVsIDFCHSLGLKMTCLFggASKGPQardLERGV----DIVVATPGRLLDF-LDNGTTNMKKCSYLVLD 283
Cdd:cd18047 78 SPTYELALQTGKV-IEQMGKFYPELKLAY--AVRGNK---LERGQkiseQIVIGTPGTVLDWcSKLKFIDPKKIKVFVLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 3877954 284 EADRML-DMGFEPQIKKIIGQIRPDRQTLMFSATWPKEVRALA 325
Cdd:cd18047 152 EADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFA 194
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
356-467 |
1.79e-11 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 66.79 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 356 EEHAKQAKLMELLNHIMNQKEcKTIIFVETKRKADELTRAMRRDGWPTLCIHGDKNQGERDWVLQEFKAGKTP--IMLAT 433
Cdd:COG0553 530 GRSAKLEALLELLEELLAEGE-KVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEApvFLISL 608
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 3877954 434 DVAARGLDV---DDikfVINYDYPNN------SEDYVHRIGRT 467
Cdd:COG0553 609 KAGGEGLNLtaaDH---VIHYDLWWNpaveeqAIDRAHRIGQT 648
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
358-469 |
6.66e-11 |
|
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: 60.45 E-value: 6.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 358 HAKQAKLMELL-NHIMNQKECKT---IIFVETKRKADELTRAMRRDGW---PTLCI-HGDK------NQGERDWVLQEFK 423
Cdd:cd18801 8 HPKLEKLEEIVkEHFKKKQEGSDtrvIIFSEFRDSAEEIVNFLSKIRPgirATRFIgQASGksskgmSQKEQKEVIEQFR 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 3877954 424 AGKTPIMLATDVAARGLDVDDIKFVINYDyPNNSE-DYVHRIGRTGR 469
Cdd:cd18801 88 KGGYNVLVATSIGEEGLDIGEVDLIICYD-ASPSPiRMIQRMGRTGR 133
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
356-466 |
8.35e-11 |
|
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: 59.91 E-value: 8.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 356 EEHAKQAKLMELLNHIMNQ----KECKTIIFVETKRKADELTRAMR-----RDGWPTLCI--HGDKNQGERDW------- 417
Cdd:cd18802 1 EEIVVIPKLQKLIEILREYfpktPDFRGIIFVERRATAVVLSRLLKehpstLAFIRCGFLigRGNSSQRKRSLmtqrkqk 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 3877954 418 -VLQEFKAGKTPIMLATDVAARGLDVDDIKFVINYDYPNNSEDYVHRIGR 466
Cdd:cd18802 81 eTLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR 130
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
133-469 |
3.78e-10 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 62.42 E-value: 3.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 133 NEAPLPGQIHELLYGKFQ----KPTVIQSiswpiAMSGRDIISIAKTGSGKTLAFMLPALVHitkqahrqrgEGpAVLVL 208
Cdd:PRK11057 8 NLESLAKQVLQETFGYQQfrpgQQEIIDA-----VLSGRDCLVVMPTGGGKSLCYQIPALVL----------DG-LTLVV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 209 LPTRELAQ-QVQEVSIDfchslGLKMTCLFGGASKGPQ----ARDLERGVDIVVATPGRLL--DFLDN-GTTNMkkcSYL 280
Cdd:PRK11057 72 SPLISLMKdQVDQLLAN-----GVAAACLNSTQTREQQlevmAGCRTGQIKLLYIAPERLMmdNFLEHlAHWNP---ALL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 281 VLDEADRMLDMG--FEPQIKKIiGQIR---PDRQTLMFSATWPKEVRA-LASDFQKDAAFLNVGSLElaaNHNITqvVDI 354
Cdd:PRK11057 144 AVDEAHCISQWGhdFRPEYAAL-GQLRqrfPTLPFMALTATADDTTRQdIVRLLGLNDPLIQISSFD---RPNIR--YTL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 355 LEEHAKqakLMELLNHIMNQKECKTIIFVETKRKADELTRAMRRDGWPTLCIHGDKNQGERDWVLQEFKAGKTPIMLATD 434
Cdd:PRK11057 218 VEKFKP---LDQLMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATV 294
|
330 340 350
....*....|....*....|....*....|....*
gi 3877954 435 VAARGLDVDDIKFVINYDYPNNSEDYVHRIGRTGR 469
Cdd:PRK11057 295 AFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGR 329
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
378-479 |
4.67e-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: 55.79 E-value: 4.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 378 KTIIFVETKRKADELTRAMRrdgwptlcihgdknqgerdwvlqefkagktpIMLATDVAARGLDVDDIKFVINYDYPNNS 457
Cdd:cd18785 5 KIIVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDPPSSA 53
|
90 100
....*....|....*....|...
gi 3877954 458 EDYVHRIGRTGR-SDKKGTAYTF 479
Cdd:cd18785 54 ASYIQRVGRAGRgGKDEGEVILF 76
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
119-478 |
6.00e-10 |
|
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: 62.16 E-value: 6.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 119 TLEGRGvprPVFEFNEAPLPGQIHELLYGK-FQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHItkqahr 197
Cdd:COG1205 26 TIPARE---ARYAPWPDWLPPELRAALKKRgIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEAL------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 198 QRGEGPAVLVLLPTRELAQ-QVQEVSiDFCHSLGLKMTC--LFGGASkgPQARD--LERGvDIVVATPgrllDFLDNG-- 270
Cdd:COG1205 97 LEDPGATALYLYPTKALARdQLRRLR-ELAEALGLGVRVatYDGDTP--PEERRwiREHP-DIVLTNP----DMLHYGll 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 271 ------TTNMKKCSYLVLDEA---------------DRML----DMGFEPQIkkiigqirpdrqtLMFSATW--PKE--- 320
Cdd:COG1205 169 phhtrwARFFRNLRYVVIDEAhtyrgvfgshvanvlRRLRricrHYGSDPQF-------------ILASATIgnPAEhae 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 321 ------VRALASD----FQKDAAFLNvgslelaanhniTQVVDILEEHAKQAKLMELLNHIMnQKECKTIIFVETKRKAd 390
Cdd:COG1205 236 rltgrpVTVVDEDgsprGERTFVLWN------------PPLVDDGIRRSALAEAARLLADLV-REGLRTLVFTRSRRGA- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 391 EL----TRAMRRDGWPTLCI---HGDKNQGERDWVLQEFKAGKTPIMLAT-------DVAarGLDVddikfVINYDYPNN 456
Cdd:COG1205 302 ELlaryARRALREPDLADRVaayRAGYLPEERREIERGLRSGELLGVVSTnalelgiDIG--GLDA-----VVLAGYPGT 374
|
410 420
....*....|....*....|..
gi 3877954 457 SEDYVHRIGRTGRSDKKGTAYT 478
Cdd:COG1205 375 RASFWQQAGRAGRRGQDSLVVL 396
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
359-465 |
2.52e-09 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 55.56 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 359 AKQAKLMELLNHIMNQKEcKTIIFVETKRKADELTRAMRRDGWPTLCIHGDKNQGERDWVLQEFKAGKTP--IMLATDVA 436
Cdd:cd18793 11 GKLEALLELLEELREPGE-KVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAG 89
|
90 100 110
....*....|....*....|....*....|....*
gi 3877954 437 ARGLDVDDIKFVINYDYPNNS------EDYVHRIG 465
Cdd:cd18793 90 GVGLNLTAANRVILYDPWWNPaveeqaIDRAHRIG 124
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
156-285 |
3.16e-09 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 56.44 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 156 QSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHITKQAHRQrgegpaVLVLLPTRELAQ-QVQEVSiDFCHSLGLKMT 234
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDPGSR------ALYLYPTKALAQdQLRSLR-ELLEQLGLGIR 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3877954 235 CLF--GGASKGPQARDLERGVDIVVATPgrllDFL--------DNGTTNMKKCSYLVLDEA 285
Cdd:cd17923 78 VATydGDTPREERRAIIRNPPRILLTNP----DMLhyallphhDRWARFLRNLRYVVLDEA 134
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
167-285 |
4.37e-09 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 56.51 E-value: 4.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 167 RDIISIAKTGSGKTL-AFMLpalvhITKQAHRQRGEGPA---VLVLLPTRELA-QQVQEVSIDfchsLGLKMTCLFGGAS 241
Cdd:cd18034 17 RNTIVVLPTGSGKTLiAVML-----IKEMGELNRKEKNPkkrAVFLVPTVPLVaQQAEAIRSH----TDLKVGEYSGEMG 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 3877954 242 KGPQARD----LERGVDIVVATPGRLLDFLDNGTTNMKKCSYLVLDEA 285
Cdd:cd18034 88 VDKWTKErwkeELEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
163-284 |
6.81e-09 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350794 [Multi-domain] Cd Length: 204 Bit Score: 55.94 E-value: 6.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 163 AMSGRDIISIAKTGSGKTLAFMLPALVHITKQahRQRGEGPAVLVLLPTRELAQQVQEVSIDFCHSlGLKMTCLFGGASK 242
Cdd:cd18036 14 ALRGKNTIICAPTGSGKTRVAVYICRHHLEKR--RSAGEKGRVVVLVNKVPLVEQQLEKFFKYFRK-GYKVTGLSGDSSH 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 3877954 243 GPQARDLERGVDIVVATPGRLLDFLDNGTTN----MKKCSYLVLDE 284
Cdd:cd18036 91 KVSFGQIVKASDVIICTPQILINNLLSGREEervyLSDFSLLIFDE 136
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
163-287 |
9.35e-08 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 52.43 E-value: 9.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 163 AMSGRDIISIAKTGSGKTLAFMLPALVHITKQAHRQRGEgpaVLVLLPTRELAQQVQEVSIDFCHSLGLKMTCLFGGASK 242
Cdd:cd17927 14 ALKGKNTIICLPTGSGKTFVAVLICEHHLKKFPAGRKGK---VVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGDTSE 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 3877954 243 GPQARDLERGVDIVVATPGRLLDFLDNGT-TNMKKCSYLVLDEADR 287
Cdd:cd17927 91 NVSVEQIVESSDVIIVTPQILVNDLKSGTiVSLSDFSLLVFDECHN 136
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
155-285 |
1.74e-07 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 51.49 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 155 IQSISWPIAMSGRDIISI-AKTGSGKTLAFMLPALVHITKQAHRqrgegpaVLVLLPTRELAQQV-QEVSIDFCHsLGLK 232
Cdd:cd17921 5 IQREALRALYLSGDSVLVsAPTSSGKTLIAELAILRALATSGGK-------AVYIAPTRALVNQKeADLRERFGP-LGKN 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 3877954 233 MTCLFGGASKGPQardLERGVDIVVATPGRLLDFLDNG-TTNMKKCSYLVLDEA 285
Cdd:cd17921 77 VGLLTGDPSVNKL---LLAEADILVATPEKLDLLLRNGgERLIQDVRLVVVDEA 127
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
165-477 |
2.33e-07 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 53.36 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 165 SGRDIISIAKTGSGKTLAFMLPALVHITKqahrqrgeGPAVLVLLPTRELAQQV-QEVSIDFcHSLGLKMTCLFGGASKG 243
Cdd:COG1204 37 EGKNLVVSAPTASGKTLIAELAILKALLN--------GGKALYIVPLRALASEKyREFKRDF-EELGIKVGVSTGDYDSD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 244 PqaRDLERgVDIVVATPGRLLDFLDNGTTNMKKCSYLVLDEA------DRmldmGfePQIKKIIGQIR---PDRQTLMFS 314
Cdd:COG1204 108 D--EWLGR-YDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAhliddeSR----G--PTLEVLLARLRrlnPEAQIVALS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 315 ATWPkEVRALASDFqkDAAF---------LNVGSLElaanHNITQVVDILEEHAKQakLMELLNHIMNQKEcKTIIFVET 385
Cdd:COG1204 179 ATIG-NAEEIAEWL--DAELvksdwrpvpLNEGVLY----DGVLRFDDGSRRSKDP--TLALALDLLEEGG-QVLVFVSS 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 386 KRKA-----------------------DELTRAMRRDGWPTL-------CI-------HGDKNQGERDWVLQEFKAGKTP 428
Cdd:COG1204 249 RRDAeslakkladelkrrltpeereelEELAEELLEVSEETHtnekladCLekgvafhHAGLPSELRRLVEDAFREGLIK 328
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 3877954 429 IMLATD-------VAARGLDVDDIKFVINYDYPNNseDYVHRIGRTGR--SDKKGTAY 477
Cdd:COG1204 329 VLVATPtlaagvnLPARRVIIRDTKRGGMVPIPVL--EFKQMAGRAGRpgYDPYGEAI 384
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
356-470 |
3.31e-07 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 53.34 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 356 EEHAKQAKLMELLNHIMNQK-ECKTIIFVETKRKADELTRAMRRDGWPTL------CIHGDK--NQGERDWVLQEFKAGK 426
Cdd:PRK13766 344 IEHPKLEKLREIVKEQLGKNpDSRIIVFTQYRDTAEKIVDLLEKEGIKAVrfvgqaSKDGDKgmSQKEQIEILDKFRAGE 423
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 3877954 427 TPIMLATDVAARGLDVDDIKFVINYDyPNNSE-DYVHRIGRTGRS 470
Cdd:PRK13766 424 FNVLVSTSVAEEGLDIPSVDLVIFYE-PVPSEiRSIQRKGRTGRQ 467
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
164-492 |
1.28e-06 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 51.44 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 164 MSGRDIISIAKTGSGKTLAFMLPALVH-------------ITKQ-AHRQRGEGPAVlVLLPTRELAQQ---VQEVSIDFC 226
Cdd:PLN03137 473 MSGYDVFVLMPTGGGKSLTYQLPALICpgitlvisplvslIQDQiMNLLQANIPAA-SLSAGMEWAEQleiLQELSSEYS 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 227 hslglKMTCLFGGASKGPQARDLERGVDIVVATpgRLLdfldngttnmkkcSYLVLDEADRMLDMG--FEPQIKK--IIG 302
Cdd:PLN03137 552 -----KYKLLYVTPEKVAKSDSLLRHLENLNSR--GLL-------------ARFVIDEAHCVSQWGhdFRPDYQGlgILK 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 303 QIRPDRQTLMFSATWPKEVRalaSDFQKDAAFLNVGSLELAANH-NI-TQVVdileehAKQAKLMELLNHIMNQK---EC 377
Cdd:PLN03137 612 QKFPNIPVLALTATATASVK---EDVVQALGLVNCVVFRQSFNRpNLwYSVV------PKTKKCLEDIDKFIKENhfdEC 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 378 KtIIFVETKRKADELTRAMRRDGWPTLCIHGDKNQGERDWVLQEFKAGKTPIMLATDVAARGLDVDDIKFVINYDYPNNS 457
Cdd:PLN03137 683 G-IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSI 761
|
330 340 350
....*....|....*....|....*....|....*
gi 3877954 458 EDYVHRIGRTGRSDKKGTAYTFFTHTNASKAKDLL 492
Cdd:PLN03137 762 EGYHQECGRAGRDGQRSSCVLYYSYSDYIRVKHMI 796
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
151-287 |
3.09e-06 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 47.89 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 151 KPTVIQSISWPIAMSGRDIIsIAKTGSGKTLAFMLPALVHITKQahrqrgeGPAVLVLLPTRELAQQVQEvsiDFCHSLG 230
Cdd:cd18035 2 ERRLYQVLIAAVALNGNTLI-VLPTGLGKTIIAILVAADRLTKK-------GGKVLILAPSRPLVEQHAE---NLKRVLN 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 3877954 231 LKMTCLFGGASKGPQAR-DLERGVDIVVATPGRLLDFLDNGTTNMKKCSYLVLDEADR 287
Cdd:cd18035 71 IPDKITSLTGEVKPEERaERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
166-284 |
1.53e-05 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 45.27 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 166 GRDIISIAKTGSGKTLAFMLPALVHItkqaHRQRGEGPAVLVLLPTRELAQQVQEVSIDFCHSLGLKMTCLF--GGASKG 243
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSL----ADEPEKGVQVLYISPLKALINDQERRLEEPLDEIDLEIPVAVrhGDTSQS 76
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 3877954 244 PQARDLERGVDIVVATPGRLLDFLDN--GTTNMKKCSYLVLDE 284
Cdd:cd17922 77 EKAKQLKNPPGILITTPESLELLLVNkkLRELFAGLRYVVVDE 119
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
165-316 |
1.56e-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: 45.79 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 165 SGRDIISIAKTGSGKTLAFMLPALVHITkqahrqrgEGPAVLVLLPTRELA-QQVQEVSIDfcHSLGLKMtclfgGASKG 243
Cdd:cd18028 16 KGENLLISIPTASGKTLIAEMAMVNTLL--------EGGKALYLVPLRALAsEKYEEFKKL--EEIGLKV-----GISTG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3877954 244 PQARDLER--GVDIVVATPGRLLDFLDNGTTNMKKCSYLVLDEADRMLDMGFEPQIKKIIGQIR---PDRQTLMFSAT 316
Cdd:cd18028 81 DYDEDDEWlgDYDIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPTLESIVARLRrlnPNTQIIGLSAT 158
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
147-219 |
1.90e-05 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 47.79 E-value: 1.90e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3877954 147 GKFQKPTVIQSISWPIAMSGRDIISIAKTGSGKTLAFMLPALVHITKQAHRQ-RGEGPAVLVLLPTRELAQQVQ 219
Cdd:COG1201 20 ARFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTLAAFLPALDELARRPRPGeLPDGLRVLYISPLKALANDIE 93
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
166-285 |
4.31e-05 |
|
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350688 [Multi-domain] Cd Length: 186 Bit Score: 44.59 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 166 GRDIISIAKTGSGKTLAFMLPALVHITkqahrqRGEGPAVLVLLPTRELAQQVQEV------------SIDFCHS----- 228
Cdd:cd17930 1 PGLVILEAPTGSGKTEAALLWALKLAA------RGGKRRIIYALPTRATINQMYERireilgrlddedKVLLLHSkaale 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3877954 229 -LGLKMTCLFGGASKGPQARDLERG--VDIVVATPGRLLDFLDNGTTNMKKC-----SYLVLDEA 285
Cdd:cd17930 75 lLESDEEPDDDPVEAVDWALLLKRSwlAPIVVTTIDQLLESLLKYKHFERRLhglanSVVVLDEV 139
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
344-472 |
4.81e-05 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 43.79 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 344 ANHNITQVVDILEEHAKqaklmellnhimnqkeckTIIFVETKRKADELTRAMRR----DGWPTL--CIHGDKNQGERDW 417
Cdd:cd18796 24 GADAYAEVIFLLERHKS------------------TLVFTNTRSQAERLAQRLRElcpdRVPPDFiaLHHGSLSRELREE 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 3877954 418 VLQEFKAGKTPIMLATDVAARGLDVDDIKFVINYDYPNNSEDYVHRIGRTGRSDK 472
Cdd:cd18796 86 VEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGHRPG 140
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
154-322 |
1.06e-04 |
|
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.
Pssm-ID: 350776 [Multi-domain] Cd Length: 201 Bit Score: 43.40 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 154 VIQSIswpiaMSGRDIISIAKTGSGKTLAFMLPALVhitkQAHRQRGegpAVLVLLPTRELAQ-QVqevsidfcHSL--G 230
Cdd:cd18018 20 AIARL-----LSGRSTLVVLPTGAGKSLCYQLPALL----LRRRGPG---LTLVVSPLIALMKdQV--------DALprA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 231 LKMTCLFGGASKGPQARDLER----GVDIVVATPGRLL--DFLDNgTTNMKKCSYLVLDEADRMLDMG--FEP---QIKK 299
Cdd:cd18018 80 IKAAALNSSLTREERRRILEKlragEVKILYVSPERLVneSFREL-LRQTPPISLLVVDEAHCISEWShnFRPdylRLCR 158
|
170 180
....*....|....*....|...
gi 3877954 300 IIGQIRPDRQTLMFSATWPKEVR 322
Cdd:cd18018 159 VLRELLGAPPVLALTATATKRVV 181
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
154-316 |
1.16e-04 |
|
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: 43.17 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 154 VIQSISWPIAMsgrDIISIAKTGSGKTLAFMLPALVHItkQAHRQrgegpaVLVLLPTRELAQQVQEVSIDFCHSLGLKM 233
Cdd:cd17918 27 IEKDLHSPEPM---DRLLSGDVGSGKTLVALGAALLAY--KNGKQ------VAILVPTEILAHQHYEEARKFLPFINVEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 234 TclfggaSKGPQARDLErGVDIVVATPGRLldFLDngtTNMKKCSYLVLDEADRmldMGFEpQIKKIIGQIRPDrqTLMF 313
Cdd:cd17918 96 V------TGGTKAQILS-GISLLVGTHALL--HLD---VKFKNLDLVIVDEQHR---FGVA-QREALYNLGATH--FLEA 157
|
...
gi 3877954 314 SAT 316
Cdd:cd17918 158 TAT 160
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
175-316 |
1.34e-04 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 42.29 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 175 TGSGKTL-AFMLPALVHITKqahrqrgegpaVLVLLPTRELAQQVQEVSIDFchsLGLKMTCLFGGASKgpqarDLERGV 253
Cdd:cd17926 27 TGSGKTLtALALIAYLKELR-----------TLIVVPTDALLDQWKERFEDF---LGDSSIGLIGGGKK-----KDFDDA 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3877954 254 DIVVATPgRLLDFLDNGTTNMKK-CSYLVLDEADRmldmGFEPQIKKIIGQIRPDRQtLMFSAT 316
Cdd:cd17926 88 NVVVATY-QSLSNLAEEEKDLFDqFGLLIVDEAHH----LPAKTFSEILKELNAKYR-LGLTAT 145
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
406-497 |
1.52e-04 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 42.33 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 406 IHGDKNQGERDWVLQEFKAGKTPIMLATDVAARGLDVDDIKFVINYDYPNNSEDYVHRI-GRTGRSDKKgtAYTFFTHTN 484
Cdd:cd18811 67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLHQLrGRVGRGDHQ--SYCLLVYKD 144
|
90
....*....|....*
gi 3877954 485 --ASKAKDLLKVLDE 497
Cdd:cd18811 145 plTETAKQRLRVMTE 159
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
359-480 |
2.07e-04 |
|
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350176 [Multi-domain] Cd Length: 153 Bit Score: 41.85 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 359 AKQAKLMELL-NHIMNQKeckTIIFVETKrkaDELTRAMRRDGWPTlcIHGDKNQGERDWVLQEFKAGKTPIMLATDVAA 437
Cdd:cd18789 34 NKLRALEELLkRHEQGDK---IIVFTDNV---EALYRYAKRLLKPF--ITGETPQSEREEILQNFREGEYNTLVVSKVGD 105
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 3877954 438 RGLDVDDIKFVINYDYPNNSE-DYVHRIGRTGRSdKKGTAYTFF 480
Cdd:cd18789 106 EGIDLPEANVAIQISGHGGSRrQEAQRLGRILRP-KKGGGKNAF 148
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
406-497 |
2.49e-04 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350179 [Multi-domain] Cd Length: 160 Bit Score: 41.87 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 406 IHGDKNQGERDWVLQEFKAGKTPIMLATDVAARGLDVDDIKFVINYDYPNNSEDYVHRI-GRTGRSDKKgtAYTFFTHTN 484
Cdd:cd18792 66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFGLSQLHQLrGRVGRGKHQ--SYCYLLYPD 143
|
90
....*....|....*..
gi 3877954 485 ASK----AKDLLKVLDE 497
Cdd:cd18792 144 PKKltetAKKRLRAIAE 160
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
162-264 |
2.69e-04 |
|
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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: 350773 [Multi-domain] Cd Length: 209 Bit Score: 42.35 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 162 IAMSGRDIISIAKTGSGKTLAFMLPALVhitkqahrqrGEGPAvLVLLPTRELAQ-QVQEvsidfCHSLGLKMTCLFGGA 240
Cdd:cd18015 29 ATMAGRDVFLVMPTGGGKSLCYQLPALC----------SDGFT-LVVSPLISLMEdQLMA-----LKKLGISATMLNASS 92
|
90 100
....*....|....*....|....
gi 3877954 241 SKGPQARDLERGVDIvvATPGRLL 264
Cdd:cd18015 93 SKEHVKWVHAALTDK--NSELKLL 114
|
|
| SF2_C_priA |
cd18804 |
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ... |
410-474 |
5.53e-04 |
|
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350191 [Multi-domain] Cd Length: 238 Bit Score: 41.85 E-value: 5.53e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3877954 410 KNQGERDWVLQEFKAGKTPIMLATDVAARGLDVDDIKFV--INYDYPNNSEDY---------VHRI-GRTGRSDKKG 474
Cdd:cd18804 128 RKKGALEKLLDQFERGEIDILIGTQMIAKGLDFPNVTLVgiLNADSGLNSPDFraserafqlLTQVsGRAGRGDKPG 204
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
173-473 |
1.01e-03 |
|
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
Pssm-ID: 187770 [Multi-domain] Cd Length: 353 Bit Score: 41.65 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 173 AKTGSGKTLAFMLPALvHITKQAHRQRgegpaVLVLLPTRELAQ-QVQEVSIDFCHSLGLKMTCLFGGASKGPQARDLER 251
Cdd:cd09639 6 APTGYGKTEAALLWAL-HSLKSQKADR-----VIIALPTRATINaMYRRAKEAFGETGLYHSSILSSRIKEMGDSEEFEH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 252 GVD-------------IVVATPGRLLDFLDNG------TTNMKKCSYLVLDEADrmldmGFEPQIKKII-----GQIRPD 307
Cdd:cd09639 80 LFPlyihsndtlfldpITVCTIDQVLKSVFGEfghyefTLASIANSLLIFDEVH-----FYDEYTLALIlavleVLKDND 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 308 RQTLMFSATWPKEVRALasdFQKDAAFLNVGSLELAANH---NITQVVDILEEHAKQAKLMELLNhimnqKECKTIIFVE 384
Cdd:cd09639 155 VPILLMSATLPKFLKEY---AEKIGYVEENEPLDLKPNErapFIKIESDKVGEISSLERLLEFIK-----KGGSVAIIVN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 385 TKRKADELTRAMRRDG--WPTLCIHGDKNQGER----DWVLQEFKAGKTPIMLATDVAARGLDVdDIKFVINYDYPNNSe 458
Cdd:cd09639 227 TVDRAQEFYQQLKEKGpeEEIMLIHSRFTEKDRakkeAELLLEFKKSEKFVIVATQVIEASLDI-SVDVMITELAPIDS- 304
|
330
....*....|....*
gi 3877954 459 dYVHRIGRTGRSDKK 473
Cdd:cd09639 305 -LIQRLGRLHRYGEK 318
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
406-497 |
1.98e-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: 38.86 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 406 IHGDKNQGERDWVLQEFKAGKTPIMLATDVAARGLDVDDIKFVI--NYDYPNNSEDYVHRiGRTGRSDKKGTAYTFFTHT 483
Cdd:cd18810 57 AHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIieRADKFGLAQLYQLR-GRVGRSKERAYAYFLYPDQ 135
|
90
....*....|....*.
gi 3877954 484 NA--SKAKDLLKVLDE 497
Cdd:cd18810 136 KKltEDALKRLEAIQE 151
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
350-469 |
2.12e-03 |
|
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350177 [Multi-domain] Cd Length: 171 Bit Score: 39.15 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 350 QVVDILEEHAKQAKLMEllnhimnqkecKTIIFVETKRKADELTRAMRRDGWPTLCIHGDKNQGERDWVLQEFKAGKTPI 429
Cdd:cd18790 12 QVDDLLGEIRKRVARGE-----------RVLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 3877954 430 MLATDVAARGLDVDDIKFVINYD-----YPNNSEDYVHRIGRTGR 469
Cdd:cd18790 81 LVGINLLREGLDLPEVSLVAILDadkegFLRSETSLIQTIGRAAR 125
|
|
| DEXHc_RIG-I_DDX58 |
cd18073 |
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ... |
163-284 |
5.39e-03 |
|
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called DEAD box protein 58 (DDX58), is a pathogen-recognition receptor that recognizes viral 5'-triphosphates carrying double-stranded RNA. Upon binding to these microbe-associated molecular patterns (MAMPs), RIG-I forms oligomers and promotes downstream processes that result in type I interferon production and induction of an antiviral state. The optimal ligand for RIG-I has been found to be base-paired or double-stranded RNA (dsRNA) molecules containing a 5' triphosphate (5'-ppp-dsRNA). RIG-I contains two N-terminal caspase activation and recruitment domains (CARDs), which are required for interaction with IPS-1, a superfamily 2 helicase/translocase/ATPase (SF2) domain and a C-terminal regulatory/repressor domain (RD). RIG-I is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350831 [Multi-domain] Cd Length: 202 Bit Score: 38.26 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 163 AMSGRDIISIAKTGSGKTLAFMLPALVHITKQAHRQRGEgpavLVLLPTR-ELAQQVQEVsidFCH---SLGLKMTCLFG 238
Cdd:cd18073 14 AMKGKNTIICAPTGCGKTFVSLLICEHHLKKFPQGQKGK----VVFFATKvPVYEQQKSV---FSKyfeRHGYRVTGISG 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 3877954 239 GASKGPQARDLERGVDIVVATPGRLLDFLDNGT-TNMKKCSYLVLDE 284
Cdd:cd18073 87 ATAENVPVEQIIENNDIIILTPQILVNNLKKGTiPSLSIFTLMIFDE 133
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
378-449 |
6.02e-03 |
|
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: 36.77 E-value: 6.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3877954 378 KTIIFVETKRKADELTRAMRRDGWPTLCIHGDKNQGER-DWVLQEFKAGKT--PIMLATDVAARGLDVDDIKFVI 449
Cdd:cd18799 8 KTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERgDEALILLFFGELkpPILVTVDLLTTGVDIPEVDNVV 82
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
165-316 |
9.11e-03 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 38.79 E-value: 9.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 165 SGRDIISIAKTGSGKTLAFMLPALVHItkqahrQRGeGPAvLVLLPTRELAQQVQEVSIDFcHSLGLKMtclfgGASKGP 244
Cdd:PRK02362 38 DGKNLLAAIPTASGKTLIAELAMLKAI------ARG-GKA-LYIVPLRALASEKFEEFERF-EELGVRV-----GISTGD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3877954 245 QARDLER-GV-DIVVATPGRLLDFLDNGTTNMKKCSYLVLDE------ADRmldmGfePQIKKIIGQIR---PDRQTLMF 313
Cdd:PRK02362 104 YDSRDEWlGDnDIIVATSEKVDSLLRNGAPWLDDITCVVVDEvhlidsANR----G--PTLEVTLAKLRrlnPDLQVVAL 177
|
...
gi 3877954 314 SAT 316
Cdd:PRK02362 178 SAT 180
|
|
| |
