|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
21-443 |
0e+00 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 550.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 21 SFAELGVRDEIVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVTTDTERplagAPRALVVV 100
Cdd:COG0513 3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPR----APQALILA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 101 PTRELCLQVYGDLAGAAKYLtadggrKLSVVSIYGGRPYEPQIEALRAGADVVVGTPGRLLDLAQQGHLQLGGLSVLVLD 180
Cdd:COG0513 79 PTRELALQVAEELRKLAKYL------GLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 181 EADEMLDLGFLPDIERILRLTPDTRQAMLFSATMPDPIITLARTFMNQPTHIRAESPQSsqTHDSTEQFIYRAHALDKVE 260
Cdd:COG0513 153 EADRMLDMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENA--TAETIEQRYYLVDKRDKLE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 261 LVSRVLQAEGRGATMIFTRTKRTAQKVADELAERGFKVGAVHGDLGQIAREKALKAFREGDVDVLVATDVAARGIDIDDI 340
Cdd:COG0513 231 LLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 341 THVINYQIPDDEQAYVHRIGRTGRAGKTGIAVTLVDWDELPRWALIDKALGLDCPEpaetysSSPHLFEELNIPADAKGS 420
Cdd:COG0513 311 SHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEE------EELPGFEPVEEKRLERLK 384
|
410 420
....*....|....*....|...
gi 2321260977 421 VGKPARREGKRTTRGERGSEQAP 443
Cdd:COG0513 385 PKIKEKLKGKKAGRGGRPGPKGE 407
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
17-393 |
4.56e-115 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 345.63 E-value: 4.56e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 17 PTGPSFAELGVRDEIVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVttDTERPlagAPRA 96
Cdd:PRK11776 1 MSMTAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL--DVKRF---RVQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 97 LVVVPTRELCLQVYGDLagaakyltadggRKLS-------VVSIYGGRPYEPQIEALRAGADVVVGTPGRLLDLAQQGHL 169
Cdd:PRK11776 76 LVLCPTRELADQVAKEI------------RRLArfipnikVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 170 QLGGLSVLVLDEADEMLDLGFLPDIERILRLTPDTRQAMLFSATMPDPIITLARTFMNQPTHIRAESpqssqTHDST--E 247
Cdd:PRK11776 144 DLDALNTLVLDEADRMLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVES-----THDLPaiE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 248 QFIYRAHALDKVELVSRVLQAEGRGATMIFTRTKRTAQKVADELAERGFKVGAVHGDLGQIAREKALKAFREGDVDVLVA 327
Cdd:PRK11776 219 QRFYEVSPDERLPALQRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVA 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2321260977 328 TDVAARGIDIDDITHVINYQIPDDEQAYVHRIGRTGRAGKTGIAVTLVDWDELPRWALIDKALGLD 393
Cdd:PRK11776 299 TDVAARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRK 364
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
21-396 |
1.82e-103 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 321.03 E-value: 1.82e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 21 SFAELGVRDEIVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVTTDTErplagAPRALVVV 100
Cdd:PRK11634 7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELK-----APQILVLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 101 PTRELCLQVYGDLAGAAKYLtadggRKLSVVSIYGGRPYEPQIEALRAGADVVVGTPGRLLDLAQQGHLQLGGLSVLVLD 180
Cdd:PRK11634 82 PTRELAVQVAEAMTDFSKHM-----RGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 181 EADEMLDLGFLPDIERILRLTPDTRQAMLFSATMPDPIITLARTFMNQPTHIRAESpqSSQTHDSTEQFIYRAHALDKVE 260
Cdd:PRK11634 157 EADEMLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQS--SVTTRPDISQSYWTVWGMRKNE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 261 LVSRVLQAEGRGATMIFTRTKRTAQKVADELAERGFKVGAVHGDLGQIAREKALKAFREGDVDVLVATDVAARGIDIDDI 340
Cdd:PRK11634 235 ALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERI 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2321260977 341 THVINYQIPDDEQAYVHRIGRTGRAGKTGIAVTLVDWDELPRWALIDKALGLDCPE 396
Cdd:PRK11634 315 SLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPE 370
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
22-439 |
1.26e-102 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 312.29 E-value: 1.26e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 22 FAELGVRDEIVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVTT---DTERPLAGaPRALV 98
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLShpaPEDRKVNQ-PRALI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 99 VVPTRELCLQVYGDlagaAKYLTADGGRKLSVVsiYGGRPYEPQIEALRAGADVVVGTPGRLLDLAQQGHLQLGGLSVLV 178
Cdd:PRK04837 89 MAPTRELAVQIHAD----AEPLAQATGLKLGLA--YGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 179 LDEADEMLDLGFLPDIERILRLTPDT--RQAMLFSATMPDPIITLARTFMNQPTHIRAEsPQSSQTHDSTEQFIYRAHAl 256
Cdd:PRK04837 163 LDEADRMFDLGFIKDIRWLFRRMPPAnqRLNMLFSATLSYRVRELAFEHMNNPEYVEVE-PEQKTGHRIKEELFYPSNE- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 257 DKVELVSRVLQAEGRGATMIFTRTKRTAQKVADELAERGFKVGAVHGDLGQIAREKALKAFREGDVDVLVATDVAARGID 336
Cdd:PRK04837 241 EKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 337 IDDITHVINYQIPDDEQAYVHRIGRTGRAGKTGIAVTLvdwdelprwALIDKALGLdcpePA-ETYSSSPhlfeelnIP- 414
Cdd:PRK04837 321 IPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL---------ACEEYALNL----PAiETYIGHS-------IPv 380
|
410 420 430
....*....|....*....|....*....|
gi 2321260977 415 ----ADA-KGSVGKPARREGKRTTRGERGS 439
Cdd:PRK04837 381 skydSDAlLTDLPKPLRLTRPRTGNGPRRS 410
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
20-375 |
2.42e-100 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 306.87 E-value: 2.42e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 20 PSFAELGVRDEIVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVTtDTERPLAGAPRALVV 99
Cdd:PRK11192 1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLL-DFPRRKSGPPRILIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 100 VPTRELCLQVygdlAGAAKYLTADggRKLSVVSIYGGRPYEPQIEALRAGADVVVGTPGRLLDLAQQGHLQLGGLSVLVL 179
Cdd:PRK11192 80 TPTRELAMQV----ADQARELAKH--THLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 180 DEADEMLDLGFLPDIERILRLTPDTRQAMLFSATMP-DPIITLARTFMNQPTHIRAESPQSSQThdSTEQFIYRAHALD- 257
Cdd:PRK11192 154 DEADRMLDMGFAQDIETIAAETRWRKQTLLFSATLEgDAVQDFAERLLNDPVEVEAEPSRRERK--KIHQWYYRADDLEh 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 258 KVELVSRVLQAEGRGATMIFTRTKRTAQKVADELAERGFKVGAVHGDLGQIAREKALKAFREGDVDVLVATDVAARGIDI 337
Cdd:PRK11192 232 KTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDI 311
|
330 340 350
....*....|....*....|....*....|....*...
gi 2321260977 338 DDITHVINYQIPDDEQAYVHRIGRTGRAGKTGIAVTLV 375
Cdd:PRK11192 312 DDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLV 349
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
21-442 |
1.01e-96 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 298.26 E-value: 1.01e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 21 SFAELGVRDEIVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVTTDTERPLAGAP-RALVV 99
Cdd:PRK10590 2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPvRALIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 100 VPTRELCLQVYGDLAGAAKYLtadggrKLSVVSIYGGRPYEPQIEALRAGADVVVGTPGRLLDLAQQGHLQLGGLSVLVL 179
Cdd:PRK10590 82 TPTRELAAQIGENVRDYSKYL------NIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 180 DEADEMLDLGFLPDIERILRLTPDTRQAMLFSATMPDPIITLARTFMNQPthiraESPQSSQTHDSTEQFIYRAHALDKV 259
Cdd:PRK10590 156 DEADRMLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNP-----LEIEVARRNTASEQVTQHVHFVDKK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 260 ---ELVSRVLQAEGRGATMIFTRTKRTAQKVADELAERGFKVGAVHGDLGQIAREKALKAFREGDVDVLVATDVAARGID 336
Cdd:PRK10590 231 rkrELLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 337 IDDITHVINYQIPDDEQAYVHRIGRTGRAGKTGIAVTLVDWDELPRWALIDKALGLDCPEPA-ETYSSSPhlfeelNIPA 415
Cdd:PRK10590 311 IEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRIAiPGYEPDP------SIKA 384
|
410 420
....*....|....*....|....*..
gi 2321260977 416 DAKGSvGKPARREGKRTTRGERGSEQA 442
Cdd:PRK10590 385 EPIQN-GRQQRGGGGRGQGGGRGQQQG 410
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
31-233 |
5.11e-89 |
|
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: 269.31 E-value: 5.11e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 31 IVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVTTDtERPLAGAPRALVVVPTRELCLQVY 110
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPE-PKKKGRGPQALVLAPTRELAMQIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 111 GDLAGAAKYLtadggrKLSVVSIYGGRPYEPQIEALRAGADVVVGTPGRLLDLAQQGHLQLGGLSVLVLDEADEMLDLGF 190
Cdd:cd00268 80 EVARKLGKGT------GLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGF 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2321260977 191 LPDIERILRLTPDTRQAMLFSATMPDPIITLARTFMNQPTHIR 233
Cdd:cd00268 154 EEDVEKILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
22-397 |
2.24e-88 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 277.56 E-value: 2.24e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 22 FAELGVRDEIVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRV--TTDTERPLAGAPRALVV 99
Cdd:PRK01297 89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLlqTPPPKERYMGEPRALII 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 100 VPTRELCLQVYGDLAGAAKYltadggRKLSVVSIYGGRPYEPQIEALRAG-ADVVVGTPGRLLDLAQQGHLQLGGLSVLV 178
Cdd:PRK01297 169 APTRELVVQIAKDAAALTKY------TGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQRGEVHLDMVEVMV 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 179 LDEADEMLDLGFLPDIERILRLTP--DTRQAMLFSATMPDPIITLARTFMNQPTHIRAESPQssQTHDSTEQFIYRAHAL 256
Cdd:PRK01297 243 LDEADRMLDMGFIPQVRQIIRQTPrkEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPEN--VASDTVEQHVYAVAGS 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 257 DKVELVSRVLQAEGRGATMIFTRTKRTAQKVADELAERGFKVGAVHGDLGQIAREKALKAFREGDVDVLVATDVAARGID 336
Cdd:PRK01297 321 DKYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIH 400
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2321260977 337 IDDITHVINYQIPDDEQAYVHRIGRTGRAGKTGIAVTLVDWDELPRWALIDKALG--LDCPEP 397
Cdd:PRK01297 401 IDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGrkISCEMP 463
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
18-374 |
1.38e-81 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 262.58 E-value: 1.38e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 18 TGPSFAELGVRDEIVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVTTdteRP-LAGA--- 93
Cdd:PRK04537 7 TDLTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLS---RPaLADRkpe 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 94 -PRALVVVPTRELCLQVYGDlagAAKYlTADGGRKLSVVsiYGGRPYEPQIEALRAGADVVVGTPGRLLD-LAQQGHLQL 171
Cdd:PRK04537 84 dPRALILAPTRELAIQIHKD---AVKF-GADLGLRFALV--YGGVDYDKQRELLQQGVDVIIATPGRLIDyVKQHKVVSL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 172 GGLSVLVLDEADEMLDLGFLPDIERILRLTPD--TRQAMLFSATMPDPIITLARTFMNQPTHIRAESpqSSQTHDSTEQF 249
Cdd:PRK04537 158 HACEICVLDEADRMFDLGFIKDIRFLLRRMPErgTRQTLLFSATLSHRVLELAYEHMNEPEKLVVET--ETITAARVRQR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 250 IYRAHALDKVELVSRVLQAEGRGATMIFTRTKRTAQKVADELAERGFKVGAVHGDLGQIAREKALKAFREGDVDVLVATD 329
Cdd:PRK04537 236 IYFPADEEKQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATD 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2321260977 330 VAARGIDIDDITHVINYQIPDDEQAYVHRIGRTGRAGKTGIAVTL 374
Cdd:PRK04537 316 VAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISF 360
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
20-379 |
5.58e-77 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 249.69 E-value: 5.58e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 20 PSFAELGVRDEIVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVTTDTERPLAGAPRALVV 99
Cdd:PTZ00110 130 VSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGDGPIVLVL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 100 VPTRELCLQVygdlagAAKYLTADGGRKLSVVSIYGGRPYEPQIEALRAGADVVVGTPGRLLDLAQQGHLQLGGLSVLVL 179
Cdd:PTZ00110 210 APTRELAEQI------REQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVL 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 180 DEADEMLDLGFLPDIERIL-RLTPDtRQAMLFSATMPDPIITLARTFM-NQPTHIRAESPQSSQTHdSTEQFIYRAHALD 257
Cdd:PTZ00110 284 DEADRMLDMGFEPQIRKIVsQIRPD-RQTLMWSATWPKEVQSLARDLCkEEPVHVNVGSLDLTACH-NIKQEVFVVEEHE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 258 KV----ELVSRVLQAEGRgaTMIFTRTKRTAQKVADELAERGFKVGAVHGDLGQIAREKALKAFREGDVDVLVATDVAAR 333
Cdd:PTZ00110 362 KRgklkMLLQRIMRDGDK--ILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASR 439
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2321260977 334 GIDIDDITHVINYQIPDDEQAYVHRIGRTGRAGKTGIAVTLVDWDE 379
Cdd:PTZ00110 440 GLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDK 485
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
21-380 |
2.59e-68 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 223.16 E-value: 2.59e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 21 SFAELGVRDEIVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVTTDTErplagAPRALVVV 100
Cdd:PTZ00424 29 SFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLN-----ACQALILA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 101 PTRELCLQVYGDLAGAAKYLtadggrKLSVVSIYGGRPYEPQIEALRAGADVVVGTPGRLLDLAQQGHLQLGGLSVLVLD 180
Cdd:PTZ00424 104 PTRELAQQIQKVVLALGDYL------KVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 181 EADEMLDLGFLPDIERILRLTPDTRQAMLFSATMPDPIITLARTFMNQPTHIRAEspQSSQTHDSTEQFIYrahALDKVE 260
Cdd:PTZ00424 178 EADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVK--KDELTLEGIRQFYV---AVEKEE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 261 LVSRVLQAEGRGATM----IFTRTKRTAQKVADELAERGFKVGAVHGDLGQIAREKALKAFREGDVDVLVATDVAARGID 336
Cdd:PTZ00424 253 WKFDTLCDLYETLTItqaiIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGID 332
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2321260977 337 IDDITHVINYQIPDDEQAYVHRIGRTGRAGKTGIAVTLVDWDEL 380
Cdd:PTZ00424 333 VQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDI 376
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
247-375 |
1.64e-56 |
|
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350174 [Multi-domain] Cd Length: 131 Bit Score: 183.09 E-value: 1.64e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 247 EQFIYRAHALDKVE-LVSRVLQAEGRGATMIFTRTKRTAQKVADELAERGFKVGAVHGDLGQIAREKALKAFREGDVDVL 325
Cdd:cd18787 2 KQLYVVVEEEEKKLlLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVL 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2321260977 326 VATDVAARGIDIDDITHVINYQIPDDEQAYVHRIGRTGRAGKTGIAVTLV 375
Cdd:cd18787 82 VATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
31-233 |
3.20e-54 |
|
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ribosomal subunits protein 1 homolog, and probable ATP-dependent RNA helicase DDX27) is involved in the processing of 5.8S and 28S ribosomal RNAs. More specifically, the encoded protein localizes to the nucleolus, where it interacts with the PeBoW complex to ensure proper 3' end formation of 47S rRNA. DDX27 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350705 [Multi-domain] Cd Length: 196 Bit Score: 179.76 E-value: 3.20e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 31 IVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVTTdteRPLAGA-PRALVVVPTRELCLQV 109
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLY---RPKKKAaTRVLVLVPTRELAMQC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 110 YGDLAGAAKYLTADGGrkLSVvsiyGGRPYEPQIEALRAGADVVVGTPGRLLDLAQQGH-LQLGGLSVLVLDEADEMLDL 188
Cdd:cd17947 78 FSVLQQLAQFTDITFA--LAV----GGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2321260977 189 GFLPDIERILRLTPDTRQAMLFSATMPDPIITLARTFMNQPTHIR 233
Cdd:cd17947 152 GFADELKEILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRVF 196
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
45-218 |
8.59e-52 |
|
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: 172.04 E-value: 8.59e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 45 AIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVttdteRPLAGAPRALVVVPTRELCLQVYGDLAGAAKYLtadg 124
Cdd:pfam00270 2 PIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAL-----DKLDNGPQALVLAPTRELAEQIYEELKKLGKGL---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 125 grKLSVVSIYGGRPYEPQIEALRaGADVVVGTPGRLLDLAQQGHLqLGGLSVLVLDEADEMLDLGFLPDIERILRLTPDT 204
Cdd:pfam00270 73 --GLKVASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKK 148
|
170
....*....|....
gi 2321260977 205 RQAMLFSATMPDPI 218
Cdd:pfam00270 149 RQILLLSATLPRNL 162
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
21-227 |
1.26e-51 |
|
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: 173.83 E-value: 1.26e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 21 SFAELGVRDEIVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVTTDTERPLAGA-----PR 95
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGrrkayPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 96 ALVVVPTRELCLQVYGDlagaAKYLTADGGRKlSVVsIYGGRPYEPQIEALRAGADVVVGTPGRLLDLAQQGHLQLGGLS 175
Cdd:cd17967 81 ALILAPTRELAIQIYEE----ARKFSYRSGVR-SVV-VYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIK 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2321260977 176 VLVLDEADEMLDLGFLPDIERILRLT----PDTRQAMLFSATMPDPIITLARTFMN 227
Cdd:cd17967 155 FLVLDEADRMLDMGFEPQIRKIVEHPdmppKGERQTLMFSATFPREIQRLAADFLK 210
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
32-226 |
4.62e-50 |
|
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: 168.87 E-value: 4.62e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 32 VRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVTTDT-ERPLAGAPRALVVVPTRELCLQVY 110
Cdd:cd17944 2 IKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQqPRKRGRAPKVLVLAPTRELANQVT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 111 GDLAgaakyltaDGGRKLSVVSIYGGRPYEPQIEALRAGADVVVGTPGRLLDLAQQGHLQLGGLSVLVLDEADEMLDLGF 190
Cdd:cd17944 82 KDFK--------DITRKLSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGF 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2321260977 191 LPDIERILRL-----TPDTRQAMLFSATMPDPIITLARTFM 226
Cdd:cd17944 154 AEQVEEILSVsykkdSEDNPQTLLFSATCPDWVYNVAKKYM 194
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
22-232 |
5.42e-50 |
|
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: 168.63 E-value: 5.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 22 FAELGVRDEIVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVttDTERPlagAPRALVVVP 101
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKI--DPKKD---VIQALILVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 102 TRELCLQVYGDLAGAAKYLtadggrKLSVVSIYGGRPYEPQIEALRAGADVVVGTPGRLLDLAQQGHLQLGGLSVLVLDE 181
Cdd:cd17940 76 TRELALQTSQVCKELGKHM------GVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDE 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2321260977 182 ADEMLDLGFLPDIERILRLTPDTRQAMLFSATMPDPIITLARTFMNQPTHI 232
Cdd:cd17940 150 ADKLLSQDFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
21-429 |
2.58e-49 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 175.75 E-value: 2.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 21 SFAELGVRDEIVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVTT-------DTERPLAga 93
Cdd:PLN00206 122 SFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTirsghpsEQRNPLA-- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 94 praLVVVPTRELCLQVygdlAGAAKYLTAdgGRKLSVVSIYGGRPYEPQIEALRAGADVVVGTPGRLLDLAQQGHLQLGG 173
Cdd:PLN00206 200 ---MVLTPTRELCVQV----EDQAKVLGK--GLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDN 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 174 LSVLVLDEADEMLDLGFLPDIERILRLTPdTRQAMLFSATMPDPIITLARTFMNQPTHIRAESPqsSQTHDSTEQFIYRA 253
Cdd:PLN00206 271 VSVLVLDEVDCMLERGFRDQVMQIFQALS-QPQVLLFSATVSPEVEKFASSLAKDIILISIGNP--NRPNKAVKQLAIWV 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 254 HALDKVELVSRVLQAEG--RGATMIFTRTKRTAQKVADELAE-RGFKVGAVHGDLGQIAREKALKAFREGDVDVLVATDV 330
Cdd:PLN00206 348 ETKQKKQKLFDILKSKQhfKPPAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGV 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 331 AARGIDIDDITHVINYQIPDDEQAYVHRIGRTGRAGKTGIAVTLVDWDelprwaliDKALgldCPEPAETYSSSPHLF-- 408
Cdd:PLN00206 428 LGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEE--------DRNL---FPELVALLKSSGAAIpr 496
|
410 420
....*....|....*....|.
gi 2321260977 409 EELNIPADAKGSVGKPARREG 429
Cdd:PLN00206 497 ELANSRYLGSGRKRKKKRRYG 517
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
31-232 |
9.41e-49 |
|
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: 165.23 E-value: 9.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 31 IVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVTTDTERPLAGAPRALVVVPTRELCLQVY 110
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGDGPIVLVLAPTRELAQQIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 111 GDlagAAKYltaDGGRKLSVVSIYGGRPYEPQIEALRAGADVVVGTPGRLLDLAQQGHLQLGGLSVLVLDEADEMLDLGF 190
Cdd:cd17966 81 QE---ANKF---GGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2321260977 191 LPDIERIL-RLTPDtRQAMLFSATMPDPIITLARTFMNQPTHI 232
Cdd:cd17966 155 EPQIRKIVdQIRPD-RQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
21-232 |
1.18e-48 |
|
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: 166.01 E-value: 1.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 21 SFAELGVRDEIVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVTTdtERPLAGA--PRALV 98
Cdd:cd17953 13 KWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKD--QRPVKPGegPIGLI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 99 VVPTRELCLQVYGDLAGAAKYLtadggrKLSVVSIYGGRPYEPQIEALRAGADVVVGTPGRLLDL--AQQGHL-QLGGLS 175
Cdd:cd17953 91 MAPTRELALQIYVECKKFSKAL------GLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDIltANNGRVtNLRRVT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2321260977 176 VLVLDEADEMLDLGFLPDIERILR-LTPDtRQAMLFSATMPDPIITLARTFMNQPTHI 232
Cdd:cd17953 165 YVVLDEADRMFDMGFEPQIMKIVNnIRPD-RQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
21-232 |
5.95e-48 |
|
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: 163.64 E-value: 5.95e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 21 SFAELGVRDEIVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVTTDTERPLagaprALVVV 100
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFF-----ALVLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 101 PTRELCLQVygdlAGAAKYLTADGGrkLSVVSIYGGRPYEPQIEALRAGADVVVGTPGRLLD-LAQQGHLQLGGLSVLVL 179
Cdd:cd17954 76 PTRELAQQI----SEQFEALGSSIG--LKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDhLENTKGFSLKSLKFLVM 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2321260977 180 DEADEMLDLGFLPDIERILRLTPDTRQAMLFSATMPDPIITLARTFMNQPTHI 232
Cdd:cd17954 150 DEADRLLNMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
31-232 |
7.73e-48 |
|
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: 163.64 E-value: 7.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 31 IVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVTT---DTERPLAGAPRALVVVPTRELCL 107
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRlppLDEETKDDGPYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 108 QVYGDlagAAKYLTADGGRklsVVSIYGGRPYEPQIEALRAGADVVVGTPGRLLDLAQQGHLQLGGLSVLVLDEADEMLD 187
Cdd:cd17945 81 QIEEE---TQKFAKPLGIR---VVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMID 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2321260977 188 LGFLPDIERILRLTPDT--------------------RQAMLFSATMPDPIITLARTFMNQPTHI 232
Cdd:cd17945 155 MGFEPQVTKILDAMPVSnkkpdteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
29-228 |
3.01e-47 |
|
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: 161.98 E-value: 3.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 29 DEIVRALGEEGIVHPFAIQELTLPLALA-GDDLIGQARTGMGKTYAFGVPLLNRVTTDTERPLAGAPRALVVVPTRELCL 107
Cdd:cd17964 3 PSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGVSALIISPTRELAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 108 QVYGDlagaAKYLTAdGGRKLSVVSIYGGRPYEPQIEAL-RAGADVVVGTPGRLLDL--AQQGHLQLGGLSVLVLDEADE 184
Cdd:cd17964 83 QIAAE----AKKLLQ-GLRKLRVQSAVGGTSRRAELNRLrRGRPDILVATPGRLIDHleNPGVAKAFTDLDYLVLDEADR 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2321260977 185 MLDLGFLPDIERILRLTP----DTRQAMLFSATMPDPIITLARTFMNQ 228
Cdd:cd17964 158 LLDMGFRPDLEQILRHLPeknaDPRQTLLFSATVPDEVQQIARLTLKK 205
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
31-232 |
4.35e-47 |
|
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: 161.04 E-value: 4.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 31 IVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVTTDTERPLAGAPRALVVVPTRELCLQVY 110
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGEGPIAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 111 GDLAGAAKYLtadggrKLSVVSIYGGRPYEPQIEALRAGADVVVGTPGRLLDLAQQGHLQLGGLSVLVLDEADEMLDLGF 190
Cdd:cd17952 81 LEAKKFGKAY------NLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2321260977 191 LPDIERIL-RLTPDtRQAMLFSATMPDPIITLARTFMNQPTHI 232
Cdd:cd17952 155 EYQVRSIVgHVRPD-RQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
21-228 |
3.58e-46 |
|
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: 160.90 E-value: 3.58e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 21 SFAELGVRDEIVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRV----TTDTERPLAGAPRA 96
Cdd:cd18052 44 TFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMmkegLTASSFSEVQEPQA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 97 LVVVPTRELCLQVYGDlagaakyltadgGRKLS------VVSIYGGRPYEPQIEALRAGADVVVGTPGRLLDLAQQGHLQ 170
Cdd:cd18052 124 LIVAPTRELANQIFLE------------ARKFSygtcirPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKIS 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2321260977 171 LGGLSVLVLDEADEMLDLGFLPDIERILRL--TPDT--RQAMLFSATMPDPIITLARTFMNQ 228
Cdd:cd18052 192 LSKLKYLILDEADRMLDMGFGPEIRKLVSEpgMPSKedRQTLMFSATFPEEIQRLAAEFLKE 253
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
31-233 |
1.05e-45 |
|
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350718 [Multi-domain] Cd Length: 202 Bit Score: 157.35 E-value: 1.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 31 IVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVTTDTERPLAGAPRALVVVPTRELCLQVY 110
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKKGQVGALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 111 gdlaGAAKYLTADGGRKLSVVSIYGGRPYEPQIEALRA-GADVVVGTPGRLLDL--AQQGHLQLGGLSVLVLDEADEMLD 187
Cdd:cd17960 81 ----EVLQSFLEHHLPKLKCQLLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELlsRKADKVKVKSLEVLVLDEADRLLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2321260977 188 LGFLPDIERILRLTPDTRQAMLFSATMPDPIITLARTFMNQPTHIR 233
Cdd:cd17960 157 LGFEADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRVV 202
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
21-233 |
1.61e-45 |
|
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: 157.08 E-value: 1.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 21 SFAELGVRDEIVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVttDTERPLAGApRALVVV 100
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKL--KAHSPTVGA-RALILS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 101 PTRELCLQVYGDLAGAAKYLtadggrKLSVVSIYGGRPYEPQIEALRAGADVVVGTPGRLLDLAQQGHLQLGGLSVLVLD 180
Cdd:cd17959 79 PTRELALQTLKVTKELGKFT------DLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2321260977 181 EADEMLDLGFLPDIERILRLTPDTRQAMLFSATMPDPIITLARTFMNQPTHIR 233
Cdd:cd17959 153 EADRLFEMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
21-232 |
3.73e-45 |
|
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: 156.35 E-value: 3.73e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 21 SFAELGVRDEIVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVTTDTerplaGAPRALVVV 100
Cdd:cd17950 3 GFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVD-----GQVSVLVIC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 101 PTRELCLQVYGDLAGAAKYLTadgGRKLSVVsiYGGRPYEPQIEALRAGA-DVVVGTPGRLLDLAQQGHLQLGGLSVLVL 179
Cdd:cd17950 78 HTRELAFQISNEYERFSKYMP---NVKTAVF--FGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2321260977 180 DEADEML-DLGFLPDIERILRLTPDTRQAMLFSATMPDPIITLARTFMNQPTHI 232
Cdd:cd17950 153 DECDKMLeQLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEI 206
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
29-229 |
4.51e-45 |
|
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: 155.82 E-value: 4.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 29 DEIVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRV-TTDTERPLAGAPRALVVVPTRELCL 107
Cdd:cd17961 3 PRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlKAKAESGEEQGTRALILVPTRELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 108 QVYGDLagaaKYLTADGGRKLSVVSIYGGRPYEPQIEALRAGADVVVGTPGRLLDLAQQGHLQL-GGLSVLVLDEADEML 186
Cdd:cd17961 83 QVSKVL----EQLTAYCRKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLlSTLKYLVIDEADLVL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2321260977 187 DLGFLPDIERILRLTPDTRQAMLFSATMPDPIITLARTFMNQP 229
Cdd:cd17961 159 SYGYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNP 201
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
31-232 |
4.75e-44 |
|
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: 153.00 E-value: 4.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 31 IVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVP-LLNRVTTDTERPLAGAPRALVVVPTRELCLQV 109
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPgFIHLDLQPIPREQRNGPGVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 110 YGDLAgaaKYLTadggRKLSVVSIYGGRPYEPQIEALRAGADVVVGTPGRLLDLAQQGHLQLGGLSVLVLDEADEMLDLG 189
Cdd:cd17958 81 EAECS---KYSY----KGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2321260977 190 FLPDIERILR-LTPDtRQAMLFSATMPDPIITLARTFMNQPTHI 232
Cdd:cd17958 154 FEPQIRKILLdIRPD-RQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
39-237 |
5.89e-44 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 153.03 E-value: 5.89e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 39 GIVHPFAIQELTLPLALAGD-DLIGQARTGMGKTYAFGVPLLNRVTTDterplaGAPRALVVVPTRELCLQVYGDLAGAA 117
Cdd:smart00487 5 GFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEALKRG------KGGRVLVLVPTRELAEQWAEELKKLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 118 KYLtadggrKLSVVSIYGGRPYEPQIEALRAG-ADVVVGTPGRLLDLAQQGHLQLGGLSVLVLDEADEMLDLGFLPDIER 196
Cdd:smart00487 79 PSL------GLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEK 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2321260977 197 ILRLTPDTRQAMLFSATMPDPIITLARTFMNQPTHIRAESP 237
Cdd:smart00487 153 LLKLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFT 193
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
22-229 |
1.13e-43 |
|
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: 152.38 E-value: 1.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 22 FAELGVRDEIVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVTTDterPLagAPRALVVVP 101
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSED---PY--GIFALVLTP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 102 TRELCLQ------VYGDLAGaakyltadggrkLSVVSIYGGRPYEPQIEALRAGADVVVGTPGRLLDLAQQGHLQLGGLS 175
Cdd:cd17955 76 TRELAYQiaeqfrALGAPLG------------LRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDTTKVLS 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2321260977 176 ---VLVLDEADEMLDLGFLPDIERILRLTPDTRQAMLFSATMPDPIITLARTFMNQP 229
Cdd:cd17955 144 rvkFLVLDEADRLLTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
31-214 |
4.80e-43 |
|
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: 151.62 E-value: 4.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 31 IVRALGEEGIVHPFAIQELTLPLALA-GDDLIGQARTGMGKTYAFGVPLLNRVTTDTERPLAGA----PRALVVVPTREL 105
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLLSQKSSNGVGGkqkpLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 106 CLQVYGDLAGAAKYLTadggrkLSVVSIYGGRPYEPQIEALRAGADVVVGTPGRLLDLAQQGHLQLG---GLSVLVLDEA 182
Cdd:cd17946 81 AVQVKDHLKAIAKYTN------IKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLAnlkSLRFLVLDEA 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 2321260977 183 DEMLDLGFLPDIERILRLTPDT-------RQAMLFSATM 214
Cdd:cd17946 155 DRMLEKGHFAELEKILELLNKDragkkrkRQTFVFSATL 193
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
24-232 |
4.64e-42 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation factor-4A (eIF4A) family consists of 3 proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA. EIF4A proteins are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350697 [Multi-domain] Cd Length: 199 Bit Score: 147.86 E-value: 4.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 24 ELGVRDEIVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVTTDTErplagAPRALVVVPTR 103
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVR-----ETQALVLAPTR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 104 ELCLQVYGDLAGAAKYLTAdggrklSVVSIYGGRPYEPQIEALRAGADVVVGTPGRLLDLAQQGHLQLGGLSVLVLDEAD 183
Cdd:cd17939 76 ELAQQIQKVVKALGDYMGV------KVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEAD 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2321260977 184 EMLDLGFLPDIERILRLTPDTRQAMLFSATMPDPIITLARTFMNQPTHI 232
Cdd:cd17939 150 EMLSRGFKDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
22-230 |
6.49e-42 |
|
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350696 [Multi-domain] Cd Length: 204 Bit Score: 147.47 E-value: 6.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 22 FAELGVRDEIVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVttdterplagapRALVVVP 101
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV------------VALILEP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 102 TRELCLQVYGDLAGAAKYLTadgGRKLSVVSIYGGRPYEPQIEALRAGADVVVGTPGRLLDLAQQGHLQLGGLSVLVLDE 181
Cdd:cd17938 69 SRELAEQTYNCIENFKKYLD---NPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDE 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2321260977 182 ADEMLDLGFLPDIERILRLTP-----DTR-QAMLFSATMPDP-IITLARTFMNQPT 230
Cdd:cd17938 146 ADRLLSQGNLETINRIYNRIPkitsdGKRlQVIVCSATLHSFeVKKLADKIMHFPT 201
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
33-232 |
1.16e-41 |
|
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: 146.67 E-value: 1.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 33 RALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVTTDTERPLAGAPrALVVVPTRELCLQVYGD 112
Cdd:cd17941 3 KGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTPEDGLG-ALIISPTRELAMQIFEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 113 LAGAAKYltadggRKLSVVSIYGGRPYEpqIEALRAGA-DVVVGTPGRLLD-LAQQGHLQLGGLSVLVLDEADEMLDLGF 190
Cdd:cd17941 82 LRKVGKY------HSFSAGLIIGGKDVK--EEKERINRmNILVCTPGRLLQhMDETPGFDTSNLQMLVLDEADRILDMGF 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2321260977 191 LPDIERILRLTPDTRQAMLFSATMPDPIITLARTFMNQPTHI 232
Cdd:cd17941 154 KETLDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYI 195
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
31-229 |
1.91e-41 |
|
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: 146.33 E-value: 1.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 31 IVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPL-LNRVTTDTERPLAG--APRALVVVPTRELCL 107
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLiMFALEQEKKLPFIKgeGPYGLIVCPSRELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 108 QVYGDLAGAAKYLTADGGRKLSVVSIYGGRPYEPQIEALRAGADVVVGTPGRLLDLAQQGHLQLGGLSVLVLDEADEMLD 187
Cdd:cd17951 81 QTHEVIEYYCKALQEGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2321260977 188 LGFLPDIERILRLTPDTRQAMLFSATMPDPIITLARTFMNQP 229
Cdd:cd17951 161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKP 202
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
31-232 |
2.10e-40 |
|
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: 143.27 E-value: 2.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 31 IVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVTTDTERPLAGAPrALVVVPTRELCLQVY 110
Cdd:cd17942 1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRNGTG-VIIISPTRELALQIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 111 GdlagAAKYLTADGGRKLSVVsiYGGRPYEPQIEALRAGADVVVGTPGRLLDlaqqgHLQLGG------LSVLVLDEADE 184
Cdd:cd17942 80 G----VAKELLKYHSQTFGIV--IGGANRKAEAEKLGKGVNILVATPGRLLD-----HLQNTKgflyknLQCLIIDEADR 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2321260977 185 MLDLGFLPDIERILRLTPDTRQAMLFSATMPDPIITLAR-TFMNQPTHI 232
Cdd:cd17942 149 ILEIGFEEEMRQIIKLLPKRRQTMLFSATQTRKVEDLARiSLKKKPLYV 197
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
22-232 |
3.42e-39 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation factor 4A-I (DDX2A) and eukaryotic initiation factor 4A-II (DDX2B) are involved in cap recognition and are required for mRNA binding to ribosome. They are DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350804 [Multi-domain] Cd Length: 201 Bit Score: 140.27 E-value: 3.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 22 FAELGVRDEIVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVTTDTErplagAPRALVVVP 101
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLK-----ATQALVLAP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 102 TRELCLQVYGDLAGAAKYLtadggrKLSVVSIYGGRPYEPQIEALRAGADVVVGTPGRLLDLAQQGHLQLGGLSVLVLDE 181
Cdd:cd18046 76 TRELAQQIQKVVMALGDYM------GIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDE 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2321260977 182 ADEMLDLGFLPDIERILRLTPDTRQAMLFSATMPDPIITLARTFMNQPTHI 232
Cdd:cd18046 150 ADEMLSRGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
43-233 |
5.25e-39 |
|
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: 139.63 E-value: 5.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 43 PFAIQELTLPLALAGDD--LIGQARTGMGKTYAFGVPLLNRVttDTERPlagAPRALVVVPTRELCLQVYGDLAGAAKYL 120
Cdd:cd17963 17 PSKIQETALPLILSDPPenLIAQSQSGTGKTAAFVLAMLSRV--DPTLK---SPQALCLAPTRELARQIGEVVEKMGKFT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 121 TADGGRKLSVVSIYGGRPYEPQIealragadvVVGTPGRLLDLAQQGHLQLGGLSVLVLDEADEMLDL-GFLPDIERILR 199
Cdd:cd17963 92 GVKVALAVPGNDVPRGKKITAQI---------VIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGHGDQSIRIKR 162
|
170 180 190
....*....|....*....|....*....|....
gi 2321260977 200 LTPDTRQAMLFSATMPDPIITLARTFMNQPTHIR 233
Cdd:cd17963 163 MLPRNCQILLFSATFPDSVRKFAEKIAPNANTIK 196
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
22-232 |
3.43e-38 |
|
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: 138.60 E-value: 3.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 22 FAELGVRDEIVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVTTDTERPLAGAPRALVVVP 101
Cdd:cd18049 26 FYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGDGPICLVLAP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 102 TRELCLQVygdlagaaKYLTADGGR--KLSVVSIYGGRPYEPQIEALRAGADVVVGTPGRLLDLAQQGHLQLGGLSVLVL 179
Cdd:cd18049 106 TRELAQQV--------QQVAAEYGRacRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2321260977 180 DEADEMLDLGFLPDIERIL-RLTPDtRQAMLFSATMPDPIITLARTFMNQPTHI 232
Cdd:cd18049 178 DEADRMLDMGFEPQIRKIVdQIRPD-RQTLMWSATWPKEVRQLAEDFLKDYIHI 230
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
31-229 |
3.97e-38 |
|
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: 137.34 E-value: 3.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 31 IVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVTTDTERplaGAPRALVVVPTRELCLQVY 110
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKK---KGLRALILAPTRELASQIY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 111 GDLAGAAKyltadgGRKLSVVSIYGG-RPYEPQIEALRAGADVVVGTPGRLLDLAQQGHLQLGGLSVLVLDEADEMLDLG 189
Cdd:cd17957 78 RELLKLSK------GTGLRIVLLSKSlEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2321260977 190 FLPDIERILR-LTPDTRQAMLFSATMPDPIITLARTFMNQP 229
Cdd:cd17957 152 FREQTDEILAaCTNPNLQRSLFSATIPSEVEELARSVMKDP 192
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
43-232 |
4.43e-37 |
|
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: 134.21 E-value: 4.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 43 PFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVTTDTERPLAgapraLVVVPTRELCLQVygdlAGAAKYLTA 122
Cdd:cd17962 13 PTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSA-----LILTPTRELAVQI----EDQAKELMK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 123 dGGRKLSVVSIYGGRPYEPQIEALRAGADVVVGTPGRLLDLAQQGHLQLGGLSVLVLDEADEMLDLGFLPDIERILRLTP 202
Cdd:cd17962 84 -GLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILENIS 162
|
170 180 190
....*....|....*....|....*....|
gi 2321260977 203 DTRQAMLFSATMPDPIITLARTFMNQPTHI 232
Cdd:cd17962 163 HDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
43-227 |
7.03e-37 |
|
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: 135.55 E-value: 7.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 43 PFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVTTDTERPLAGA-----------PRALVVVPTRELCLQVYg 111
Cdd:cd18051 44 PTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQGPGESLPSesgyygrrkqyPLALVLAPTRELASQIY- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 112 dlagaakyltaDGGRKLSVVS------IYGGRPYEPQIEALRAGADVVVGTPGRLLDLAQQGHLQLGGLSVLVLDEADEM 185
Cdd:cd18051 123 -----------DEARKFAYRSrvrpcvVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDYCKYLVLDEADRM 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2321260977 186 LDLGFLPDIERILR--LTPDT--RQAMLFSATMPDPIITLARTFMN 227
Cdd:cd18051 192 LDMGFEPQIRRIVEqdTMPPTgeRQTLMFSATFPKEIQMLARDFLD 237
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
31-233 |
1.02e-36 |
|
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: 133.16 E-value: 1.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 31 IVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVttdteRPLAGAPRALVVVPTRELCLQVY 110
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESL-----DLERRHPQVLILAPTREIAVQIH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 111 GDLAGAAKYLtadggRKLSVVSIYGGRPYEPQIEALRaGADVVVGTPGRLLDLAQQGHLQLGGLSVLVLDEADEMLDLGF 190
Cdd:cd17943 76 DVFKKIGKKL-----EGLKCEVFIGGTPVKEDKKKLK-GCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSF 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2321260977 191 LPDIERILRLTPDTRQAMLFSATMPDPIITLARTFMNQPTHIR 233
Cdd:cd17943 150 QKDVNWIFSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
257-366 |
2.78e-36 |
|
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: 129.25 E-value: 2.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 257 DKVELVSRVLQAEGRGATMIFTRTKRTAQkvADELAER-GFKVGAVHGDLGQIAREKALKAFREGDVDVLVATDVAARGI 335
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLE--AELLLEKeGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
|
90 100 110
....*....|....*....|....*....|.
gi 2321260977 336 DIDDITHVINYQIPDDEQAYVHRIGRTGRAG 366
Cdd:pfam00271 79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
31-232 |
3.47e-36 |
|
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: 134.37 E-value: 3.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 31 IVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVTTDTERPLAGAPRALVVVPTRELCLQVy 110
Cdd:cd18050 73 VMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQV- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 111 gdlagaaKYLTADGGR--KLSVVSIYGGRPYEPQIEALRAGADVVVGTPGRLLDLAQQGHLQLGGLSVLVLDEADEMLDL 188
Cdd:cd18050 152 -------QQVADDYGKssRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDM 224
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2321260977 189 GFLPDIERIL-RLTPDtRQAMLFSATMPDPIITLARTFMNQPTHI 232
Cdd:cd18050 225 GFEPQIRKIVdQIRPD-RQTLMWSATWPKEVRQLAEDFLRDYVQI 268
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
22-232 |
1.66e-35 |
|
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: 130.28 E-value: 1.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 22 FAELGVRDEIVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVTTDTERPlagapRALVVVP 101
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRET-----QALILSP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 102 TRELCLQVYGDLAGAAKYLTadggrkLSVVSIYGGRPYEPQIEALRAGADVVVGTPGRLLDLAQQGHLQLGGLSVLVLDE 181
Cdd:cd18045 76 TRELAVQIQKVLLALGDYMN------VQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDE 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2321260977 182 ADEMLDLGFLPDIERILRLTPDTRQAMLFSATMPDPIITLARTFMNQPTHI 232
Cdd:cd18045 150 ADEMLNKGFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
39-233 |
8.68e-34 |
|
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: 126.16 E-value: 8.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 39 GIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVTTDTER--PLAGaPRALVVVPTRELCLQVYGDLAGA 116
Cdd:cd17949 10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRvdRSDG-TLALVLVPTRELALQIYEVLEKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 117 AKYLTAdggrkLSVVSIYGGRPYEPQIEALRAGADVVVGTPGRLLDlaqqgHLQ------LGGLSVLVLDEADEMLDLGF 190
Cdd:cd17949 89 LKPFHW-----IVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLD-----HLKntqsfdVSNLRWLVLDEADRLLDMGF 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2321260977 191 LPDIERILRL-------------TPDTRQAMLFSATMPDPIITLARTFMNQPTHIR 233
Cdd:cd17949 159 EKDITKILELlddkrskaggeksKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
285-366 |
5.41e-30 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 111.53 E-value: 5.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 285 QKVADELAERGFKVGAVHGDLGQIAREKALKAFREGDVDVLVATDVAARGIDIDDITHVINYQIPDDEQAYVHRIGRTGR 364
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 2321260977 365 AG 366
Cdd:smart00490 81 AG 82
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
31-215 |
5.45e-29 |
|
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350706 [Multi-domain] Cd Length: 231 Bit Score: 113.62 E-value: 5.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 31 IVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVTTD---TERPLaGAPRALVVVPTRELCL 107
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYkllAEGPF-NAPRGLVITPSRELAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 108 QVygdlAGAAKYLTADGGrkLSVVSIYGGRPYEPQIEALRAGADVVVGTPGRLLDLAQQGHLQLGGLSVLVLDEADEMLD 187
Cdd:cd17948 80 QI----GSVAQSLTEGLG--LKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLD 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2321260977 188 LGFLPDIERILRLTP-------DTR------QAMLFSATMP 215
Cdd:cd17948 154 DSFNEKLSHFLRRFPlasrrseNTDgldpgtQLVLVSATMP 194
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
17-233 |
7.19e-27 |
|
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: 107.80 E-value: 7.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 17 PTGP-----SFAELGVRDEIVRALGEEGIVHPFAIQELTLPLALAG--DDLIGQARTGMGKTYAFGVPLLNRVTTdterp 89
Cdd:cd18048 10 PTSPlfsvkSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDA----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 90 LAGAPRALVVVPTRELCLQVYGDLAGAAKYLTadgGRKLsVVSIYGGRPYE-PQIEalragADVVVGTPGRLLDLAQQGH 168
Cdd:cd18048 85 LKLYPQCLCLSPTFELALQTGKVVEEMGKFCV---GIQV-IYAIRGNRPGKgTDIE-----AQIVIGTPGTVLDWCFKLR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2321260977 169 L-QLGGLSVLVLDEADEMLDL-GFLPDIERILRLTPDTRQAMLFSATMPDPIITLARTFMNQPTHIR 233
Cdd:cd18048 156 LiDVTNISVFVLDEADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIK 222
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
31-214 |
3.39e-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: 103.10 E-value: 3.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 31 IVRALGEEGIVHPFAIQELTLPLALAGD---------DLIGQARTGMGKTYAFGVPLLNRVTTDTERPLagapRALVVVP 101
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSSkstppyrpgDLCVSAPTGSGKTLAYVLPIVQALSKRVVPRL----RALIVVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 102 TRELCLQVYgdlaGAAKYLTAdgGRKLSVVSIYGGRPYEPQIEALRAG--------ADVVVGTPGRLLD-LAQQGHLQLG 172
Cdd:cd17956 77 TKELVQQVY----KVFESLCK--GTGLKVVSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRLVDhLNSTPGFTLK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2321260977 173 GLSVLVLDEADEMLDLGF---LPDIERILRLTPDTR-----------------QAMLFSATM 214
Cdd:cd17956 151 HLRFLVIDEADRLLNQSFqdwLETVMKALGRPTAPDlgsfgdanllersvrplQKLLFSATL 212
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
27-237 |
3.17e-23 |
|
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: 98.22 E-value: 3.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 27 VRDEIV-----RALGEEGIVHPFAIQELTLPlALAGDDLIGQ-----------------ARTGMGKTYAFGVPLLNRVTT 84
Cdd:cd17965 10 VREAIIkeilkGSNKTDEEIKPSPIQTLAIK-KLLKTLMRKVtkqtsneepklevfllaAETGSGKTLAYLAPLLDYLKR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 85 DTERPL------------AGAPRALVVVPTRELCLQVYGDLAGAAKYLtadgGRKLSVVSIYGGRPYEPQIEALRAGADV 152
Cdd:cd17965 89 QEQEPFeeaeeeyesakdTGRPRSVILVPTHELVEQVYSVLKKLSHTV----KLGIKTFSSGFGPSYQRLQLAFKGRIDI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 153 VVGTPGRLLDLAQQGHLQLGGLSVLVLDEADEMLDLGFLPDIERILRLTPDTRQAMLFSATMPDPII-TLARTFmnqPTH 231
Cdd:cd17965 165 LVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDkTLRKLF---PDV 241
|
....*.
gi 2321260977 232 IRAESP 237
Cdd:cd17965 242 VRIATP 247
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
17-374 |
1.11e-18 |
|
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: 88.74 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 17 PTGPSFAEL--GVRDEIVRALGEEGIVHPFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVTTDterplaGAP 94
Cdd:COG1205 29 AREARYAPWpdWLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLED------PGA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 95 RALVVVPTRELClqvyGDLAGAAKYLTADGGRKLSVVSIYGGRPYEpQIEALRAGADVVVGTPgrllDLAQQGHLQ---- 170
Cdd:COG1205 103 TALYLYPTKALA----RDQLRRLRELAEALGLGVRVATYDGDTPPE-ERRWIREHPDIVLTNP----DMLHYGLLPhhtr 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 171 ----LGGLSVLVLDEADE----------MLdlgflpdIERILRLTPDTRQAMLF---SATMPDPIiTLARTFMNQP-THI 232
Cdd:COG1205 174 warfFRNLRYVVIDEAHTyrgvfgshvaNV-------LRRLRRICRHYGSDPQFilaSATIGNPA-EHAERLTGRPvTVV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 233 RAE-SPQSSQTH-----DSTEQFIYRAHALDKVELVSRVLQAEGRgaTMIFTRTKRTAQKVA----DELAERGF--KVGA 300
Cdd:COG1205 246 DEDgSPRGERTFvlwnpPLVDDGIRRSALAEAARLLADLVREGLR--TLVFTRSRRGAELLAryarRALREPDLadRVAA 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2321260977 301 VHGDLGQIAREKALKAFREGDVDVLVATDVAARGIDIDDITHVINYQIPDDEQAYVHRIGRTGRAGKTGIAVTL 374
Cdd:COG1205 324 YRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVLV 397
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
21-233 |
1.92e-18 |
|
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: 83.62 E-value: 1.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 21 SFAELGVRDEIVRALGEEGIVHPFAIQELTLPLALAG--DDLIGQARTGMGKTYAFGVPLLNRVTtdterPLAGAPRALV 98
Cdd:cd18047 2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVE-----PANKYPQCLC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 99 VVPTRELCLQvygdlagAAKYLTADGGRKLSVVSIYGGRPYEPQiEALRAGADVVVGTPGRLLDLAQQGHL-QLGGLSVL 177
Cdd:cd18047 77 LSPTYELALQ-------TGKVIEQMGKFYPELKLAYAVRGNKLE-RGQKISEQIVIGTPGTVLDWCSKLKFiDPKKIKVF 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2321260977 178 VLDEADEMLDL-GFLPDIERILRLTPDTRQAMLFSATMPDPIITLARTFMNQPTHIR 233
Cdd:cd18047 149 VLDEADVMIATqGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
259-375 |
7.96e-18 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 86.32 E-value: 7.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 259 VELVSRVLQAEGRGATMIFTRTKRTAQKVADELAERGFKV------GAVHGDLG--QIAREKALKAFREGDVDVLVATDV 330
Cdd:COG1111 341 REILKEQLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAgrfvgqASKEGDKGltQKEQIEILERFRAGEFNVLVATSV 420
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2321260977 331 AARGIDIDDITHVINYQ-IPdDEQAYVHRIGRTGRAGKtGIAVTLV 375
Cdd:COG1111 421 AEEGLDIPEVDLVIFYEpVP-SEIRSIQRKGRTGRKRE-GRVVVLI 464
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
257-374 |
1.42e-17 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 84.81 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 257 DKVELVSRVLQAEGRGATMIFTRTKRTAQKVADELAERGFKVGAVHGDLGQIAREKALKAFREGDVDVLVATdVA-ARGI 335
Cdd:COG0514 216 DKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGI 294
|
90 100 110
....*....|....*....|....*....|....*....
gi 2321260977 336 DIDDITHVINYQIPDDEQAYVHRIGRTGRAGKTGIAVTL 374
Cdd:COG0514 295 DKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLL 333
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
45-376 |
1.91e-17 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 84.69 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 45 AIQELTLPLALAGDDLIGQARTGMGKTYAFGvpllnrvtTDTERpLAGAPRALVVVPTRELCLQVYGDLAGAAKYLTADG 124
Cdd:COG1061 88 ALEALLAALERGGGRGLVVAPTGTGKTVLAL--------ALAAE-LLRGKRVLVLVPRRELLEQWAEELRRFLGDPLAGG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 125 GRKlsvvsiyggrpyepqiealRAGADVVVGTPGRLLDLAQQGHLQlGGLSVLVLDEA--------DEMLDLGflpDIER 196
Cdd:COG1061 159 GKK-------------------DSDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAhhagapsyRRILEAF---PAAY 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 197 ILRLT-----PDTRQAMLFSATmpDPIITL-ARTFMNQ----PTH---IRAESPQSSQTHDSTEQFIYRA---HALDKVE 260
Cdd:COG1061 216 RLGLTatpfrSDGREILLFLFD--GIVYEYsLKEAIEDgylaPPEyygIRVDLTDERAEYDALSERLREAlaaDAERKDK 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 261 LVSRVLQAEGRG-ATMIFTRTKRTAQKVADELAERGFKVGAVHGDLGQIAREKALKAFREGDVDVLVATDVAARGIDIDD 339
Cdd:COG1061 294 ILRELLREHPDDrKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPR 373
|
330 340 350
....*....|....*....|....*....|....*..
gi 2321260977 340 ITHVINYQIPDDEQAYVHRIGRTGRAGKTGIAVTLVD 376
Cdd:COG1061 374 LDVAILLRPTGSPREFIQRLGRGLRPAPGKEDALVYD 410
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
264-374 |
2.57e-15 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350181 [Multi-domain] Cd Length: 134 Bit Score: 72.63 E-value: 2.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 264 RVLQAEGRGATMIFTRTKRTAQKVADELAERGFKVGAVHGDLGQIAREKALKAFREGDVDVLVATdVA-ARGIDIDDITH 342
Cdd:cd18794 23 RIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVAT-VAfGMGIDKPDVRF 101
|
90 100 110
....*....|....*....|....*....|..
gi 2321260977 343 VINYQIPDDEQAYVHRIGRTGRAGKTGIAVTL 374
Cdd:cd18794 102 VIHYSLPKSMESYYQESGRAGRDGLPSECILF 133
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
57-213 |
2.83e-14 |
|
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: 69.74 E-value: 2.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 57 GDDLIGQARTGMGKTYAFGVPLLNRVttdterpLAGAPRALVVVPTRELCLQVYGDLAGAAKyltadggRKLSVVSIYGG 136
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLL-------LKKGKKVLVLVPTKALALQTAERLRELFG-------PGIRVAVLVGG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 137 RPYEPQIEALRAGADVVVGTPGRLLDLAQQ-GHLQLGGLSVLVLDEADEMLDLGF--LPDIERILRLTPDTRQAMLFSAT 213
Cdd:cd00046 67 SSAEEREKNKLGDADIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLIDSRgaLILDLAVRKAGLKNAQVILLSAT 146
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
256-375 |
1.60e-13 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 72.98 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 256 LDKV-ELVSRVLQAEGRGATMIFTRTKRTAQKVADELAERGFKVGAVhgdLGQIARE-----------KALKAFREGDVD 323
Cdd:PRK13766 349 LEKLrEIVKEQLGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVRF---VGQASKDgdkgmsqkeqiEILDKFRAGEFN 425
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2321260977 324 VLVATDVAARGIDIDDITHVINYQ-IPdDEQAYVHRIGRTGRaGKTGIAVTLV 375
Cdd:PRK13766 426 VLVSTSVAEEGLDIPSVDLVIFYEpVP-SEIRSIQRKGRTGR-QEEGRVVVLI 476
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
258-360 |
2.55e-12 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 64.03 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 258 KVELVSRVLQA--EGRGATMIFTRTKRTAQKVADELAERGFKVGAVHGDLGQIAREKALKAFRE--GDVDVLVATDVAAR 333
Cdd:cd18793 12 KLEALLELLEElrEPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEdpDIRVFLLSTKAGGV 91
|
90 100 110
....*....|....*....|....*....|...
gi 2321260977 334 GIDIDDITHVINYQIP----DDEQAY--VHRIG 360
Cdd:cd18793 92 GLNLTAANRVILYDPWwnpaVEEQAIdrAHRIG 124
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
274-365 |
5.69e-11 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350189 [Multi-domain] Cd Length: 142 Bit Score: 60.30 E-value: 5.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 274 TMIFTRTKRTAQKVADELAER---------GFKVGAVHG------DLGQIAREKALKAFREGDVDVLVATDVAARGIDID 338
Cdd:cd18802 28 GIIFVERRATAVVLSRLLKEHpstlafircGFLIGRGNSsqrkrsLMTQRKQKETLDKFRDGELNLLIATSVLEEGIDVP 107
|
90 100
....*....|....*....|....*..
gi 2321260977 339 DITHVINYQIPDDEQAYVHRIGRtGRA 365
Cdd:cd18802 108 ACNLVIRFDLPKTLRSYIQSRGR-ARA 133
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
274-367 |
9.47e-11 |
|
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: 59.97 E-value: 9.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 274 TMIFTRTKRTAQKVADELAER------GFKVGAVHGDLGQIAREKALKAFREGDVDVLVATDVAARGIDIDDITHVINYQ 347
Cdd:cd18796 41 TLVFTNTRSQAERLAQRLRELcpdrvpPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIG 120
|
90 100
....*....|....*....|
gi 2321260977 348 IPDDEQAYVHRIGRTGRAGK 367
Cdd:cd18796 121 SPKSVARLLQRLGRSGHRPG 140
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
27-388 |
9.48e-11 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 63.76 E-value: 9.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 27 VRDEIVRALGEEGIVHPFAIQELTLPLAL-AGDDLIGQARTGMGKTYAFGVPLLNRVTTDterplagaPRALVVVPTREL 105
Cdd:COG1204 7 PLEKVIEFLKERGIEELYPPQAEALEAGLlEGKNLVVSAPTASGKTLIAELAILKALLNG--------GKALYIVPLRAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 106 CLQVYGDLAgaaKYLTADGgrkLSVVSIYGgrPYEPQIEALrAGADVVVGTPGRLLDLAQQGHLQLGGLSVLVLDEA--- 182
Cdd:COG1204 79 ASEKYREFK---RDFEELG---IKVGVSTG--DYDSDDEWL-GRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAhli 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 183 -D-------EMLdlgflpdIERILRLTPDTrQAMLFSATMPDPIItLARtFMNQP---THIRAeSPQSSQTHDSTEQFIY 251
Cdd:COG1204 150 dDesrgptlEVL-------LARLRRLNPEA-QIVALSATIGNAEE-IAE-WLDAElvkSDWRP-VPLNEGVLYDGVLRFD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 252 RAHALDKVELVSRVLQA-EGRGATMIFTRTKRTAQKVADELA-------------------------------------- 292
Cdd:COG1204 219 DGSRRSKDPTLALALDLlEEGGQVLVFVSSRRDAESLAKKLAdelkrrltpeereeleelaeellevseethtnekladc 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 293 -ERGfkVGAVHGDLGQIAREKALKAFREGDVDVLVATD-------VAARGIDIDDITHVINYQIPDDEqayVHR-IGRTG 363
Cdd:COG1204 299 lEKG--VAFHHAGLPSELRRLVEDAFREGLIKVLVATPtlaagvnLPARRVIIRDTKRGGMVPIPVLE---FKQmAGRAG 373
|
410 420
....*....|....*....|....*..
gi 2321260977 364 RAGK--TGIAVtLVDWDELPRWALIDK 388
Cdd:COG1204 374 RPGYdpYGEAI-LVAKSSDEADELFER 399
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
64-338 |
5.06e-10 |
|
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: 61.64 E-value: 5.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 64 ARTGMGKTYAFGVPLLNrvttdterpLA---GAPRALVVVPTRELCLQVYGDLAGA--AKYLTADGGRKLSVVSIYGGRP 138
Cdd:COG1203 154 APTGGGKTEAALLFALR---------LAakhGGRRIIYALPFTSIINQTYDRLRDLfgEDVLLHHSLADLDLLEEEEEYE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 139 YEPQIEALRAG---ADVVVGTPGRLLD--LAQQGH-----LQLGGlSVLVLDEADeMLDLGFLPDIERILRL--TPDTRq 206
Cdd:COG1203 225 SEARWLKLLKElwdAPVVVTTIDQLFEslFSNRKGqerrlHNLAN-SVIILDEVQ-AYPPYMLALLLRLLEWlkNLGGS- 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 207 AMLFSATMPDPIitlaRTFMNQPTHIRAESPQssQTHDSTEQFI-----YRAHALDKVELVSRVLQA-EGRGATMIFTRT 280
Cdd:COG1203 302 VILMTATLPPLL----REELLEAYELIPDEPE--ELPEYFRAFVrkrveLKEGPLSDEELAELILEAlHKGKSVLVIVNT 375
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2321260977 281 KRTAQKVADELAERGFKVGAVHgdL-GQI------AREKALKA-FREGDVDVLVATDVAARGIDID 338
Cdd:COG1203 376 VKDAQELYEALKEKLPDEEVYL--LhSRFcpadrsEIEKEIKErLERGKPCILVSTQVVEAGVDID 439
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
250-380 |
1.07e-09 |
|
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: 56.97 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 250 IYRAHALDKV-ELVSRVLqAEGRGATMIFTRTK-------RTAQKVADELAER---GFKVGAVHGDLGQIAREKALKAFR 318
Cdd:cd18811 6 LIFHTRLDKVyEFVREEI-AKGRQAYVIYPLIEesekldlKAAVAMYEYLKERfrpELNVGLLHGRLKSDEKDAVMAEFR 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2321260977 319 EGDVDVLVATDVAARGIDIDDITHVInyqIPDDEQ---AYVHRI-GRTGRAGKTGIAVtLVDWDEL 380
Cdd:cd18811 85 EGEVDILVSTTVIEVGVDVPNATVMV---IEDAERfglSQLHQLrGRVGRGDHQSYCL-LVYKDPL 146
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
256-364 |
2.81e-09 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350188 [Multi-domain] Cd Length: 143 Bit Score: 55.44 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 256 LDKV-ELVSRVLQAEGRGAT---MIFTRTKRTAQKVADELAERGFKVGA--------VHGDLGQIAREK--ALKAFREGD 321
Cdd:cd18801 11 LEKLeEIVKEHFKKKQEGSDtrvIIFSEFRDSAEEIVNFLSKIRPGIRAtrfigqasGKSSKGMSQKEQkeVIEQFRKGG 90
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2321260977 322 VDVLVATDVAARGIDIDDITHVINYQIPDDEQAYVHRIGRTGR 364
Cdd:cd18801 91 YNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
258-362 |
6.51e-09 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 58.31 E-value: 6.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 258 KVELVSRVLQ---AEGRGAtMIFTRTKRTAQKVADELAERGFKVGAVHGDLGQIAREKALKAFREGD--VDVLVATDVAA 332
Cdd:COG0553 534 KLEALLELLEellAEGEKV-LVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGG 612
|
90 100 110
....*....|....*....|....*....|....*.
gi 2321260977 333 RGIDIDDITHVINYQIPDD----EQAY--VHRIGRT 362
Cdd:COG0553 613 EGLNLTAADHVIHYDLWWNpaveEQAIdrAHRIGQT 648
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
257-381 |
1.46e-07 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350179 [Multi-domain] Cd Length: 160 Bit Score: 50.73 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 257 DKVELVSRVLQAE---GRGATMIFTRTKRT-------AQKVADELAER--GFKVGAVHGDLGQIAREKALKAFREGDVDV 324
Cdd:cd18792 10 DDLDLVYEAIERElarGGQVYYVYPRIEESekldlksIEALAEELKELvpEARVALLHGKMTEDEKEAVMLEFREGEYDI 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2321260977 325 LVATDVAARGIDIDDITHVInyqIPDDEQ---AYVHRI-GRTGRAGKTGIAVtLVDWDELP 381
Cdd:cd18792 90 LVSTTVIEVGIDVPNANTMI---IEDADRfglSQLHQLrGRVGRGKHQSYCY-LLYPDPKK 146
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
269-367 |
1.77e-07 |
|
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: 50.33 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 269 EGRGATMIFTRTKRTAQkvadELAERgFKVGAVHGDLGQIAREKALKAFREGDVDVLVATDVAARGIDIDDITHVInyQI 348
Cdd:cd18789 47 EQGDKIIVFTDNVEALY----RYAKR-LLKPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPEANVAI--QI 119
|
90 100
....*....|....*....|..
gi 2321260977 349 ---PDDEQAYVHRIGRTGRAGK 367
Cdd:cd18789 120 sghGGSRRQEAQRLGRILRPKK 141
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
260-364 |
2.10e-07 |
|
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350177 [Multi-domain] Cd Length: 171 Bit Score: 50.71 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 260 ELVSRVLQAEGrgaTMIFTRTKRTAQKVADELAERGFKVGAVHGDLGQIAREKALKAFREGDVDVLVATDVAARGIDIDD 339
Cdd:cd18790 19 EIRKRVARGER---VLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPE 95
|
90 100 110
....*....|....*....|....*....|...
gi 2321260977 340 ITHVInyqIPD--------DEQAYVHRIGRTGR 364
Cdd:cd18790 96 VSLVA---ILDadkegflrSETSLIQTIGRAAR 125
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
274-344 |
2.20e-07 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350186 [Multi-domain] Cd Length: 116 Bit Score: 49.09 E-value: 2.20e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2321260977 274 TMIFTRTKRTAQKVADELAERGFKVGAVHGDLGQIAREKA---LKAFREGDVDVLVATDVAARGIDIDDITHVI 344
Cdd:cd18799 9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDEaliLLFFGELKPPILVTVDLLTTGVDIPEVDNVV 82
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
257-380 |
2.46e-07 |
|
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: 50.38 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 257 DKVELVSRVlqaeGRGaTMIFTRT---KRTAQKVADELAERGFKVGAVHGDlgqiaREKALKAFREGDVDVLVAT----D 329
Cdd:cd18798 15 KLLELVKKL----GDG-GLIFVSIdygKEYAEELKEFLERHGIKAELALSS-----TEKNLEKFEEGEIDVLIGVasyyG 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2321260977 330 VAARGIDIDD-ITHVINYQIPddEQAYVHRIGRTGR--AGK--TGIAVTLVDWDEL 380
Cdd:cd18798 85 VLVRGIDLPErIKYAIFYGVP--VTTYIQASGRTSRlyAGGltKGLSVVLVDDPEL 138
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
324-376 |
3.66e-07 |
|
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: 47.31 E-value: 3.66e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2321260977 324 VLVATDVAARGIDIDDITHVINYQIPDDEQAYVHRIGRTGRAGKTGIAVTLVD 376
Cdd:cd18785 25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILFV 77
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
259-376 |
1.09e-06 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 50.87 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 259 VELVSRVLQAEGRGATMIFTRTKRTAQKVADELAERGFKVGAVHGDLGQIAREKALKAFREGDVDVLVATDVAARGIDID 338
Cdd:PRK11057 224 LDQLMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKP 303
|
90 100 110
....*....|....*....|....*....|....*...
gi 2321260977 339 DITHVINYQIPDDEQAYVHRIGRTGRAGKTGIAVTLVD 376
Cdd:PRK11057 304 NVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYD 341
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
274-372 |
3.23e-06 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 46.48 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 274 TMIFTRTKRTAQKVADELAER-------GFKVGAVHGDLGQIAREKALKAFREGDVDVLVATDVAARGIDIDDITHVINY 346
Cdd:cd18797 38 TIVFCRSRKLAELLLRYLKARlveegplASKVASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLA 117
|
90 100
....*....|....*....|....*.
gi 2321260977 347 QIPDDEQAYVHRIGRTGRAGKTGIAV 372
Cdd:cd18797 118 GYPGSLASLWQQAGRAGRRGKDSLVI 143
|
|
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
282-330 |
3.82e-06 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 49.28 E-value: 3.82e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2321260977 282 RTAQKVADELAER--GFKVGAVHGDLGQIAREKALKAFREGDVDVLVATDV 330
Cdd:COG1200 488 QAAEETYEELREAfpGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTV 538
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
173-367 |
1.03e-05 |
|
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.
Pssm-ID: 273707 [Multi-domain] Cd Length: 359 Bit Score: 47.45 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 173 GLSVLVLDEADEMLD--LGFlpdIERILRLTPDTRQ-AMLFSATMPDPIITLARTFMNQPTHiraESPQSSQTHDSTEQF 249
Cdd:TIGR01587 124 ANSLLIFDEVHFYDEytLAL---ILAVLEVLKDNDVpILLMSATLPKFLKEYAEKIGYVEFN---EPLDLKEERRFENHR 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 250 IYRAHALDKVELVS--RVLQA-EGRGATMIFTRTKRTAQKVADELAERG--FKVGAVHGDLGQIAREKA-----LKAFRE 319
Cdd:TIGR01587 198 FILIESDKVGEISSleRLLEFiKKGGSIAIIVNTVDRAQEFYQQLKEKApeEEIILYHSRFTEKDRAKKeaellREMKKS 277
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2321260977 320 GDVDVLVATDVAARGIDID-DIthVINYQIPDDeqAYVHRIGRTGRAGK 367
Cdd:TIGR01587 278 NEKFVIVATQVIEASLDISaDV--MITELAPID--SLIQRLGRLHRYGR 322
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
173-381 |
1.50e-05 |
|
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
Pssm-ID: 187770 [Multi-domain] Cd Length: 353 Bit Score: 47.04 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 173 GLSVLVLDEADEMLD--LGFlpdIERILRLTPDTRQ-AMLFSATMPDPIITLARTFMNqpthirAESPQSSQTHDSTEQF 249
Cdd:cd09639 123 ANSLLIFDEVHFYDEytLAL---ILAVLEVLKDNDVpILLMSATLPKFLKEYAEKIGY------VEENEPLDLKPNERAP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 250 IYRAHALDKVELVS--RVLQA-EGRGATMIFTRTKRTAQKVADELAERG--FKVGAVHGDLGQIAREKA----LKAFREG 320
Cdd:cd09639 194 FIKIESDKVGEISSleRLLEFiKKGGSVAIIVNTVDRAQEFYQQLKEKGpeEEIMLIHSRFTEKDRAKKeaelLLEFKKS 273
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2321260977 321 DVDVLVATDVAARGIDID-DIthVINYQIPDDeqAYVHRIGRTGRAGKtGIAVTLVDWDELP 381
Cdd:cd09639 274 EKFVIVATQVIEASLDISvDV--MITELAPID--SLIQRLGRLHRYGE-KNGEEVYIITDAP 330
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
43-217 |
5.97e-05 |
|
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: 43.73 E-value: 5.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 43 PFAIQELTLPLALAGDDLIGQARTGMGKTYAFGVPLLNRVTTDTERplagapRALVVVPTRELClqvyGDLAGAAKYLTA 122
Cdd:cd17923 1 LYSHQAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDPGS------RALYLYPTKALA----QDQLRSLRELLE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 123 DGGRKLSVVSIYGGRPYEPQIEALRAGADVVVGTPGRL----LDLAQQGHLQLGGLSVLVLDEADEM-----LDLGFLpd 193
Cdd:cd17923 71 QLGLGIRVATYDGDTPREERRAIIRNPPRILLTNPDMLhyalLPHHDRWARFLRNLRYVVLDEAHTYrgvfgSHVALL-- 148
|
170 180
....*....|....*....|....*..
gi 2321260977 194 IERILRLTPDTR---QAMLFSATMPDP 217
Cdd:cd17923 149 LRRLRRLCRRYGadpQFILTSATIGNP 175
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
275-367 |
1.10e-04 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 44.89 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 275 MIFTRTKRTAQKVADELAERGFKVGAVHGDLGQIAREKALKAFREGDVDVLVATDVAARGIDIDDITHVINYQIPDDEQA 354
Cdd:PLN03137 684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEG 763
|
90
....*....|...
gi 2321260977 355 YVHRIGRTGRAGK 367
Cdd:PLN03137 764 YHQECGRAGRDGQ 776
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
282-337 |
1.20e-04 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 44.37 E-value: 1.20e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2321260977 282 RTAQKVADELAER--GFKVGAVHGDLGQIAREKALKAFREGDVDVLVATDVAARGIDI 337
Cdd:PRK10917 490 QSAEETYEELQEAfpELRVGLLHGRMKPAEKDAVMAAFKAGEIDILVATTVIEVGVDV 547
|
|
| DinG |
COG1199 |
Rad3-related DNA helicase DinG [Replication, recombination and repair]; |
253-344 |
1.50e-04 |
|
Rad3-related DNA helicase DinG [Replication, recombination and repair];
Pssm-ID: 440812 [Multi-domain] Cd Length: 629 Bit Score: 44.15 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 253 AHALDKVELVSRVLQAEGrGATMIFTRTKRTAQKVADELAER-GFKVgAVHGDLgqiAREKALKAFREGDVDVLVATDVA 331
Cdd:COG1199 443 GYLEAIAEAIAELLEASG-GNTLVLFTSYRALEQVAELLRERlDIPV-LVQGDG---SREALLERFREGGNSVLVGTGSF 517
|
90
....*....|....*
gi 2321260977 332 ARGIDI--DDITHVI 344
Cdd:COG1199 518 WEGVDLpgDALSLVI 532
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
265-376 |
6.13e-04 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350182 [Multi-domain] Cd Length: 154 Bit Score: 40.23 E-value: 6.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 265 VLQAEGRGATMIFTRTKRTAQKVADELAergfKVGAVHGDLGQIAREKALKAFREGDVDVLVATDVAARGID-------I 337
Cdd:cd18795 37 IETVSEGKPVLVFCSSRKECEKTAKDLA----GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNlpartviI 112
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2321260977 338 DDITHVINYQIPD-DEQAYVHRIGRTGRAGK--TGIAVTLVD 376
Cdd:cd18795 113 KGTQRYDGKGYRElSPLEYLQMIGRAGRPGFdtRGEAIIMTK 154
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
53-217 |
9.80e-04 |
|
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: 39.94 E-value: 9.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 53 LALAGDDLIGQARTGMGKTYAFGVPLLNRVTTdterplaGAPRALVVVPTRELCLQVYGDlagaakyLTADGGRKLSVVS 132
Cdd:cd17921 13 LYLSGDSVLVSAPTSSGKTLIAELAILRALAT-------SGGKAVYIAPTRALVNQKEAD-------LRERFGPLGKNVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 133 IYGGRPYEPQIEAlrAGADVVVGTPGRLLDLAQQGHLQLGG-LSVLVLDEADEMLDlgflPD--------IERILRLTPD 203
Cdd:cd17921 79 LLTGDPSVNKLLL--AEADILVATPEKLDLLLRNGGERLIQdVRLVVVDEAHLIGD----GErgvvlellLSRLLRINKN 152
|
170
....*....|....*
gi 2321260977 204 TRqaMLF-SATMPDP 217
Cdd:cd17921 153 AR--FVGlSATLPNA 165
|
|
| ComFA |
COG4098 |
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ... |
275-364 |
3.33e-03 |
|
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, recombination and repair];
Pssm-ID: 443274 [Multi-domain] Cd Length: 451 Bit Score: 39.86 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 275 MIFTRTKRTAQKVADELAER--GFKVGAVHGdlGQIAREKALKAFREGDVDVLVATDVAARGIDIDDItHVINYQIPD-- 350
Cdd:COG4098 323 LIFVPTIELLEQLVALLQKLfpEERIAGVHA--EDPERKEKVQAFRDGEIPILVTTTILERGVTFPNV-DVAVLGADHpv 399
|
90
....*....|....*
gi 2321260977 351 -DEQAYVHRIGRTGR 364
Cdd:COG4098 400 fTEAALVQIAGRVGR 414
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
285-375 |
4.35e-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: 37.71 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 285 QKVADELAE--RGFKVGAVHGDLGQIAREKALKAFREGDVDVLVATDVAARGIDIDDithvINYQIPDDEQ----AYVHR 358
Cdd:cd18810 39 EKLATQLRQlvPEARIAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPN----ANTIIIERADkfglAQLYQ 114
|
90
....*....|....*...
gi 2321260977 359 I-GRTGRAGKTGIAVTLV 375
Cdd:cd18810 115 LrGRVGRSKERAYAYFLY 132
|
|
| PRK07413 |
PRK07413 |
cob(I)yrinic acid a,c-diamide adenosyltransferase; |
175-272 |
4.37e-03 |
|
cob(I)yrinic acid a,c-diamide adenosyltransferase;
Pssm-ID: 180968 [Multi-domain] Cd Length: 382 Bit Score: 39.32 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 175 SVLVLDEADEMLDLGFLP--DIERILRLTPDTRQAMLFSATMPDPIITLARTFMNQPTHIRAESPQSSQTHDSTEQF-IY 251
Cdd:PRK07413 127 SVVVLDELNPVLDLGLLPvdEVVNTLKSRPEGLEIIITGRAAPQSLLDIADLHSEMRPHRRPTASELGVPFNSSGGIeIY 206
|
90 100
....*....|....*....|..
gi 2321260977 252 RAHALDK-VELVSRVLQAEGRG 272
Cdd:PRK07413 207 TGEGKGKsTSALGKALQAIGRG 228
|
|
| fabG |
PRK05557 |
3-ketoacyl-(acyl-carrier-protein) reductase; Validated |
271-326 |
7.43e-03 |
|
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
Pssm-ID: 235500 [Multi-domain] Cd Length: 248 Bit Score: 37.87 E-value: 7.43e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2321260977 271 RGATMIFT--RTKRTAQKVADELAERGFKVGAVHGDLG---QIAR--EKALKAFreGDVDVLV 326
Cdd:PRK05557 28 QGANVVINyaSSEAGAEALVAEIGALGGKALAVQGDVSdaeSVERavDEAKAEF--GGVDILV 88
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
55-217 |
7.48e-03 |
|
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: 37.31 E-value: 7.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 55 LAGDDLIGQARTGMGKTYAFGVPLLNRVttdterpLAGApRALVVVPTRELCLQVYGDLagaaKYLTADGGRklsvVSIY 134
Cdd:cd18028 15 LKGENLLISIPTASGKTLIAEMAMVNTL-------LEGG-KALYLVPLRALASEKYEEF----KKLEEIGLK----VGIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 135 GGRpYEPQIEALrAGADVVVGTPGRLLDLAQQGHLQLGGLSVLVLDEADEMLDLGFLPDIE----RILRLTPDTRQAMLf 210
Cdd:cd18028 79 TGD-YDEDDEWL-GDYDIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPTLEsivaRLRRLNPNTQIIGL- 155
|
....*..
gi 2321260977 211 SATMPDP 217
Cdd:cd18028 156 SATIGNP 162
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
64-218 |
7.72e-03 |
|
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350688 [Multi-domain] Cd Length: 186 Bit Score: 37.27 E-value: 7.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 64 ARTGMGKTYAFGVPLLNRvttdteRPLAGAPRALVVVPTRELCLQVYGDLAGAAKYLTAD-------GGRKLSVVSIYGG 136
Cdd:cd17930 8 APTGSGKTEAALLWALKL------AARGGKRRIIYALPTRATINQMYERIREILGRLDDEdkvlllhSKAALELLESDEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 137 RPYEPQIEALRA-------GADVVVGTPGRLLDLAQQG---HLQLGGL--SVLVLDEAdEMLDLGFLPDI-ERILRLTPD 203
Cdd:cd17930 82 PDDDPVEAVDWAlllkrswLAPIVVTTIDQLLESLLKYkhfERRLHGLanSVVVLDEV-QAYDPEYMALLlKALLELLGE 160
|
170
....*....|....*.
gi 2321260977 204 TR-QAMLFSATMPDPI 218
Cdd:cd17930 161 LGgPVVLMTATLPALL 176
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
238-369 |
8.08e-03 |
|
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family members are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350178 [Multi-domain] Cd Length: 171 Bit Score: 37.13 E-value: 8.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 238 QSSQTHDSTEQFIYRAHALDKVElvsRVLQAEGRGATMIF-------TRTKRTAQKVADELAERGFKVGAVHGDLGQIAR 310
Cdd:cd18791 13 ELLGISSEKEDPDYVDAAVRLIL---QIHRTEEPGDILVFlpgqeeiERLCELLREELLSPDLGKLLVLPLHSSLPPEEQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2321260977 311 EKALKAFREGDVDVLVATDVAARGIDIDDITHVInyqipdD-----EQAYVHRIG----------------RTGRAGKTG 369
Cdd:cd18791 90 QRVFEPPPPGVRKVVLATNIAETSITIPGVVYVI------DsglvkEKVYDPRTGlsslvtvwiskasaeqRAGRAGRTR 163
|
|
| PRK05298 |
PRK05298 |
excinuclease ABC subunit UvrB; |
274-326 |
9.92e-03 |
|
excinuclease ABC subunit UvrB;
Pssm-ID: 235395 [Multi-domain] Cd Length: 652 Bit Score: 38.49 E-value: 9.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2321260977 274 TMIFTRTKRTAQKVADELAERGFKVGAVHGDLGQIAREKALKAFREGDVDVLV 326
Cdd:PRK05298 449 VLVTTLTKRMAEDLTDYLKELGIKVRYLHSDIDTLERVEIIRDLRLGEFDVLV 501
|
|
| |
