|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
145-544 |
6.68e-167 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 481.95 E-value: 6.68e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 145 TFADIDLGDALNENIRRCKYVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGIMKAPsAGRPQrgggmgmr 224
Cdd:COG0513 3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSR-PRAPQ-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 225 taypsALILSPTRELSMQIHEEARKFSYQTGVRVVVAYGGAPITQQLRELERGVDILVATPGRLVDLLERARVSLQSIRY 304
Cdd:COG0513 74 -----ALILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVET 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 305 LALDEADRMLDMGFEPQVRRIVEQmdmpLPGARQTMLFSATFPKEIQKMASDFLDNYIFLAVGRVGSSTDLIAQRVEFVQ 384
Cdd:COG0513 149 LVLDEADRMLDMGFIEDIERILKL----LPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 385 EADKRSHLMDLLHAQRDTgkqtLTLVFVETKRGADSLESWLCMNGFPATSIHGDRNQQEREYALRSFKSGQTPILVATDV 464
Cdd:COG0513 225 KRDKLELLRRLLRDEDPE----RAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 465 AARGLDIPHVAHVVNFDLPNDIDDYVHRIGRTGRAGKSGLATAFFNDNNSSLARSLADLMQES--NQEVPAWLLRYAARP 542
Cdd:COG0513 301 AARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKieEEELPGFEPVEEKRL 380
|
..
gi 1008909313 543 SY 544
Cdd:COG0513 381 ER 382
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
145-370 |
1.08e-155 |
|
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: 445.78 E-value: 1.08e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 145 TFADIDLGDALNENIRRCKYVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGIMKAPSAGRPQRGggmgmR 224
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGR-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 225 TAYPSALILSPTRELSMQIHEEARKFSYQTGVRVVVAYGGAPITQQLRELERGVDILVATPGRLVDLLERARVSLQSIRY 304
Cdd:cd17967 76 KAYPSALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1008909313 305 LALDEADRMLDMGFEPQVRRIVEQMDMPLPGARQTMLFSATFPKEIQKMASDFLDNYIFLAVGRVG 370
Cdd:cd17967 156 LVLDEADRMLDMGFEPQIRKIVEHPDMPPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVGRVG 221
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
124-371 |
2.81e-143 |
|
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: 415.21 E-value: 2.81e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 124 FDAYEDIPVEMSGRDIPPPVSTFADIDLGDALNENIRRCKYVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPII 203
Cdd:cd18051 1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 204 SGIMK-APSAGRPQRGGGMGMRTAYPSALILSPTRELSMQIHEEARKFSYQTGVRVVVAYGGAPITQQLRELERGVDILV 282
Cdd:cd18051 81 SQIYEqGPGESLPSESGYYGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 283 ATPGRLVDLLERARVSLQSIRYLALDEADRMLDMGFEPQVRRIVEQMDMPLPGARQTMLFSATFPKEIQKMASDFLDNYI 362
Cdd:cd18051 161 ATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFLDNYI 240
|
....*....
gi 1008909313 363 FLAVGRVGS 371
Cdd:cd18051 241 FLAVGRVGS 249
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
116-370 |
2.19e-136 |
|
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: 398.19 E-value: 2.19e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 116 EHQNTGINFDAYEDIPVEMSGRDIPPPVSTFADIDLGDALNENIRRCKYVRPTPVQRHAIPISLAGRDLMACAQTGSGKT 195
Cdd:cd18052 15 ATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 196 AALCFPIISGIMKAPSAGrPQRGGgmgmrTAYPSALILSPTRELSMQIHEEARKFSYQTGVRVVVAYGGAPITQQLRELE 275
Cdd:cd18052 95 AAFLLPVLTGMMKEGLTA-SSFSE-----VQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 276 RGVDILVATPGRLVDLLERARVSLQSIRYLALDEADRMLDMGFEPQVRRIVEQMDMPLPGARQTMLFSATFPKEIQKMAS 355
Cdd:cd18052 169 KGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQTLMFSATFPEEIQRLAA 248
|
250
....*....|....*.
gi 1008909313 356 DFL-DNYIFLAVGRVG 370
Cdd:cd18052 249 EFLkEDYLFLTVGRVG 264
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
112-544 |
4.23e-136 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 408.01 E-value: 4.23e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 112 VPFD-----EHQN-TGINFDAYEDIPVE-----MSGRDIPPPVSTFADIDLGDALNENIRRCKYVRPTPVQRHAIPISLA 180
Cdd:PTZ00110 87 VPFEknfykEHPEvSALSSKEVDEIRKEkeitiIAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALS 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 181 GRDLMACAQTGSGKTAALCFPIISGIMKAPSAgRPQRGggmgmrtayPSALILSPTRELSMQIHEEARKFSYQTGVRVVV 260
Cdd:PTZ00110 167 GRDMIGIAETGSGKTLAFLLPAIVHINAQPLL-RYGDG---------PIVLVLAPTRELAEQIREQCNKFGASSKIRNTV 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 261 AYGGAPITQQLRELERGVDILVATPGRLVDLLERARVSLQSIRYLALDEADRMLDMGFEPQVRRIVEQMDmplPGaRQTM 340
Cdd:PTZ00110 237 AYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIR---PD-RQTL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 341 LFSATFPKEIQKMASDFL-DNYIFLAVGrvgsSTDL-----IAQRVEFVQEADKRSHLMDLL-HAQRDTGKqtlTLVFVE 413
Cdd:PTZ00110 313 MWSATWPKEVQSLARDLCkEEPVHVNVG----SLDLtachnIKQEVFVVEEHEKRGKLKMLLqRIMRDGDK---ILIFVE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 414 TKRGADSLESWLCMNGFPATSIHGDRNQQEREYALRSFKSGQTPILVATDVAARGLDIPHVAHVVNFDLPNDIDDYVHRI 493
Cdd:PTZ00110 386 TKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRI 465
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1008909313 494 GRTGRAGKSGLATAFFNDNNSSLARSLADLMQESNQEVPAWLLRYAARPSY 544
Cdd:PTZ00110 466 GRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSNERSN 516
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
164-532 |
4.51e-100 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 312.13 E-value: 4.51e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 164 YVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGIMKAPSAG---RPQRgggmgmrtaypsALILSPTRELS 240
Cdd:PRK10590 21 YREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAkgrRPVR------------ALILTPTRELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 241 MQIHEEARKFSYQTGVRVVVAYGGAPITQQLRELERGVDILVATPGRLVDLLERARVSLQSIRYLALDEADRMLDMGFEP 320
Cdd:PRK10590 89 AQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFIH 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 321 QVRRIVEQmdmpLPGARQTMLFSATFPKEIQKMASDFLDNYIFLAVGRVGSSTDLIAQRVEFVQEADKRSHLMDLLhaQR 400
Cdd:PRK10590 169 DIRRVLAK----LPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQMI--GK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 401 DTGKQTLtlVFVETKRGADSLESWLCMNGFPATSIHGDRNQQEREYALRSFKSGQTPILVATDVAARGLDIPHVAHVVNF 480
Cdd:PRK10590 243 GNWQQVL--VFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNY 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1008909313 481 DLPNDIDDYVHRIGRTGRAGKSGLATAFFNDNNSSLARSLADLMQesnQEVP 532
Cdd:PRK10590 321 ELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLK---KEIP 369
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
144-525 |
1.32e-96 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 303.26 E-value: 1.32e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 144 STFADIDLGDALNENIRRCKYVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGImkAPSAGRPQrgggmgm 223
Cdd:PRK11776 4 TAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL--DVKRFRVQ------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 224 rtaypsALILSPTRELSMQIHEEARKFSYQT-GVRVVVAYGGAPITQQLRELERGVDILVATPGRLVDLLERARVSLQSI 302
Cdd:PRK11776 75 ------ALVLCPTRELADQVAKEIRRLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 303 RYLALDEADRMLDMGFEPQVRRIVEQMdmplPGARQTMLFSATFPKEIQKMASDFLDNYIFLAVGRVGSSTDlIAQRVEF 382
Cdd:PRK11776 149 NTLVLDEADRMLDMGFQDAIDAIIRQA----PARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPA-IEQRFYE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 383 VQEADKRSHLMDLL-HAQRDTgkqtlTLVFVETKRGADSLESWLCMNGFPATSIHGDRNQQEREYALRSFKSGQTPILVA 461
Cdd:PRK11776 224 VSPDERLPALQRLLlHHQPES-----CVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVA 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1008909313 462 TDVAARGLDIPHVAHVVNFDLPNDIDDYVHRIGRTGRAGKSGLATAFFNDNNSSLARSLADLMQ 525
Cdd:PRK11776 299 TDVAARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLG 362
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
155-364 |
1.16e-94 |
|
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: 288.57 E-value: 1.16e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 155 LNENIRRCKYVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGIMKAPSAGRPQrgggmgmrtayPSALILS 234
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRG-----------PQALVLA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 235 PTRELSMQIHEEARKFSYQTGVRVVVAYGGAPITQQLRELERGVDILVATPGRLVDLLERARVSLQSIRYLALDEADRML 314
Cdd:cd00268 70 PTRELAMQIAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRML 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1008909313 315 DMGFEPQVRRIVEQmdmpLPGARQTMLFSATFPKEIQKMASDFLDNYIFL 364
Cdd:cd00268 150 DMGFEEDVEKILSA----LPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
128-536 |
1.94e-94 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 299.40 E-value: 1.94e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 128 EDIPVEMSGRDIPPPVSTFADIDLGDALNENIRRCKYVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGIM 207
Cdd:PLN00206 105 RKLEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCC 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 208 KAPSAGRPQRGGgmgmrtayPSALILSPTRELSMQIHEEARKFSYQTGVRVVVAYGGAPITQQLRELERGVDILVATPGR 287
Cdd:PLN00206 185 TIRSGHPSEQRN--------PLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGR 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 288 LVDLLERARVSLQSIRYLALDEADRMLDMGFEPQVRRIVEQMDMPlpgarQTMLFSATFPKEIQKMASDFLDNYIFLAVG 367
Cdd:PLN00206 257 LIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQALSQP-----QVLLFSATVSPEVEKFASSLAKDIILISIG 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 368 RVGSSTDLIAQRVEFVQEADKRSHLMDLLHAQRDTgkQTLTLVFVETKRGADSL-ESWLCMNGFPATSIHGDRNQQEREY 446
Cdd:PLN00206 332 NPNRPNKAVKQLAIWVETKQKKQKLFDILKSKQHF--KPPAVVFVSSRLGADLLaNAITVVTGLKALSIHGEKSMKERRE 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 447 ALRSFKSGQTPILVATDVAARGLDIPHVAHVVNFDLPNDIDDYVHRIGRTGRAGKSGLATAFFNDNNSSLARSLADLMQE 526
Cdd:PLN00206 410 VMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKS 489
|
410
....*....|
gi 1008909313 527 SNQEVPAWLL 536
Cdd:PLN00206 490 SGAAIPRELA 499
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
145-508 |
8.69e-94 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 294.93 E-value: 8.69e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 145 TFADIDLGDALNENIRRCKYVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGIMKAPsagRPQRGggmgmr 224
Cdd:PRK11192 2 TFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFP---RRKSG------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 225 taYPSALILSPTRELSMQIHEEARKFSYQTGVRVVVAYGGAPITQQLRELERGVDILVATPGRLVDLLERARVSLQSIRY 304
Cdd:PRK11192 73 --PPRILILTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVET 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 305 LALDEADRMLDMGFEPQVRRIVEQMDmplpGARQTMLFSATFPKE-IQKMASDFLDNYIFLAVGRVGSSTDLIAQrveFV 383
Cdd:PRK11192 151 LILDEADRMLDMGFAQDIETIAAETR----WRKQTLLFSATLEGDaVQDFAERLLNDPVEVEAEPSRRERKKIHQ---WY 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 384 QEADKRSHLMDLL-H--AQRDTGKqtlTLVFVETKRGADSLESWLCMNGFPATSIHGDRNQQEREYALRSFKSGQTPILV 460
Cdd:PRK11192 224 YRADDLEHKTALLcHllKQPEVTR---SIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLV 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1008909313 461 ATDVAARGLDIPHVAHVVNFDLPNDIDDYVHRIGRTGRAGKSGLATAF 508
Cdd:PRK11192 301 ATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
131-514 |
8.26e-88 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 281.03 E-value: 8.26e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 131 PVEMSGRdipppvstFADIDLGDALNENIRRCKYVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGIMKAP 210
Cdd:PRK01297 82 PQEGKTR--------FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 211 sagrPQRGGGMGMrtayPSALILSPTRELSMQIHEEARKFSYQTGVRVVVAYGGAPITQQLRELE-RGVDILVATPGRLV 289
Cdd:PRK01297 154 ----PPKERYMGE----PRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 290 DLLERARVSLQSIRYLALDEADRMLDMGFEPQVRRIVEQMdmPLPGARQTMLFSATFPKEIQKMASDFLDNYIFLAVGRV 369
Cdd:PRK01297 226 DFNQRGEVHLDMVEVMVLDEADRMLDMGFIPQVRQIIRQT--PRKEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 370 GSSTDLIAQRVEFVQEADKRSHLMDLLhaqRDTGKQTLtLVFVETKRGADSLESWLCMNGFPATSIHGDRNQQEREYALR 449
Cdd:PRK01297 304 NVASDTVEQHVYAVAGSDKYKLLYNLV---TQNPWERV-MVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLE 379
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1008909313 450 SFKSGQTPILVATDVAARGLDIPHVAHVVNFDLPNDIDDYVHRIGRTGRAGKSGLATAFFNDNNS 514
Cdd:PRK01297 380 GFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDA 444
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
146-508 |
2.22e-84 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 270.30 E-value: 2.22e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 146 FADIDLG----DALNEN-IRRCkyvrpTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGIMKAPSAGrpqrggg 220
Cdd:PRK04837 10 FSDFALHpqvvEALEKKgFHNC-----TPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPE------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 221 mGMRTAYPSALILSPTRELSMQIHEEARKFSYQTGVRVVVAYGGAPITQQLRELERGVDILVATPGRLVDLLERARVSLQ 300
Cdd:PRK04837 78 -DRKVNQPRALIMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 301 SIRYLALDEADRMLDMGFEPQVRRIVEQmdMPLPGARQTMLFSATFPKEIQKMASDFLDNYIFLAVGRVGSSTDLIAQRV 380
Cdd:PRK04837 157 AIQVVVLDEADRMFDLGFIKDIRWLFRR--MPPANQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEEL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 381 EFVQEADKrshlMDLLhaqrdtgkQTL--------TLVFVETKRGADSLESWLCMNGFPATSIHGDRNQQEREYALRSFK 452
Cdd:PRK04837 235 FYPSNEEK----MRLL--------QTLieeewpdrAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFT 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1008909313 453 SGQTPILVATDVAARGLDIPHVAHVVNFDLPNDIDDYVHRIGRTGRAGKSGLATAF 508
Cdd:PRK04837 303 RGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
138-532 |
4.52e-81 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 266.05 E-value: 4.52e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 138 DIPPPVSTFADIDLGDALNENIRRCKYVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGIMKAPSAG--RP 215
Cdd:PRK04537 3 DKPLTDLTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALAdrKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 216 QRgggmgmrtayPSALILSPTRELSMQIHEEARKFSYQTGVRVVVAYGGAPITQQLRELERGVDILVATPGRLVDLLERA 295
Cdd:PRK04537 83 ED----------PRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 296 RV-SLQSIRYLALDEADRMLDMGFEPQVRRIVEQMdmPLPGARQTMLFSATFPKEIQKMASDFLDNYIFLAVGRVGSSTD 374
Cdd:PRK04537 153 KVvSLHACEICVLDEADRMFDLGFIKDIRFLLRRM--PERGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 375 LIAQRVEFVQEADKRSHLMDLLhaQRDTGKQTLtlVFVETKRGADSLESWLCMNGFPATSIHGDRNQQEREYALRSFKSG 454
Cdd:PRK04537 231 RVRQRIYFPADEEKQTLLLGLL--SRSEGARTM--VFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKG 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1008909313 455 QTPILVATDVAARGLDIPHVAHVVNFDLPNDIDDYVHRIGRTGRAGKSGLATAFFNDNnssLARSLADLMQESNQEVP 532
Cdd:PRK04537 307 QLEILVATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACER---YAMSLPDIEAYIEQKIP 381
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
144-531 |
1.99e-76 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 255.16 E-value: 1.99e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 144 STFADIDLGDALNENIRRCKYVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGImkAPSAGRPQrgggmgm 223
Cdd:PRK11634 6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNL--DPELKAPQ------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 224 rtaypsALILSPTRELSMQIHEEARKFS-YQTGVRVVVAYGGAPITQQLRELERGVDILVATPGRLVDLLERARVSLQSI 302
Cdd:PRK11634 77 ------ILVLAPTRELAVQVAEAMTDFSkHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 303 RYLALDEADRMLDMGFEPQVRRIVEQmdmpLPGARQTMLFSATFPKEIQKMASDFLDNYIFLavgRVGSSTDL---IAQR 379
Cdd:PRK11634 151 SGLVLDEADEMLRMGFIEDVETIMAQ----IPEGHQTALFSATMPEAIRRITRRFMKEPQEV---RIQSSVTTrpdISQS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 380 VEFVQEADKRSHLMDLLHAQRDTGkqtlTLVFVETKRGADSLESWLCMNGFPATSIHGDRNQQEREYALRSFKSGQTPIL 459
Cdd:PRK11634 224 YWTVWGMRKNEALVRFLEAEDFDA----AIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDIL 299
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1008909313 460 VATDVAARGLDIPHVAHVVNFDLPNDIDDYVHRIGRTGRAGKSGLATAFFNDNNSSLARSLADLMQESNQEV 531
Cdd:PRK11634 300 IATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEV 371
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
157-364 |
1.32e-75 |
|
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: 239.19 E-value: 1.32e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 157 ENIRRCKYVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGIMKAPsagRPQRGGGmgmrtayPSALILSPT 236
Cdd:cd17966 3 DELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQP---PLERGDG-------PIVLVLAPT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 237 RELSMQIHEEARKFSYQTGVRVVVAYGGAPITQQLRELERGVDILVATPGRLVDLLERARVSLQSIRYLALDEADRMLDM 316
Cdd:cd17966 73 RELAQQIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDM 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1008909313 317 GFEPQVRRIVEQMDmplPGaRQTMLFSATFPKEIQKMASDFLDNYIFL 364
Cdd:cd17966 153 GFEPQIRKIVDQIR---PD-RQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
135-362 |
2.37e-71 |
|
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: 229.19 E-value: 2.37e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 135 SGRDIPPPVSTFADIDLGDALNENIRRCKYVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGIMKAPSagr 214
Cdd:cd17953 3 RGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRP--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 215 PQRGGGmgmrtayPSALILSPTRELSMQIHEEARKFSYQTGVRVVVAYGGAPITQQLRELERGVDILVATPGRLVDLL-- 292
Cdd:cd17953 80 VKPGEG-------PIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILta 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1008909313 293 ERARV-SLQSIRYLALDEADRMLDMGFEPQVRRIVEQM--DmplpgaRQTMLFSATFPKEIQKMASDFLDNYI 362
Cdd:cd17953 153 NNGRVtNLRRVTYVVLDEADRMFDMGFEPQIMKIVNNIrpD------RQTVLFSATFPRKVEALARKVLHKPI 219
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
159-364 |
5.15e-68 |
|
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and PRP28 homolog) is involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation. Diseases associated with DDX23 include distal hereditary motor neuropathy, type II. DDX23 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350703 [Multi-domain] Cd Length: 220 Bit Score: 220.27 E-value: 5.15e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 159 IRRCKYVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGIMKAPSagRPQRGGGMGmrtayPSALILSPTRE 238
Cdd:cd17945 5 IRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPP--LDEETKDDG-----PYALILAPTRE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 239 LSMQIHEEARKFSYQTGVRVVVAYGGAPITQQLRELERGVDILVATPGRLVDLLERARVSLQSIRYLALDEADRMLDMGF 318
Cdd:cd17945 78 LAQQIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1008909313 319 EPQVRRIVEQMDMPLPG----------------ARQTMLFSATFPKEIQKMASDFLDNYIFL 364
Cdd:cd17945 158 EPQVTKILDAMPVSNKKpdteeaeklaasgkhrYRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
132-367 |
6.33e-67 |
|
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: 217.95 E-value: 6.33e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 132 VEMSGRDIPPPVSTFADIDLGDALNENIRRCKYVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGIMKAPS 211
Cdd:cd18049 12 ITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 212 AgrpQRGGGmgmrtayPSALILSPTRELSMQIHEEARKFSYQTGVRVVVAYGGAPITQQLRELERGVDILVATPGRLVDL 291
Cdd:cd18049 92 L---ERGDG-------PICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDF 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1008909313 292 LERARVSLQSIRYLALDEADRMLDMGFEPQVRRIVEQMDmplPGaRQTMLFSATFPKEIQKMASDFLDNYIFLAVG 367
Cdd:cd18049 162 LEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIR---PD-RQTLMWSATWPKEVRQLAEDFLKDYIHINIG 233
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
155-362 |
1.78e-66 |
|
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: 215.36 E-value: 1.78e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 155 LNENIRRCKYVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGIMKAPSAgrpQRGGGmgmrtayPSALILS 234
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQREL---EKGEG-------PIAVIVA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 235 PTRELSMQIHEEARKFSYQTGVRVVVAYGGAPITQQLRELERGVDILVATPGRLVDLLERARVSLQSIRYLALDEADRML 314
Cdd:cd17952 71 PTRELAQQIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMF 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1008909313 315 DMGFEPQVRRIVEQMDmplPGaRQTMLFSATFPKEIQKMASDFLDNYI 362
Cdd:cd17952 151 DMGFEYQVRSIVGHVR---PD-RQTLLFSATFKKKIEQLARDILSDPI 194
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
164-360 |
3.83e-63 |
|
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: 206.72 E-value: 3.83e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 164 YVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGIMKAPSAGRPQRgggmgmrtaypsALILSPTRELSMQI 243
Cdd:cd17947 10 FTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAATR------------VLVLVPTRELAMQC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 244 HEEARKFSYQTGVRVVVAYGGAPITQQLRELERGVDILVATPGRLVDLLERAR-VSLQSIRYLALDEADRMLDMGFEPQV 322
Cdd:cd17947 78 FSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGFADEL 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 1008909313 323 RRIVEQmdmpLPGARQTMLFSATFPKEIQKMASDFLDN 360
Cdd:cd17947 158 KEILRL----CPRTRQTMLFSATMTDEVKDLAKLSLNK 191
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
155-367 |
6.95e-62 |
|
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: 203.20 E-value: 6.95e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 155 LNENIRRCKYVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGImkapsaGRPQRGGGmgmrtayPSALILS 234
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKL------GKPRKKKG-------LRALILA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 235 PTRELSMQIHEEARKFSYQTGVRVVV-AYGGAPITQQLRELERGVDILVATPGRLVDLLERARVSLQSIRYLALDEADRM 313
Cdd:cd17957 68 PTRELASQIYRELLKLSKGTGLRIVLlSKSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1008909313 314 LDMGFEPQVRRIVEQMDMPLpgaRQTMLFSATFPKEIQKMASDFLDNYIFLAVG 367
Cdd:cd17957 148 FEPGFREQTDEILAACTNPN---LQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
168-352 |
3.22e-61 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 200.55 E-value: 3.22e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 168 TPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGIMKAPSAGRpqrgggmgmrtaypsALILSPTRELSMQIHEEA 247
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQ---------------ALVLAPTRELAEQIYEEL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 248 RKFSYQTGVRVVVAYGGAPITQQLRELeRGVDILVATPGRLVDLLERaRVSLQSIRYLALDEADRMLDMGFEPQVRRIVE 327
Cdd:pfam00270 66 KKLGKGLGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQE-RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILR 143
|
170 180
....*....|....*....|....*
gi 1008909313 328 QmdmpLPGARQTMLFSATFPKEIQK 352
Cdd:pfam00270 144 R----LPKKRQILLLSATLPRNLED 164
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
132-367 |
1.65e-60 |
|
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: 202.55 E-value: 1.65e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 132 VEMSGRDIPPPVSTFADIDLGDALNENIRRCKYVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGIMKAPS 211
Cdd:cd18050 50 ITIRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPY 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 212 AgrpQRGGGmgmrtayPSALILSPTRELSMQIHEEARKFSYQTGVRVVVAYGGAPITQQLRELERGVDILVATPGRLVDL 291
Cdd:cd18050 130 L---ERGDG-------PICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDF 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1008909313 292 LERARVSLQSIRYLALDEADRMLDMGFEPQVRRIVEQMDmplpGARQTMLFSATFPKEIQKMASDFLDNYIFLAVG 367
Cdd:cd18050 200 LEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIR----PDRQTLMWSATWPKEVRQLAEDFLRDYVQINIG 271
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
143-538 |
5.46e-60 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 205.06 E-value: 5.46e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 143 VSTFADIDLGDALNENIRRCKYVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAAlcFPIISGIMKAPSAGRPQrgggmg 222
Cdd:PTZ00424 27 VDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTAT--FVIAALQLIDYDLNACQ------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 223 mrtaypsALILSPTRELSMQIHEEARKFSYQTGVRVVVAYGGAPITQQLRELERGVDILVATPGRLVDLLERARVSLQSI 302
Cdd:PTZ00424 99 -------ALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 303 RYLALDEADRMLDMGFEPQVRRIVEQmdmpLPGARQTMLFSATFPKEIQKMASDFLDNYIFLAVGRVGSSTDLIAQrveF 382
Cdd:PTZ00424 172 KLFILDEADEMLSRGFKGQIYDVFKK----LPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQ---F 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 383 VQEADKRSHLMDLLHAQRDTGKQTLTLVFVETKRGADSLESWLCMNGFPATSIHGDRNQQEREYALRSFKSGQTPILVAT 462
Cdd:PTZ00424 245 YVAVEKEEWKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITT 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1008909313 463 DVAARGLDIPHVAHVVNFDLPNDIDDYVHRIGRTGRAGKSGLATAFFNDNNSSLARSLADLMQESNQEVPAWLLRY 538
Cdd:PTZ00424 325 DLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEVADY 400
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
376-509 |
7.75e-60 |
|
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: 195.42 E-value: 7.75e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 376 IAQRVEFVQEADKRSHLMDLLHAQRDTGKqtlTLVFVETKRGADSLESWLCMNGFPATSIHGDRNQQEREYALRSFKSGQ 455
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGK---AIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGK 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1008909313 456 TPILVATDVAARGLDIPHVAHVVNFDLPNDIDDYVHRIGRTGRAGKSGLATAFF 509
Cdd:cd18787 78 VRVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
159-355 |
7.85e-59 |
|
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: 195.88 E-value: 7.85e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 159 IRRCKYVRPTPVQRHAIPISLA-GRDLMACAQTGSGKTAALCFPIISGIMKAPSAGRPQRgggmgmrtayPSALILSPTR 237
Cdd:cd17964 9 LTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSG----------VSALIISPTR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 238 ELSMQIHEEARKF-SYQTGVRVVVAYGGAPITQQLRELER-GVDILVATPGRLVDLLE--RARVSLQSIRYLALDEADRM 313
Cdd:cd17964 79 ELALQIAAEAKKLlQGLRKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1008909313 314 LDMGFEPQVRRIVEQMDMPLPGARQTMLFSATFPKEIQKMAS 355
Cdd:cd17964 159 LDMGFRPDLEQILRHLPEKNADPRQTLLFSATVPDEVQQIAR 200
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
157-360 |
2.14e-57 |
|
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: 191.52 E-value: 2.14e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 157 ENIRRCKYVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGIMKAPSAgRPQRGGgmgmrtayPSALILSPT 236
Cdd:cd17958 3 KEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIP-REQRNG--------PGVLVLTPT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 237 RELSMQIHEEARKFSYQtGVRVVVAYGGAPITQQLRELERGVDILVATPGRLVDLLERARVSLQSIRYLALDEADRMLDM 316
Cdd:cd17958 74 RELALQIEAECSKYSYK-GLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDM 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1008909313 317 GFEPQVRRIVeqmdMPLPGARQTMLFSATFPKEIQKMASDFLDN 360
Cdd:cd17958 153 GFEPQIRKIL----LDIRPDRQTIMTSATWPDGVRRLAQSYLKD 192
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
146-363 |
5.27e-57 |
|
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: 190.51 E-value: 5.27e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 146 FADIDLGDALNENIRRCKYVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGIMKAPSAgrpqrgggmgmrt 225
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYG------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 226 ayPSALILSPTRELSMQIHEEARKFSYQTGVRVVVAYGGAPITQQLRELERGVDILVATPGRLVDLLE---RARVSLQSI 302
Cdd:cd17955 68 --IFALVLTPTRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1008909313 303 RYLALDEADRMLDMGFEPQVRRIVEQmdmpLPGARQTMLFSATFPKEIQKMASDFLDNYIF 363
Cdd:cd17955 146 KFLVLDEADRLLTGSFEDDLATILSA----LPPKRQTLLFSATLTDALKALKELFGNKPFF 202
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
144-364 |
1.12e-56 |
|
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: 189.82 E-value: 1.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 144 STFADIDLGDALNENIRRCKYVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGiMKAPSAGrpqrgggMGM 223
Cdd:cd17959 1 GGFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEK-LKAHSPT-------VGA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 224 RtaypsALILSPTRELSMQIHEEARKFSYQTGVRVVVAYGGAPITQQLRELERGVDILVATPGRLVDLLERARVSLQSIR 303
Cdd:cd17959 73 R-----ALILSPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVE 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1008909313 304 YLALDEADRMLDMGFEPQVRRIVEQmdmpLPGARQTMLFSATFPKEIQKMASDFLDNYIFL 364
Cdd:cd17959 148 YVVFDEADRLFEMGFAEQLHEILSR----LPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
145-353 |
4.62e-56 |
|
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can shuttle between the nucleus and the cytoplasm, and has an RNA-independent ATPase activity. DX47 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350712 [Multi-domain] Cd Length: 203 Bit Score: 188.29 E-value: 4.62e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 145 TFADIDLGDALNENIRRCKYVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGIMKAPSagrpqrgggmgmr 224
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQ------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 225 taYPSALILSPTRELSMQIHEEARKFSYQTGVRVVVAYGGAPITQQLRELERGVDILVATPGRLVDLLERAR-VSLQSIR 303
Cdd:cd17954 68 --RFFALVLAPTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLK 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1008909313 304 YLALDEADRMLDMGFEPQVRRIVEQmdmpLPGARQTMLFSATFPKEIQKM 353
Cdd:cd17954 146 FLVMDEADRLLNMDFEPEIDKILKV----IPRERTTYLFSATMTTKVAKL 191
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
159-368 |
2.28e-53 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 181.15 E-value: 2.28e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 159 IRRCKYVRPTPVQRHAIPISLAG-RDLMACAQTGSGKTAALCFPIISgimkapsagrpqrgggMGMRTAYPSALILSPTR 237
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALE----------------ALKRGKGGRVLVLVPTR 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 238 ELSMQIHEEARKFSYQTGVRVVVAYGGAPITQQLRELERGV-DILVATPGRLVDLLERARVSLQSIRYLALDEADRMLDM 316
Cdd:smart00487 65 ELAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1008909313 317 GFEPQVRRIVEQmdmpLPGARQTMLFSATFPKEIQKMASDFLDNYIFLAVGR 368
Cdd:smart00487 145 GFGDQLEKLLKL----LPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGF 192
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
163-354 |
4.00e-53 |
|
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: 180.61 E-value: 4.00e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 163 KYVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGI----MKAPSAgrpqRGGGmgmrtayPSALILSPTRE 238
Cdd:cd17951 9 GIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFAleqeKKLPFI----KGEG-------PYGLIVCPSRE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 239 LSMQIHEEARKFSYQ------TGVRVVVAYGGAPITQQLRELERGVDILVATPGRLVDLLERARVSLQSIRYLALDEADR 312
Cdd:cd17951 78 LARQTHEVIEYYCKAlqeggyPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADR 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1008909313 313 MLDMGFEPQVRRIVEQmdmpLPGARQTMLFSATFPKEIQKMA 354
Cdd:cd17951 158 MIDMGFEEDIRTIFSY----FKGQRQTLLFSATMPKKIQNFA 195
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
155-362 |
1.21e-49 |
|
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer development by promoting DNA replication. DDX59 knockdown mice showed reduced cell proliferation, anchorage-independent cell growth, and reduction of tumor formation. Recent work shows that EGFR and Ras regulate DDX59 during lung cancer development. Diseases associated with DDX59 (also called zinc finger HIT domain-containing protein 5) include orofaciodigital syndrome V and orofaciodigital syndrome. DDX59 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350720 [Multi-domain] Cd Length: 193 Bit Score: 170.81 E-value: 1.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 155 LNENIRRCKYVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGIMKAPSAgrpqrgggmgmrtayPSALILS 234
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRN---------------PSALILT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 235 PTRELSMQIHEEARKF-SYQTGVRVVVAYGGAPITQQLRELERGVDILVATPGRLVDLLERARVSLQSIRYLALDEADRM 313
Cdd:cd17962 66 PTRELAVQIEDQAKELmKGLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTM 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1008909313 314 LDMGFEPQVRRIVEQmdmpLPGARQTMLFSATFPKEIQKMASDFLDNYI 362
Cdd:cd17962 146 LKMGFQQQVLDILEN----ISHDHQTILVSATIPRGIEQLAGQLLQNPV 190
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
159-366 |
3.39e-49 |
|
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: 170.07 E-value: 3.39e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 159 IRRCKYVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGIMKAPSAGRPQRGggmgmrtayPSALILSPTRE 238
Cdd:cd17961 9 IAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGEEQG---------TRALILVPTRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 239 LSMQIHEEARKFSYQTG--VRVVVAYGGAPITQQLRELERGVDILVATPGRLVDLLERARVSLQS-IRYLALDEADRMLD 315
Cdd:cd17961 80 LAQQVSKVLEQLTAYCRkdVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLLStLKYLVIDEADLVLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1008909313 316 MGFEPQVRRIVEQmdmpLPGARQTMLFSATFPKEIQKMASDFLDNYIFLAV 366
Cdd:cd17961 160 YGYEEDLKSLLSY----LPKNYQTFLMSATLSEDVEALKKLVLHNPAILKL 206
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
146-360 |
1.95e-48 |
|
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or p54) participates in mRNA regulation mediated by miRNA-mediated silencing. It also plays a role in global and transcript-specific messenger RNA (mRNA) storage, translational repression, and decay. It is a member of the DEAD-box helicase family, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350698 [Multi-domain] Cd Length: 201 Bit Score: 167.86 E-value: 1.95e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 146 FADIDLGDALNENIRRCKYVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGImkAPSAGRPQrgggmgmrt 225
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKI--DPKKDVIQ--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 226 aypsALILSPTRELSMQIHEEARKFSYQTGVRVVVAYGGAPITQQLRELERGVDILVATPGRLVDLLERARVSLQSIRYL 305
Cdd:cd17940 70 ----ALILVPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1008909313 306 ALDEADRMLDMGFEPQVRRIVEQmdmpLPGARQTMLFSATFPKEIQKMASDFLDN 360
Cdd:cd17940 146 VLDEADKLLSQDFQPIIEKILNF----LPKERQILLFSATFPLTVKNFMDRHMHN 196
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
151-364 |
2.24e-48 |
|
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1. DDX31 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350707 [Multi-domain] Cd Length: 214 Bit Score: 168.15 E-value: 2.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 151 LGDALNENIrrcKYVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGIMKAPSagRPQRGGGmgmrtayPSA 230
Cdd:cd17949 1 LVSHLKSKM---GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEP--RVDRSDG-------TLA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 231 LILSPTRELSMQIHEEARK----FSYqtgvrVVVAY--GGAPITQQLRELERGVDILVATPGRLVDLLERARV-SLQSIR 303
Cdd:cd17949 69 LVLVPTRELALQIYEVLEKllkpFHW-----IVPGYliGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQSfDVSNLR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 304 YLALDEADRMLDMGFEPQVRRIVEQMD---------MPLPGARQTMLFSATFPKEIQKMASDFLDNYIFL 364
Cdd:cd17949 144 WLVLDEADRLLDMGFEKDITKILELLDdkrskaggeKSKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
159-366 |
3.39e-47 |
|
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin gene, NUP98, by inversion 11 (p15q22) chromosome translocation is found in the patients with de novo or therapy-related myeloid malignancies. Diseases associated with DDX10 (also known as DDX10-NUP98 Fusion Protein Type 2) include myelodysplastic syndrome and leukemia, acute myeloid. DDX10 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350699 [Multi-domain] Cd Length: 198 Bit Score: 164.39 E-value: 3.39e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 159 IRRCKYVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGIMkapsagRPQRGGGMGMrtaypSALILSPTRE 238
Cdd:cd17941 5 LKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLY------RERWTPEDGL-----GALIISPTRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 239 LSMQIHEEARKFSYQTGVRVVVAYGGAPITQqlrELER--GVDILVATPGRLVDLLERArVSLQS--IRYLALDEADRML 314
Cdd:cd17941 74 LAMQIFEVLRKVGKYHSFSAGLIIGGKDVKE---EKERinRMNILVCTPGRLLQHMDET-PGFDTsnLQMLVLDEADRIL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1008909313 315 DMGFEPQVRRIVEQmdmpLPGARQTMLFSATFPKEIQKMASDFLDNYIFLAV 366
Cdd:cd17941 150 DMGFKETLDAIVEN----LPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
167-360 |
1.96e-45 |
|
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350718 [Multi-domain] Cd Length: 202 Bit Score: 159.66 E-value: 1.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 167 PTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGIMKA-PSAGRPQRGggmgmrtaypsALILSPTRELSMQIHE 245
Cdd:cd17960 13 MTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRkANLKKGQVG-----------ALIISPTRELATQIYE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 246 EARKF--SYQTGVRVVVAYGGAPITQQLRELER-GVDILVATPGRLVDLLERA--RVSLQSIRYLALDEADRMLDMGFEP 320
Cdd:cd17960 82 VLQSFleHHLPKLKCQLLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLSRKadKVKVKSLEVLVLDEADRLLDLGFEA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1008909313 321 QVRRIVEQmdmpLPGARQTMLFSATFPKEIQKMASDFLDN 360
Cdd:cd17960 162 DLNRILSK----LPKQRRTGLFSATQTDAVEELIKAGLRN 197
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
159-351 |
4.18e-44 |
|
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: 157.02 E-value: 4.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 159 IRRCKYVRPTPVQRHAIPISLA-GRDLMACAQTGSGKTAALCFPIISGIMKAPS---AGRPQRgggmgmrtaYPSALILS 234
Cdd:cd17946 5 LADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLLSQKSsngVGGKQK---------PLRALILT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 235 PTRELSMQI--H-EEARKFsyqTGVRVVVAYGGAPITQQLRELERGVDILVATPGRLVDLLERAR---VSLQSIRYLALD 308
Cdd:cd17946 76 PTRELAVQVkdHlKAIAKY---TNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNehlANLKSLRFLVLD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1008909313 309 EADRMLDMG-FEpQVRRIVEQMDMPLPGA---RQTMLFSATFPKEIQ 351
Cdd:cd17946 153 EADRMLEKGhFA-ELEKILELLNKDRAGKkrkRQTFVFSATLTLDHQ 198
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
146-360 |
1.31e-43 |
|
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: 154.79 E-value: 1.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 146 FADIDLGDALNENIRRCKYVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGIMkapsagrpqrgggmgmrt 225
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIVV------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 226 aypsALILSPTRELSMQIHEEARKFS-YQTGVRVVVAY--GGAPITQQLRELERGVDILVATPGRLVDLLERARVSLQSI 302
Cdd:cd17938 63 ----ALILEPSRELAEQTYNCIENFKkYLDNPKLRVALliGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSV 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1008909313 303 RYLALDEADRMLDMGFEPQVRRIVEQmdMPLPGAR----QTMLFSATFPK-EIQKMASDFLDN 360
Cdd:cd17938 139 RFFVLDEADRLLSQGNLETINRIYNR--IPKITSDgkrlQVIVCSATLHSfEVKKLADKIMHF 199
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
159-354 |
7.26e-43 |
|
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: 152.51 E-value: 7.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 159 IRRCKYVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGIMKapSAGRPQRGGGmgmrtaypsALILSPTRE 238
Cdd:cd17942 5 IEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYK--LKFKPRNGTG---------VIIISPTRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 239 LSMQIHEEAR---KFSYQTGVRVVvayGGAPITQQLRELERGVDILVATPGRLVDLLERARVSL-QSIRYLALDEADRML 314
Cdd:cd17942 74 LALQIYGVAKellKYHSQTFGIVI---GGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLyKNLQCLIIDEADRIL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1008909313 315 DMGFEPQVRRIVEQmdmpLPGARQTMLFSATFPKEIQKMA 354
Cdd:cd17942 151 EIGFEEEMRQIIKL----LPKRRQTMLFSATQTRKVEDLA 186
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
157-363 |
2.33e-41 |
|
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, Component Of Gems 3, Gemin-3, and SMN-Interacting Protein) interacts directly with SMN (survival of motor neurons), the spinal muscular atrophy gene product, and may play a catalytic role in the function of the SMN complex on ribonucleoproteins. Diseases associated with DDX20 include spinal muscular atrophy and muscular atrophy. DDX20 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350701 [Multi-domain] Cd Length: 192 Bit Score: 148.18 E-value: 2.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 157 ENIRRCKYVRPTPVQRHAIPISLAGRDLMACAQTGSGKTaaLCFPIISGIMKAPSAGRPQrgggmgmrtaypsALILSPT 236
Cdd:cd17943 3 EGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKT--LVFVVIALESLDLERRHPQ-------------VLILAPT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 237 RELSMQIHEEARKF-SYQTGVRVVVAYGGAPITQQLRELeRGVDILVATPGRLVDLLERARVSLQSIRYLALDEADRMLD 315
Cdd:cd17943 68 REIAVQIHDVFKKIgKKLEGLKCEVFIGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLME 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1008909313 316 MGFEPQVRRIVEQmdmpLPGARQTMLFSATFPKEIQKMASDFLDNYIF 363
Cdd:cd17943 147 GSFQKDVNWIFSS----LPKNKQVIAFSATYPKNLDNLLARYMRKPVL 190
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
164-360 |
2.73e-38 |
|
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: 140.15 E-value: 2.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 164 YVRPTPVQRHAI-PISLaGRDLMACAQTGSGKTAalCFPIisgimkapsaGRPQRgggMGMRTAYPSALILSPTRELSMQ 242
Cdd:cd17939 17 FEKPSAIQQRAIvPIIK-GRDVIAQAQSGTGKTA--TFSI----------GALQR---IDTTVRETQALVLAPTRELAQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 243 IHEEARKFSYQTGVRVVVAYGGAPITQQLRELERGVDILVATPGRLVDLLERARVSLQSIRYLALDEADRMLDMGFEPQV 322
Cdd:cd17939 81 IQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQI 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 1008909313 323 RRIVeQMdmpLPGARQTMLFSATFPKEIQKMASDFLDN 360
Cdd:cd17939 161 YDIF-QF---LPPETQVVLFSATMPHEVLEVTKKFMRD 194
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
154-364 |
7.25e-37 |
|
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called DEAD box RNA helicase DEAD5) and DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH)) are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350721 [Multi-domain] Cd Length: 196 Bit Score: 136.17 E-value: 7.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 154 ALNENIRRCKYVRPTPVQRHAIPISLAG--RDLMACAQTGSGKTAALCfpiisgimkapsagrpqrgggMGM------RT 225
Cdd:cd17963 4 ELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFV---------------------LAMlsrvdpTL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 226 AYPSALILSPTRELSMQIHEEARKFSYQTGVRVVVA------YGGAPITQQlrelergvdILVATPGRLVDLLERARVSL 299
Cdd:cd17963 63 KSPQALCLAPTRELARQIGEVVEKMGKFTGVKVALAvpgndvPRGKKITAQ---------IVIGTPGTVLDWLKKRQLDL 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1008909313 300 QSIRYLALDEADRMLDM-GFEPQVRRIveqMDMpLPGARQTMLFSATFPKEIQKMASDFLDNYIFL 364
Cdd:cd17963 134 KKIKILVLDEADVMLDTqGHGDQSIRI---KRM-LPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
143-360 |
8.12e-37 |
|
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: 136.32 E-value: 8.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 143 VSTFADIDLGDALNENIRRCKYVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGIMKAPSAgrpqrgggmg 222
Cdd:cd17950 1 SSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 223 mrtayPSALILSPTRELSMQIHEEARKFS-YQTGVRVVVAYGGAPITQQLRELERGV-DILVATPGRLVDLLERARVSLQ 300
Cdd:cd17950 71 -----VSVLVICHTRELAFQISNEYERFSkYMPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLS 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1008909313 301 SIRYLALDEADRM---LDMgfepqvRRIVEQMDMPLPGARQTMLFSATFPKEIQKMASDFLDN 360
Cdd:cd17950 146 HVKHFVLDECDKMleqLDM------RRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQD 202
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
387-500 |
1.18e-35 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 129.64 E-value: 1.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 387 DKRSHLMDLLHAQRDtGKqtlTLVFVETKRGADsLESWLCMNGFPATSIHGDRNQQEREYALRSFKSGQTPILVATDVAA 466
Cdd:pfam00271 1 EKLEALLELLKKERG-GK---VLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAE 75
|
90 100 110
....*....|....*....|....*....|....
gi 1008909313 467 RGLDIPHVAHVVNFDLPNDIDDYVHRIGRTGRAG 500
Cdd:pfam00271 76 RGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
155-359 |
4.60e-35 |
|
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350706 [Multi-domain] Cd Length: 231 Bit Score: 132.11 E-value: 4.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 155 LNENIRRCKYVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGIMKAPSAgrpqrgggMGMRTAYPSALILS 234
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLL--------AEGPFNAPRGLVIT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 235 PTRELSMQIHEEARKFSYQTGVRVVVAYGGApITQQLRELERG-VDILVATPGRLVDLLERARVSLQSIRYLALDEADRM 313
Cdd:cd17948 73 PSRELAEQIGSVAQSLTEGLGLKVKVITGGR-TKRQIRNPHFEeVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1008909313 314 LDMGFEPQVRRIVEQ---------MDMPLPGARQTMLFSATFPKEIQKMASDFLD 359
Cdd:cd17948 152 LDDSFNEKLSHFLRRfplasrrseNTDGLDPGTQLVLVSATMPSGVGEVLSKVID 206
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
164-360 |
1.15e-34 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor 4A-III (EIF4AIII, also known as DDX48) is part of the exon junction complex (EJC) that plays a major role in posttranscriptional regulation of mRNA. EJC consists of four proteins (eIF4AIII, Barentsz [Btz], Mago, and Y14), mRNA, and ATP. DDX48 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350803 [Multi-domain] Cd Length: 201 Bit Score: 130.28 E-value: 1.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 164 YVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGImkAPSAGRPQrgggmgmrtaypsALILSPTRELSMQI 243
Cdd:cd18045 19 FEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCL--DIQVRETQ-------------ALILSPTRELAVQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 244 HEEARKFSYQTGVRVVVAYGGAPITQQLRELERGVDILVATPGRLVDLLERARVSLQSIRYLALDEADRMLDMGFEPQVR 323
Cdd:cd18045 84 QKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKEQIY 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 1008909313 324 RIVEQmdmpLPGARQTMLFSATFPKEIQKMASDFLDN 360
Cdd:cd18045 164 DVYRY----LPPATQVVLVSATLPQDILEMTNKFMTD 196
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
169-358 |
1.69e-33 |
|
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: 126.89 E-value: 1.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 169 PVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISgimkapsagRPQRGGGMGMRTAYPSALILSPTRELSMQIHEEAR 248
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIE---------KLQEDQQPRKRGRAPKVLVLAPTRELANQVTKDFK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 249 KFSYQtgVRVVVAYGGAPITQQLRELERGVDILVATPGRLVDLLERARVSLQSIRYLALDEADRMLDMGFEPQVRRIV-- 326
Cdd:cd17944 86 DITRK--LSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILsv 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 1008909313 327 ----EQMDMPlpgarQTMLFSATFPKEIQKMASDFL 358
Cdd:cd17944 164 sykkDSEDNP-----QTLLFSATCPDWVYNVAKKYM 194
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
155-353 |
1.28e-32 |
|
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: 125.44 E-value: 1.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 155 LNENIRRCKYVRPTPVQRHAIPISLAG---------RDLMACAQTGSGKTAALCFPIISGIMKAPSAgrpqrgggmgmRT 225
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKRVVP-----------RL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 226 aypSALILSPTRELSMQIHEEARKFSYQTGVRVVVAYGGAPI---TQQLRELERG-----VDILVATPGRLVD-LLERAR 296
Cdd:cd17956 70 ---RALIVVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFkkeQKLLLVDTSGrylsrVDILVATPGRLVDhLNSTPG 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 297 VSLQSIRYLALDEADRMLDMGFE---PQVRRIVEQMDMPLPGARQTMLFSATFPKEIQKM 353
Cdd:cd17956 147 FTLKHLRFLVIDEADRLLNQSFQdwlETVMKALGRPTAPDLGSFGDANLLERSVRPLQKL 206
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
146-362 |
5.95e-32 |
|
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: 122.55 E-value: 5.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 146 FADIDLGDALNENIRRCKYVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGImkAPSAGRPQrgggmgmrt 225
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQI--DTSLKATQ--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 226 aypsALILSPTRELSMQIHEEARKFSYQTGVRVVVAYGGAPITQQLRELERGVDILVATPGRLVDLLERARVSLQSIRYL 305
Cdd:cd18046 70 ----ALVLAPTRELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMF 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1008909313 306 ALDEADRMLDMGFEPQVRRIVEQmdmpLPGARQTMLFSATFPKEIQKMASDFLDNYI 362
Cdd:cd18046 146 VLDEADEMLSRGFKDQIYDIFQK----LPPDTQVVLLSATMPNDVLEVTTKFMRDPI 198
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
419-500 |
1.17e-29 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 111.92 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 419 DSLESWLCMNGFPATSIHGDRNQQEREYALRSFKSGQTPILVATDVAARGLDIPHVAHVVNFDLPNDIDDYVHRIGRTGR 498
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 1008909313 499 AG 500
Cdd:smart00490 81 AG 82
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
164-365 |
2.34e-28 |
|
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: 114.01 E-value: 2.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 164 YVRPTPVQRHAIPI---SLAGRD--------------LMAcAQTGSGKTAALCFPIISGIMK---APSAGRPQRGGGMGm 223
Cdd:cd17965 28 EIKPSPIQTLAIKKllkTLMRKVtkqtsneepklevfLLA-AETGSGKTLAYLAPLLDYLKRqeqEPFEEAEEEYESAK- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 224 RTAYPSALILSPTRELSMQIHEEARKFSYQTGVRV-VVAYGGAPITQQLRELERG-VDILVATPGRLVDLLERARVSLQS 301
Cdd:cd17965 106 DTGRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIkTFSSGFGPSYQRLQLAFKGrIDILVTTPGKLASLAKSRPKILSR 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1008909313 302 IRYLALDEADRMLDMGFEPQVRRIVEQMdmplPGARQTMLFSATFPKEIQKMASDFLDNYIFLA 365
Cdd:cd17965 186 VTHLVVDEADTLFDRSFLQDTTSIIKRA----PKLKHLILCSATIPKEFDKTLRKLFPDVVRIA 245
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
132-354 |
2.72e-23 |
|
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: 98.94 E-value: 2.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 132 VEMSGRDIPPP---VSTFADIDLGDALNENIRRCKYVRPTPVQRHAIPISLAG--RDLMACAQTGSGKTAALCFPIISGI 206
Cdd:cd18048 3 VEVLQRDPTSPlfsVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 207 mkapsagrpqrgggmGMRTAYPSALILSPTRELSMQ---IHEEARKFSyqTGVRVVVAYGGAPITQQLReLERgvDILVA 283
Cdd:cd18048 83 ---------------DALKLYPQCLCLSPTFELALQtgkVVEEMGKFC--VGIQVIYAIRGNRPGKGTD-IEA--QIVIG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1008909313 284 TPGRLVDLLERAR-VSLQSIRYLALDEADRMLDM-GFEPQVRRIVEQMdmplPGARQTMLFSATFPKEIQKMA 354
Cdd:cd18048 143 TPGTVLDWCFKLRlIDVTNISVFVLDEADVMINVqGHSDHSVRVKRSM----PKECQMLLFSATFEDSVWAFA 211
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
169-530 |
4.13e-17 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 84.42 E-value: 4.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 169 PVQRHAIPISLAGRDLMACAQTGSGKTaaLCFPIisgimkaPSAGRPqrgggmGMrtaypsALILSPTreLS-M--QIhE 245
Cdd:COG0514 20 PGQEEIIEAVLAGRDALVVMPTGGGKS--LCYQL-------PALLLP------GL------TLVVSPL--IAlMkdQV-D 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 246 EARkfsyQTGVRVVVAYGGAPITQQ---LRELERG-VDILVATPGRL-----VDLLERARVSLqsiryLALDEA------ 310
Cdd:COG0514 76 ALR----AAGIRAAFLNSSLSAEERrevLRALRAGeLKLLYVAPERLlnprfLELLRRLKISL-----FAIDEAhcisqw 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 311 --DrmldmgFEP---QVRRIVEQmdmpLPGaRQTMLFSATFPKEIQKmasDFLDN------YIFLavgrvgSSTDL--IA 377
Cdd:COG0514 147 ghD------FRPdyrRLGELRER----LPN-VPVLALTATATPRVRA---DIAEQlgledpRVFV------GSFDRpnLR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 378 QRVEFVQEADKRSHLMDLLHAQRD-TGkqtltLVFVETKRGADSLESWLCMNGFPATSIHGDRNQQEREYALRSFKSGQT 456
Cdd:COG0514 207 LEVVPKPPDDKLAQLLDFLKEHPGgSG-----IVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEV 281
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1008909313 457 PILVATdVA-ARGLDIPHVAHVVNFDLPNDIDDYVHRIGRTGRAGKSGLATAFFNDNNSSLARSLADLMQESNQE 530
Cdd:COG0514 282 DVIVAT-IAfGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEER 355
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
180-478 |
1.05e-16 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 83.54 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 180 AGRDLMACAQTGSGKTAalcfpIISGIMKAPSAGRPqrgggmgmrtaypsALILSPTRELSMQIHEEARKFsyqtgvrvv 259
Cdd:COG1061 99 GGGRGLVVAPTGTGKTV-----LALALAAELLRGKR--------------VLVLVPRRELLEQWAEELRRF--------- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 260 vaYGGAPITQQLRELERgvDILVATPGRLVDLLERARVSlQSIRYLALDEADRMLDMGFepqvRRIVEQMDmplpgARQT 339
Cdd:COG1061 151 --LGDPLAGGGKKDSDA--PITVATYQSLARRAHLDELG-DRFGLVIIDEAHHAGAPSY----RRILEAFP-----AAYR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 340 MLFSAT------FPKEIQK-------------MASDFLDNYIFLAVgrvgsSTDLIAQRVEFVQEADKRSHLMD------ 394
Cdd:COG1061 217 LGLTATpfrsdgREILLFLfdgivyeyslkeaIEDGYLAPPEYYGI-----RVDLTDERAEYDALSERLREALAadaerk 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 395 ---LLHAQRDTGKQTLTLVFVETKRGADSLESWLCMNGFPATSIHGDRNQQEREYALRSFKSGQTPILVATDVAARGLDI 471
Cdd:COG1061 292 dkiLRELLREHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDV 371
|
....*..
gi 1008909313 472 PHVAHVV 478
Cdd:COG1061 372 PRLDVAI 378
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
145-354 |
3.45e-16 |
|
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: 77.45 E-value: 3.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 145 TFADIDLGDALNENIRRCKYVRPTPVQRHAIPISLAG--RDLMACAQTGSGKTAALCFPIISGIMKApsagrpqrgggmg 222
Cdd:cd18047 2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPA------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 223 mrTAYPSALILSPTRELSMQ---IHEEARKFSYQtgvrVVVAYGgapitQQLRELERGV----DILVATPGRLVDLLERA 295
Cdd:cd18047 69 --NKYPQCLCLSPTYELALQtgkVIEQMGKFYPE----LKLAYA-----VRGNKLERGQkiseQIVIGTPGTVLDWCSKL 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1008909313 296 R-VSLQSIRYLALDEADRML-DMGFEPQVRRIvEQMdmpLPGARQTMLFSATFPKEIQKMA 354
Cdd:cd18047 138 KfIDPKKIKVFVLDEADVMIaTQGHQDQSIRI-QRM---LPRNCQMLLFSATFEDSVWKFA 194
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
392-502 |
1.73e-15 |
|
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: 73.78 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 392 LMDLLHAQRDTGKQTLTLVFVETKRGADSLESWL-----CMNGFPATSI--HGDRNQQEREY--------ALRSFKSGQT 456
Cdd:cd18802 12 LIEILREYFPKTPDFRGIIFVERRATAVVLSRLLkehpsTLAFIRCGFLigRGNSSQRKRSLmtqrkqkeTLDKFRDGEL 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1008909313 457 PILVATDVAARGLDIPHVAHVVNFDLPNDIDDYVHRIGRtGRAGKS 502
Cdd:cd18802 92 NLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARAPNS 136
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
181-345 |
8.28e-15 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 71.67 E-value: 8.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 181 GRDLMACAQTGSGKTaaLCFPIIsgimkAPSAGRPQRGGgmgmrtaypsALILSPTRELSMQIHEEARKFsYQTGVRVVV 260
Cdd:cd00046 1 GENVLITAPTGSGKT--LAALLA-----ALLLLLKKGKK----------VLVLVPTKALALQTAERLREL-FGPGIRVAV 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 261 AYGGAPITQQLRELERGVDILVATPGRLVDLLERA-RVSLQSIRYLALDEADRMLDMGFEPQVRRIVEQMDMPLPGarQT 339
Cdd:cd00046 63 LVGGSSAEEREKNKLGDADIIIATPDMLLNLLLREdRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNA--QV 140
|
....*.
gi 1008909313 340 MLFSAT 345
Cdd:cd00046 141 ILLSAT 146
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
380-501 |
2.07e-13 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 73.23 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 380 VEFVQEAD----KRSHLMDLLHAQRDTGKQTLTLVFVETKRGADSLESWLCMNGFPAT------SIHGDR--NQQEREYA 447
Cdd:COG1111 324 MRLAEEADiehpKLSKLREILKEQLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGrfvgqaSKEGDKglTQKEQIEI 403
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1008909313 448 LRSFKSGQTPILVATDVAARGLDIPHVAHVVNFDL-PNDIdDYVHRIGRTGRAGK 501
Cdd:COG1111 404 LERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYEPvPSEI-RSIQRKGRTGRKRE 457
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
382-501 |
1.01e-11 |
|
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: 62.61 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 382 FVQEADKRSHLMDLLHAQRDTGKQTLTLVFVETKRGADSLESWLCMNGFPATSIHGDRNQQEREYALRSFKSGQTPILVA 461
Cdd:cd18794 7 SVRPKDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVA 86
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1008909313 462 TDVAARGLDIPHVAHVVNFDLPNDIDDYVHRIGRTGRAGK 501
Cdd:cd18794 87 TVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGL 126
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
168-310 |
2.92e-11 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 66.07 E-value: 2.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 168 TPVQRHAIPISL-AGRDLMACAQTGSGKTAALCFPIISGImkapsagrpQRGGgmgmrtaypSALILSPTRELSMQIHEE 246
Cdd:COG1204 24 YPPQAEALEAGLlEGKNLVVSAPTASGKTLIAELAILKAL---------LNGG---------KALYIVPLRALASEKYRE 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1008909313 247 ARKFSYQTGVRVVVAYGgaPITQQLRELERgVDILVATPGRLvDLLERARVS-LQSIRYLALDEA 310
Cdd:COG1204 86 FKRDFEELGIKVGVSTG--DYDSDDEWLGR-YDILVATPEKL-DSLLRNGPSwLRDVDLVVVDEA 146
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
137-505 |
8.80e-11 |
|
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: 64.86 E-value: 8.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 137 RDIPPPVSTFADI--DLGDALNENIRRCKYVRPTPVQRHAIPISLAGRDLMACAQTGSGKTaaLCF--PIISGIMKAPSA 212
Cdd:COG1205 25 RTIPAREARYAPWpdWLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKS--LAYllPVLEALLEDPGA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 213 grpqrgggmgmrtaypSALILSPTRELSmqiHEEARKFS-----YQTGVRVVVAYGGAPitQQLRE--LERGvDILVATP 285
Cdd:COG1205 103 ----------------TALYLYPTKALA---RDQLRRLRelaeaLGLGVRVATYDGDTP--PEERRwiREHP-DIVLTNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 286 grlvDLLERA------RVS--LQSIRYLALDEA---------------DRMldmgfepqvRRIVEQMdmplpGARQTMLF 342
Cdd:COG1205 161 ----DMLHYGllphhtRWArfFRNLRYVVIDEAhtyrgvfgshvanvlRRL---------RRICRHY-----GSDPQFIL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 343 -SATF--PKEiqkMASDFLDNYiFLAVGRVGSSTdliaQRVEFV-------QEADKRSHL---MDLLHAQRDTGKQtlTL 409
Cdd:COG1205 223 aSATIgnPAE---HAERLTGRP-VTVVDEDGSPR----GERTFVlwnpplvDDGIRRSALaeaARLLADLVREGLR--TL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 410 VFVETKRGADSLESWL---CMNGFPATSI---HGDRNQQEREYALRSFKSGQTPILVATDVAARGLDIPHVAHVVNFDLP 483
Cdd:COG1205 293 VFTRSRRGAELLARYArraLREPDLADRVaayRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYP 372
|
410 420
....*....|....*....|..
gi 1008909313 484 NDIDDYVHRIGRTGRAGKSGLA 505
Cdd:COG1205 373 GTRASFWQQAGRAGRRGQDSLV 394
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
392-494 |
8.68e-10 |
|
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: 57.10 E-value: 8.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 392 LMDLLHAQRDTGKQTLtlVFVETKRGADSLESWLCMNGFPATSIHGDRNQQEREYALRSFKSGQTP--ILVATDVAARGL 469
Cdd:cd18793 16 LLELLEELREPGEKVL--IFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGVGL 93
|
90 100 110
....*....|....*....|....*....|.
gi 1008909313 470 DIPHVAHVVNFDL---PNDID---DYVHRIG 494
Cdd:cd18793 94 NLTAANRVILYDPwwnPAVEEqaiDRAHRIG 124
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
181-309 |
3.49e-09 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 56.05 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 181 GRDLMACAQTGSGKTAALCFPIISGIMKAPSAGRpqrgggmgmrtaypSALILSPTRELSMQIHEEARKFS--YQTGVRV 258
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGV--------------QVLYISPLKALINDQERRLEEPLdeIDLEIPV 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1008909313 259 VVAYGGAPITQQLRELERGVDILVATPGRLVDLL--ERARVSLQSIRYLALDE 309
Cdd:cd17922 67 AVRHGDTSQSEKAKQLKNPPGILITTPESLELLLvnKKLRELFAGLRYVVVDE 119
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
458-503 |
4.19e-09 |
|
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: 53.48 E-value: 4.19e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1008909313 458 ILVATDVAARGLDIPHVAHVVNFDLPNDIDDYVHRIGRTGRAGKSG 503
Cdd:cd18785 25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDE 70
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
171-310 |
7.24e-09 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 55.67 E-value: 7.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 171 QRHAIPISLAGRDLMACAQTGSGKTaaLCF--PIISGIMKAPSAgrpqrgggmgmrtaypSALILSPTRELSMQIHEEAR 248
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKS--LCYqlPILEALLRDPGS----------------RALYLYPTKALAQDQLRSLR 66
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1008909313 249 KFSYQTGVRVVVA-YGG-APITQQLRELERGVDILVATPgrlvDLLE--------RARVSLQSIRYLALDEA 310
Cdd:cd17923 67 ELLEQLGLGIRVAtYDGdTPREERRAIIRNPPRILLTNP----DMLHyallphhdRWARFLRNLRYVVLDEA 134
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
163-309 |
3.23e-08 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 56.65 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 163 KYVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGIMKAPSAGRPQRgggmGMRTAYpsaliLSPTRELSMQ 242
Cdd:COG1201 21 RFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTLAAFLPALDELARRPRPGELPD----GLRVLY-----ISPLKALAND 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1008909313 243 IH-------EEARKFSYQT--GVRVVVAYGGAPITQQLRELERGVDILVATPGRLVDLL--ERARVSLQSIRYLALDE 309
Cdd:COG1201 92 IErnlraplEEIGEAAGLPlpEIRVGVRTGDTPASERQRQRRRPPHILITTPESLALLLtsPDARELLRGVRTVIVDE 169
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
368-496 |
5.40e-08 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 56.00 E-value: 5.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 368 RVGSSTDLIAQRVEFVQEAD-KRSHLMDLLHAQRDTGKQTLtlVFVETKRGADSLESWLCMNGFPATSIHGDRNQQEREY 446
Cdd:COG0553 513 QICSHPALLLEEGAELSGRSaKLEALLELLEELLAEGEKVL--VFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDE 590
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1008909313 447 ALRSFKSGQTP--ILVATDVAARGLDIPHVAHVVNFDL---PNDID---DYVHRIGRT 496
Cdd:COG0553 591 LVDRFQEGPEApvFLISLKAGGEGLNLTAADHVIHYDLwwnPAVEEqaiDRAHRIGQT 648
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
168-310 |
1.06e-07 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 52.26 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 168 TPVQRHAI-PISLAGRDLMACAQTGSGKTAALCFPIISGIMKAPSagrpqrgggmgmrtaypSALILSPTRELSMQIHEE 246
Cdd:cd17921 3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRALATSGG-----------------KAVYIAPTRALVNQKEAD 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1008909313 247 ARKFSYQTGVRVVVAYGGAPITqqlRELERGVDILVATPGRLVDLLERARV-SLQSIRYLALDEA 310
Cdd:cd17921 66 LRERFGPLGKNVGLLTGDPSVN---KLLLAEADILVATPEKLDLLLRNGGErLIQDVRLVVVDEA 127
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
388-501 |
4.77e-07 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 52.95 E-value: 4.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 388 KRSHLMDLLHAQRDTGKQTLTLVFVETKRGADSLESWLCMNGFPA------TSIHGDR--NQQEREYALRSFKSGQTPIL 459
Cdd:PRK13766 348 KLEKLREIVKEQLGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKgmSQKEQIEILDKFRAGEFNVL 427
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1008909313 460 VATDVAARGLDIPHVAHVVNFD-LPNDIdDYVHRIGRTGRAGK 501
Cdd:PRK13766 428 VSTSVAEEGLDIPSVDLVIFYEpVPSEI-RSIQRKGRTGRQEE 469
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
408-478 |
5.29e-07 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350186 [Multi-domain] Cd Length: 116 Bit Score: 48.71 E-value: 5.29e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1008909313 408 TLVFVETKRGADSLESWLCMNGFPATSIHGDRNQQEREY-ALRSFKSGQT--PILVATDVAARGLDIPHVAHVV 478
Cdd:cd18799 9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDeALILLFFGELkpPILVTVDLLTTGVDIPEVDNVV 82
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
425-504 |
9.60e-07 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 51.64 E-value: 9.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 425 LCMNGFPATSIHGDRNQQEREYALRSFKSGQTPILVATDVAARGLDIPHVAHVVNFDLPNDIDDYVHrigRTGRAGKSGL 504
Cdd:PRK11057 256 LQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQ---ETGRAGRDGL 332
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
163-309 |
1.11e-06 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 51.81 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 163 KYVRPTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGIMKapsagrpqrgggMGMRTAYPS---ALILSPTREL 239
Cdd:PRK13767 29 KFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIIDELFR------------LGREGELEDkvyCLYVSPLRAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 240 SMQIH-----------EEARKFSYQ-TGVRVVVAYGGAPITQQLRELERGVDILVATPGRLVDLLE--RARVSLQSIRYL 305
Cdd:PRK13767 97 NNDIHrnleeplteirEIAKERGEElPEIRVAIRTGDTSSYEKQKMLKKPPHILITTPESLAILLNspKFREKLRTVKWV 176
|
....
gi 1008909313 306 ALDE 309
Cdd:PRK13767 177 IVDE 180
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
188-471 |
1.21e-06 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 51.24 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 188 AQTGSGKT-AALCFpiISGIMKAPSAGRpqrgggmgmrtaypsaLILS-PTRELSMQIHEEARKFSyqtGVRVVVAYGGA 265
Cdd:COG1203 154 APTGGGKTeAALLF--ALRLAAKHGGRR----------------IIYAlPFTSIINQTYDRLRDLF---GEDVLLHHSLA 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 266 PI------------TQQLRELERGVD--ILVATPGRLVDLLERARVSlQSIRYLAL-------DEADrMLDMGFEPQVRR 324
Cdd:COG1203 213 DLdlleeeeeyeseARWLKLLKELWDapVVVTTIDQLFESLFSNRKG-QERRLHNLansviilDEVQ-AYPPYMLALLLR 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 325 IVEQMDMplPGARqTMLFSATFPKEIqkmaSDFLDNYIFLAVGRVGSSTDLIAQ----RVEFVQEADKRSHLMDLLHAQR 400
Cdd:COG1203 291 LLEWLKN--LGGS-VILMTATLPPLL----REELLEAYELIPDEPEELPEYFRAfvrkRVELKEGPLSDEELAELILEAL 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 401 DTGKQtlTLVFVETKRGA----DSLESWLcmNGFPATSIHG-----DRNQQEREyALRSFKSGQTPILVATDVAARGLDI 471
Cdd:COG1203 364 HKGKS--VLVIVNTVKDAqelyEALKEKL--PDEEVYLLHSrfcpaDRSEIEKE-IKERLERGKPCILVSTQVVEAGVDI 438
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
440-498 |
1.83e-06 |
|
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: 47.74 E-value: 1.83e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 440 NQQEREYALRSFKSGQTPILVATDVAARGLDIPHVAHVVNFD-LPNDIdDYVHRIGRTGR 498
Cdd:cd18801 75 SQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDaSPSPI-RMIQRMGRTGR 133
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
182-310 |
2.13e-06 |
|
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: 48.80 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 182 RDLMACAQTGSGKTaalcfpIISgIMKAPSAGRPQRGGGMGMRTAypsaLILSPTRELSMQIHEEARKfsyQTGVRVVVA 261
Cdd:cd18034 17 RNTIVVLPTGSGKT------LIA-VMLIKEMGELNRKEKNPKKRA----VFLVPTVPLVAQQAEAIRS---HTDLKVGEY 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1008909313 262 YGGA----PITQQLRELERGVDILVATPGRLVDLLERARVSLQSIRYLALDEA 310
Cdd:cd18034 83 SGEMgvdkWTKERWKEELEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
390-502 |
3.35e-06 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 47.26 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 390 SHLMDLLHAQRDTgkqtltLVFVETKRGAdslESW------LCMNGFPATSI---HGDRNQQEREYALRSFKSGQTPILV 460
Cdd:cd18796 29 AEVIFLLERHKST------LVFTNTRSQA---ERLaqrlreLCPDRVPPDFIalhHGSLSRELREEVEAALKRGDLKVVV 99
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1008909313 461 ATDVAARGLDIPHVAHVVNFDLPNDIDDYVHRIGRTGRAGKS 502
Cdd:cd18796 100 ATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGHRPGA 141
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
169-350 |
1.15e-05 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 46.17 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 169 PVQRHAIPISLA-GRDLMACAQTGSGKTAALCFPIISGIMKapsagrpqrgGGMgmrtaypsALILSPTRELSMQIHEEA 247
Cdd:cd18028 4 PPQAEAVRAGLLkGENLLISIPTASGKTLIAEMAMVNTLLE----------GGK--------ALYLVPLRALASEKYEEF 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 248 RKFsYQTGVRVVVAYGGAPITQqlrELERGVDILVATPGRLvDLLERARVS-LQSIRYLALDEADRMLDMGFEPQVRRIV 326
Cdd:cd18028 66 KKL-EEIGLKVGISTGDYDEDD---EWLGDYDIIVATYEKF-DSLLRHSPSwLRDVGVVVVDEIHLISDEERGPTLESIV 140
|
170 180
....*....|....*....|....*.
gi 1008909313 327 EQMDMPLPGARQTMLfSATF--PKEI 350
Cdd:cd18028 141 ARLRRLNPNTQIIGL-SATIgnPDEL 165
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
435-509 |
4.34e-05 |
|
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350176 [Multi-domain] Cd Length: 153 Bit Score: 44.16 E-value: 4.34e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1008909313 435 IHGDRNQQEREYALRSFKSGQTPILVATDVAARGLDIP--HVAHVVNFdLPNDIDDYVHRIGRTGRAGKSGLATAFF 509
Cdd:cd18789 74 ITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPeaNVAIQISG-HGGSRRQEAQRLGRILRPKKGGGKNAFF 149
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
187-310 |
5.08e-05 |
|
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350779 [Multi-domain] Cd Length: 191 Bit Score: 44.56 E-value: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 187 CAQTGSGKTAALCFPIISGIMKAPSAgrpqrgggmgmRTAYpsaliLSPTRELSMQIHEE-ARKFSYQTGVRVVVAYGGA 265
Cdd:cd18021 25 GAPTGSGKTVCAELALLRHWRQNPKG-----------RAVY-----IAPMQELVDARYKDwRAKFGPLLGKKVVKLTGET 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1008909313 266 piTQQLRELERGvDILVATPGRLvDLLER---ARVSLQSIRYLALDEA 310
Cdd:cd18021 89 --STDLKLLAKS-DVILATPEQW-DVLSRrwkQRKNVQSVELFIADEL 132
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
305-501 |
6.05e-05 |
|
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
Pssm-ID: 187770 [Multi-domain] Cd Length: 353 Bit Score: 45.50 E-value: 6.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 305 LALDEADRMLD--MGFEPQVRRIVEQMDMPLpgarqtMLFSATFPKEIQKMASDfLDNYIFLavgrvgSSTDLIAQRVEF 382
Cdd:cd09639 127 LIFDEVHFYDEytLALILAVLEVLKDNDVPI------LLMSATLPKFLKEYAEK-IGYVEEN------EPLDLKPNERAP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 383 VQEADKR-----SHLMDLLHAQRDTGKQtltLVFVETKRGADSLESWLCMNG--FPATSIHG-----DRNQQEREYaLRS 450
Cdd:cd09639 194 FIKIESDkvgeiSSLERLLEFIKKGGSV---AIIVNTVDRAQEFYQQLKEKGpeEEIMLIHSrftekDRAKKEAEL-LLE 269
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1008909313 451 FKSGQTPILVATDVAARGLDIphvahvvNFDL----PNDIDDYVHRIGRTGRAGK 501
Cdd:cd09639 270 FKKSEKFVIVATQVIEASLDI-------SVDVmiteLAPIDSLIQRLGRLHRYGE 317
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
391-481 |
7.33e-05 |
|
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350177 [Multi-domain] Cd Length: 171 Bit Score: 43.77 E-value: 7.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 391 HLMDLLHAQRDTGKQTLtlVFVETKRGADSLESWLCMNGFPATSIHGDRNQQEREYALRSFKSGQTPILVATDVAARGLD 470
Cdd:cd18790 15 DLLGEIRKRVARGERVL--VTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLD 92
|
90
....*....|.
gi 1008909313 471 IPHVAHVVNFD 481
Cdd:cd18790 93 LPEVSLVAILD 103
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
188-497 |
9.16e-05 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 45.69 E-value: 9.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 188 AQTGSGKTAALCFPIISGIMKAPSAGRPQRGGGMGMRTAYPS---ALILSPTRELSMQIH----EEARKFSYQTGVRVVV 260
Cdd:PRK09751 3 APTGSGKTLAAFLYALDRLFREGGEDTREAHKRKTSRILYISpikALGTDVQRNLQIPLKgiadERRRRGETEVNLRVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 261 AYGGAPITQQLRELERGVDILVATPGRLVDLL-ERARVSLQSIRYLALDEADRMLDMGFEPQVRRIVEQMDMPLPGARQT 339
Cdd:PRK09751 83 RTGDTPAQERSKLTRNPPDILITTPESLYLMLtSRARETLRGVETVIIDEVHAVAGSKRGAHLALSLERLDALLHTSAQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 340 MLFSATF-PKE--------------IQKMASDFLDNYIFLAV-------------------GRVGSS---------TDLI 376
Cdd:PRK09751 163 IGLSATVrSASdvaaflggdrpvtvVNPPAMRHPQIRIVVPVanmddvssvasgtgedshaGREGSIwpyietgilDEVL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 377 AQRVEFVQE-----ADKRSHLMDLLHAQRDTGKQTL--TLVFVETKRGADSLESwLCMNGFPATSIHGDRNQQEREYALR 449
Cdd:PRK09751 243 RHRSTIVFTnsrglAEKLTARLNELYAARLQRSPSIavDAAHFESTSGATSNRV-QSSDVFIARSHHGSVSKEQRAITEQ 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1008909313 450 SFKSGQTPILVATDVAARGLDIPHVAHVVNFDLPNDIDDYVHRIGRTG 497
Cdd:PRK09751 322 ALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
435-501 |
2.74e-04 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 41.95 E-value: 2.74e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1008909313 435 IHGDRNQQEREYALRSFKSGQTPILVATDVAARGLDIPH-----VAHVVNFDLPNdiddyVHRI-GRTGRAGK 501
Cdd:cd18811 67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNatvmvIEDAERFGLSQ-----LHQLrGRVGRGDH 134
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
183-501 |
3.98e-04 |
|
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.
Pssm-ID: 273707 [Multi-domain] Cd Length: 359 Bit Score: 42.83 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 183 DLMACAQTGSGKT-AALCFP------------IISGIMKAPSAGRPQRgggmgMRTAYPSALIL----SPTRELSMQIHE 245
Cdd:TIGR01587 1 LLVIEAPTGYGKTeAALLWAlhsiksqkadrvIIALPTRATINAMYRR-----AKELFGSELVGlhhsSSFSRIKEMGDS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 246 E--ARKFS-YQTGVRVVVAYGGAPITqqlrelergVDILVATPGRLVDLLERARVSLQSIRyLALDEADRMLD--MGFEP 320
Cdd:TIGR01587 76 EefEHLFPlYIHSNDKLFLDPITVCT---------IDQVLKSVFGEFGHYEFTLASIANSL-LIFDEVHFYDEytLALIL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 321 QVRRIVEQMDMPLpgarqtMLFSATFPKEIQKMASDfLDNYIFLavgrvgSSTDLI----AQRVEFVQEADKR----SHL 392
Cdd:TIGR01587 146 AVLEVLKDNDVPI------LLMSATLPKFLKEYAEK-IGYVEFN------EPLDLKeerrFENHRFILIESDKvgeiSSL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 393 MDLLHAQRDTGKQtltLVFVETKRGADSLESWLCMNG--FPATSIHG-----DRNQQEREYALRSFKSGQTPILVATDVA 465
Cdd:TIGR01587 213 ERLLEFIKKGGSI---AIIVNTVDRAQEFYQQLKEKApeEEIILYHSrftekDRAKKEAELLREMKKSNEKFVIVATQVI 289
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1008909313 466 ARGLDIphvahvvNFDL----PNDIDDYVHRIGRTGRAGK 501
Cdd:TIGR01587 290 EASLDI-------SADVmiteLAPIDSLIQRLGRLHRYGR 322
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
164-312 |
4.73e-04 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 43.32 E-value: 4.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 164 YVRPTPVQRHAIPISLAGRDL----MACAQTGSGKTaalcfpIISgIMKApsAGRPQRGGGmgmrtaypSALILSPTREL 239
Cdd:PRK13766 8 LIKPNTIEARLYQQLLAATALkkntLVVLPTGLGKT------AIA-LLVI--AERLHKKGG--------KVLILAPTKPL 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1008909313 240 SMQiHEEA-RKFSYQTGVRVVVAYGGAPITQQLRELERGvDILVATPgRLV--DLLERaRVSLQSIRYLALDEADR 312
Cdd:PRK13766 71 VEQ-HAEFfRKFLNIPEEKIVVFTGEVSPEKRAELWEKA-KVIVATP-QVIenDLIAG-RISLEDVSLLIFDEAHR 142
|
|
| SF2_C_priA |
cd18804 |
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ... |
439-504 |
6.64e-04 |
|
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350191 [Multi-domain] Cd Length: 238 Bit Score: 41.85 E-value: 6.64e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1008909313 439 RNQQEREYALRSFKSGQTPILVATDVAARGLDIPHV--AHVVNFDLPNDIDDY---------VHRI-GRTGRAGKSGL 504
Cdd:cd18804 128 RKKGALEKLLDQFERGEIDILIGTQMIAKGLDFPNVtlVGILNADSGLNSPDFraserafqlLTQVsGRAGRGDKPGK 205
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
166-284 |
7.49e-04 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 40.86 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 166 RPTPVQRHAIP------ISLAGRDLMACAQTGSGKTAALCFPIISgimkAPSAGRpqrgggmgmrtaypSALILSPTREL 239
Cdd:cd17918 15 SLTKDQAQAIKdiekdlHSPEPMDRLLSGDVGSGKTLVALGAALL----AYKNGK--------------QVAILVPTEIL 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1008909313 240 SMQIHEEARKFSYQTGVRVVVAYGGAPITQqlrelerGVDILVAT 284
Cdd:cd17918 77 AHQHYEEARKFLPFINVELVTGGTKAQILS-------GISLLVGT 114
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
185-333 |
1.11e-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: 40.19 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 185 MACAQTGSGKTaalcfpiISGIMKApsAGRPQRGGGmgmrtaypSALILSPTRELSMQIHEEARKFsyQTGVRVVVAYGG 264
Cdd:cd18035 20 LIVLPTGLGKT-------IIAILVA--ADRLTKKGG--------KVLILAPSRPLVEQHAENLKRV--LNIPDKITSLTG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 265 APITQQLRELERGVDILVATPGRLVDLLERARVSLQSIRYLALDEADRML-DMGFEPQVRRIVEQMDMPL 333
Cdd:cd18035 81 EVKPEERAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHHAVgNYAYVYIAHRYKREANNPL 150
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
167-309 |
2.85e-03 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350794 [Multi-domain] Cd Length: 204 Bit Score: 39.38 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 167 PTPVQRHAIPISLAGRDLMACAQTGSGKTAALCFPIISGIMKAPSAGRPQRgggmgmrtaypsALILSPTRELSMQiheE 246
Cdd:cd18036 3 LRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKRRSAGEKGR------------VVVLVNKVPLVEQ---Q 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1008909313 247 ARKFS--YQTGVRVVVAYGGAPITQQLRELERGVDILVATPGRLVDLL----ERARVSLQSIRYLALDE 309
Cdd:cd18036 68 LEKFFkyFRKGYKVTGLSGDSSHKVSFGQIVKASDVIICTPQILINNLlsgrEEERVYLSDFSLLIFDE 136
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
179-312 |
5.64e-03 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 38.57 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 179 LAGRDLMACAQTGSGKT--AALcfpiisgIMKAPSAGRPQRGGGmgmrtaypSALILSPTRELSMQIHEEARKFSYQTGV 256
Cdd:cd17927 15 LKGKNTIICLPTGSGKTfvAVL-------ICEHHLKKFPAGRKG--------KVVFLANKVPLVEQQKEVFRKHFERPGY 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1008909313 257 RVVVAYGGAPITQQLRELERGVDILVATPGRLV-DLLERARVSLQSIRYLALDEADR 312
Cdd:cd17927 80 KVTGLSGDTSENVSVEQIVESSDVIIVTPQILVnDLKSGTIVSLSDFSLLVFDECHN 136
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
435-505 |
6.11e-03 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350179 [Multi-domain] Cd Length: 160 Bit Score: 37.63 E-value: 6.11e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1008909313 435 IHGDRNQQEREYALRSFKSGQTPILVATDVAARGLDIPH-----VAHVVNFDLPNdiddyVHRI-GRTGRAGKSGLA 505
Cdd:cd18792 66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNantmiIEDADRFGLSQ-----LHQLrGRVGRGKHQSYC 137
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
166-284 |
9.41e-03 |
|
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase 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: 350682 [Multi-domain] Cd Length: 189 Bit Score: 37.69 E-value: 9.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909313 166 RPTPVQRHAIPISLAGRDLMACAQTGSGKTAalcFPIISGIMKAPSAGRpqrgggmgmrtaypSALILsPTRELSMQIHE 245
Cdd:cd17924 17 PPWGAQRTWAKRLLRGKSFAIIAPTGVGKTT---FGLATSLYLASKGKR--------------SYLIF-PTKSLVKQAYE 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1008909313 246 EARKFSYQTG--VRVVVAYGGAPITQQLRELER----GVDILVAT 284
Cdd:cd17924 79 RLSKYAEKAGveVKILVYHSRLKKKEKEELLEKiekgDFDILVTT 123
|
|
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