|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
26-409 |
2.16e-104 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 332.88 E-value: 2.16e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 26 TFEELRLYRNLLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQSFNPNI-NQPHAMIVVPTRE 104
Cdd:COG0513 3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRpRAPQALILAPTRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 105 LAIQVQDTFFHLCKsFRDFKCSAFIGGTDVAKDRKRMNE-SRVIIGTPGRLLHLYENRVFDVSKLRLLVLDEADQLyqtk 183
Cdd:COG0513 83 LALQVAEELRKLAK-YLGLRVATVYGGVSIGRQIRALKRgVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRM---- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 184 sL----QHTVSKLIEAMPKNRQIIACSATYDQNLDERLAKVMDKPMLISNSERATVLLGIRQFVYELPQQNnsveemrlK 259
Cdd:COG0513 158 -LdmgfIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRD--------K 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 260 LQILGQIFNQLPYEQAIIFASSQMRADSYKNYLTASGIDCHLISGAMEQSERLHVFEGYRNFTMRILVATDLMARGVDSP 339
Cdd:COG0513 229 LELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDID 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 340 HANLVINIDPPQDHVTYLHRIGRAGRFGSKGIAITFIaSKKESQRFREMSKKIAtawsvLEFPKEPMPNE 409
Cdd:COG0513 309 DVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLV-TPDERRLLRAIEKLIG-----QKIEEEELPGF 372
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
36-228 |
8.64e-101 |
|
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: 314.59 E-value: 8.64e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 36 LLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQSFNPNINQPHAMIVVPTRELAIQVQDTFFH 115
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 116 LCKSFRDFKCSAFIGGTDVAKDRKRMNESRVIIGTPGRLLHLYENRVFDVSKLRLLVLDEADQLYQtKSLQHTVSKLIEA 195
Cdd:cd17943 81 IGKKLEGLKCEVFIGGTPVKEDKKKLKGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLME-GSFQKDVNWIFSS 159
|
170 180 190
....*....|....*....|....*....|...
gi 17647335 196 MPKNRQIIACSATYDQNLDERLAKVMDKPMLIS 228
Cdd:cd17943 160 LPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
24-383 |
1.52e-63 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 220.85 E-value: 1.52e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 24 VKTFEELRLYRNLLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQSFNPNINQPHAMIVVPTR 103
Cdd:PTZ00424 27 VDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 104 ELAIQVQDTFFHLcKSFRDFKCSAFIGGTDVAKDRKRMNES-RVIIGTPGRLLHLYENRVFDVSKLRLLVLDEADQLYqT 182
Cdd:PTZ00424 107 ELAQQIQKVVLAL-GDYLKVRCHACVGGTVVRDDINKLKAGvHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEML-S 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 183 KSLQHTVSKLIEAMPKNRQIIACSATYDQNLDERLAKVMDKPMLISNSERATVLLGIRQFVYelpqqnnSVEEMRLKLQI 262
Cdd:PTZ00424 185 RGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYV-------AVEKEEWKFDT 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 263 LGQIFNQLPYEQAIIFASSQMRADSYKNYLTASGIDCHLISGAMEQSERLHVFEGYRNFTMRILVATDLMARGVDSPHAN 342
Cdd:PTZ00424 258 LCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVS 337
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 17647335 343 LVINIDPPQDHVTYLHRIGRAGRFGSKGIAITFIASKKESQ 383
Cdd:PTZ00424 338 LVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQ 378
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
36-228 |
3.98e-55 |
|
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: 189.58 E-value: 3.98e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 36 LLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQSFNPN----INQPHAMIVVPTRELAIQVQD 111
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEpkkkGRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 112 TFFHLCKsFRDFKCSAFIGGTDVAKDRKRMNE-SRVIIGTPGRLLHLYENRVFDVSKLRLLVLDEADQLYQtKSLQHTVS 190
Cdd:cd00268 81 VARKLGK-GTGLKVAAIYGGAPIKKQIEALKKgPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLD-MGFEEDVE 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 17647335 191 KLIEAMPKNRQIIACSATYDQNLDERLAKVMDKPMLIS 228
Cdd:cd00268 159 KILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
27-384 |
6.91e-53 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 192.32 E-value: 6.91e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 27 FEELRLYRNLLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQSFNPNINQPHAMIVVPTRELA 106
Cdd:PRK11776 6 FSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTRELA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 107 IQVQDTFFHLCKSFRDFKCSAFIGGTDVAKDRkrmnES-----RVIIGTPGRLL-HLYENRVfDVSKLRLLVLDEADQLy 180
Cdd:PRK11776 86 DQVAKEIRRLARFIPNIKVLTLCGGVPMGPQI----DSlehgaHIIVGTPGRILdHLRKGTL-DLDALNTLVLDEADRM- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 181 qtksL----QHTVSKLIEAMPKNRQIIACSATYDQNLdERLAK-VMDKPMLISnSERATVLLGIRQFVYELPQQNnsvee 255
Cdd:PRK11776 160 ----LdmgfQDAIDAIIRQAPARRQTLLFSATYPEGI-AAISQrFQRDPVEVK-VESTHDLPAIEQRFYEVSPDE----- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 256 mrlKLQILGQIFNQLPYEQAIIFASSQMRADSYKNYLTASGIDCHLISGAMEQSERLHVFEGYRNFTMRILVATDLMARG 335
Cdd:PRK11776 229 ---RLPALQRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARG 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 17647335 336 VDSPHANLVINIDPPQDHVTYLHRIGRAGRFGSKGIAITFIASkKESQR 384
Cdd:PRK11776 306 LDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAP-EEMQR 353
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
25-376 |
3.29e-52 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 189.77 E-value: 3.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 25 KTFEELRLYRNLLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQSF------NPNinQPHAMI 98
Cdd:PRK11192 1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLldfprrKSG--PPRILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 99 VVPTRELAIQVQDTFFHLCKsFRDFKCSAFIGGTDVAKDRKRMNESR-VIIGTPGRLLHLYENRVFDVSKLRLLVLDEAD 177
Cdd:PRK11192 79 LTPTRELAMQVADQARELAK-HTHLDIATITGGVAYMNHAEVFSENQdIVVATPGRLLQYIKEENFDCRAVETLILDEAD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 178 QLyqtksLQHTVSKLIEAMPKN----RQIIACSATYDQNLDERLAK-VMDKPMLI----SNSERATvllgIRQFVYElpq 248
Cdd:PRK11192 158 RM-----LDMGFAQDIETIAAEtrwrKQTLLFSATLEGDAVQDFAErLLNDPVEVeaepSRRERKK----IHQWYYR--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 249 qnnsVEEMRLKLQILGQIFNQLPYEQAIIFASSQMRADSYKNYLTASGIDCHLISGAMEQSERLHVFEGYRNFTMRILVA 328
Cdd:PRK11192 226 ----ADDLEHKTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVA 301
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 17647335 329 TDLMARGVDSPHANLVINIDPPQDHVTYLHRIGRAGRFGSKGIAITFI 376
Cdd:PRK11192 302 TDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLV 349
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
49-215 |
5.41e-48 |
|
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: 168.19 E-value: 5.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 49 TKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQSFNPNINQPHAMIVVPTRELAIQVQDTFFHLCKsFRDFKCSAF 128
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGK-GLGLKVASL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 129 IGGTDVAKDRKRMNESRVIIGTPGRLLHLYENRVFdVSKLRLLVLDEADQLYQtKSLQHTVSKLIEAMPKNRQIIACSAT 208
Cdd:pfam00270 80 LGGDSRKEQLEKLKGPDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLD-MGFGPDLEEILRRLPKKRQILLLSAT 157
|
....*..
gi 17647335 209 YDQNLDE 215
Cdd:pfam00270 158 LPRNLED 164
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
25-375 |
8.70e-46 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 170.54 E-value: 8.70e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 25 KTFEELRLYRNLLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAvvqSFN----------PNINQP 94
Cdd:PRK04837 8 QKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTA---TFHyllshpapedRKVNQP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 95 HAMIVVPTRELAIQVQDTFFHLCKSfRDFKCSAFIGGTDVAKDRKRMNES-RVIIGTPGRLLHLYENRVFDVSKLRLLVL 173
Cdd:PRK04837 85 RALIMAPTRELAVQIHADAEPLAQA-TGLKLGLAYGGDGYDKQLKVLESGvDILIGTTGRLIDYAKQNHINLGAIQVVVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 174 DEADQLYQ---TKSLQHtvskLIEAMPknrqiiacsatydqNLDERLAkvmdkpMLISnserATVLLGIRQFVYE----- 245
Cdd:PRK04837 164 DEADRMFDlgfIKDIRW----LFRRMP--------------PANQRLN------MLFS----ATLSYRVRELAFEhmnnp 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 246 -----LPQQNNSV------------EEMRLkLQILgqIFNQLPyEQAIIFASSQMRADSYKNYLTASGIDCHLISGAMEQ 308
Cdd:PRK04837 216 eyvevEPEQKTGHrikeelfypsneEKMRL-LQTL--IEEEWP-DRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQ 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17647335 309 SERLHVFEGYRNFTMRILVATDLMARGVDSPHANLVINIDPPQDHVTYLHRIGRAGRFGSKGIAITF 375
Cdd:PRK04837 292 KKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
19-407 |
1.61e-44 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 168.55 E-value: 1.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 19 VAPGQVKT-FEELRLYRNLLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQSFNPN------- 90
Cdd:PRK01297 80 VEPQEGKTrFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTpppkery 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 91 INQPHAMIVVPTRELAIQVQDTFFHLCKsFRDFKCSAFIGGTDVAKDRKRMNESR--VIIGTPGRLLHLYENRVFDVSKL 168
Cdd:PRK01297 160 MGEPRALIIAPTRELVVQIAKDAAALTK-YTGLNVMTFVGGMDFDKQLKQLEARFcdILVATPGRLLDFNQRGEVHLDMV 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 169 RLLVLDEADQLYQTKSLQHtVSKLIEAMPK--NRQIIACSATYDQNLDERLAKVMDKPMLISNSERATVLLGIRQFVYEL 246
Cdd:PRK01297 239 EVMVLDEADRMLDMGFIPQ-VRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAV 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 247 PQQNnsveemrlKLQILGQIFNQLPYEQAIIFASSQMRADSYKNYLTASGIDCHLISGAMEQSERLHVFEGYRNFTMRIL 326
Cdd:PRK01297 318 AGSD--------KYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVL 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 327 VATDLMARGVDSPHANLVINIDPPQDHVTYLHRIGRAGRFGSKGIAITFiASKKESQRFREMSKKIATAWSVLEFPKE-- 404
Cdd:PRK01297 390 VATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISF-AGEDDAFQLPEIEELLGRKISCEMPPAEll 468
|
....
gi 17647335 405 -PMP 407
Cdd:PRK01297 469 kPVP 472
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
21-380 |
3.68e-44 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 168.80 E-value: 3.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 21 PGQVKTFEELRLYRNLLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQSFN--PNINQ---PH 95
Cdd:PTZ00110 126 PKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINaqPLLRYgdgPI 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 96 AMIVVPTRELAIQVQDTFFHLCKSFRdFKCSAFIGGtdVAKDRKRMNESR---VIIGTPGRLLHLYENRVFDVSKLRLLV 172
Cdd:PTZ00110 206 VLVLAPTRELAEQIREQCNKFGASSK-IRNTVAYGG--VPKRGQIYALRRgveILIACPGRLIDFLESNVTNLRRVTYLV 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 173 LDEADQLYQTkSLQHTVSKLIEAMPKNRQIIACSATYD---QNLDERLAKvmDKPMLIS-NSERATVLLGIRQFVYELPQ 248
Cdd:PTZ00110 283 LDEADRMLDM-GFEPQIRKIVSQIRPDRQTLMWSATWPkevQSLARDLCK--EEPVHVNvGSLDLTACHNIKQEVFVVEE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 249 QnnsveEMRLKLQ-ILGQIFNQLPyeQAIIFASSQMRADSYKNYLTASGIDCHLISGAMEQSERLHVFEGYRNFTMRILV 327
Cdd:PTZ00110 360 H-----EKRGKLKmLLQRIMRDGD--KILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMI 432
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 17647335 328 ATDLMARGVDSPHANLVINIDPPQDHVTYLHRIGRAGRFGSKGIAITFIASKK 380
Cdd:PTZ00110 433 ATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDK 485
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
239-376 |
2.91e-43 |
|
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: 153.43 E-value: 2.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 239 IRQFVYElpqqnnsVEEMRLKLQILGQIFNQLPYEQAIIFASSQMRADSYKNYLTASGIDCHLISGAMEQSERLHVFEGY 318
Cdd:cd18787 1 IKQLYVV-------VEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKF 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 17647335 319 RNFTMRILVATDLMARGVDSPHANLVINIDPPQDHVTYLHRIGRAGRFGSKGIAITFI 376
Cdd:cd18787 74 RSGKVRVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
27-227 |
3.35e-43 |
|
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: 155.92 E-value: 3.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 27 FEELRLYRNLLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQSFNPNINQPHAMIVVPTRELA 106
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 107 IQVQDTFFHLCKsFRDFKCSAFIGGTDVAKDRKRMNES-RVIIGTPGRLLHLYENRVFDVSKLRLLVLDEADQLYqTKSL 185
Cdd:cd17940 81 LQTSQVCKELGK-HMGVKVMVTTGGTSLRDDIMRLYQTvHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLL-SQDF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17647335 186 QHTVSKLIEAMPKNRQIIACSATYDQNLDERLAKVMDKPMLI 227
Cdd:cd17940 159 QPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
26-408 |
7.96e-43 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 166.56 E-value: 7.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 26 TFEELRLYRNLLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQSFNPNINQPHAMIVVPTREL 105
Cdd:PRK11634 7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 106 AIQVQDTFFHLCKSFRDFKCSAFIGGT--DVaKDRKRMNESRVIIGTPGRLLHLYENRVFDVSKLRLLVLDEADQLYQTK 183
Cdd:PRK11634 87 AVQVAEAMTDFSKHMRGVNVVALYGGQryDV-QLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 184 SLQhTVSKLIEAMPKNRQIIACSATYDQNLDERLAKVMDKPMLISNSERATVLLGIRQFVYelpqqnnSVEEMRlKLQIL 263
Cdd:PRK11634 166 FIE-DVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYW-------TVWGMR-KNEAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 264 GQIFNQLPYEQAIIFASSQMRADSYKNYLTASGIDCHLISGAMEQSERLHVFEGYRNFTMRILVATDLMARGVDSPHANL 343
Cdd:PRK11634 237 VRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISL 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17647335 344 VINIDPPQDHVTYLHRIGRAGRFGSKGIAITFIaSKKESQRFREMSKKIAtawsvLEFPKEPMPN 408
Cdd:PRK11634 317 VVNYDIPMDSESYVHRIGRTGRAGRAGRALLFV-ENRERRLLRNIERTMK-----LTIPEVELPN 375
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
29-227 |
1.67e-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: 154.02 E-value: 1.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 29 ELRLYRNLLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQSFNPNINQPHAMIVVPTRELAIQ 108
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 109 VQDTFFHLcKSFRDFKCSAFIGGTDVAKDRKRMNES-RVIIGTPGRLLHLYENRVFDVSKLRLLVLDEADQLYqTKSLQH 187
Cdd:cd17939 81 IQKVVKAL-GDYMGVKVHACIGGTSVREDRRKLQYGpHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEML-SRGFKD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17647335 188 TVSKLIEAMPKNRQIIACSATYDQNLDERLAKVMDKPMLI 227
Cdd:cd17939 159 QIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
37-228 |
4.48e-42 |
|
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: 152.44 E-value: 4.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 37 LNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQSFNPNINQPH----AMIVVPTRELAIQvqdT 112
Cdd:cd17941 2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTPEdglgALIISPTRELAMQ---I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 113 FFHLCK--SFRDFKCSAFIGGTDVAKDRKRMNESRVIIGTPGRLL-HLYENRVFDVSKLRLLVLDEADQLYQTkSLQHTV 189
Cdd:cd17941 79 FEVLRKvgKYHSFSAGLIIGGKDVKEEKERINRMNILVCTPGRLLqHMDETPGFDTSNLQMLVLDEADRILDM-GFKETL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17647335 190 SKLIEAMPKNRQIIACSATYDQNLDeRLAKVMDK-PMLIS 228
Cdd:cd17941 158 DAIVENLPKSRQTLLFSATQTKSVK-DLARLSLKnPEYIS 196
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
26-410 |
9.69e-42 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 162.04 E-value: 9.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 26 TFEELRLYRNLLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQSF-------NPNINQPHAMI 98
Cdd:PRK04537 10 TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlsrpalaDRKPEDPRALI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 99 VVPTRELAIQVQDTFFHLCKSFrDFKCSAFIGGTDVAKDRKRMNES-RVIIGTPGRLL-HLYENRVFDVSKLRLLVLDEA 176
Cdd:PRK04537 90 LAPTRELAIQIHKDAVKFGADL-GLRFALVYGGVDYDKQRELLQQGvDVIIATPGRLIdYVKQHKVVSLHACEICVLDEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 177 DQLYQTKSLQhTVSKLIEAMPK--NRQIIACSATYDQNLDERLAKVMDKP-MLISNSERATVLLgIRQFVYeLPQQnnsv 253
Cdd:PRK04537 169 DRMFDLGFIK-DIRFLLRRMPErgTRQTLLFSATLSHRVLELAYEHMNEPeKLVVETETITAAR-VRQRIY-FPAD---- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 254 EEmrlKLQILGQIFNQLPYEQAIIFASSQMRADSYKNYLTASGIDCHLISGAMEQSERLHVFEGYRNFTMRILVATDLMA 333
Cdd:PRK04537 242 EE---KQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAA 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17647335 334 RGVDSPHANLVINIDPPQDHVTYLHRIGRAGRFGSKGIAITFIAskkesQRFrEMSKKIATAWSVLEFPKEPMPNEF 410
Cdd:PRK04537 319 RGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFAC-----ERY-AMSLPDIEAYIEQKIPVEPVTAEL 389
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
35-227 |
1.74e-40 |
|
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called DEAD box RNA helicase DEAD5) and DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH)) are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350721 [Multi-domain] Cd Length: 196 Bit Score: 148.11 E-value: 1.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 35 NLLNGLKRNNFVTPTKIQAAAIPMALAK--MDLIIQSKSGTGKTLIYVIAVVQSFNPNINQPHAMIVVPTRELAIQVQDT 112
Cdd:cd17963 4 ELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQIGEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 113 FFHLCKsFRDFKCSAFIGGTDVAKDRKrmNESRVIIGTPGRLLHLYENRVFDVSKLRLLVLDEADQLYQTKSLQHTVSKL 192
Cdd:cd17963 84 VEKMGK-FTGVKVALAVPGNDVPRGKK--ITAQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTQGHGDQSIRI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 17647335 193 IEAMPKNRQIIACSATYDQNLDERLAKVMDKPMLI 227
Cdd:cd17963 161 KRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
27-227 |
2.17e-40 |
|
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and is required for the export of mRNA out of the nucleus. DDX39B is an essential splicing factor required for association of U2 small nuclear ribonucleoprotein with pre-mRNA, and it also plays an important role in mRNA export from the nucleus to the cytoplasm. Diseases associated with DDX39A (also called UAP56-Related Helicase, 49 kDa) include gastrointestinal stromal tumor and inflammatory bowel disease 6, while diseases associated with DDX39B (also called 56 kDa U2AF65-Associated Protein) include Plasmodium vivax malaria. DDX39 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350708 [Multi-domain] Cd Length: 208 Bit Score: 148.26 E-value: 2.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 27 FEELRLYRNLLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQSFNPNINQPHAMIVVPTRELA 106
Cdd:cd17950 4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRELA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 107 IQVQDTFFHLCKSFRDFKCSAFIGGTDVAKDRKRMNES--RVIIGTPGRLLHLYENRVFDVSKLRLLVLDEADQLYQTKS 184
Cdd:cd17950 84 FQISNEYERFSKYMPNVKTAVFFGGVPIKKDIEVLKNKcpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLEQLD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17647335 185 LQHTVSKLIEAMPKNRQIIACSATYDQNLDERLAKVMDKPMLI 227
Cdd:cd17950 164 MRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEI 206
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
26-376 |
1.62e-39 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 153.04 E-value: 1.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 26 TFEELRLYRNLLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQSFNPNinQPH--------AM 97
Cdd:PRK10590 2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITR--QPHakgrrpvrAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 98 IVVPTRELAIQVQDTFFHLCKsFRDFKCSAFIGGTDVakdRKRMNESR----VIIGTPGRLLHLYENRVFDVSKLRLLVL 173
Cdd:PRK10590 80 ILTPTRELAAQIGENVRDYSK-YLNIRSLVVFGGVSI---NPQMMKLRggvdVLVATPGRLLDLEHQNAVKLDQVEILVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 174 DEADQLYQTKSLqHTVSKLIEAMPKNRQIIACSATYDQNLDERLAKVMDKPMLISNSERATVLLGIRQFVYelpqqnnSV 253
Cdd:PRK10590 156 DEADRMLDMGFI-HDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVH-------FV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 254 EEMRlKLQILGQIFNQLPYEQAIIFASSQMRADSYKNYLTASGIDCHLISGAMEQSERLHVFEGYRNFTMRILVATDLMA 333
Cdd:PRK10590 228 DKKR-KRELLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAA 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 17647335 334 RGVDS---PHanlVINIDPPQDHVTYLHRIGRAGRFGSKGIAITFI 376
Cdd:PRK10590 307 RGLDIeelPH---VVNYELPNVPEDYVHRIGRTGRAAATGEALSLV 349
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
40-242 |
2.48e-39 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 144.94 E-value: 2.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 40 LKRNNFVTPTKIQAAAIPMALA-KMDLIIQSKSGTGKTLIYVIAVVQSFNPNiNQPHAMIVVPTRELAIQVQDTFFHLCK 118
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSgLRDVILAAPTGSGKTLAALLPALEALKRG-KGGRVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 119 SFRdFKCSAFIGGTDVAKDRKRMNESR--VIIGTPGRLLHLYENRVFDVSKLRLLVLDEADQLYQtKSLQHTVSKLIEAM 196
Cdd:smart00487 80 SLG-LKVVGLYGGDSKREQLRKLESGKtdILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLD-GGFGDQLEKLLKLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17647335 197 PKNRQIIACSATYDQNLDERLAKVMDKPMLISNSERAtvLLGIRQF 242
Cdd:smart00487 158 PKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFTP--LEPIEQF 201
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
36-220 |
1.05e-38 |
|
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350718 [Multi-domain] Cd Length: 202 Bit Score: 143.10 E-value: 1.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 36 LLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQSF-----NPNINQPHAMIVVPTRELAIQVQ 110
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrkaNLKKGQVGALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 111 DTFFHLCK-SFRDFKCSAFIGGTDVAKDRKRMNESR--VIIGTPGRLLHLYENR--VFDVSKLRLLVLDEADQLYQTkSL 185
Cdd:cd17960 81 EVLQSFLEhHLPKLKCQLLIGGTNVEEDVKKFKRNGpnILVGTPGRLEELLSRKadKVKVKSLEVLVLDEADRLLDL-GF 159
|
170 180 190
....*....|....*....|....*....|....*
gi 17647335 186 QHTVSKLIEAMPKNRQIIACSATYDQNLDErLAKV 220
Cdd:cd17960 160 EADLNRILSKLPKQRRTGLFSATQTDAVEE-LIKA 193
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
18-404 |
1.65e-38 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 151.48 E-value: 1.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 18 DVAPGQVKTFEELRLYRNLLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVV------QSFNPNI 91
Cdd:PLN00206 114 EAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIIsrcctiRSGHPSE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 92 NQ-PHAMIVVPTRELAIQVQDTFFHLCKSFrDFKCSAFIGGTDVAKDRKRMNES-RVIIGTPGRLLHLYENRVFDVSKLR 169
Cdd:PLN00206 194 QRnPLAMVLTPTRELCVQVEDQAKVLGKGL-PFKTALVVGGDAMPQQLYRIQQGvELIVGTPGRLIDLLSKHDIELDNVS 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 170 LLVLDEADQLYQtKSLQHTVSKLIEAMPKNrQIIACSATYDQNLdERLAKVMDK-PMLIS--NSERATVllGIRQFVYEL 246
Cdd:PLN00206 273 VLVLDEVDCMLE-RGFRDQVMQIFQALSQP-QVLLFSATVSPEV-EKFASSLAKdIILISigNPNRPNK--AVKQLAIWV 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 247 pqqnnsveEMRLKLQilgQIFNQLPYEQ-----AIIFASSQMRADSYKNYLT-ASGIDCHLISGAMEQSERLHVFEGYRN 320
Cdd:PLN00206 348 --------ETKQKKQ---KLFDILKSKQhfkppAVVFVSSRLGADLLANAITvVTGLKALSIHGEKSMKERREVMKSFLV 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 321 FTMRILVATDLMARGVDSPHANLVINIDPPQDHVTYLHRIGRAGRFGSKGIAITFIasKKESQR-FREMSKKIATAWSVL 399
Cdd:PLN00206 417 GEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFV--NEEDRNlFPELVALLKSSGAAI 494
|
....*
gi 17647335 400 efPKE 404
Cdd:PLN00206 495 --PRE 497
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
41-228 |
2.01e-38 |
|
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: 142.72 E-value: 2.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 41 KRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQ---SFNPNINQ---PHAMIVVPTRELAIQVQDTFF 114
Cdd:cd17949 7 SKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQrllSLEPRVDRsdgTLALVLVPTRELALQIYEVLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 115 HLCKSFRDFKCSAFIGGTDVAKD----RKRMNesrVIIGTPGRLL-HLYENRVFDVSKLRLLVLDEADQLYQTkSLQHTV 189
Cdd:cd17949 87 KLLKPFHWIVPGYLIGGEKRKSEkarlRKGVN---ILIATPGRLLdHLKNTQSFDVSNLRWLVLDEADRLLDM-GFEKDI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17647335 190 SKLIEAM-------------PKNRQIIACSATYDQNLdERLAKVM-DKPMLIS 228
Cdd:cd17949 163 TKILELLddkrskaggekskPSRRQTVLVSATLTDGV-KRLAGLSlKDPVYID 214
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
27-227 |
1.15e-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: 134.52 E-value: 1.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 27 FEELRLYRNLLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQSFNPNINQPHAMIVVPTRELA 106
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 107 IQVQDTFFHLCKsFRDFKCSAFIGGTDVAKDRKRMNES-RVIIGTPGRLLHLYENRVFDVSKLRLLVLDEADQLYqTKSL 185
Cdd:cd18045 81 VQIQKVLLALGD-YMNVQCHACIGGTSVGDDIRKLDYGqHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEML-NKGF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17647335 186 QHTVSKLIEAMPKNRQIIACSATYDQNLDERLAKVMDKPMLI 227
Cdd:cd18045 159 KEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
27-228 |
1.19e-35 |
|
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350713 [Multi-domain] Cd Length: 204 Bit Score: 134.27 E-value: 1.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 27 FEELRLYRNLLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQSFNPNinqPH---AMIVVPTR 103
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSED---PYgifALVLTPTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 104 ELAIQVQDTFFHLCKSFrDFKCSAFIGGTDVAKDRKR-MNESRVIIGTPGRLLHLYENRV---FDVSKLRLLVLDEADQL 179
Cdd:cd17955 78 ELAYQIAEQFRALGAPL-GLRCCVIVGGMDMVKQALElSKRPHIVVATPGRLADHLRSSDdttKVLSRVKFLVLDEADRL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17647335 180 YqTKSLQHTVSKLIEAMPKNRQIIACSATYDQNLDERLAKVMDKPMLIS 228
Cdd:cd17955 157 L-TGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFFWE 204
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
26-208 |
5.37e-35 |
|
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: 132.44 E-value: 5.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 26 TFEELRLYRNLLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQSFnpnINQP---HAMIVVPT 102
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQAL---LENPqrfFALVLAPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 103 RELAIQVQDTFFHLCKSFrDFKCSAFIGGTDVAKDRKR-MNESRVIIGTPGRLLHLYEN-RVFDVSKLRLLVLDEADQLY 180
Cdd:cd17954 78 RELAQQISEQFEALGSSI-GLKSAVLVGGMDMMAQAIAlAKKPHVIVATPGRLVDHLENtKGFSLKSLKFLVMDEADRLL 156
|
170 180
....*....|....*....|....*...
gi 17647335 181 qTKSLQHTVSKLIEAMPKNRQIIACSAT 208
Cdd:cd17954 157 -NMDFEPEIDKILKVIPRERTTYLFSAT 183
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
27-227 |
1.09e-34 |
|
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: 131.41 E-value: 1.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 27 FEELRLYRNLLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQSFNPNINQPHAMIVVPTRELA 106
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 107 IQVQDTFFHLcKSFRDFKCSAFIGGTDVAKDRKRMNES-RVIIGTPGRLLHLYENRVFDVSKLRLLVLDEADQLYqTKSL 185
Cdd:cd18046 81 QQIQKVVMAL-GDYMGIKCHACIGGTSVRDDAQKLQAGpHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEML-SRGF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17647335 186 QHTVSKLIEAMPKNRQIIACSATYDQNLDERLAKVMDKPMLI 227
Cdd:cd18046 159 KDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
36-228 |
5.74e-34 |
|
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ribosomal subunits protein 1 homolog, and probable ATP-dependent RNA helicase DDX27) is involved in the processing of 5.8S and 28S ribosomal RNAs. More specifically, the encoded protein localizes to the nucleolus, where it interacts with the PeBoW complex to ensure proper 3' end formation of 47S rRNA. DDX27 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350705 [Multi-domain] Cd Length: 196 Bit Score: 129.30 E-value: 5.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 36 LLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQSFnpnINQP------HAMIVVPTRELAIQV 109
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERL---LYRPkkkaatRVLVLVPTRELAMQC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 110 QDTFFHLCKsFRDFKCSAFIGGTDVaKDRKRMNESR--VIIGTPGRLL-HLYENRVFDVSKLRLLVLDEADQLYQTkSLQ 186
Cdd:cd17947 78 FSVLQQLAQ-FTDITFALAVGGLSL-KAQEAALRARpdIVIATPGRLIdHLRNSPSFDLDSIEILVLDEADRMLEE-GFA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17647335 187 HTVSKLIEAMPKNRQIIACSATYDQNLDErLAKV-MDKPMLIS 228
Cdd:cd17947 155 DELKEILRLCPRTRQTMLFSATMTDEVKD-LAKLsLNKPVRVF 196
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
35-223 |
7.18e-34 |
|
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: 129.63 E-value: 7.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 35 NLLNGLKRNNFVTPTKIQAAAIPMALA-KMDLIIQSKSGTGKTLIYVIAVVQS-----FNPNINQPHAMIVVPTRELAIQ 108
Cdd:cd17964 4 SLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSllntkPAGRRSGVSALIISPTRELALQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 109 VQDTFFHLCKSFRDFKCSAFIGGTDVAKDRKRMNESR--VIIGTPGRLL-HLYENRVFDV-SKLRLLVLDEADQLYQ--- 181
Cdd:cd17964 84 IAAEAKKLLQGLRKLRVQSAVGGTSRRAELNRLRRGRpdILVATPGRLIdHLENPGVAKAfTDLDYLVLDEADRLLDmgf 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17647335 182 TKSLQHTVSKLIEAMPKNRQIIACSATYDQNLDERLAKVMDK 223
Cdd:cd17964 164 RPDLEQILRHLPEKNADPRQTLLFSATVPDEVQQIARLTLKK 205
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
36-223 |
7.05e-32 |
|
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: 124.66 E-value: 7.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 36 LLNGLKRNNFVTPTKIQAAAIPMALA-KMDLIIQSKSGTGKTLIYVIAVVQ------SFNPNINQ---PHAMIVVPTREL 105
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILErllsqkSSNGVGGKqkpLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 106 AIQVQDTFFHLCKsFRDFKCSAFIGGTDVAKDRKRMNES-RVIIGTPGRLLHLYENR---VFDVSKLRLLVLDEADQLYQ 181
Cdd:cd17946 81 AVQVKDHLKAIAK-YTNIKIASIVGGLAVQKQERLLKKRpEIVVATPGRLWELIQEGnehLANLKSLRFLVLDEADRMLE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17647335 182 TKSLQHtVSKLIEAMPKN-------RQIIACSATYDQNLDERLAKVMDK 223
Cdd:cd17946 160 KGHFAE-LEKILELLNKDragkkrkRQTFVFSATLTLDHQLPLKLNSKK 207
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
36-208 |
1.12e-31 |
|
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: 123.08 E-value: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 36 LLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQ------SFNPNINQPHAMIVVPTRELAIQV 109
Cdd:cd17961 5 LLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQkilkakAESGEEQGTRALILVPTRELAQQV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 110 QDTFFHLCKS-FRDFKCSAFIGG-TDVAKDRKRMNESRVIIGTPGRLL-HLYENRVFDVSKLRLLVLDEADqLYQTKSLQ 186
Cdd:cd17961 85 SKVLEQLTAYcRKDVRVVNLSASsSDSVQRALLAEKPDIVVSTPARLLsHLESGSLLLLSTLKYLVIDEAD-LVLSYGYE 163
|
170 180
....*....|....*....|..
gi 17647335 187 HTVSKLIEAMPKNRQIIACSAT 208
Cdd:cd17961 164 EDLKSLLSYLPKNYQTFLMSAT 185
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
27-225 |
5.75e-31 |
|
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: 120.89 E-value: 5.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 27 FEELRLYRNLLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQsfnpnINQphAMIVVPTRELA 106
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQ-----IVV--ALILEPSRELA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 107 IQVQDTFFHLCKSFRD--FKCSAFIGGTDV-AKDRKRMNESRVIIGTPGRLLHLYENRVFDVSKLRLLVLDEADQLYQTK 183
Cdd:cd17938 74 EQTYNCIENFKKYLDNpkLRVALLIGGVKArEQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17647335 184 SLQhTVSKLIEAMPK------NRQIIACSATYDQNLDERLA-KVMDKPM 225
Cdd:cd17938 154 NLE-TINRIYNRIPKitsdgkRLQVIVCSATLHSFEVKKLAdKIMHFPT 201
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
24-227 |
6.50e-31 |
|
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: 121.67 E-value: 6.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 24 VKTFEELRLYRNLLNGLKRNNFVTPTKIQAAAIPMALAK--MDLIIQSKSGTGKTLIYVIAVVQSFNPNINQPHAMIVVP 101
Cdd:cd18048 17 VKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLSP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 102 TRELAIQVQDTFFHLCKSFRDFKCSAFIGGTDVAKDRKRmnESRVIIGTPGRLLH-LYENRVFDVSKLRLLVLDEADQLY 180
Cdd:cd18048 97 TFELALQTGKVVEEMGKFCVGIQVIYAIRGNRPGKGTDI--EAQIVIGTPGTVLDwCFKLRLIDVTNISVFVLDEADVMI 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17647335 181 QTKSLQHTVSKLIEAMPKNRQIIACSATYDQNLDERLAKVMDKPMLI 227
Cdd:cd18048 175 NVQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNII 221
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
36-218 |
1.47e-30 |
|
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: 120.81 E-value: 1.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 36 LLNGLKRNNFVTPTKIQAAAIPMALA---------KMDLIIQSKSGTGKTLIYVIAVVQS-FNPNINQPHAMIVVPTREL 105
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPsskstppyrPGDLCVSAPTGSGKTLAYVLPIVQAlSKRVVPRLRALIVVPTKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 106 AIQVQDTFFHLCKSFrDFKCSAFIGGTDVAK-------DRKRMNESRV--IIGTPGRLL-HLYENRVFDVSKLRLLVLDE 175
Cdd:cd17956 81 VQQVYKVFESLCKGT-GLKVVSLSGQKSFKKeqklllvDTSGRYLSRVdiLVATPGRLVdHLNSTPGFTLKHLRFLVIDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17647335 176 ADQLYQtKSLQ---HTVSKLIEAMPKNR-----------------QIIACSATYDQNLdERLA 218
Cdd:cd17956 160 ADRLLN-QSFQdwlETVMKALGRPTAPDlgsfgdanllersvrplQKLLFSATLTRDP-EKLS 220
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
26-227 |
6.15e-30 |
|
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: 118.18 E-value: 6.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 26 TFEELRLYRNLLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQSFNPN--INQPHAMIVVPTR 103
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHspTVGARALILSPTR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 104 ELAIQVQDTFFHLCKsFRDFKCSAFIGGTDVAKDRKRMNES-RVIIGTPGRLLHLYENRVFDVSKLRLLVLDEADQLYQT 182
Cdd:cd17959 82 ELALQTLKVTKELGK-FTDLRTALLVGGDSLEEQFEALASNpDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17647335 183 kSLQHTVSKLIEAMPKNRQIIACSATYDQNLDErLAKVM-DKPMLI 227
Cdd:cd17959 161 -GFAEQLHEILSRLPENRQTLLFSATLPKLLVE-FAKAGlNEPVLI 204
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
259-367 |
1.80e-28 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 110.38 E-value: 1.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 259 KLQILGQIFNQLPYEQAIIFASSQMRADsYKNYLTASGIDCHLISGAMEQSERLHVFEGYRNFTMRILVATDLMARGVDS 338
Cdd:pfam00271 2 KLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDL 80
|
90 100
....*....|....*....|....*....
gi 17647335 339 PHANLVINIDPPQDHVTYLHRIGRAGRFG 367
Cdd:pfam00271 81 PDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
36-224 |
2.40e-28 |
|
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: 113.07 E-value: 2.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 36 LLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQSFNPNINQ--PHAMIVVPTRELAIQVQDTF 113
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKkgLRALILAPTRELASQIYREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 114 FHLCKSfRDFKCsAFIGGTDVAKDRKRMNESR---VIIGTPGRLLHLYENRVFDVSKLRLLVLDEADQLYQtKSLQHTVS 190
Cdd:cd17957 81 LKLSKG-TGLRI-VLLSKSLEAKAKDGPKSITkydILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFE-PGFREQTD 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 17647335 191 KLIEAMpKNRQIIAC--SATYDQNLDERLAKVMDKP 224
Cdd:cd17957 158 EILAAC-TNPNLQRSlfSATIPSEVEELARSVMKDP 192
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
36-228 |
5.10e-28 |
|
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: 112.26 E-value: 5.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 36 LLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQSFNPNINQPHAMIVVPTRELAIQVQDTFFH 115
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 116 LCKSFRDFKCSAFIGGTDVAKDRKRMNES-RVIIGTPGRLLHLYENRVFDVSKLRLLVLDEADQLYQtKSLQHTVSKLIE 194
Cdd:cd17962 81 LMKGLPPMKTALLVGGLPLPPQLYRLQQGvKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLK-MGFQQQVLDILE 159
|
170 180 190
....*....|....*....|....*....|....
gi 17647335 195 AMPKNRQIIACSATYDQNLDERLAKVMDKPMLIS 228
Cdd:cd17962 160 NISHDHQTILVSATIPRGIEQLAGQLLQNPVRIT 193
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
36-219 |
8.09e-28 |
|
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: 112.41 E-value: 8.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 36 LLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQSF-------NPNINQ-PHAMIVVPTRELAI 107
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYIsrlppldEETKDDgPYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 108 QVQDTFFHLCKsFRDFKCSAFIGGTDVAKDRKRMNES-RVIIGTPGRLLHLYENRVFDVSKLRLLVLDEADQLYQTkSLQ 186
Cdd:cd17945 81 QIEEETQKFAK-PLGIRVVSIVGGHSIEEQAFSLRNGcEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDM-GFE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17647335 187 HTVSKLIEAMP--------------------KNRQIIACSATYDQNLdERLAK 219
Cdd:cd17945 159 PQVTKILDAMPvsnkkpdteeaeklaasgkhRYRQTMMFTATMPPAV-EKIAK 210
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
25-227 |
1.71e-27 |
|
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: 110.97 E-value: 1.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 25 KTFEELRLYRNLLNGLKRNNFVTPTKIQAAAIPMALAK--MDLIIQSKSGTGKTLIYVIAVVQSFNPNINQPHAMIVVPT 102
Cdd:cd18047 1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 103 RELAIQVQDTFFHLCKSFRDFKCSAFIGGTDVakDRKRMNESRVIIGTPGRLLH-LYENRVFDVSKLRLLVLDEADQLYQ 181
Cdd:cd18047 81 YELALQTGKVIEQMGKFYPELKLAYAVRGNKL--ERGQKISEQIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADVMIA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17647335 182 TKSLQHTVSKLIEAMPKNRQIIACSATYDQNLDERLAKVMDKPMLI 227
Cdd:cd18047 159 TQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVI 204
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
26-177 |
2.78e-26 |
|
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: 107.96 E-value: 2.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 26 TFEELRLYRNLLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQSF---NPNIN-------QPH 95
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLledGPPSVgrgrrkaYPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 96 AMIVVPTRELAIQVQDtffHLCK-SFRDF-KCSAFIGGTDVAKDRKRMneSR---VIIGTPGRLLHLYENRVFDVSKLRL 170
Cdd:cd17967 81 ALILAPTRELAIQIYE---EARKfSYRSGvRSVVVYGGADVVHQQLQL--LRgcdILVATPGRLVDFIERGRISLSSIKF 155
|
....*..
gi 17647335 171 LVLDEAD 177
Cdd:cd17967 156 LVLDEAD 162
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
21-227 |
9.83e-26 |
|
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: 106.31 E-value: 9.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 21 PGQVKTFEELRLYRNLLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVV-----QSFNPNINQPH 95
Cdd:cd17953 8 PKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFrhikdQRPVKPGEGPI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 96 AMIVVPTRELAIQVqdtfFHLCKSFR---DFKCSAFIGGTDVAK---DRKRMNEsrVIIGTPGRL---LHLYENRVFDVS 166
Cdd:cd17953 88 GLIMAPTRELALQI----YVECKKFSkalGLRVVCVYGGSGISEqiaELKRGAE--IVVCTPGRMidiLTANNGRVTNLR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17647335 167 KLRLLVLDEADQLYQTkSLQHTVSKLIEAMPKNRQIIACSATYDQNLDERLAKVMDKPMLI 227
Cdd:cd17953 162 RVTYVVLDEADRMFDM-GFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
20-209 |
1.02e-25 |
|
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: 107.75 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 20 APGQVKTFEELRLYRNLLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQ----------SFNp 89
Cdd:cd18052 38 PPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTgmmkegltasSFS- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 90 NINQPHAMIVVPTRELAIQVqdtfFHLCKSFRDFKC---SAFIGGTDVA-KDRKRMNESRVIIGTPGRLLHLYENRVFDV 165
Cdd:cd18052 117 EVQEPQALIVAPTRELANQI----FLEARKFSYGTCirpVVVYGGVSVGhQIRQIEKGCHILVATPGRLLDFIGRGKISL 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 17647335 166 SKLRLLVLDEADQLYQTkSLQHTVSKLIEA--MP--KNRQIIACSATY 209
Cdd:cd18052 193 SKLKYLILDEADRMLDM-GFGPEIRKLVSEpgMPskEDRQTLMFSATF 239
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
36-228 |
4.52e-25 |
|
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: 103.65 E-value: 4.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 36 LLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVV-----QSFNPNINQPHAMIVVPTRELAIQVQ 110
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLvhimdQRELEKGEGPIAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 111 DTFFHLCKSFrDFKCSAFIGGTDVAKDRKRMNE-SRVIIGTPGRLLHLYENRVFDVSKLRLLVLDEADQLYQTkSLQHTV 189
Cdd:cd17952 81 LEAKKFGKAY-NLRVVAVYGGGSKWEQAKALQEgAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDM-GFEYQV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17647335 190 SKLIEAMPKNRQIIACSATYDQNLdERLAK-VMDKPMLIS 228
Cdd:cd17952 159 RSIVGHVRPDRQTLLFSATFKKKI-EQLARdILSDPIRVV 197
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
36-218 |
5.23e-25 |
|
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: 103.60 E-value: 5.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 36 LLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVI-AVVqsfnpNIN-QPH--------AMIVVPTREL 105
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLpAIV-----HINaQPPlergdgpiVLVLAPTREL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 106 AIQVQDTFFHLCKSFRdFKCSAFIGGTD---VAKDRKRMNEsrVIIGTPGRLLHLYENRVFDVSKLRLLVLDEADQLYQT 182
Cdd:cd17966 76 AQQIQQEANKFGGSSR-LRNTCVYGGAPkgpQIRDLRRGVE--ICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDM 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 17647335 183 kSLQHTVSKLIEAMPKNRQIIACSATYDQNLdERLA 218
Cdd:cd17966 153 -GFEPQIRKIVDQIRPDRQTLMWSATWPKEV-RRLA 186
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
21-209 |
1.40e-24 |
|
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: 103.55 E-value: 1.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 21 PGQVKTFEELRLYRNLLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVV-----QSFNPNINQPH 95
Cdd:cd18049 20 PKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIvhinhQPFLERGDGPI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 96 AMIVVPTRELAIQVQDTFFHLCKSFRdFKCSAFIGGTDVA---KDRKRMNEsrVIIGTPGRLLHLYENRVFDVSKLRLLV 172
Cdd:cd18049 100 CLVLAPTRELAQQVQQVAAEYGRACR-LKSTCIYGGAPKGpqiRDLERGVE--ICIATPGRLIDFLEAGKTNLRRCTYLV 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 17647335 173 LDEADQLYQTkSLQHTVSKLIEAMPKNRQIIACSATY 209
Cdd:cd18049 177 LDEADRMLDM-GFEPQIRKIVDQIRPDRQTLMWSATW 212
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
37-228 |
1.47e-24 |
|
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: 102.44 E-value: 1.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 37 LNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQ-----SFNPNiNQPHAMIVVPTRELAIQVQD 111
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIEllyklKFKPR-NGTGVIIISPTRELALQIYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 112 TFFHLCKsFRDFKCSAFIGG----TDVAKDRKRMNesrVIIGTPGRLL-HLYENRVFDVSKLRLLVLDEADQLYQTkSLQ 186
Cdd:cd17942 81 VAKELLK-YHSQTFGIVIGGanrkAEAEKLGKGVN---ILVATPGRLLdHLQNTKGFLYKNLQCLIIDEADRILEI-GFE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 17647335 187 HTVSKLIEAMPKNRQIIACSATYDQNLdERLAKV--MDKPMLIS 228
Cdd:cd17942 156 EEMRQIIKLLPKRRQTMLFSATQTRKV-EDLARIslKKKPLYVG 198
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
36-222 |
2.58e-23 |
|
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: 99.75 E-value: 2.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 36 LLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQ-----SFNPN--INQPHAMIVVPTRELAIQ 108
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQrllryKLLAEgpFNAPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 109 VQDTFFHLCKSFrDFKCSAFIGGTDVAKDRK-RMNESRVIIGTPGRLLHLYENRVFDVSKLRLLVLDEADQLYQ---TKS 184
Cdd:cd17948 81 IGSVAQSLTEGL-GLKVKVITGGRTKRQIRNpHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDdsfNEK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17647335 185 LQHTVSK---------LIEAMPKNRQIIACSATYDQNLDERLAKVMD 222
Cdd:cd17948 160 LSHFLRRfplasrrseNTDGLDPGTQLVLVSATMPSGVGEVLSKVID 206
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
36-227 |
1.62e-22 |
|
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: 96.64 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 36 LLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVV------QSFNPNINQ--PHAMIVVPTRELAI 107
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLImfaleqEKKLPFIKGegPYGLIVCPSRELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 108 QVQDTFFHLCKSFRD-----FKCSAFIGGTDVakdRKRMNESR----VIIGTPGRLLHLYENRVFDVSKLRLLVLDEADQ 178
Cdd:cd17951 81 QTHEVIEYYCKALQEggypqLRCLLCIGGMSV---KEQLEVIRkgvhIVVATPGRLMDMLNKKKINLDICRYLCLDEADR 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17647335 179 LYQTkSLQHTVSKLIEAMPKNRQIIACSATYDQNLDERLAKVMDKPMLI 227
Cdd:cd17951 158 MIDM-GFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
36-227 |
2.62e-22 |
|
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: 95.61 E-value: 2.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 36 LLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYV----IAVVQSFNPNI--NQPHAMIVVPTRELAIQV 109
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLlpgfIHLDLQPIPREqrNGPGVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 110 QDtffHLCK-SFRDFKCSAFIGGTDVAKDRKRMNES-RVIIGTPGRLLHLYENRVFDVSKLRLLVLDEADQLYQTKSLQH 187
Cdd:cd17958 81 EA---ECSKySYKGLKSVCVYGGGNRNEQIEDLSKGvDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQ 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 17647335 188 TVSKLIEAMPkNRQIIACSATYDQNLdERLA-KVMDKPMLI 227
Cdd:cd17958 158 IRKILLDIRP-DRQTIMTSATWPDGV-RRLAqSYLKDPMIV 196
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
286-367 |
4.91e-22 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 91.12 E-value: 4.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 286 DSYKNYLTASGIDCHLISGAMEQSERLHVFEGYRNFTMRILVATDLMARGVDSPHANLVINIDPPQDHVTYLHRIGRAGR 365
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 17647335 366 FG 367
Cdd:smart00490 81 AG 82
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
19-209 |
6.53e-21 |
|
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: 93.92 E-value: 6.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 19 VAPGQVKTFEELRLYRNLLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQSFN--PNINQ--- 93
Cdd:cd18050 56 GCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINhqPYLERgdg 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 94 PHAMIVVPTRELAIQVQDTFFHLCKSFRdFKCSAFIGGTDVA---KDRKRMNEsrVIIGTPGRLLHLYENRVFDVSKLRL 170
Cdd:cd18050 136 PICLVLAPTRELAQQVQQVADDYGKSSR-LKSTCIYGGAPKGpqiRDLERGVE--ICIATPGRLIDFLEAGKTNLRRCTY 212
|
170 180 190
....*....|....*....|....*....|....*....
gi 17647335 171 LVLDEADQLYQTkSLQHTVSKLIEAMPKNRQIIACSATY 209
Cdd:cd18050 213 LVLDEADRMLDM-GFEPQIRKIVDQIRPDRQTLMWSATW 250
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
72-490 |
2.27e-19 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 93.17 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 72 GTGKTLIYVIAVVQSFNPninqPHAMIVVPTRELAIQVQDTFfhlcksfrdfkcSAFIGGTDVAKDRKRmNESRVIIGTP 151
Cdd:COG1061 110 GTGKTVLALALAAELLRG----KRVLVLVPRRELLEQWAEEL------------RRFLGDPLAGGGKKD-SDAPITVATY 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 152 GRLLHLYENRVFDvSKLRLLVLDEAdQLYQTKSLQhtvsKLIEAMPKNRqIIACSAT------------------YDQNL 213
Cdd:COG1061 173 QSLARRAHLDELG-DRFGLVIIDEA-HHAGAPSYR----RILEAFPAAY-RLGLTATpfrsdgreillflfdgivYEYSL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 214 DE-----RLAKVMDKPMLISNSERATVLLGIRQFVYELPQQNNsveemRLKLQILGQIFNQLP-YEQAIIFASSQMRADS 287
Cdd:COG1061 246 KEaiedgYLAPPEYYGIRVDLTDERAEYDALSERLREALAADA-----ERKDKILRELLREHPdDRKTLVFCSSVDHAEA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 288 YKNYLTASGIDCHLISGAMEQSERLHVFEGYRNFTMRILVATDLMARGVDSPHANLVINIDPPQDHVTYLHRIGRAGR-F 366
Cdd:COG1061 321 LAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLRpA 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 367 GSKGIA--ITFIASKKEsqRFREMSKKIATAWSV-LEFPKEPMPNEFNFWDFEKYNFDYYIKEENPLQEMPMPIKENRSK 443
Cdd:COG1061 401 PGKEDAlvYDFVGNDVP--VLEELAKDLRDLAGYrVEFLDEEESEELALLIAVKPALEVKGELEEELLEELELLEDALLL 478
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 17647335 444 ENVDASSVDLENLQKDQDGKRRDPDKLPVALENVETQKELELENLPE 490
Cdd:COG1061 479 VLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLK 525
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
46-219 |
2.38e-18 |
|
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: 85.89 E-value: 2.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 46 VTPTKIQAAAIPmALAKMDLIIQSK-----------------SGTGKTLIYVIAVV---------------QSFNP--NI 91
Cdd:cd17965 29 IKPSPIQTLAIK-KLLKTLMRKVTKqtsneepklevfllaaeTGSGKTLAYLAPLLdylkrqeqepfeeaeEEYESakDT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 92 NQPHAMIVVPTRELAIQVQDTFFHLcKSFRDFKCSAFIGGTDVA-KDRKRMNESR--VIIGTPGRLLHLYENRVFDVSKL 168
Cdd:cd17965 108 GRPRSVILVPTHELVEQVYSVLKKL-SHTVKLGIKTFSSGFGPSyQRLQLAFKGRidILVTTPGKLASLAKSRPKILSRV 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17647335 169 RLLVLDEADQLYQTKSLQHTVSkLIEAMPKNRQIIACSATYDQNLDERLAK 219
Cdd:cd17965 187 THLVVDEADTLFDRSFLQDTTS-IIKRAPKLKHLILCSATIPKEFDKTLRK 236
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
63-208 |
5.99e-17 |
|
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: 78.60 E-value: 5.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 63 MDLIIQSKSGTGKTLIYVIAVVQSFNPNINQphAMIVVPTRELAIQVQdtffhlcKSFRDF-----KCSAFIGGTDVAKD 137
Cdd:cd00046 2 ENVLITAPTGSGKTLAALLAALLLLLKKGKK--VLVLVPTKALALQTA-------ERLRELfgpgiRVAVLVGGSSAEER 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17647335 138 RKRMN-ESRVIIGTPGRLLHLYE-NRVFDVSKLRLLVLDEADqLYQTKSLQHTVSKLIE--AMPKNRQIIACSAT 208
Cdd:cd00046 73 EKNKLgDADIIIATPDMLLNLLLrEDRLFLKDLKLIIVDEAH-ALLIDSRGALILDLAVrkAGLKNAQVILLSAT 146
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
51-180 |
6.14e-17 |
|
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: 80.28 E-value: 6.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 51 IQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQSFNPNINQ------PHAMIVVPTRELAIQVQDTFFHLCksfRDFK 124
Cdd:cd17944 16 IQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPrkrgraPKVLVLAPTRELANQVTKDFKDIT---RKLS 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 17647335 125 CSAFIGGTDVAKDRKRM-NESRVIIGTPGRLLHLYENRVFDVSKLRLLVLDEADQLY 180
Cdd:cd17944 93 VACFYGGTPYQQQIFAIrNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQML 149
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
20-209 |
1.35e-16 |
|
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: 80.47 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 20 APGQVKTFEELRLYRNLLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQS------FNPNINQ 93
Cdd:cd18051 16 CPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQiyeqgpGESLPSE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 94 ----------PHAMIVVPTRELAIQVQDTF--FHLCKSFRdfKCSAFiGGTDVAKDRKRMNES-RVIIGTPGRLLHLYEN 160
Cdd:cd18051 96 sgyygrrkqyPLALVLAPTRELASQIYDEArkFAYRSRVR--PCVVY-GGADIGQQMRDLERGcHLLVATPGRLVDMLER 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17647335 161 RVFDVSKLRLLVLDEADQLYQTkSLQHTVSKLIE--AMPK--NRQIIACSATY 209
Cdd:cd18051 173 GKIGLDYCKYLVLDEADRMLDM-GFEPQIRRIVEqdTMPPtgERQTLMFSATF 224
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
47-208 |
9.55e-12 |
|
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: 64.59 E-value: 9.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 47 TPTKIQAAAIPMALAKMD-LIIQSKSGTGKTLIYVIAVVQSFNPNINQphAMIVVPTRELAIQVQDTFFHLcksFRDF-- 123
Cdd:cd17921 1 LLNPIQREALRALYLSGDsVLVSAPTSSGKTLIAELAILRALATSGGK--AVYIAPTRALVNQKEADLRER---FGPLgk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 124 KCSAFIGgtDVAKDRKRMNESRVIIGTPGRL-LHLYENRVFDVSKLRLLVLDEADQLYQTK---SLQHTVSKLIeAMPKN 199
Cdd:cd17921 76 NVGLLTG--DPSVNKLLLAEADILVATPEKLdLLLRNGGERLIQDVRLVVVDEAHLIGDGErgvVLELLLSRLL-RINKN 152
|
....*....
gi 17647335 200 RQIIACSAT 208
Cdd:cd17921 153 ARFVGLSAT 161
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
3-378 |
1.32e-10 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 65.63 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 3 REIAHSLAGGEERSSDVA-----PGQVKTFEELR--LYRNLLNGLKRNNFVTPTKIQAAAIPMALAKMDLIIQSKSGTGK 75
Cdd:COG1205 5 EELLERLRASPRYGDQIVhvrtiPAREARYAPWPdwLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 76 TLIYVIAVVQSF--NPNinqPHAMIVVPTRELAiQVQDTFFH-LCKSF-RDFKCSAFIGGTDvAKDRKRM-NESRVIIGT 150
Cdd:COG1205 85 SLAYLLPVLEALleDPG---ATALYLYPTKALA-RDQLRRLReLAEALgLGVRVATYDGDTP-PEERRWIrEHPDIVLTN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 151 P-----GRLLHLYENRVFdVSKLRLLVLDEAdqlyqtkslqHT--------VSKLI-------EAMPKNRQIIACSATYD 210
Cdd:COG1205 160 PdmlhyGLLPHHTRWARF-FRNLRYVVIDEA----------HTyrgvfgshVANVLrrlrricRHYGSDPQFILASATIG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 211 qNLDERLAKVMDKPM-LISNSERATvllGIRQFV-YELPQQNNSVEemRLKLQILGQIFNQLPYE--QAIIFASSQMRAD 286
Cdd:COG1205 229 -NPAEHAERLTGRPVtVVDEDGSPR---GERTFVlWNPPLVDDGIR--RSALAEAARLLADLVREglRTLVFTRSRRGAE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 287 SYKNYL---TASGIDCHLIS---GAMEQSERLHVFEGYRNFTMRILVATDLMARGVDSPHANLVINIDPPQDHVTYLHRI 360
Cdd:COG1205 303 LLARYArraLREPDLADRVAayrAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQA 382
|
410
....*....|....*...
gi 17647335 361 GRAGRFGSKGIAItFIAS 378
Cdd:COG1205 383 GRAGRRGQDSLVV-LVAG 399
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
52-208 |
9.78e-10 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 58.75 E-value: 9.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 52 QAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQSFnpnINQPH--AMIVVPTRELAiqvQDTFFHL----CKSFRDFKC 125
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEAL---LRDPGsrALYLYPTKALA---QDQLRSLrellEQLGLGIRV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 126 SAFIGGTDvAKDRKRM--NESRVIIGTPgRLLHL------YENRVFdVSKLRLLVLDEAdqlyqtkslqHT--------V 189
Cdd:cd17923 79 ATYDGDTP-REERRAIirNPPRILLTNP-DMLHYallphhDRWARF-LRNLRYVVLDEA----------HTyrgvfgshV 145
|
170 180
....*....|....*....|....*.
gi 17647335 190 SKLIE------AMPKNR-QIIACSAT 208
Cdd:cd17923 146 ALLLRrlrrlcRRYGADpQFILTSAT 171
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
256-454 |
2.15e-09 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 61.67 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 256 MRLKLQILGQIFNQLPYEQAIIFASSQMRADSYKNYLTASGIDCHLISG--------AMEQSERLHVFEGYRNFTMRILV 327
Cdd:COG1111 337 LSKLREILKEQLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGqaskegdkGLTQKEQIEILERFRAGEFNVLV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 328 ATDLMARGVDSPHANLVINIDPPQDHVTYLHRIGRAGRFGSkGIAITFIA-----------SKKESQRFREMSKKIATAW 396
Cdd:COG1111 417 ATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGRKRE-GRVVVLIAkgtrdeayywsSRRKEKKMKSILKKLKKLL 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17647335 397 SVLEFPKEPMPNEFNFWDFEKYNFDyyiKEENPLQEMPMPIKENRSKENVDASSVDLE 454
Cdd:COG1111 496 DKQEKEKLKESAQATLDEFESIKEL---AEDEINEKDLDEIESSENGAHVDWREPVLL 550
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
323-376 |
1.42e-08 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 52.71 E-value: 1.42e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 17647335 323 MRILVATDLMARGVDSPHANLVINIDPPQDHVTYLHRIGRAGRFGSK-GIAITFI 376
Cdd:cd18785 23 LEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDeGEVILFV 77
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
52-387 |
3.03e-08 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 57.59 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 52 QAAAIPMALAKMDLIIQSKSGTGKTLIYVIAVVQSFNPNINqphAMIVVPTRELAIQVQDTFFHLcksfRDF--KCSAFI 129
Cdd:PRK01172 27 QRMAIEQLRKGENVIVSVPTAAGKTLIAYSAIYETFLAGLK---SIYIVPLRSLAMEKYEELSRL----RSLgmRVKISI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 130 GGTDVAKDRKRMNEsrVIIGTPGRLLHLYENRVFDVSKLRLLVLDEADQL---YQTKSLQhTVSKLIEAMPKNRQIIACS 206
Cdd:PRK01172 100 GDYDDPPDFIKRYD--VVILTSEKADSLIHHDPYIINDVGLIVADEIHIIgdeDRGPTLE-TVLSSARYVNPDARILALS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 207 ATYdQNLDErLAKVMDKPMLISNSERATVLLGI--RQFVYELPQQNNSVEEmrlkLQILGQIFNQlpYEQAIIFASSQMR 284
Cdd:PRK01172 177 ATV-SNANE-LAQWLNASLIKSNFRPVPLKLGIlyRKRLILDGYERSQVDI----NSLIKETVND--GGQVLVFVSSRKN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 285 ADSYKNYLT---------------ASGIDCHLIS----------GAMEQSERLHVFEGYRNFTMRILVATDLMARGVDSP 339
Cdd:PRK01172 249 AEDYAEMLIqhfpefndfkvssenNNVYDDSLNEmlphgvafhhAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLP 328
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 17647335 340 hANLVINIDPPQ---DHVTYL------HRIGRAGR--FGSKGIAITFIASKKESQRFRE 387
Cdd:PRK01172 329 -ARLVIVRDITRygnGGIRYLsnmeikQMIGRAGRpgYDQYGIGYIYAASPASYDAAKK 386
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
167-375 |
1.46e-06 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 52.07 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 167 KLRLLVLDEAdqlyqtkslqHTVS--------------KLIEAMPkNRQIIACSATYD--------QNLDERLAKVmdkp 224
Cdd:COG0514 131 KISLFAIDEA----------HCISqwghdfrpdyrrlgELRERLP-NVPVLALTATATprvradiaEQLGLEDPRV---- 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 225 mLISNSERATVLLGIRqfvyELPQQNnsveemRLKlQILGQIfNQLPYEQAIIFASSQMRADSYKNYLTASGIDCHLISG 304
Cdd:COG0514 196 -FVGSFDRPNLRLEVV----PKPPDD------KLA-QLLDFL-KEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHA 262
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17647335 305 AMEQSERLHVFEGYRNFTMRILVATDL--MarGVDSPHANLVINIDPPQDHVTYLHRIGRAGRFGSKGIAITF 375
Cdd:COG0514 263 GLDAEEREANQDRFLRDEVDVIVATIAfgM--GIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLL 333
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
52-208 |
3.28e-06 |
|
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: 48.48 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 52 QAAAIPMALAKMD-LIIQSKSGTGKTLIYVIAVVQSFnpnINQPHAMIVVPTRELAIQVQDTFfhlcKSFRD--FKCSAF 128
Cdd:cd18028 6 QAEAVRAGLLKGEnLLISIPTASGKTLIAEMAMVNTL---LEGGKALYLVPLRALASEKYEEF----KKLEEigLKVGIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 129 IGgtDVAKDRKRMNESRVIIGTPGRLLHLYENRVFDVSKLRLLVLDE---ADQLYQTKSLQHTVSKLiEAMPKNRQIIAC 205
Cdd:cd18028 79 TG--DYDEDDEWLGDYDIIVATYEKFDSLLRHSPSWLRDVGVVVVDEihlISDEERGPTLESIVARL-RRLNPNTQIIGL 155
|
...
gi 17647335 206 SAT 208
Cdd:cd18028 156 SAT 158
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
251-375 |
3.30e-06 |
|
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: 47.59 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 251 NSVEEMRLKLQILGQIFNQLPYEQ---AIIFASSQMRADSYKNYLTASGIDCHLISGAMEQSERLHVFEGYRNFTMRILV 327
Cdd:cd18794 6 YSVRPKDKKDEKLDLLKRIKVEHLggsGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIV 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 17647335 328 ATDLMARGVDSPHANLVINIDPPQDHVTYLHRIGRAGRFGSKGIAITF 375
Cdd:cd18794 86 ATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILF 133
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
47-175 |
3.81e-06 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 48.57 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 47 TPTKIQAAAIpMALAK-------MDLIIQSKSGTGKTLIYVIAVVQSFNpniNQPHAMIVVPTRELAIQVQDTFFhlcKS 119
Cdd:cd17918 15 SLTKDQAQAI-KDIEKdlhspepMDRLLSGDVGSGKTLVALGAALLAYK---NGKQVAILVPTEILAHQHYEEAR---KF 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 17647335 120 FRDFKCSAFIGGTDvAKDRKRMNesrVIIGTPGrLLHLYENRvfdvSKLRLLVLDE 175
Cdd:cd17918 88 LPFINVELVTGGTK-AQILSGIS---LLVGTHA-LLHLDVKF----KNLDLVIVDE 134
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
72-176 |
1.22e-05 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 47.26 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 72 GTGKTLIYVI---AVVQSFNPNINqPHAMIV--VPTRELAIQvQDTFFhlcKSFRDFKCSAFIGGTDVAKDRKR-----M 141
Cdd:cd18034 26 GSGKTLIAVMlikEMGELNRKEKN-PKKRAVflVPTVPLVAQ-QAEAI---RSHTDLKVGEYSGEMGVDKWTKErwkeeL 100
|
90 100 110
....*....|....*....|....*....|....*
gi 17647335 142 NESRVIIGTPGRLLHLYENRVFDVSKLRLLVLDEA 176
Cdd:cd18034 101 EKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
66-176 |
7.59e-05 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 44.20 E-value: 7.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 66 IIQSKSGTGKTLIYvIAVVQSFNPNINQPHAMIVVPTRELAIQVQDTFfhlcKSFRDFKCSA--FIGGTdvaKDRKRMNE 143
Cdd:pfam04851 27 LIVMATGSGKTLTA-AKLIARLFKKGPIKKVLFLVPRKDLLEQALEEF----KKFLPNYVEIgeIISGD---KKDESVDD 98
|
90 100 110
....*....|....*....|....*....|....*.
gi 17647335 144 SRVIIGTP---GRLLHLYENRvFDVSKLRLLVLDEA 176
Cdd:pfam04851 99 NKIVVTTIqslYKALELASLE-LLPDFFDVIIIDEA 133
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
271-376 |
1.07e-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: 43.70 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 271 PYEQAIIFASSQMRADSYKNYLtaSGIDCHliSGAMEQSERLHVFEGYRNFTMRILVATDLMARGVDSPhANLVI----N 346
Cdd:cd18795 42 EGKPVLVFCSSRKECEKTAKDL--AGIAFH--HAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLP-ARTVIikgtQ 116
|
90 100 110
....*....|....*....|....*....|....*..
gi 17647335 347 IDPPQDHV-----TYLHRIGRAGR--FGSKGIAITFI 376
Cdd:cd18795 117 RYDGKGYRelsplEYLQMIGRAGRpgFDTRGEAIIMT 153
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
259-369 |
1.58e-04 |
|
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: 42.85 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 259 KLQILGQIFNQL--PYEQAIIFasSQMRA--DSYKNYLTASGIDCHLISGAMEQSERLHVFEGYRNFT--MRILVATDLM 332
Cdd:cd18793 12 KLEALLELLEELrePGEKVLIF--SQFTDtlDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdiRVFLLSTKAG 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 17647335 333 ARGVDSPHANLVINIDPP-------QdhvtylhRIGRAGRFGSK 369
Cdd:cd18793 90 GVGLNLTAANRVILYDPWwnpaveeQ-------AIDRAHRIGQK 126
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
72-231 |
2.51e-04 |
|
DEAH-box helicase domain of FANCM; 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. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM 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: 350791 [Multi-domain] Cd Length: 182 Bit Score: 43.08 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 72 GTGKTLIyviAVVQSFNPNINQPHAMIV--VPTRELAIQvQdtfFHLCKSFRDFKCSA---FIGGTDVAKDRKRMNESRV 146
Cdd:cd18033 26 GLGKTFI---AAVVMLNYYRWFPKGKIVfmAPTKPLVSQ-Q---IEACYKITGIPSSQtaeLTGSVPPTKRAELWASKRV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 147 IIGTPGRLLHLYENRVFDVSKLRLLVLDEADQlyQTKSLQHT-VSKLIEAMPKNRQIIACSATYDQNLdERLAKVMDKpM 225
Cdd:cd18033 99 FFLTPQTLENDLKEGDCDPKSIVCLVIDEAHR--ATGNYAYCqVVRELMRYNSHFRILALTATPGSKL-EAVQQVIDN-L 174
|
....*.
gi 17647335 226 LISNSE 231
Cdd:cd18033 175 LISHIE 180
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
240-347 |
8.17e-04 |
|
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350176 [Multi-domain] Cd Length: 153 Bit Score: 41.08 E-value: 8.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 240 RQFVYELPQQNNSVEEMRL------KLQILGQIFNQL-PYEQAIIFAssqmrADSYKNYLTASGIDCHLISGAMEQSERL 312
Cdd:cd18789 10 PEFYREYLGLGAHRKRRLLaamnpnKLRALEELLKRHeQGDKIIVFT-----DNVEALYRYAKRLLKPFITGETPQSERE 84
|
90 100 110
....*....|....*....|....*....|....*
gi 17647335 313 HVFEGYRNFTMRILVATDLMARGVDSPHANLVINI 347
Cdd:cd18789 85 EILQNFREGEYNTLVVSKVGDEGIDLPEANVAIQI 119
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
276-375 |
8.42e-04 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 43.16 E-value: 8.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 276 IIFASSQMRADSYKNYLTASGIDCHLISGAMEQSERLHVFEGYRNFTMRILVATDLMARGVDSPHANLVINIDPPQDHVT 355
Cdd:PRK11057 240 IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIES 319
|
90 100
....*....|....*....|
gi 17647335 356 YLHRIGRAGRFGSKGIAITF 375
Cdd:PRK11057 320 YYQETGRAGRDGLPAEAMLF 339
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
301-365 |
1.11e-03 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 40.79 E-value: 1.11e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17647335 301 LISGAMEQSERLHVFEGYRNFTMRILVATDLMARGVDSPHANLVINIDPPQDHVTYLHRI-GRAGR 365
Cdd:cd18811 66 LLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLHQLrGRVGR 131
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
306-369 |
1.66e-03 |
|
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: 39.88 E-value: 1.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17647335 306 MEQSERLHVFEGYRNFTMRILVATDLMARGVDSPHANLVINIDPPQDHVTYLHRIGRAGRFGSK 369
Cdd:cd18802 74 MTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPNSK 137
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| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
273-365 |
2.16e-03 |
|
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: 39.65 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 273 EQAIIFASSQMRADSYKNYLT--ASGIDCHLISG--------AMEQSERLHVFEGYRNFTMRILVATDLMARGVDSPHAN 342
Cdd:cd18801 31 TRVIIFSEFRDSAEEIVNFLSkiRPGIRATRFIGqasgksskGMSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVD 110
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90 100
....*....|....*....|...
gi 17647335 343 LVINIDPPQDHVTYLHRIGRAGR 365
Cdd:cd18801 111 LIICYDASPSPIRMIQRMGRTGR 133
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| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
52-176 |
3.15e-03 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 39.81 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 52 QAAAIPMALAKMDLIIQSkSGTGKTLIYVIavVQSFNPNINQPHAMIVVPTRELAIQVQDTFFHLCKSfrDFKCSAFIGG 131
Cdd:cd18035 7 QVLIAAVALNGNTLIVLP-TGLGKTIIAIL--VAADRLTKKGGKVLILAPSRPLVEQHAENLKRVLNI--PDKITSLTGE 81
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90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 17647335 132 TDVAKDRKRMNESRVIIGTPGRLLHLYENRVFDVSKLRLLVLDEA 176
Cdd:cd18035 82 VKPEERAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEA 126
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| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
272-365 |
5.01e-03 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350186 [Multi-domain] Cd Length: 116 Bit Score: 37.92 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647335 272 YEQAIIFASSQMRADSYKNYLTASGID-CHLISG-AMEQ--SERLHVFEgYRNFTMRILVATDLMARGVDSPHANLVINI 347
Cdd:cd18799 6 EIKTLIFCVSIEHAEFMAEAFNEAGIDaVALNSDySDRErgDEALILLF-FGELKPPILVTVDLLTTGVDIPEVDNVVFL 84
|
90
....*....|....*...
gi 17647335 348 DPPQDHVTYLHRIGRAGR 365
Cdd:cd18799 85 RPTESRTLFLQMLGRGLR 102
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