|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
305-680 |
2.44e-155 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 465.01 E-value: 2.44e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 305 TSFGHYGFDDILLQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHIMDqpylEKGDGPIALFL 384
Cdd:COG0513 2 MSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDP----SRPRAPQALIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 385 APTRELAHQIYLETLKYSKYFKLKTTVLYGGVSKQQQCKELKAGCEIIVATPGRLIDMIKLKATKLNRVSYLVLDEADKM 464
Cdd:COG0513 78 APTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 465 FDFGFGPQVLSIVNHVRPDRQTLLFSATFKPNVEEFARTILSDPIKISIGMIGSANSDITQIVqVLKSDSDKwnwlTNQL 544
Cdd:COG0513 158 LDMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRY-YLVDKRDK----LELL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 545 ALLLSQ---GSVLIFVSTKVAVEQLSSNLTKFGFQTCTLHGDKNQIERSQTIQTFKEGKINILIATDVAARGLDIPLIKN 621
Cdd:COG0513 233 RRLLRDedpERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSH 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 66805957 622 VVNYDTSRDIESHTHRIGRTGRAGNTGVAYTLITPKDIHfsvdLIKNLESASQFVPPEL 680
Cdd:COG0513 313 VINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERR----LLRAIEKLIGQKIEEE 367
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
252-687 |
6.77e-147 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 448.07 E-value: 6.77e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 252 LPPIDHSKEEYIEFNKIFYEEHPDIANLTEEQVFEIRKNLDIRMT-GTDLINPVTSFGHYGFDDILLQAIAKQSIETPTP 330
Cdd:PTZ00110 76 LQPIDWKSINLVPFEKNFYKEHPEVSALSSKEVDEIRKEKEITIIaGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTP 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 331 IQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHIMDQPYLEKGDGPIALFLAPTRELAHQIYLETLKYSKYFKLKTT 410
Cdd:PTZ00110 156 IQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNT 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 411 VLYGGVSKQQQCKELKAGCEIIVATPGRLIDMIKLKATKLNRVSYLVLDEADKMFDFGFGPQVLSIVNHVRPDRQTLLFS 490
Cdd:PTZ00110 236 VAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWS 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 491 ATFKPNVEEFARTILSD-PIKISIGMIG-SANSDITQIVQVLKSDSDKwnwltNQLALLLSQ-----GSVLIFVSTKVAV 563
Cdd:PTZ00110 316 ATWPKEVQSLARDLCKEePVHVNVGSLDlTACHNIKQEVFVVEEHEKR-----GKLKMLLQRimrdgDKILIFVETKKGA 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 564 EQLSSNLTKFGFQTCTLHGDKNQIERSQTIQTFKEGKINILIATDVAARGLDIPLIKNVVNYDTSRDIESHTHRIGRTGR 643
Cdd:PTZ00110 391 DFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGR 470
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 66805957 644 AGNTGVAYTLITPKDIHFSVDLIKNLESASQFVPPELIDVAMNN 687
Cdd:PTZ00110 471 AGAKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSNER 514
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
316-512 |
1.70e-128 |
|
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: 386.39 E-value: 1.70e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 316 LLQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHIMDQPYLEKGDGPIALFLAPTRELAHQIY 395
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGEGPIAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 396 LETLKYSKYFKLKTTVLYGGVSKQQQCKELKAGCEIIVATPGRLIDMIKLKATKLNRVSYLVLDEADKMFDFGFGPQVLS 475
Cdd:cd17952 81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 66805957 476 IVNHVRPDRQTLLFSATFKPNVEEFARTILSDPIKIS 512
Cdd:cd17952 161 IVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRVV 197
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
294-511 |
3.41e-94 |
|
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: 297.37 E-value: 3.41e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 294 RMTGTDLINPVTSFGHYGFDDILLQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHIMDQPYL 373
Cdd:cd17953 1 KVRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 374 EKGDGPIALFLAPTRELAHQIYLETLKYSKYFKLKTTVLYGGVSKQQQCKELKAGCEIIVATPGRLIDMIKL---KATKL 450
Cdd:cd17953 81 KPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTAnngRVTNL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66805957 451 NRVSYLVLDEADKMFDFGFGPQVLSIVNHVRPDRQTLLFSATFKPNVEEFARTILSDPIKI 511
Cdd:cd17953 161 RRVTYVVLDEADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
306-654 |
1.56e-91 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 299.03 E-value: 1.56e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 306 SFGHYGFDDILLQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHIMDQPYLEKGDGPI-ALFL 384
Cdd:PRK10590 2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVrALIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 385 APTRELAHQIYLETLKYSKYFKLKTTVLYGGVSKQQQCKELKAGCEIIVATPGRLIDMIKLKATKLNRVSYLVLDEADKM 464
Cdd:PRK10590 82 TPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 465 FDFGFGPQVLSIVNHVRPDRQTLLFSATFKPNVEEFARTILSDPIKISIGMIGSANSDITQIVQVLksDSDKWNWLtnqL 544
Cdd:PRK10590 162 LDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFV--DKKRKREL---L 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 545 ALLLSQGS---VLIFVSTKVAVEQLSSNLTKFGFQTCTLHGDKNQIERSQTIQTFKEGKINILIATDVAARGLDIPLIKN 621
Cdd:PRK10590 237 SQMIGKGNwqqVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPH 316
|
330 340 350
....*....|....*....|....*....|...
gi 66805957 622 VVNYDTSRDIESHTHRIGRTGRAGNTGVAYTLI 654
Cdd:PRK10590 317 VVNYELPNVPEDYVHRIGRTGRAAATGEALSLV 349
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
316-512 |
6.86e-91 |
|
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: 287.42 E-value: 6.86e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 316 LLQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHIMDQPyLEKGDGPIALFLAPTRELAHQIY 395
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEP-KKKGRGPQALVLAPTRELAMQIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 396 LETLKYSKYFKLKTTVLYGGVSKQQQCKELKAGCEIIVATPGRLIDMIKLKATKLNRVSYLVLDEADKMFDFGFGPQVLS 475
Cdd:cd00268 80 EVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 66805957 476 IVNHVRPDRQTLLFSATFKPNVEEFARTILSDPIKIS 512
Cdd:cd00268 160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
305-659 |
6.65e-90 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 293.77 E-value: 6.65e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 305 TSFGHYGFDDILLQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHIMDQPYlEKGDGPIALFL 384
Cdd:PRK11192 1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPR-RKSGPPRILIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 385 APTRELAHQIYLETLKYSKYFKLKTTVLYGGVSKQQQCKELKAGCEIIVATPGRLIDMIKLKATKLNRVSYLVLDEADKM 464
Cdd:PRK11192 80 TPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 465 FDFGFGPQVLSIVNHVRPDRQTLLFSATFKPN-VEEFARTILSDPIKISIGMIGSANSDITQIVQVLKSDSDKwnwlTNQ 543
Cdd:PRK11192 160 LDMGFAQDIETIAAETRWRKQTLLFSATLEGDaVQDFAERLLNDPVEVEAEPSRRERKKIHQWYYRADDLEHK----TAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 544 LALLLSQGSV---LIFVSTKVAVEQLSSNLTKFGFQTCTLHGDKNQIERSQTIQTFKEGKINILIATDVAARGLDIPLIK 620
Cdd:PRK11192 236 LCHLLKQPEVtrsIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVS 315
|
330 340 350
....*....|....*....|....*....|....*....
gi 66805957 621 NVVNYDTSRDIESHTHRIGRTGRAGNTGVAYTLITPKDI 659
Cdd:PRK11192 316 HVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDH 354
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
326-660 |
5.22e-89 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 292.48 E-value: 5.22e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 326 ETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHIMDQPYlekgdGPIALFLAPTRELAHQIYLETLKYSKYF 405
Cdd:PRK11776 25 TEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRF-----RVQALVLCPTRELADQVAKEIRRLARFI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 406 -KLKTTVLYGGVSKQQQCKELKAGCEIIVATPGRLIDMIKLKATKLNRVSYLVLDEADKMFDFGFGPQVLSIVNHVRPDR 484
Cdd:PRK11776 100 pNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMGFQDAIDAIIRQAPARR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 485 QTLLFSATFKPNVEEFARTILSDPIKISIGMiGSANSDITQIV-QVlkSDSDKwnwlTNQLALLLSQ---GSVLIFVSTK 560
Cdd:PRK11776 180 QTLLFSATYPEGIAAISQRFQRDPVEVKVES-THDLPAIEQRFyEV--SPDER----LPALQRLLLHhqpESCVVFCNTK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 561 VAVEQLSSNLTKFGFQTCTLHGDKNQIERSQTIQTFKEGKINILIATDVAARGLDIPLIKNVVNYDTSRDIESHTHRIGR 640
Cdd:PRK11776 253 KECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRIGR 332
|
330 340
....*....|....*....|
gi 66805957 641 TGRAGNTGVAYTLITPKDIH 660
Cdd:PRK11776 333 TGRAGSKGLALSLVAPEEMQ 352
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
316-512 |
9.30e-89 |
|
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: 281.95 E-value: 9.30e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 316 LLQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHIMDQPYLEKGDGPIALFLAPTRELAHQIY 395
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGDGPIVLVLAPTRELAQQIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 396 LETLKYSKYFKLKTTVLYGGVSKQQQCKELKAGCEIIVATPGRLIDMIKLKATKLNRVSYLVLDEADKMFDFGFGPQVLS 475
Cdd:cd17966 81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 66805957 476 IVNHVRPDRQTLLFSATFKPNVEEFARTILSDPIKIS 512
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 ... |
260-514 |
1.16e-84 |
|
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: 273.81 E-value: 1.16e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 260 EEYIEFNKIFYEEHPDIANLTEEQVFEIRKNLDIRMTGTDLINPVTSFGHYGFDDILLQAIAKQSIETPTPIQKQAIPIA 339
Cdd:cd18050 17 SELPKFEKNFYVEHPEVARMTQYDVEELRRKKEITIRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 340 LSGRDLIAIAKTGSGKTATFIWPSISHIMDQPYLEKGDGPIALFLAPTRELAHQIYLETLKYSKYFKLKTTVLYGGVSKQ 419
Cdd:cd18050 97 LSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 420 QQCKELKAGCEIIVATPGRLIDMIKLKATKLNRVSYLVLDEADKMFDFGFGPQVLSIVNHVRPDRQTLLFSATFKPNVEE 499
Cdd:cd18050 177 PQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQ 256
|
250
....*....|....*
gi 66805957 500 FARTILSDPIKISIG 514
Cdd:cd18050 257 LAEDFLRDYVQINIG 271
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
306-517 |
2.17e-79 |
|
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: 257.42 E-value: 2.17e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 306 SFGHYGFDDILLQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHIMDQPYLEKGDG-----PI 380
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGrrkayPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 381 ALFLAPTRELAHQIYLETLKYSKYFKLKTTVLYGGVSKQQQCKELKAGCEIIVATPGRLIDMIKLKATKLNRVSYLVLDE 460
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66805957 461 ADKMFDFGFGPQVLSIVNH----VRPDRQTLLFSATFKPNVEEFARTILSDPIKISIGMIG 517
Cdd:cd17967 161 ADRMLDMGFEPQIRKIVEHpdmpPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVGRVG 221
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
237-682 |
4.28e-77 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 262.03 E-value: 4.28e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 237 SLKNGQSKGKRIIEPLPPIDHSKEEYIEF-NKIFYEEHPDIAN-LTEEQVFEIRKNLDIRMTGTDLINPVTSFGHYGFDD 314
Cdd:PLN00206 51 SLECKQALLRRVAKSRVAVGAPKPKRLPAtDECFYVRDPGSTSgLSSSQAELLRRKLEIHVKGEAVPPPILSFSSCGLPP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 315 ILLQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISH--IMDQPYLEKGDGPIALFLAPTRELAH 392
Cdd:PLN00206 131 KLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRccTIRSGHPSEQRNPLAMVLTPTRELCV 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 393 QIYLETLKYSKYFKLKTTVLYGGVSKQQQCKELKAGCEIIVATPGRLIDMIKLKATKLNRVSYLVLDEADKMFDFGFGPQ 472
Cdd:PLN00206 211 QVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQ 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 473 VLSIVNHVrPDRQTLLFSATFKPNVEEFARTILSDPIKISIGMIGSANSDITQIVQVLKSDSDKwnwlTNQLALLLSQG- 551
Cdd:PLN00206 291 VMQIFQAL-SQPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKK----QKLFDILKSKQh 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 552 ---SVLIFVSTKVAVEQLSSNLTKF-GFQTCTLHGDKNQIERSQTIQTFKEGKINILIATDVAARGLDIPLIKNVVNYDT 627
Cdd:PLN00206 366 fkpPAVVFVSSRLGADLLANAITVVtGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDM 445
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 66805957 628 SRDIESHTHRIGRTGRAGNTGVAYTLITPKDIHFSVDLIKNLESASQFVPPELID 682
Cdd:PLN00206 446 PNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKSSGAAIPRELAN 500
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
282-514 |
5.72e-77 |
|
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: 251.47 E-value: 5.72e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 282 EQVFEIRKNLDIRMTGTDLINPVTSFGHYGFDDILLQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIW 361
Cdd:cd18049 1 QEVEQYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 362 PSISHIMDQPYLEKGDGPIALFLAPTRELAHQIYLETLKYSKYFKLKTTVLYGGVSKQQQCKELKAGCEIIVATPGRLID 441
Cdd:cd18049 81 PAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLID 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66805957 442 MIKLKATKLNRVSYLVLDEADKMFDFGFGPQVLSIVNHVRPDRQTLLFSATFKPNVEEFARTILSDPIKISIG 514
Cdd:cd18049 161 FLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIG 233
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
305-658 |
6.56e-77 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 260.23 E-value: 6.56e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 305 TSFGHYGFDDILLQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHIMDQPYLEK---GDgPIA 381
Cdd:PRK01297 87 TRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKErymGE-PRA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 382 LFLAPTRELAHQIYLETLKYSKYFKLKTTVLYGGVSKQQQCKELKAG-CEIIVATPGRLIDMIKLKATKLNRVSYLVLDE 460
Cdd:PRK01297 166 LIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQRGEVHLDMVEVMVLDE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 461 ADKMFDFGFGPQVLSIVNHVRP--DRQTLLFSATFKPNVEEFARTILSDPIKISIGMIGSANSDITQIVQVLkSDSDKWN 538
Cdd:PRK01297 246 ADRMLDMGFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAV-AGSDKYK 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 539 WLTNqlalLLSQ---GSVLIFVSTKVAVEQLSSNLTKFGFQTCTLHGDKNQIERSQTIQTFKEGKINILIATDVAARGLD 615
Cdd:PRK01297 325 LLYN----LVTQnpwERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIH 400
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 66805957 616 IPLIKNVVNYDTSRDIESHTHRIGRTGRAGNTGVAYTLITPKD 658
Cdd:PRK01297 401 IDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDD 443
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
305-680 |
4.25e-74 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 256.70 E-value: 4.25e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 305 TSFGHYGFDDILLQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHImdQPYLEkgdGPIALFL 384
Cdd:PRK11634 6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNL--DPELK---APQILVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 385 APTRELAHQIYLETLKYSKYFK-LKTTVLYGGVSKQQQCKELKAGCEIIVATPGRLIDMIKLKATKLNRVSYLVLDEADK 463
Cdd:PRK11634 81 APTRELAVQVAEAMTDFSKHMRgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 464 MFDFGFGPQVLSIVNHVRPDRQTLLFSATFKPNVEEFARTILSDPIKISIGMIGSANSDITQ---IVQVLKSDSDKWNWL 540
Cdd:PRK11634 161 MLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQsywTVWGMRKNEALVRFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 541 TNQlalllSQGSVLIFVSTKVAVEQLSSNLTKFGFQTCTLHGDKNQIERSQTIQTFKEGKINILIATDVAARGLDIPLIK 620
Cdd:PRK11634 241 EAE-----DFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERIS 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 621 NVVNYDTSRDIESHTHRIGRTGRAGNTGVAYTLITPKDIHfsvdLIKNLESASQFVPPEL 680
Cdd:PRK11634 316 LVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERR----LLRNIERTMKLTIPEV 371
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
303-650 |
6.15e-69 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 241.01 E-value: 6.15e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 303 PVTSFGHYGFD--DILLQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHIMDQPYL--EKGDG 378
Cdd:PRK04537 5 PLTDLTFSSFDlhPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALadRKPED 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 379 PIALFLAPTRELAHQIYLETLKYSKYFKLKTTVLYGGVSKQQQCKELKAGCEIIVATPGRLIDMIKL-KATKLNRVSYLV 457
Cdd:PRK04537 85 PRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQhKVVSLHACEICV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 458 LDEADKMFDFGFGPQVLSIVNHV--RPDRQTLLFSATFKPNVEEFARTILSDPIKISIGMIGSANSDITQIVqVLKSDSD 535
Cdd:PRK04537 165 LDEADRMFDLGFIKDIRFLLRRMpeRGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRI-YFPADEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 536 KwnwLTNQLALL-LSQGS-VLIFVSTKVAVEQLSSNLTKFGFQTCTLHGDKNQIERSQTIQTFKEGKINILIATDVAARG 613
Cdd:PRK04537 244 K---QTLLLGLLsRSEGArTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARG 320
|
330 340 350
....*....|....*....|....*....|....*..
gi 66805957 614 LDIPLIKNVVNYDTSRDIESHTHRIGRTGRAGNTGVA 650
Cdd:PRK04537 321 LHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDA 357
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
285-517 |
6.56e-69 |
|
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: 230.62 E-value: 6.56e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 285 FEIRKNLDIRMTGTDLINPVTSFGHYGFDDILLQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSI 364
Cdd:cd18052 23 FDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 365 SHIMDQ----PYLEKGDGPIALFLAPTRELAHQIYLETLKYSKYFKLKTTVLYGGVSKQQQCKELKAGCEIIVATPGRLI 440
Cdd:cd18052 103 TGMMKEgltaSSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 441 DMIKLKATKLNRVSYLVLDEADKMFDFGFGPQVLSIVNHV----RPDRQTLLFSATFKPNVEEFARTIL-SDPIKISIGM 515
Cdd:cd18052 183 DFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPgmpsKEDRQTLMFSATFPEEIQRLAAEFLkEDYLFLTVGR 262
|
..
gi 66805957 516 IG 517
Cdd:cd18052 263 VG 264
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
305-653 |
5.42e-68 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 233.71 E-value: 5.42e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 305 TSFGHYGFDDILLQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHIMDQPYLE--KGDGPIAL 382
Cdd:PRK04837 8 QKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEdrKVNQPRAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 383 FLAPTRELAHQIYLETLKYSKYFKLKTTVLYGGVSKQQQCKELKAGCEIIVATPGRLIDMIKLKATKLNRVSYLVLDEAD 462
Cdd:PRK04837 88 IMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEAD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 463 KMFDFGFgpqvlsiVNHVR------PD---RQTLLFSATFKPNVEEFARTILSDPIKISIGMIGSANSDITQIVqVLKSD 533
Cdd:PRK04837 168 RMFDLGF-------IKDIRwlfrrmPPanqRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEEL-FYPSN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 534 SDKwnwltnqLALLLS------QGSVLIFVSTKVAVEQLSSNLTKFGFQTCTLHGDKNQIERSQTIQTFKEGKINILIAT 607
Cdd:PRK04837 240 EEK-------MRLLQTlieeewPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVAT 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 66805957 608 DVAARGLDIPLIKNVVNYDTSRDIESHTHRIGRTGRAGNTGVAYTL 653
Cdd:PRK04837 313 DVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
316-512 |
9.94e-68 |
|
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: 225.66 E-value: 9.94e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 316 LLQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHIMDQP---YLEKGDGPIALFLAPTRELAH 392
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPpldEETKDDGPYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 393 QIYLETLKYSKYFKLKTTVLYGGVSKQQQCKELKAGCEIIVATPGRLIDMIKLKATKLNRVSYLVLDEADKMFDFGFGPQ 472
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 473 VLSIVNHV-----RPD---------------RQTLLFSATFKPNVEEFARTILSDPIKIS 512
Cdd:cd17945 161 VTKILDAMpvsnkKPDteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVVT 220
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
285-518 |
1.37e-65 |
|
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: 221.07 E-value: 1.37e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 285 FEIRKNLDIRMTGTDLINPVTSFGHYGFDDILLQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSI 364
Cdd:cd18051 1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 365 SHIMDQ---PYLEKGDG--------PIALFLAPTRELAHQIYLETLKYSKYFKLKTTVLYGGVSKQQQCKELKAGCEIIV 433
Cdd:cd18051 81 SQIYEQgpgESLPSESGyygrrkqyPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 434 ATPGRLIDMIKLKATKLNRVSYLVLDEADKMFDFGFGPQVLSIV--NHVRP--DRQTLLFSATFKPNVEEFARTILSDPI 509
Cdd:cd18051 161 ATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVeqDTMPPtgERQTLMFSATFPKEIQMLARDFLDNYI 240
|
....*....
gi 66805957 510 KISIGMIGS 518
Cdd:cd18051 241 FLAVGRVGS 249
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
316-514 |
6.36e-63 |
|
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350715 [Multi-domain] Cd Length: 198 Bit Score: 211.68 E-value: 6.36e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 316 LLQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHIMDQpylEKGDGPIALFLAPTRELAHQIY 395
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKP---RKKKGLRALILAPTRELASQIY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 396 LETLKYSKYFKLKTTVLYGG-VSKQQQCKELKAGCEIIVATPGRLIDMIKLKATKLNRVSYLVLDEADKMFDFGFGPQVL 474
Cdd:cd17957 78 RELLKLSKGTGLRIVLLSKSlEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 66805957 475 SIVNHVR-PDRQTLLFSATFKPNVEEFARTILSDPIKISIG 514
Cdd:cd17957 158 EILAACTnPNLQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
316-511 |
1.80e-62 |
|
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: 210.40 E-value: 1.80e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 316 LLQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHIMDQPYL-EKGDGPIALFLAPTRELAHQI 394
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPrEQRNGPGVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 395 YLETLKYSkYFKLKTTVLYGGVSKQQQCKELKAGCEIIVATPGRLIDMIKLKATKLNRVSYLVLDEADKMFDFGFGPQVL 474
Cdd:cd17958 81 EAECSKYS-YKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 66805957 475 SIVNHVRPDRQTLLFSATFKPNVEEFARTILSDPIKI 511
Cdd:cd17958 160 KILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
329-500 |
4.59e-61 |
|
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: 205.17 E-value: 4.59e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 329 TPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHImdqpyLEKGDGPIALFLAPTRELAHQIYLETLKYSKYFKLK 408
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAL-----DKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 409 TTVLYGGVSKQQQCKELKaGCEIIVATPGRLIDMIKlKATKLNRVSYLVLDEADKMFDFGFGPQVLSIVNHVRPDRQTLL 488
Cdd:pfam00270 76 VASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQ-ERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILL 153
|
170
....*....|..
gi 66805957 489 FSATFKPNVEEF 500
Cdd:pfam00270 154 LSATLPRNLEDL 165
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
304-671 |
1.31e-59 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 209.68 E-value: 1.31e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 304 VTSFGHYGFDDILLQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHImDQPYLEKGdgpiALF 383
Cdd:PTZ00424 27 VDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLI-DYDLNACQ----ALI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 384 LAPTRELAHQIYLETLKYSKYFKLKTTVLYGGVSKQQQCKELKAGCEIIVATPGRLIDMIKLKATKLNRVSYLVLDEADK 463
Cdd:PTZ00424 102 LAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 464 MFDFGFGPQVLSIVNHVRPDRQTLLFSATFKPNVEEFARTILSDPIKISIGMIGSANSDITQIVQVLKSDSDKWNWLTNq 543
Cdd:PTZ00424 182 MLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCD- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 544 LALLLSQGSVLIFVSTKVAVEQLSSNLTKFGFQTCTLHGDKNQIERSQTIQTFKEGKINILIATDVAARGLDIPLIKNVV 623
Cdd:PTZ00424 261 LYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVI 340
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 66805957 624 NYDTSRDIESHTHRIGRTGRAGNTGVAYTLITPKDIhfsvDLIKNLES 671
Cdd:PTZ00424 341 NYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDI----EQLKEIER 384
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
306-511 |
4.30e-57 |
|
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: 195.60 E-value: 4.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 306 SFGHYGFDDILLQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHIMDQpylEKGDGPIALFLA 385
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAH---SPTVGARALILS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 386 PTRELAHQIYLETLKYSKYFKLKTTVLYGGVSKQQQCKELKAGCEIIVATPGRLIDMIKLKATKLNRVSYLVLDEADKMF 465
Cdd:cd17959 79 PTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 66805957 466 DFGFGPQVLSIVNHVRPDRQTLLFSATFKPNVEEFARTILSDPIKI 511
Cdd:cd17959 159 EMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
316-512 |
9.79e-57 |
|
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ribosomal subunits protein 1 homolog, and probable ATP-dependent RNA helicase DDX27) is involved in the processing of 5.8S and 28S ribosomal RNAs. More specifically, the encoded protein localizes to the nucleolus, where it interacts with the PeBoW complex to ensure proper 3' end formation of 47S rRNA. DDX27 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350705 [Multi-domain] Cd Length: 196 Bit Score: 194.01 E-value: 9.79e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 316 LLQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHIMDQPYleKGDGPIALFLAPTRELAHQIY 395
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPK--KKAATRVLVLVPTRELAMQCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 396 LETLKYSKYFKLKTTVLYGGVSKQQQCKELKAGCEIIVATPGRLIDMIK-LKATKLNRVSYLVLDEADKMFDFGFGPQVL 474
Cdd:cd17947 79 SVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRnSPSFDLDSIEILVLDEADRMLEEGFADELK 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 66805957 475 SIVNHVRPDRQTLLFSATFKPNVEEFARTILSDPIKIS 512
Cdd:cd17947 159 EILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRVF 196
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
306-512 |
9.82e-56 |
|
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: 191.76 E-value: 9.82e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 306 SFGHYGFDDILLQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHIMD--QPYLekgdgpiALF 383
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLEnpQRFF-------ALV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 384 LAPTRELAHQIYLETLKYSKYFKLKTTVLYGGVSKQQQCKELKAGCEIIVATPGRLIDMIK-LKATKLNRVSYLVLDEAD 462
Cdd:cd17954 74 LAPTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLEnTKGFSLKSLKFLVMDEAD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 66805957 463 KMFDFGFGPQVLSIVNHVRPDRQTLLFSATFKPNVEEFARTILSDPIKIS 512
Cdd:cd17954 154 RLLNMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKIE 203
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
316-511 |
1.07e-55 |
|
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: 191.78 E-value: 1.07e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 316 LLQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHIMDQ----PYLeKGDGPIALFLAPTRELA 391
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQekklPFI-KGEGPYGLIVCPSRELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 392 HQI------YLETLKYSKYFKLKTTVLYGGVSKQQQCKELKAGCEIIVATPGRLIDMIKLKATKLNRVSYLVLDEADKMF 465
Cdd:cd17951 80 RQThevieyYCKALQEGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 66805957 466 DFGFGPQVLSIVNHVRPDRQTLLFSATFKPNVEEFARTILSDPIKI 511
Cdd:cd17951 160 DMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
320-526 |
9.91e-54 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 185.77 E-value: 9.91e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 320 IAKQSIETPTPIQKQAIPIALSG-RDLIAIAKTGSGKTATFIWPSISHIMdqpyleKGDGPIALFLAPTRELAHQIYLET 398
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALK------RGKGGRVLVLVPTRELAEQWAEEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 399 LKYSKYFKLKTTVLYGGVSKQQQCKELKAGC-EIIVATPGRLIDMIKLKATKLNRVSYLVLDEADKMFDFGFGPQVLSIV 477
Cdd:smart00487 75 KKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 66805957 478 NHVRPDRQTLLFSATFKPNVEEFARTILSDPIKISIGmiGSANSDITQI 526
Cdd:smart00487 155 KLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVG--FTPLEPIEQF 201
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
523-654 |
2.86e-52 |
|
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: 178.86 E-value: 2.86e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 523 ITQIVQVLKSDsDKWNWLTNQLALLLSQGSVLIFVSTKVAVEQLSSNLTKFGFQTCTLHGDKNQIERSQTIQTFKEGKIN 602
Cdd:cd18787 1 IKQLYVVVEEE-EKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 66805957 603 ILIATDVAARGLDIPLIKNVVNYDTSRDIESHTHRIGRTGRAGNTGVAYTLI 654
Cdd:cd18787 80 VLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
316-508 |
1.83e-51 |
|
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: 179.73 E-value: 1.83e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 316 LLQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHIMDQPYlekgdGPIALFLAPTRELAHQIY 395
Cdd:cd17955 10 LVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPY-----GIFALVLTPTRELAYQIA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 396 LETLKYSKYFKLKTTVLYGGVSKQQQCKELKAGCEIIVATPGRLIDMIK---LKATKLNRVSYLVLDEADKMFDFGFGPQ 472
Cdd:cd17955 85 EQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEADRLLTGSFEDD 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 66805957 473 VLSIVNHVRPDRQTLLFSATFKPNVEEFARTILSDP 508
Cdd:cd17955 165 LATILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
312-505 |
7.39e-51 |
|
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: 178.16 E-value: 7.39e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 312 FDDILLQAIAKQSIETPTPIQKQAIPIALS-GRDLIAIAKTGSGKTATFIWPSISHIMDQPYLEKGDGPIALFLAPTREL 390
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGVSALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 391 AHQIYLETLKYSKYF-KLKTTVLYGGVSKQQQCKEL-KAGCEIIVATPGRLIDMIK--LKATKLNRVSYLVLDEADKMFD 466
Cdd:cd17964 81 ALQIAAEAKKLLQGLrKLRVQSAVGGTSRRAELNRLrRGRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRLLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 66805957 467 FGFGPQVLSIVNHVRP----DRQTLLFSATFKPNVEEFARTIL 505
Cdd:cd17964 161 MGFRPDLEQILRHLPEknadPRQTLLFSATVPDEVQQIARLTL 203
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
316-512 |
3.63e-49 |
|
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: 172.73 E-value: 3.63e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 316 LLQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHIMdqpylEKGDGPIALFLAPTRELAHQIY 395
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCL-----TEHRNPSALILTPTRELAVQIE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 396 LETLKYSK-YFKLKTTVLYGGVSKQQQCKELKAGCEIIVATPGRLIDMIKLKATKLNRVSYLVLDEADKMFDFGFGPQVL 474
Cdd:cd17962 76 DQAKELMKgLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVL 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 66805957 475 SIVNHVRPDRQTLLFSATFKPNVEEFARTILSDPIKIS 512
Cdd:cd17962 156 DILENISHDHQTILVSATIPRGIEQLAGQLLQNPVRIT 193
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
307-511 |
5.59e-49 |
|
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: 172.48 E-value: 5.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 307 FGHYGFDDILLQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHI-MDQPYLEkgdgpiALFLA 385
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIdPKKDVIQ------ALILV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 386 PTRELAHQIYLETLKYSKYFKLKTTVLYGGVSKQQQCKELKAGCEIIVATPGRLIDMIKLKATKLNRVSYLVLDEADKMF 465
Cdd:cd17940 75 PTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 66805957 466 DFGFGPQVLSIVNHVRPDRQTLLFSATFKPNVEEFARTILSDPIKI 511
Cdd:cd17940 155 SQDFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
325-512 |
4.43e-48 |
|
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1. DDX31 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350707 [Multi-domain] Cd Length: 214 Bit Score: 170.46 E-value: 4.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 325 IETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHIM-DQPYLEKGDGPIALFLAPTRELAHQIYlETLK--Y 401
Cdd:cd17949 11 IEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLsLEPRVDRSDGTLALVLVPTRELALQIY-EVLEklL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 402 SKYFKLKTTVLYGGVSKQQQCKELKAGCEIIVATPGRLIDMIK-LKATKLNRVSYLVLDEADKMFDFGFGPQVLSIVNHV 480
Cdd:cd17949 90 KPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKnTQSFDVSNLRWLVLDEADRLLDMGFEKDITKILELL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 66805957 481 R-------------PDRQTLLFSATFKPNVEEFARTILSDPIKIS 512
Cdd:cd17949 170 DdkrskaggekskpSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
316-493 |
3.21e-47 |
|
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: 168.57 E-value: 3.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 316 LLQAIAKQSIETPTPIQKQAIPIALS-GRDLIAIAKTGSGKTATFIWPSISHIMDQ----PYLEKGDGPIALFLAPTREL 390
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLLSQkssnGVGGKQKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 391 AHQI--YLETLKysKYFKLKTTVLYGGVSKQQQCKELKAGCEIIVATPGRLIDMIKLKATKLNR---VSYLVLDEADKMF 465
Cdd:cd17946 81 AVQVkdHLKAIA--KYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLANlksLRFLVLDEADRML 158
|
170 180 190
....*....|....*....|....*....|....*
gi 66805957 466 DFG-FGP--QVLSIVN----HVRPDRQTLLFSATF 493
Cdd:cd17946 159 EKGhFAEleKILELLNkdraGKKRKRQTFVFSATL 193
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
317-513 |
8.49e-47 |
|
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: 165.93 E-value: 8.49e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 317 LQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHImdqpYLEK---GDGPIALFLAPTRELAHQ 393
Cdd:cd17941 2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKL----YRERwtpEDGLGALIISPTRELAMQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 394 IYlETL-KYSKYFKLKTTVLYGGVSKQQQcKELKAGCEIIVATPGRLID-MIKLKATKLNRVSYLVLDEADKMFDFGFGP 471
Cdd:cd17941 78 IF-EVLrKVGKYHSFSAGLIIGGKDVKEE-KERINRMNILVCTPGRLLQhMDETPGFDTSNLQMLVLDEADRILDMGFKE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 66805957 472 QVLSIVNHVRPDRQTLLFSATFKPNVEEFARTILSDPIKISI 513
Cdd:cd17941 156 TLDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
316-512 |
2.28e-46 |
|
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: 165.06 E-value: 2.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 316 LLQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHIMDQPYLEKGDGPIALFLAPTRELAHQIY 395
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKKGQVGALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 396 LETLKYSKY--FKLKTTVLYGGVSKQQQCKELKA-GCEIIVATPGRLIDMIKLKATKLN--RVSYLVLDEADKMFDFGFG 470
Cdd:cd17960 81 EVLQSFLEHhlPKLKCQLLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLSRKADKVKvkSLEVLVLDEADRLLDLGFE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 66805957 471 PQVLSIVNHVRPDRQTLLFSATFKPNVEEFARTILSDPIKIS 512
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRVV 202
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
310-511 |
9.42e-45 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation factor-4A (eIF4A) family consists of 3 proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA. EIF4A proteins are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350697 [Multi-domain] Cd Length: 199 Bit Score: 160.18 E-value: 9.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 310 YGFDDILLQAIAKQSIETPTPIQKQAI-PIaLSGRDLIAIAKTGSGKTATFiwpSISHImdQPYLEKGDGPIALFLAPTR 388
Cdd:cd17939 2 MGLSEDLLRGIYAYGFEKPSAIQQRAIvPI-IKGRDVIAQAQSGTGKTATF---SIGAL--QRIDTTVRETQALVLAPTR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 389 ELAHQIYLETLKYSKYFKLKTTVLYGGVSKQQQCKELKAGCEIIVATPGRLIDMIKLKATKLNRVSYLVLDEADKMFDFG 468
Cdd:cd17939 76 ELAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRG 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 66805957 469 FGPQVLSIVNHVRPDRQTLLFSATFKPNVEEFARTILSDPIKI 511
Cdd:cd17939 156 FKDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
313-509 |
3.25e-43 |
|
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: 156.20 E-value: 3.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 313 DDILLQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHIMDQ-PYLEKGDGPIALFLAPTRELA 391
Cdd:cd17961 2 DPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAkAESGEEQGTRALILVPTRELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 392 HQIYLETLKYSKYF--KLKTTVLYGGVSKQQQCKELKAGCEIIVATPGRLIDMIKLKATKL-NRVSYLVLDEADKMFDFG 468
Cdd:cd17961 82 QQVSKVLEQLTAYCrkDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLlSTLKYLVIDEADLVLSYG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 66805957 469 FGPQVLSIVNHVRPDRQTLLFSATFKPNVEEFARTILSDPI 509
Cdd:cd17961 162 YEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
316-512 |
6.14e-41 |
|
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: 148.95 E-value: 6.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 316 LLQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSIsHIMDqpyLEKGdGPIALFLAPTRELAHQIY 395
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIAL-ESLD---LERR-HPQVLILAPTREIAVQIH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 396 LETLKYSKYFK-LKTTVLYGGVSKQQQCKELKaGCEIIVATPGRLIDMIKLKATKLNRVSYLVLDEADKMFDFGFGPQVL 474
Cdd:cd17943 76 DVFKKIGKKLEgLKCEVFIGGTPVKEDKKKLK-GCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVN 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 66805957 475 SIVNHVRPDRQTLLFSATFKPNVEEFARTILSDPIKIS 512
Cdd:cd17943 155 WIFSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
304-513 |
2.95e-40 |
|
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: 147.88 E-value: 2.95e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 304 VTSFGHYGFDDILLQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHImdqpylEKGDGPI-AL 382
Cdd:cd17950 1 SSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQL------EPVDGQVsVL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 383 FLAPTRELAHQIYLETLKYSKYFK-LKTTVLYGGVSKQQQCKELKAGC-EIIVATPGRLIDMIKLKATKLNRVSYLVLDE 460
Cdd:cd17950 75 VICHTRELAFQISNEYERFSKYMPnVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 66805957 461 ADKMF-DFGFGPQVLSIVNHVRPDRQTLLFSATFKPNVEEFARTILSDPIKISI 513
Cdd:cd17950 155 CDKMLeQLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
316-511 |
5.76e-40 |
|
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: 146.57 E-value: 5.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 316 LLQAIAKQSIETPTPIQKQAIPIALSG--RDLIAIAKTGSGKTATFIWPSISHImdQPYLEKgdgPIALFLAPTRELAHQ 393
Cdd:cd17963 5 LLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRV--DPTLKS---PQALCLAPTRELARQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 394 IYLETLKYSKYFKLKTTVLYGGVSKQQQcKELKAgcEIIVATPGRLIDMIKLKATKLNRVSYLVLDEADKMFDF-GFGPQ 472
Cdd:cd17963 80 IGEVVEKMGKFTGVKVALAVPGNDVPRG-KKITA--QIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGHGDQ 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 66805957 473 VLSIVNHVRPDRQTLLFSATFKPNVEEFARTILSDPIKI 511
Cdd:cd17963 157 SIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
317-512 |
3.15e-39 |
|
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: 144.43 E-value: 3.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 317 LQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHIMDQPYLEKgDGPIALFLAPTRELAHQIY- 395
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPR-NGTGVIIISPTRELALQIYg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 396 --LETLKY-SKYFKLkttvLYGGVSKQQQCKELKAGCEIIVATPGRLIDMIKLKATKLNR-VSYLVLDEADKMFDFGFGP 471
Cdd:cd17942 81 vaKELLKYhSQTFGI----VIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKnLQCLIIDEADRILEIGFEE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 66805957 472 QVLSIVNHVRPDRQTLLFSATFKPNVEEFARTIL-SDPIKIS 512
Cdd:cd17942 157 EMRQIIKLLPKRRQTMLFSATQTRKVEDLARISLkKKPLYVG 198
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
312-511 |
4.06e-39 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation factor 4A-I (DDX2A) and eukaryotic initiation factor 4A-II (DDX2B) are involved in cap recognition and are required for mRNA binding to ribosome. They are DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350804 [Multi-domain] Cd Length: 201 Bit Score: 144.13 E-value: 4.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 312 FDDI-----LLQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFiwpSIShIMDQPYLEKgDGPIALFLAP 386
Cdd:cd18046 1 FDDMnlkesLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATF---SIS-ILQQIDTSL-KATQALVLAP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 387 TRELAHQIYLETLKYSKYFKLKTTVLYGGVSKQQQCKELKAGCEIIVATPGRLIDMIKLKATKLNRVSYLVLDEADKMFD 466
Cdd:cd18046 76 TRELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 66805957 467 FGFGPQVLSIVNHVRPDRQTLLFSATFKPNVEEFARTILSDPIKI 511
Cdd:cd18046 156 RGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
307-508 |
3.60e-38 |
|
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: 141.69 E-value: 3.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 307 FGHYGFDDILLQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHIMdqpylekgdgpiALFLAP 386
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIVV------------ALILEP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 387 TRELAHQIYLETLKYSKYF---KLKTTVLYGGVSKQQQCKELKAGCEIIVATPGRLIDMIKLKATKLNRVSYLVLDEADK 463
Cdd:cd17938 69 SRELAEQTYNCIENFKKYLdnpKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADR 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 66805957 464 MFDFGFGPQVLSIVNH-----VRPDR-QTLLFSATF-KPNVEEFARTILSDP 508
Cdd:cd17938 149 LLSQGNLETINRIYNRipkitSDGKRlQVIVCSATLhSFEVKKLADKIMHFP 200
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
316-512 |
1.47e-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: 132.11 E-value: 1.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 316 LLQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHIMDQPYLEKG--DGPIALFLAPTRELAHQ 393
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGpfNAPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 394 IYLETLKYSKYFKLKTTVLYGGVSKQQQCKELKAGCEIIVATPGRLIDMIKLKATKLNRVSYLVLDEADKMFDFGFGPQV 473
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 66805957 474 LSIVNH-----VRPDR--------QTLLFSATFKPNVEEfartILSDPIKIS 512
Cdd:cd17948 161 SHFLRRfplasRRSENtdgldpgtQLVLVSATMPSGVGE----VLSKVIDVD 208
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
307-511 |
2.38e-33 |
|
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: 127.58 E-value: 2.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 307 FGHYGFDDILLQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFiwpSISHI-MDQPYLEKgdgPIALFLA 385
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATF---SISVLqCLDIQVRE---TQALILS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 386 PTRELAHQIYLETLKYSKYFKLKTTVLYGGVSKQQQCKELKAGCEIIVATPGRLIDMIKLKATKLNRVSYLVLDEADKMF 465
Cdd:cd18045 75 PTRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEML 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 66805957 466 DFGFGPQVLSIVNHVRPDRQTLLFSATFKPNVEEFARTILSDPIKI 511
Cdd:cd18045 155 NKGFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
330-492 |
1.32e-32 |
|
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: 125.35 E-value: 1.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 330 PIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHIM-DQPYLEKGDGPIALFLAPTRELAHQIYLETLKYSKyfKLK 408
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQeDQQPRKRGRAPKVLVLAPTRELANQVTKDFKDITR--KLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 409 TTVLYGGVSKQQQCKELKAGCEIIVATPGRLIDMIKLKATKLNRVSYLVLDEADKMFDFGFGPQVLSIVnHVR------P 482
Cdd:cd17944 93 VACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEIL-SVSykkdseD 171
|
170
....*....|
gi 66805957 483 DRQTLLFSAT 492
Cdd:cd17944 172 NPQTLLFSAT 181
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
535-645 |
4.83e-29 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 111.92 E-value: 4.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 535 DKWNWLTNQLALLlSQGSVLIFVSTK--VAVEQLssnLTKFGFQTCTLHGDKNQIERSQTIQTFKEGKINILIATDVAAR 612
Cdd:pfam00271 1 EKLEALLELLKKE-RGGKVLIFSQTKktLEAELL---LEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAER 76
|
90 100 110
....*....|....*....|....*....|...
gi 66805957 613 GLDIPLIKNVVNYDTSRDIESHTHRIGRTGRAG 645
Cdd:pfam00271 77 GLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
564-645 |
3.12e-27 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 105.76 E-value: 3.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 564 EQLSSNLTKFGFQTCTLHGDKNQIERSQTIQTFKEGKINILIATDVAARGLDIPLIKNVVNYDTSRDIESHTHRIGRTGR 643
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 66805957 644 AG 645
Cdd:smart00490 81 AG 82
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
316-508 |
2.50e-25 |
|
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350714 [Multi-domain] Cd Length: 231 Bit Score: 105.41 E-value: 2.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 316 LLQAIAKQSIETPTPIQKQAIPIALSG---------RDLIAIAKTGSGKTATFIWPSISHIMDQPylekgdGPI--ALFL 384
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKRV------VPRlrALIV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 385 APTRELAHQIYLETLKYSKYFKLKTTVLYGGVS---KQQQCKELKAG-----CEIIVATPGRLIDmiKLKATK---LNRV 453
Cdd:cd17956 75 VPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSfkkEQKLLLVDTSGrylsrVDILVATPGRLVD--HLNSTPgftLKHL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66805957 454 SYLVLDEADKMFD---FGFGPQVLSIVNHVRPDR-----------------QTLLFSATFKPNVEEFARTILSDP 508
Cdd:cd17956 153 RFLVIDEADRLLNqsfQDWLETVMKALGRPTAPDlgsfgdanllersvrplQKLLFSATLTRDPEKLSSLKLHRP 227
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
316-645 |
8.42e-23 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 103.44 E-value: 8.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 316 LLQAIAKQSIETPTPIQKQAIP-IALSGRDLIAIAKTGSGKT--ATFIwpSISHIMDqpylekgdGPIALFLAPTRELAH 392
Cdd:COG1204 11 VIEFLKERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTliAELA--ILKALLN--------GGKALYIVPLRALAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 393 QIYLETLKYSKYFKLKTTVLYGGVSKQqqcKELKAGCEIIVATPGRLIDMIKLKATKLNRVSYLVLDEADKMFDFGFGPQ 472
Cdd:COG1204 81 EKYREFKRDFEELGIKVGVSTGDYDSD---DEWLGRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAHLIDDESRGPT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 473 ---VLSIVNHVRPDRQTLLFSATFkPNVEEFAR-----TILSD--PIKISIGMIgsaNSDITQIVQVLKSDSDKWNWLTn 542
Cdd:COG1204 158 levLLARLRRLNPEAQIVALSATI-GNAEEIAEwldaeLVKSDwrPVPLNEGVL---YDGVLRFDDGSRRSKDPTLALA- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 543 qLALLLSQGSVLIFVSTKVAVE----QLSSNLTKFG-----------------FQTCTL----------------HGDKN 585
Cdd:COG1204 233 -LDLLEEGGQVLVFVSSRRDAEslakKLADELKRRLtpeereeleelaeelleVSEETHtnekladclekgvafhHAGLP 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66805957 586 QIERSQTIQTFKEGKINILIATDVAARGLDIPlIKNVVNYDTSRDIESH-THR-----IGRTGRAG 645
Cdd:COG1204 312 SELRRLVEDAFREGLIKVLVATPTLAAGVNLP-ARRVIIRDTKRGGMVPiPVLefkqmAGRAGRPG 376
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
314-506 |
3.52e-22 |
|
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: 97.06 E-value: 3.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 314 DILLQAIAKQSIET-----PTPIQKQAIPIALSGRD-----------------LIAiAKTGSGKTATFIWPSISHIMDQP 371
Cdd:cd17965 12 EAIIKEILKGSNKTdeeikPSPIQTLAIKKLLKTLMrkvtkqtsneepklevfLLA-AETGSGKTLAYLAPLLDYLKRQE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 372 YLEKGDG------------PIALFLAPTRELAHQIYlETLK-YSKYFKLKTTVLYG--GVSKQQQCKELKAGCEIIVATP 436
Cdd:cd17965 91 QEPFEEAeeeyesakdtgrPRSVILVPTHELVEQVY-SVLKkLSHTVKLGIKTFSSgfGPSYQRLQLAFKGRIDILVTTP 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 437 GRLIDMIKLKATKLNRVSYLVLDEADKMFDFGFGPQVLSIVNHVRPDRQTLLFSATFkPNveEFARTILS 506
Cdd:cd17965 170 GKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATI-PK--EFDKTLRK 236
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
304-508 |
6.38e-22 |
|
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: 95.47 E-value: 6.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 304 VTSFGHYGFDDILLQAIAKQSIETPTPIQKQAIPIALSG--RDLIAIAKTGSGKTATFIWPSISHI-MDQPYlekgdgPI 380
Cdd:cd18048 17 VKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVdALKLY------PQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 381 ALFLAPTRELAHQIYLETLKYSKyFKLKTTVLYGgVSKQQQCKELKAGCEIIVATPGRLID-MIKLKATKLNRVSYLVLD 459
Cdd:cd18048 91 CLCLSPTFELALQTGKVVEEMGK-FCVGIQVIYA-IRGNRPGKGTDIEAQIVIGTPGTVLDwCFKLRLIDVTNISVFVLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 66805957 460 EADKMFDF-GFGPQVLSIVNHVRPDRQTLLFSATFKPNVEEFARTILSDP 508
Cdd:cd18048 169 EADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDP 218
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
316-508 |
7.94e-19 |
|
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both mRNA (mRNA) export from the nucleus into the cytoplasm and in mRNA translation. DDX19 functions in the nucleus in resolving RNA:DNA hybrids (R-loops). Activation of a DNA damage response pathway dependent upon the ATR kinase, a major regulator of replication fork progression, stimulates translocation of DDX19 from the cytoplasm into the nucleus. Only nuclear Ddx19 is competent to resolve R-loops. DDX19 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350805 [Multi-domain] Cd Length: 205 Bit Score: 85.93 E-value: 7.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 316 LLQAIAKQSIETPTPIQKQAIPIALSG--RDLIAIAKTGSGKTATFIWPSISHImdQPYLEKGDgpiALFLAPTRELAHQ 393
Cdd:cd18047 12 LLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV--EPANKYPQ---CLCLSPTYELALQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 394 IYLETLKYSKYFKlKTTVLYGgVSKQQQCKELKAGCEIIVATPGRLIDM-IKLKATKLNRVSYLVLDEADKMFDF-GFGP 471
Cdd:cd18047 87 TGKVIEQMGKFYP-ELKLAYA-VRGNKLERGQKISEQIVIGTPGTVLDWcSKLKFIDPKKIKVFVLDEADVMIATqGHQD 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 66805957 472 QVLSIVNHVRPDRQTLLFSATFKPNVEEFARTILSDP 508
Cdd:cd18047 165 QSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
327-617 |
8.92e-19 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 91.24 E-value: 8.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 327 TPTPIQKQAI-----PIALSGRDLIAIAKTGSGKTATFIwpsisHIMDQPYlekgDGPIALFLAPTRELAHQIYlETLKy 401
Cdd:COG1061 80 ELRPYQQEALeallaALERGGGRGLVVAPTGTGKTVLAL-----ALAAELL----RGKRVLVLVPRRELLEQWA-EELR- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 402 skyfKLKTTVLYGGVSKQQQCKelkagceIIVATPGRLIDMIKLKATKlNRVSYLVLDEA----DKMFDfgfgpqvlSIV 477
Cdd:COG1061 149 ----RFLGDPLAGGGKKDSDAP-------ITVATYQSLARRAHLDELG-DRFGLVIIDEAhhagAPSYR--------RIL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 478 NHVRPDRqTLLFSATFK------PNVEEFARTILSDPIK--ISIGMIGSAnsDITQIVQVLKSDSDKWNWLTNQLALLLS 549
Cdd:COG1061 209 EAFPAAY-RLGLTATPFrsdgreILLFLFDGIVYEYSLKeaIEDGYLAPP--EYYGIRVDLTDERAEYDALSERLREALA 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 550 QGS-------------------VLIFVSTKVAVEQLSSNLTKFGFQTCTLHGDKNQIERSQTIQTFKEGKINILIATDVA 610
Cdd:COG1061 286 ADAerkdkilrellrehpddrkTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVL 365
|
....*..
gi 66805957 611 ARGLDIP 617
Cdd:COG1061 366 NEGVDVP 372
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
342-492 |
1.58e-15 |
|
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: 74.75 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 342 GRDLIAIAKTGSGKTATFiwpsiSHIMDQPYLEKGDGpiALFLAPTRELAHQIYLEtlkYSKYFKLKTTV--LYGGVSKQ 419
Cdd:cd00046 1 GENVLITAPTGSGKTLAA-----LLAALLLLLKKGKK--VLVLVPTKALALQTAER---LRELFGPGIRVavLVGGSSAE 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66805957 420 QQCKELKAGCEIIVATPGRLIDMIK-LKATKLNRVSYLVLDEADkMFD---FGFGPQVLSIVNHVRPDRQTLLFSAT 492
Cdd:cd00046 71 EREKNKLGDADIIIATPDMLLNLLLrEDRLFLKDLKLIIVDEAH-ALLidsRGALILDLAVRKAGLKNAQVILLSAT 146
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
327-502 |
3.41e-14 |
|
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: 71.91 E-value: 3.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 327 TPTPIQKQAI-PIALSGRDLIAIAKTGSGKTATFIWPSISHIMDQpylekgdGPIALFLAPTRELAHQIYLETLKYSKYF 405
Cdd:cd17921 1 LLNPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRALATS-------GGKAVYIAPTRALVNQKEADLRERFGPL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 406 KLKTTVLYGGVSKqqqCKELKAGCEIIVATPGRLIDMI-KLKATKLNRVSYLVLDEADKMFDFGFGP---QVLSIVNHVR 481
Cdd:cd17921 74 GKNVGLLTGDPSV---NKLLLAEADILVATPEKLDLLLrNGGERLIQDVRLVVVDEAHLIGDGERGVvleLLLSRLLRIN 150
|
170 180
....*....|....*....|.
gi 66805957 482 PDRQTLLFSATFkPNVEEFAR 502
Cdd:cd17921 151 KNARFVGLSATL-PNAEDLAE 170
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
330-501 |
4.87e-13 |
|
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: 68.51 E-value: 4.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 330 PIQKQAIPIAL-SGRDLIAIAKTGSGKTATFIWPSISHIMDqpylekgdGPIALFLAPTRELAHQIYLETLKYSKY-FKL 407
Cdd:cd18028 4 PPQAEAVRAGLlKGENLLISIPTASGKTLIAEMAMVNTLLE--------GGKALYLVPLRALASEKYEEFKKLEEIgLKV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 408 KTTVlyggvSKQQQCKELKAGCEIIVATPGRLIDMIKLKATKLNRVSYLVLDEADKMFDFGFGPQVLSIVNHVR---PDR 484
Cdd:cd18028 76 GIST-----GDYDEDDEWLGDYDIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPTLESIVARLRrlnPNT 150
|
170
....*....|....*..
gi 66805957 485 QTLLFSATFkPNVEEFA 501
Cdd:cd18028 151 QIIGLSATI-GNPDELA 166
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
553-655 |
8.67e-13 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 72.46 E-value: 8.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 553 VLIFVSTKVAVEQLSSNLTKFGFQTCTLHG-----------DKNQIErsqTIQTFKEGKINILIATDVAARGLDIPLIKN 621
Cdd:COG1111 356 IIVFTQYRDTAEMIVEFLSEPGIKAGRFVGqaskegdkgltQKEQIE---ILERFRAGEFNVLVATSVAEEGLDIPEVDL 432
|
90 100 110
....*....|....*....|....*....|....*...
gi 66805957 622 VVNYD--TS--RDIEshthRIGRTGRaGNTGVAYTLIT 655
Cdd:COG1111 433 VIFYEpvPSeiRSIQ----RKGRTGR-KREGRVVVLIA 465
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
311-653 |
1.81e-12 |
|
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: 71.41 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 311 GFDDILLQAIAKQSIETPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHIMDQPylekgdGPIALFLAPTREL 390
Cdd:COG1205 40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDP------GATALYLYPTKAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 391 AH-QiyLETL-KYSKYFKLKTTV-LYGGVSKQQQCKELKAGCEIIVATPgrliDM----IKLKATK----LNRVSYLVLD 459
Cdd:COG1205 114 ARdQ--LRRLrELAEALGLGVRVaTYDGDTPPEERRWIREHPDIVLTNP----DMlhygLLPHHTRwarfFRNLRYVVID 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 460 EAdKMFDFGFGPQV-------LSIVNHVRPDRQTLLFSATFKpNVEEFART---------------------ILSDPIKI 511
Cdd:COG1205 188 EA-HTYRGVFGSHVanvlrrlRRICRHYGSDPQFILASATIG-NPAEHAERltgrpvtvvdedgsprgertfVLWNPPLV 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 512 SIGMIGSANSDITQIvqvlksdsdkwnwltnqLALLLSQG-SVLIFVSTKVAVEQLSSNLTKFgfqtCTLHGDKNQI--- 587
Cdd:COG1205 266 DDGIRRSALAEAARL-----------------LADLVREGlRTLVFTRSRRGAELLARYARRA----LREPDLADRVaay 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 588 -------ERSQTIQTFKEGKINILIAT-------DVAarGLDIPLIknvVNYDTSRDieSHTHRIGRTGRAGNTGVAYTL 653
Cdd:COG1205 325 ragylpeERREIERGLRSGELLGVVSTnalelgiDIG--GLDAVVL---AGYPGTRA--SFWQQAGRAGRRGQDSLVVLV 397
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
343-461 |
4.66e-11 |
|
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: 63.05 E-value: 4.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 343 RDLIAIAKTGSGKTatFIwpSISHIM---DQPYLEKGDGPIALFLAPTRELAHQ--IYLETlkyskYFKLKTTVLYGGVS 417
Cdd:cd18034 17 RNTIVVLPTGSGKT--LI--AVMLIKemgELNRKEKNPKKRAVFLVPTVPLVAQqaEAIRS-----HTDLKVGEYSGEMG 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 66805957 418 KQQQCKELKAGC----EIIVATPGRLIDMIKLKATKLNRVSYLVLDEA 461
Cdd:cd18034 88 VDKWTKERWKEElekyDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
332-504 |
6.95e-10 |
|
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: 59.14 E-value: 6.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 332 QKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHIMDQPylekgdGPIALFLAPTRELAH-QiyLETL-KYSKYFKLKT 409
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDP------GSRALYLYPTKALAQdQ--LRSLrELLEQLGLGI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 410 TV-LYGG-VSKQQQCKELKAGCEIIVATPgrliDMI--------KLKATKLNRVSYLVLDEAdKMFDFGFGPQV------ 473
Cdd:cd17923 77 RVaTYDGdTPREERRAIIRNPPRILLTNP----DMLhyallphhDRWARFLRNLRYVVLDEA-HTYRGVFGSHValllrr 151
|
170 180 190
....*....|....*....|....*....|..
gi 66805957 474 -LSIVNHVRPDRQTLLFSATFKpNVEEFARTI 504
Cdd:cd17923 152 lRRLCRRYGADPQFILTSATIG-NPAEHARTL 182
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
531-659 |
1.28e-09 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 61.70 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 531 KSDSDKWNWLTNQLALLlSQGSVLIFVSTKVAVEQLSSNLTKFGFQTCTLHGDKNQIERSQTIQTFKEGKINILIATdVA 610
Cdd:COG0514 212 KPPDDKLAQLLDFLKEH-PGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IA 289
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 66805957 611 -ARGLDIPLIKNVVNYDTSRDIESHTHRIGRTGRAGNTGVAYTLITPKDI 659
Cdd:COG0514 290 fGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDV 339
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
554-644 |
4.55e-09 |
|
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: 56.06 E-value: 4.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 554 LIFVSTKVAV-------EQLSSNLTKF--------GFQTCTLHGDKNQIERSQTIQTFKEGKINILIATDVAARGLDIPL 618
Cdd:cd18802 29 IIFVERRATAvvlsrllKEHPSTLAFIrcgfligrGNSSQRKRSLMTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPA 108
|
90 100
....*....|....*....|....*.
gi 66805957 619 IKNVVNYDTSRDIESHthrIGRTGRA 644
Cdd:cd18802 109 CNLVIRFDLPKTLRSY---IQSRGRA 131
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
553-654 |
1.26e-08 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350188 [Multi-domain] Cd Length: 143 Bit Score: 54.67 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 553 VLIFVSTKVAVEQLSSNLTKFGFQT--------CTLHGDK--NQIERSQTIQTFKEGKINILIATDVAARGLDIPLIKNV 622
Cdd:cd18801 33 VIIFSEFRDSAEEIVNFLSKIRPGIratrfigqASGKSSKgmSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLI 112
|
90 100 110
....*....|....*....|....*....|..
gi 66805957 623 VNYDTSRDIESHTHRIGRTGRaGNTGVAYTLI 654
Cdd:cd18801 113 ICYDASPSPIRMIQRMGRTGR-KRQGRVVVLL 143
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
550-645 |
2.77e-08 |
|
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: 53.37 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 550 QGSVLIFVSTKVAVEQLSSNLTKFGFQTCTLHGDKNQIERSQTIQTFKEGKINILIATdVA-ARGLDIPLIKNVVNYDTS 628
Cdd:cd18794 30 GGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVAT-VAfGMGIDKPDVRFVIHYSLP 108
|
90
....*....|....*..
gi 66805957 629 RDIESHTHRIGRTGRAG 645
Cdd:cd18794 109 KSMESYYQESGRAGRDG 125
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
600-655 |
3.95e-08 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 51.17 E-value: 3.95e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 66805957 600 KINILIATDVAARGLDIPLIKNVVNYDTSRDIESHTHRIGRTGRAGNTGVAYTLIT 655
Cdd:cd18785 22 SLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILFV 77
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
330-659 |
5.50e-08 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 56.65 E-value: 5.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 330 PIQKQAIPIALSGRDLIAIAKTGSGKTATF-------------IWPSISHIMDQPYLEKGDGPIALFLAPTRelahqiyl 396
Cdd:PRK11057 28 PGQQEIIDAVLSGRDCLVVMPTGGGKSLCYqipalvldgltlvVSPLISLMKDQVDQLLANGVAAACLNSTQ-------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 397 etlkyskyfklkttvlyggvSKQQQcKELKAGC-----EIIVATPGRLIDMIKLKATKLNRVSYLVLDEADKMFDFG--F 469
Cdd:PRK11057 100 --------------------TREQQ-LEVMAGCrtgqiKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGhdF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 470 GPQ--VLSIVNHVRPDRQTLLFSATF-KPNVEEFARTI-LSDPIkISIGMIGSANSDITqIVQVLKSDSDKWNWLTNQla 545
Cdd:PRK11057 159 RPEyaALGQLRQRFPTLPFMALTATAdDTTRQDIVRLLgLNDPL-IQISSFDRPNIRYT-LVEKFKPLDQLMRYVQEQ-- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 546 lllsQG-SVLIFVSTKVAVEQLSSNLTKFGFQTCTLHGDKNQIERSQTIQTFKEGKINILIATDVAARGLDIPLIKNVVN 624
Cdd:PRK11057 235 ----RGkSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVH 310
|
330 340 350
....*....|....*....|....*....|....*
gi 66805957 625 YDTSRDIESHTHRIGRTGRAGNTGVAYTLITPKDI 659
Cdd:PRK11057 311 FDIPRNIESYYQETGRAGRDGLPAEAMLFYDPADM 345
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
311-688 |
2.18e-07 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 54.89 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 311 GFDDILLQAIAKQSIETPTPiQKQAIPIALSGRDLIAIAKTGSGKTATfiwpSISHImdqpYLEKGDGPIALFLAPTREL 390
Cdd:PRK01172 7 GYDDEFLNLFTGNDFELYDH-QRMAIEQLRKGENVIVSVPTAAGKTLI----AYSAI----YETFLAGLKSIYIVPLRSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 391 AHQIYLETLKYsKYFKLKTTVLYGGVSKQqqcKELKAGCEIIVATPGRLIDMIKLKATKLNRVSYLVLDEADKMFDFGFG 470
Cdd:PRK01172 78 AMEKYEELSRL-RSLGMRVKISIGDYDDP---PDFIKRYDVVILTSEKADSLIHHDPYIINDVGLIVADEIHIIGDEDRG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 471 PQ---VLSIVNHVRPDRQTLLFSATFKpNVEEFAR-----TILSD--PIKISIGMI--------GSANS--DITQIVQVL 530
Cdd:PRK01172 154 PTletVLSSARYVNPDARILALSATVS-NANELAQwlnasLIKSNfrPVPLKLGILyrkrlildGYERSqvDINSLIKET 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 531 KSDSdkwnwltnqlalllsqGSVLIFVSTKVAVEQLSSNLTK-FG-FQTCTLHGDKNQI--------------------- 587
Cdd:PRK01172 233 VNDG----------------GQVLVFVSSRKNAEDYAEMLIQhFPeFNDFKVSSENNNVyddslnemlphgvafhhagls 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 588 --ERSQTIQTFKEGKINILIATDVAARGLDIP----LIKNVVNY--DTSRDIESH--THRIGRTGRAGNTGVAYTLITPK 657
Cdd:PRK01172 297 neQRRFIEEMFRNRYIKVIVATPTLAAGVNLParlvIVRDITRYgnGGIRYLSNMeiKQMIGRAGRPGYDQYGIGYIYAA 376
|
410 420 430
....*....|....*....|....*....|.
gi 66805957 658 DIHfSVDLIKNLESASqfvpPELIDVAMNNP 688
Cdd:PRK01172 377 SPA-SYDAAKKYLSGE----PEPVISYMGSQ 402
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
313-643 |
5.33e-07 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 53.67 E-value: 5.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 313 DDILLQAIAKQSIETPTPIQKQAIPI-ALSGRDLIAIAKTGSGKTAtfiwpsISHI-MDQPYLEKGDGpiALFLAPTREL 390
Cdd:PRK00254 9 DERIKRVLKERGIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTL------VAEIvMVNKLLREGGK--AVYLVPLKAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 391 AHQIYLEtLKYSKYFKLKTTVLYGGVSKQQqckELKAGCEIIVATPGRLIDMIKLKATKLNRVSYLVLDEADKMFDFGFG 470
Cdd:PRK00254 81 AEEKYRE-FKDWEKLGLRVAMTTGDYDSTD---EWLGKYDIIIATAEKFDSLLRHGSSWIKDVKLVVADEIHLIGSYDRG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 471 PQVLSIVNHVRPDRQTLLFSATFKpNVEEF-----ARTILSD--PIKISIGMIGSAnsdiTQIVQVLKSDSDKWNWLTNQ 543
Cdd:PRK00254 157 ATLEMILTHMLGRAQILGLSATVG-NAEELaewlnAELVVSDwrPVKLRKGVFYQG----FLFWEDGKIERFPNSWESLV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 544 LALLLSQGSVLIFVST-----KVAVE----------------------QLSSNLTKFGFQTCTL------HGDKNQIERS 590
Cdd:PRK00254 232 YDAVKKGKGALVFVNTrrsaeKEALElakkikrfltkpelralkeladSLEENPTNEKLKKALRggvafhHAGLGRTERV 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66805957 591 QTIQTFKEGKINILIATDVAARGLDIPLIKnVVNYDTSRDIESHTHRI---------GRTGR 643
Cdd:PRK00254 312 LIEDAFREGLIKVITATPTLSAGINLPAFR-VIIRDTKRYSNFGWEDIpvleiqqmmGRAGR 372
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
342-460 |
6.39e-07 |
|
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: 50.27 E-value: 6.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 342 GRDLIAIAKTGSGKTATFIWPSISHIMDQPylekGDGPIALFLAPTRELAHQIY--LETLKYSKYFKLKTTVLYGGVSKQ 419
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEP----EKGVQVLYISPLKALINDQErrLEEPLDEIDLEIPVAVRHGDTSQS 76
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 66805957 420 QQCKELKAGCEIIVATPGRLIDMIKLKAT--KLNRVSYLVLDE 460
Cdd:cd17922 77 EKAKQLKNPPGILITTPESLELLLVNKKLreLFAGLRYVVVDE 119
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
584-655 |
7.25e-07 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 53.34 E-value: 7.25e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66805957 584 KNQIErsqTIQTFKEGKINILIATDVAARGLDIPLIKNVVNYDTS----RDIEshthRIGRTGRaGNTGVAYTLIT 655
Cdd:PRK13766 410 KEQIE---ILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEPVpseiRSIQ----RKGRTGR-QEEGRVVVLIA 477
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
332-461 |
2.11e-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: 49.05 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 332 QKQAIPIALSGRDLIaIAKTGSGKTAtfiwpsISHIMDQPYLEKGDGPIaLFLAPTRELAHQIYlETLKYSKYFKLKTTV 411
Cdd:cd18035 7 QVLIAAVALNGNTLI-VLPTGLGKTI------IAILVAADRLTKKGGKV-LILAPSRPLVEQHA-ENLKRVLNIPDKITS 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 66805957 412 LYGGVSKQQQCKELKAgCEIIVATPGRLIDMIKLKATKLNRVSYLVLDEA 461
Cdd:cd18035 78 LTGEVKPEERAERWDA-SKIIVATPQVIENDLLAGRITLDDVSLLIFDEA 126
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
327-461 |
2.79e-06 |
|
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: 48.97 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 327 TPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHIMDQPYLEKGDgpiALFLAPTRELAHQiylETLKYSKYF- 405
Cdd:cd17927 2 KPRNYQLELAQPALKGKNTIICLPTGSGKTFVAVLICEHHLKKFPAGRKGK---VVFLANKVPLVEQ---QKEVFRKHFe 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 66805957 406 --KLKTTVLYGGVSKQQQCKELKAGCEIIVATPGRLIDMIK-LKATKLNRVSYLVLDEA 461
Cdd:cd17927 76 rpGYKVTGLSGDTSENVSVEQIVESSDVIIVTPQILVNDLKsGTIVSLSDFSLLVFDEC 134
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
534-639 |
4.27e-06 |
|
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: 47.09 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 534 SDKWNWLTNQLALLLSQGS-VLIFV-STKVAvEQLSSNLTKFGFQTCTLHGDKNQIERSQTIQTFKEG-KINI-LIATDV 609
Cdd:cd18793 10 SGKLEALLELLEELREPGEkVLIFSqFTDTL-DILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDpDIRVfLLSTKA 88
|
90 100 110
....*....|....*....|....*....|....*...
gi 66805957 610 AARGLDipLI--KNVVNYDT----SRDI--ESHTHRIG 639
Cdd:cd18793 89 GGVGLN--LTaaNRVILYDPwwnpAVEEqaIDRAHRIG 124
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
327-460 |
4.67e-06 |
|
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: 48.63 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 327 TPTPIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPSISHIMDQPylEKGDGPIALFLAPTRELAHQiylETLKYSKYFK 406
Cdd:cd18036 2 ELRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKRR--SAGEKGRVVVLVNKVPLVEQ---QLEKFFKYFR 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66805957 407 --LKTTVLYGGVSKQQQCKELKAGCEIIVATPGRLIDMIkLKATKLNRV-----SYLVLDE 460
Cdd:cd18036 77 kgYKVTGLSGDSSHKVSFGQIVKASDVIICTPQILINNL-LSGREEERVylsdfSLLIFDE 136
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
313-526 |
7.52e-06 |
|
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: 47.41 E-value: 7.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 313 DDILLQAIAKQSIETPTPIQKQAIPIALSG------RDLIAIAKTGSGKTATFIWPSIShimdqpYLEKGDGpiALFLAP 386
Cdd:cd17918 1 DRALIQELCKSLPFSLTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAALL------AYKNGKQ--VAILVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 387 TRELAHQIYLETLKYskYFKLKTTVLYGGvsKQQQckeLKAGCEIIVATPGrlidMIKLKATKLNrVSYLVLDEADKmfd 466
Cdd:cd17918 73 TEILAHQHYEEARKF--LPFINVELVTGG--TKAQ---ILSGISLLVGTHA----LLHLDVKFKN-LDLVIVDEQHR--- 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66805957 467 fgFG-PQVLSIVNHVRPDrqTLLFSATfkpnveefartilsdPIKISIGMIGSANSDITQI 526
Cdd:cd17918 138 --FGvAQREALYNLGATH--FLEATAT---------------PIPRTLALALSGLLDLSVI 179
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
551-655 |
8.25e-06 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350182 [Multi-domain] Cd Length: 154 Bit Score: 46.78 E-value: 8.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 551 GSVLIFVSTKVAVEQLSSNLTKFGFqtctLHGDKNQIERsQTIQT-FKEGKINILIATDVAARGLDIP----LIKNVVNY 625
Cdd:cd18795 44 KPVLVFCSSRKECEKTAKDLAGIAF----HHAGLTREDR-ELVEElFREGLIKVLVATSTLAAGVNLPartvIIKGTQRY 118
|
90 100 110
....*....|....*....|....*....|....*.
gi 66805957 626 D--TSRDIESHTHR--IGRTGRAG--NTGVAYTLIT 655
Cdd:cd18795 119 DgkGYRELSPLEYLqmIGRAGRPGfdTRGEAIIMTK 154
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
553-617 |
1.18e-05 |
|
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350176 [Multi-domain] Cd Length: 153 Bit Score: 46.47 E-value: 1.18e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66805957 553 VLIFVSTKVAVEQLSSNLTKFGfqtctLHGDKNQIERSQTIQTFKEGKINILIATDVAARGLDIP 617
Cdd:cd18789 52 IIVFTDNVEALYRYAKRLLKPF-----ITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLP 111
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
537-646 |
2.26e-05 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 45.33 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 537 WNWLTNQLALLLSQG-SVLIFVSTKVAVEQLSSNLTKFgfqtCTLHGDKNQIE----------RSQTIQTFKEGKINILI 605
Cdd:cd18796 24 GADAYAEVIFLLERHkSTLVFTNTRSQAERLAQRLREL----CPDRVPPDFIAlhhgslsrelREEVEAALKRGDLKVVV 99
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 66805957 606 ATDVAARGLDIPLIKNVVNYDTSRDIESHTHRIGRTGRAGN 646
Cdd:cd18796 100 ATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGHRPG 140
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
528-641 |
3.73e-05 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 47.53 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 528 QVLKSDSDKWNWLTNQLALLLSQG-SVLIF---VSTkvaVEQLSSNLTKFGFQTCTLHGDKNQIERSQTIQTFKEGKIN- 602
Cdd:COG0553 526 AELSGRSAKLEALLELLEELLAEGeKVLVFsqfTDT---LDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAp 602
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 66805957 603 -ILIATDVAARGLdiplikN------VVNYD-----------TSRdieshTHRIGRT 641
Cdd:COG0553 603 vFLISLKAGGEGL------NltaadhVIHYDlwwnpaveeqaIDR-----AHRIGQT 648
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
327-461 |
5.51e-05 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 44.59 E-value: 5.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 327 TPTPIQKQAIPIALSGRD------LIAIAkTGSGKTATFIwpsisHIMDQpYLEKGDGPIALFLAPTRELAHQIYLETLK 400
Cdd:pfam04851 3 ELRPYQIEAIENLLESIKngqkrgLIVMA-TGSGKTLTAA-----KLIAR-LFKKGPIKKVLFLVPRKDLLEQALEEFKK 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66805957 401 YSKyFKLKTTVLYGGVSKQQQckelKAGCEIIVATPGRLIDMIKLKATKL--NRVSYLVLDEA 461
Cdd:pfam04851 76 FLP-NYVEIGEIISGDKKDES----VDDNKIVVTTIQSLYKALELASLELlpDFFDVIIIDEA 133
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
326-371 |
6.14e-05 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 47.02 E-value: 6.14e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 66805957 326 ETPTPIQKQAIPIALSGRDLIAIAKTGSGKT-ATFIWpSISHIMDQP 371
Cdd:COG1201 23 GAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAFLP-ALDELARRP 68
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
553-644 |
7.65e-05 |
|
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: 44.16 E-value: 7.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 553 VLIFVSTKVAVEQLSSNLTKFGFQTCTLHGDKNQIERSQTIQTFKEGKINILIATDVAARGLDIPLIKNVVNYDTsrDIE 632
Cdd:cd18790 30 VLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDA--DKE 107
|
90
....*....|....*.
gi 66805957 633 ----SHTHRIGRTGRA 644
Cdd:cd18790 108 gflrSETSLIQTIGRA 123
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
330-616 |
9.75e-05 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 46.23 E-value: 9.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 330 PIQKQAIPIALSGRDL-----IAIAKTGSGKT-ATFIWpsISHIMDQPYLEKgdgpiaLFLA-PTRELAHQIYLEtlkYS 402
Cdd:COG1203 130 PLQNEALELALEAAEEepglfILTAPTGGGKTeAALLF--ALRLAAKHGGRR------IIYAlPFTSIINQTYDR---LR 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 403 KYFKLKTTVLYGGV---------SKQQQCKELKAGCE-----IIVATPGRLIDMIKLKATKLNRV------SYLVLDEAD 462
Cdd:COG1203 199 DLFGEDVLLHHSLAdldlleeeeEYESEARWLKLLKElwdapVVVTTIDQLFESLFSNRKGQERRlhnlanSVIILDEVQ 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 463 kMFDFGFGPQVLSIVNHVR-PDRQTLLFSATFkPnveEFARTILSDPIKIsigmIGSANSDITQIVQVLKSDS-----DK 536
Cdd:COG1203 279 -AYPPYMLALLLRLLEWLKnLGGSVILMTATL-P---PLLREELLEAYEL----IPDEPEELPEYFRAFVRKRvelkeGP 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 537 WNW--LTNQL-ALLLSQGSVLIFVST-KVAVE---QLSSNLTKFGfqTCTLHG-----DKNQIERsQTIQTFKEGKINIL 604
Cdd:COG1203 350 LSDeeLAELIlEALHKGKSVLVIVNTvKDAQElyeALKEKLPDEE--VYLLHSrfcpaDRSEIEK-EIKERLERGKPCIL 426
|
330
....*....|..
gi 66805957 605 IATDVAARGLDI 616
Cdd:COG1203 427 VSTQVVEAGVDI 438
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
544-659 |
1.15e-04 |
|
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350185 [Multi-domain] Cd Length: 174 Bit Score: 43.83 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 544 LALLLSQGS-VLIFVST---KVAVEQLSSNLTKFGFQTCTLH-GDKNQIERsqtiqtFKEGKINILIAT----DVAARGL 614
Cdd:cd18798 17 LELVKKLGDgGLIFVSIdygKEYAEELKEFLERHGIKAELALsSTEKNLEK------FEEGEIDVLIGVasyyGVLVRGI 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 66805957 615 DIPL-IKNVVNYDTSrdIESHTHRIGRTGR--AGN--TGVAYTLITPKDI 659
Cdd:cd18798 91 DLPErIKYAIFYGVP--VTTYIQASGRTSRlyAGGltKGLSVVLVDDPEL 138
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
330-461 |
1.64e-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: 42.68 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 330 PIQKQAIPIAL---SGRDLIAIAKTGSGKTATfiwpSISHImdqpyLEKGDGPIaLFLAPTRELAHQIYLETLKYSKYFK 406
Cdd:cd17926 3 PYQEEALEAWLahkNNRRGILVLPTGSGKTLT----ALALI-----AYLKELRT-LIVVPTDALLDQWKERFEDFLGDSS 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 66805957 407 LKttVLYGGVSKqqqckeLKAGCEIIVATPGRLIDMIKLKATKLNRVSYLVLDEA 461
Cdd:cd17926 73 IG--LIGGGKKK------DFDDANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEA 119
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
339-461 |
1.81e-04 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 45.63 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 339 ALSGRDLIaIAKTGSGKT--ATFIWPSIshimdqpyLEKGDGPIaLFLAPTRELAHQiYLETLKysKYFKL---KTTVLY 413
Cdd:PRK13766 27 ALKKNTLV-VLPTGLGKTaiALLVIAER--------LHKKGGKV-LILAPTKPLVEQ-HAEFFR--KFLNIpeeKIVVFT 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 66805957 414 GGVSKQQQcKELKAGCEIIVATP---------GRLidmiklkatKLNRVSYLVLDEA 461
Cdd:PRK13766 94 GEVSPEKR-AELWEKAKVIVATPqviendliaGRI---------SLEDVSLLIFDEA 140
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
540-653 |
3.62e-04 |
|
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family members are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350178 [Multi-domain] Cd Length: 171 Bit Score: 42.14 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 540 LTNQLALLLSQGSVLIFVST----KVAVEQLSSNLTKFG---FQTCTLHGDKNQIERSQTIQTFKEGKINILIATDVAAR 612
Cdd:cd18791 33 LILQIHRTEEPGDILVFLPGqeeiERLCELLREELLSPDlgkLLVLPLHSSLPPEEQQRVFEPPPPGVRKVVLATNIAET 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 66805957 613 GLDIPLIKNVV--------NYDTSRDIES-HTHRIG------RTGRAGNT--GVAYTL 653
Cdd:cd18791 113 SITIPGVVYVIdsglvkekVYDPRTGLSSlVTVWISkasaeqRAGRAGRTrpGKCYRL 170
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
580-645 |
5.49e-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: 41.56 E-value: 5.49e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66805957 580 LHGDKNQIERSQTIQTFKEGKINILIATDVAARGLDIPLIKNVVNYDTSRDIESHTHRI-GRTGRAG 645
Cdd:cd18811 67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLHQLrGRVGRGD 133
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
580-657 |
5.93e-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: 41.48 E-value: 5.93e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66805957 580 LHGDKNQIERSQTIQTFKEGKINILIATDVAARGLDIPLIKNVVNYDTSRDIESHTHRI-GRTGRAGNTGVAYTLITPK 657
Cdd:cd18792 66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFGLSQLHQLrGRVGRGKHQSYCYLLYPDP 144
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
552-640 |
6.11e-04 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350186 [Multi-domain] Cd Length: 116 Bit Score: 40.62 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 552 SVLIFVSTKVAVEQLSSNLTKFGFQTCTLHGDKNQIERS-QTIQTFKEGKI--NILIATDVAARGLDIPLIKNVVnydTS 628
Cdd:cd18799 8 KTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGdEALILLFFGELkpPILVTVDLLTTGVDIPEVDNVV---FL 84
|
90
....*....|....*
gi 66805957 629 RDIESHT---HRIGR 640
Cdd:cd18799 85 RPTESRTlflQMLGR 99
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
330-510 |
6.88e-04 |
|
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 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: 350777 [Multi-domain] Cd Length: 214 Bit Score: 41.97 E-value: 6.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 330 PIQKQAIPIAL-SGRDLIAIAKTGSGKTATFIWpSISHIMDQPYLEKGDGPIALF----LAPTRELAHQIYLETLKYSKY 404
Cdd:cd18019 20 RIQSKLFPAAFeTDENLLLCAPTGAGKTNVALL-TILREIGKHRNPDGTINLDAFkivyIAPMKALVQEMVGNFSKRLAP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 405 FKLKTTVLYGgvsKQQQCKELKAGCEIIVATPGRLiDMIKLKATKL---NRVSYLVLDEADKMFDfGFGPQVLSIVnhVR 481
Cdd:cd18019 99 YGITVAELTG---DQQLTKEQISETQIIVTTPEKW-DIITRKSGDRtytQLVRLIIIDEIHLLHD-DRGPVLESIV--AR 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 66805957 482 PDRQTLL---------FSATFkPNVEEFARTILSDPIK 510
Cdd:cd18019 172 TIRQIEQtqeyvrlvgLSATL-PNYEDVATFLRVDPKK 208
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
331-502 |
1.94e-03 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350781 [Multi-domain] Cd Length: 206 Bit Score: 40.80 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 331 IQKQAIPIAL-SGRDLIAIAKTGSGKTATFIWPSISHIMDQPYLEKGDgPIALFLAPTRELAHQIYLE-TLKYSKyFKLK 408
Cdd:cd18023 5 IQSEVFPDLLySDKNFVVSAPTGSGKTVLFELAILRLLKERNPLPWGN-RKVVYIAPIKALCSEKYDDwKEKFGP-LGLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 409 TTVLYGgvskQQQCKELK--AGCEIIVATPGRLIDMIKLKATKLN---RVSYLVLDE---------------ADKMFDFG 468
Cdd:cd18023 83 CAELTG----DTEMDDTFeiQDADIILTTPEKWDSMTRRWRDNGNlvqLVALVLIDEvhiikenrgatlevvVSRMKTLS 158
|
170 180 190
....*....|....*....|....*....|....
gi 66805957 469 FGPQVLSivNHVRPDRQTLLfSATFkPNVEEFAR 502
Cdd:cd18023 159 SSSELRG--STVRPMRFVAV-SATI-PNIEDLAE 188
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
554-645 |
2.08e-03 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 42.19 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 554 LIFVSTKVAVEQLSSNLTKFGFQTCTLHGDKNQIERSQTIQTFKEGKINILIATDVAARGLDIPLIKNVVNYDTSRDIES 633
Cdd:PLN03137 684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEG 763
|
90
....*....|..
gi 66805957 634 HTHRIGRTGRAG 645
Cdd:PLN03137 764 YHQECGRAGRDG 775
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
330-499 |
2.71e-03 |
|
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: 40.21 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 330 PIQKQAIPIALSGRDLIAIAKTGSGKTATFIWPsishimdqPYLEKGdgpIALFLAPTRELAH-QIY-LETLkyskyfKL 407
Cdd:cd17920 15 PGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLP--------ALLLDG---VTLVVSPLISLMQdQVDrLQQL------GI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 408 KTTVLYGGVSKQQQ---CKELKAG-CEIIVATPGRL-----IDMIKlKATKLNRVSYLVLDEA--------DkmfdfgFG 470
Cdd:cd17920 78 RAAALNSTLSPEEKrevLLRIKNGqYKLLYVTPERLlspdfLELLQ-RLPERKRLALIVVDEAhcvsqwghD------FR 150
|
170 180 190
....*....|....*....|....*....|.
gi 66805957 471 PQV--LSIVNHVRPDRQTLLFSATFKPNVEE 499
Cdd:cd17920 151 PDYlrLGRLRRALPGVPILALTATATPEVRE 181
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
580-670 |
4.42e-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: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805957 580 LHGDKNQIERSQTIQTFKEGKINILIATDVAARGLDIPLIKNVVNYDTSRDIESHTHRI-GRTGRAGNTGVAYtLITPKD 658
Cdd:cd18810 57 AHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIERADKFGLAQLYQLrGRVGRSKERAYAY-FLYPDQ 135
|
90
....*....|..
gi 66805957 659 IHFSVDLIKNLE 670
Cdd:cd18810 136 KKLTEDALKRLE 147
|
|
| |
