|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
1-404 |
0e+00 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 796.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 1 MTNSEQNPPSEenvQVASTGEIESNYDEIVECFEALNLEGDLLRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTG 80
Cdd:PTZ00424 1 MATSEQKNQSE---QVASTGTIESNYDEIVDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 81 KTATFVIAALQKIDYSLNACQVLLLAPTRELAQQIQKVALALGDYCELRCHACVGGTSVRDDMNKLKSGVHMVVGTPGRV 160
Cdd:PTZ00424 78 KTATFVIAALQLIDYDLNACQALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 161 FDMLDKGYLRVDNLKLFILDEADEMLSRGFKVQIHDIFKKLPQDVQVALFSATMPNEILHLTTQFMRDPKRILVKQEELT 240
Cdd:PTZ00424 158 YDMIDKRHLRVDDLKLFILDEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 241 LEGIRQFYVGVEKDEWKMDTLIDLYETLTIVQAIIYCNTRRRVDQLTKQMRERDFTCSSMHGDMDQKDREVIMRQFRSGS 320
Cdd:PTZ00424 238 LEGIRQFYVAVEKEEWKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 321 SRVLITTDLLARGIDVQQVSLVINYDLPVSPETYIHRIGRSGRFGKKGVSINFVTDDDIVCLRDIERHYNTQIEEMPMGI 400
Cdd:PTZ00424 318 TRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEV 397
|
....
gi 126643927 401 TDIL 404
Cdd:PTZ00424 398 ADYL 401
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
33-398 |
9.97e-163 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 463.46 E-value: 9.97e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 33 FEALNLEGDLLRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKIDYSL-NACQVLLLAPTREL 111
Cdd:COG0513 4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRpRAPQALILAPTREL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 112 AQQIQKVALALGDYCELRCHACVGGTSVRDDMNKLKSGVHMVVGTPGRVFDMLDKGYLRVDNLKLFILDEADEMLSRGFK 191
Cdd:COG0513 84 ALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGFI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 192 VQIHDIFKKLPQDVQVALFSATMPNEILHLTTQFMRDPKRILVKQEELTLEGIRQFYVGVEKDEwKMDTLIDLYETLTIV 271
Cdd:COG0513 164 EDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRD-KLELLRRLLRDEDPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 272 QAIIYCNTRRRVDQLTKQMRERDFTCSSMHGDMDQKDREVIMRQFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPVSP 351
Cdd:COG0513 243 RAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDP 322
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 126643927 352 ETYIHRIGRSGRFGKKGVSINFVTDDDIVCLRDIERHYNTQIEEMPM 398
Cdd:COG0513 323 EDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEEL 369
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
33-233 |
1.34e-138 |
|
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: 393.73 E-value: 1.34e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 33 FEALNLEGDLLRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKIDYSLNACQVLLLAPTRELA 112
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 113 QQIQKVALALGDYCELRCHACVGGTSVRDDMNKLKSGVHMVVGTPGRVFDMLDKGYLRVDNLKLFILDEADEMLSRGFKV 192
Cdd:cd18046 81 QQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 126643927 193 QIHDIFKKLPQDVQVALFSATMPNEILHLTTQFMRDPKRIL 233
Cdd:cd18046 161 QIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRIL 201
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
35-233 |
1.19e-117 |
|
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: 340.46 E-value: 1.19e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 35 ALNLEGDLLRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKIDYSLNACQVLLLAPTRELAQQ 114
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 115 IQKVALALGDYCELRCHACVGGTSVRDDMNKLKSGVHMVVGTPGRVFDMLDKGYLRVDNLKLFILDEADEMLSRGFKVQI 194
Cdd:cd17939 81 IQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQI 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 126643927 195 HDIFKKLPQDVQVALFSATMPNEILHLTTQFMRDPKRIL 233
Cdd:cd17939 161 YDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRIL 199
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
33-394 |
3.88e-107 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 323.29 E-value: 3.88e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 33 FEALNLEGDLLRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKIDYSLNACQVLLLAPTRELA 112
Cdd:PRK11776 6 FSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTRELA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 113 QQIQKvalalgdycELRCHAC----------VGGTSVRDDMNKLKSGVHMVVGTPGRVFDMLDKGYLRVDNLKLFILDEA 182
Cdd:PRK11776 86 DQVAK---------EIRRLARfipnikvltlCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 183 DEMLSRGFKVQIHDIFKKLPQDVQVALFSATMPNEILHLTTQFMRDPKRILVKQEElTLEGIRQFYVGVEKDEwKMDTLI 262
Cdd:PRK11776 157 DRMLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTH-DLPAIEQRFYEVSPDE-RLPALQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 263 DLYETLTIVQAIIYCNTRRRVDQLTKQMRERDFTCSSMHGDMDQKDREVIMRQFRSGSSRVLITTDLLARGIDVQQVSLV 342
Cdd:PRK11776 235 RLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAV 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 126643927 343 INYDLPVSPETYIHRIGRSGRFGKKGVSINFVTDDDIVCLRDIERHYNTQIE 394
Cdd:PRK11776 315 INYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLN 366
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
33-233 |
9.70e-97 |
|
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: 287.44 E-value: 9.70e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 33 FEALNLEGDLLRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKIDYSLNACQVLLLAPTRELA 112
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 113 QQIQKVALALGDYCELRCHACVGGTSVRDDMNKLKSGVHMVVGTPGRVFDMLDKGYLRVDNLKLFILDEADEMLSRGFKV 192
Cdd:cd18045 81 VQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 126643927 193 QIHDIFKKLPQDVQVALFSATMPNEILHLTTQFMRDPKRIL 233
Cdd:cd18045 161 QIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRIL 201
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
28-404 |
1.60e-87 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 277.88 E-value: 1.60e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 28 EIVECFEALNLEGDLLRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKIDYSLNACQVLLLAP 107
Cdd:PRK11634 3 EFETTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 108 TRELAQQiqkVALALGDYCE----LRCHACVGGTSVRDDMNKLKSGVHMVVGTPGRVFDMLDKGYLRVDNLKLFILDEAD 183
Cdd:PRK11634 83 TRELAVQ---VAEAMTDFSKhmrgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 184 EMLSRGFKVQIHDIFKKLPQDVQVALFSATMPNEILHLTTQFMRDPKRILVKQEELTLEGIRQFY---VGVEKDEwkmdT 260
Cdd:PRK11634 160 EMLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYwtvWGMRKNE----A 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 261 LIDLYETLTIVQAIIYCNTRRRVDQLTKQMRERDFTCSSMHGDMDQKDREVIMRQFRSGSSRVLITTDLLARGIDVQQVS 340
Cdd:PRK11634 236 LVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERIS 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126643927 341 LVINYDLPVSPETYIHRIGRSGRFGKKGVSINFVTDDDIVCLRDIERHYNTQIEEMPMGITDIL 404
Cdd:PRK11634 316 LVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAELL 379
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
42-232 |
1.20e-84 |
|
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: 256.21 E-value: 1.20e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 42 LLRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKIDYSL----NACQVLLLAPTRELAQQIQK 117
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPkkkgRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 118 VALALGDYCELRCHACVGGTSVRDDMNKLKSGVHMVVGTPGRVFDMLDKGYLRVDNLKLFILDEADEMLSRGFKVQIHDI 197
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 126643927 198 FKKLPQDVQVALFSATMPNEILHLTTQFMRDPKRI 232
Cdd:cd00268 161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
33-388 |
6.40e-81 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 255.25 E-value: 6.40e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 33 FEALNLEGDLLRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQK-IDY---SLNACQVLLLAPT 108
Cdd:PRK11192 3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHlLDFprrKSGPPRILILTPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 109 RELAQQIQKVALALGDYCELRCHACVGGTSVRDDMNKLKSGVHMVVGTPGRVFDMLDKGYLRVDNLKLFILDEADEMLSR 188
Cdd:PRK11192 83 RELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLDM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 189 GFKVQIHDIFKKLPQDVQVALFSATMPNE-ILHLTTQFMRDPKRILVKQEELTLEGIRQFYVGVEKDEWKMDTLIDLYET 267
Cdd:PRK11192 163 GFAQDIETIAAETRWRKQTLLFSATLEGDaVQDFAERLLNDPVEVEAEPSRRERKKIHQWYYRADDLEHKTALLCHLLKQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 268 LTIVQAIIYCNTRRRVDQLTKQMRERDFTCSSMHGDMDQKDREVIMRQFRSGSSRVLITTDLLARGIDVQQVSLVINYDL 347
Cdd:PRK11192 243 PEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDM 322
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 126643927 348 PVSPETYIHRIGRSGRFGKKGVSINFVTDDDIVCLRDIERH 388
Cdd:PRK11192 323 PRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERY 363
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
33-396 |
1.19e-75 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 242.02 E-value: 1.19e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 33 FEALNLEGDLLRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKIDYS------LNACQVLLLA 106
Cdd:PRK10590 3 FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRqphakgRRPVRALILT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 107 PTRELAQQIQKVALALGDYCELRCHACVGGTSVRDDMNKLKSGVHMVVGTPGRVFDMLDKGYLRVDNLKLFILDEADEML 186
Cdd:PRK10590 83 PTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRML 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 187 SRGFkvqIHDI---FKKLPQDVQVALFSATMPNEILHLTTQFMRDPKRILVKQEELTLEGIRQFYVGVEKDEwKMDTLID 263
Cdd:PRK10590 163 DMGF---IHDIrrvLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKR-KRELLSQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 264 LYETLTIVQAIIYCNTRRRVDQLTKQMRERDFTCSSMHGDMDQKDREVIMRQFRSGSSRVLITTDLLARGIDVQQVSLVI 343
Cdd:PRK10590 239 MIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVV 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 126643927 344 NYDLPVSPETYIHRIGRSGRFGKKGVSINFVTDDDIVCLRDIERHYNTQIEEM 396
Cdd:PRK10590 319 NYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRI 371
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
8-397 |
1.57e-73 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 237.12 E-value: 1.57e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 8 PPSEENVQVASTGEIESNYDEIVEC---FEALNLEGDLLRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTAT 84
Cdd:PRK01297 61 PRRERKPKPASLWKLEDFVVEPQEGktrFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 85 FVIAALQKIDYS-------LNACQVLLLAPTRELAQQIQKVALALGDYCELRCHACVGGTSVRDDMNKLKSG-VHMVVGT 156
Cdd:PRK01297 141 FLISIINQLLQTpppkeryMGEPRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVAT 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 157 PGRVFDMLDKGYLRVDNLKLFILDEADEMLSRGFKVQIHDIFKKLP--QDVQVALFSATMPNEILHLTTQFMRDPKRILV 234
Cdd:PRK01297 221 PGRLLDFNQRGEVHLDMVEVMVLDEADRMLDMGFIPQVRQIIRQTPrkEERQTLLFSATFTDDVMNLAKQWTTDPAIVEI 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 235 KQEELTLEGIRQ-FYVGVEKDEWKMdtLIDLYETLTIVQAIIYCNTRRRVDQLTKQMRERDFTCSSMHGDMDQKDREVIM 313
Cdd:PRK01297 301 EPENVASDTVEQhVYAVAGSDKYKL--LYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTL 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 314 RQFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPVSPETYIHRIGRSGRFGKKGVSINFVTDDDIVCLRDIERHYNTQI 393
Cdd:PRK01297 379 EGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKI 458
|
....*
gi 126643927 394 E-EMP 397
Cdd:PRK01297 459 ScEMP 463
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
30-387 |
1.68e-72 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 236.59 E-value: 1.68e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 30 VECFEALNLEGDLLRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKID--YSLNACQ---VLL 104
Cdd:PTZ00110 129 VVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINaqPLLRYGDgpiVLV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 105 LAPTRELAQQIQKVALALGDYCELRCHACVGGTSVRDDMNKLKSGVHMVVGTPGRVFDMLDKGYLRVDNLKLFILDEADE 184
Cdd:PTZ00110 209 LAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADR 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 185 MLSRGFKVQIHDIFKKLPQDVQVALFSATMPNEILHLTTQFMRD-PKRILVKQEELTL-EGIRQFYVGVEKDEwKMDTLI 262
Cdd:PTZ00110 289 MLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDLTAcHNIKQEVFVVEEHE-KRGKLK 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 263 DLYETLTI--VQAIIYCNTRRRVDQLTKQMRERDFTCSSMHGDMDQKDREVIMRQFRSGSSRVLITTDLLARGIDVQQVS 340
Cdd:PTZ00110 368 MLLQRIMRdgDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVK 447
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 126643927 341 LVINYDLPVSPETYIHRIGRSGRFGKKGVSINFVTDDDIVCLRDIER 387
Cdd:PTZ00110 448 YVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVK 494
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
33-232 |
1.20e-69 |
|
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: 218.32 E-value: 1.20e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 33 FEALNLEGDLLRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKIDYSLNACQVLLLAPTRELA 112
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 113 QQIQKVALALGDYCELRCHACVGGTSVRDDMNKLKSGVHMVVGTPGRVFDMLDKGYLRVDNLKLFILDEADEMLSRGFKV 192
Cdd:cd17940 81 LQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 126643927 193 QIHDIFKKLPQDVQVALFSATMPNEILHLTTQFMRDPKRI 232
Cdd:cd17940 161 IIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
33-398 |
3.25e-66 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 220.59 E-value: 3.25e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 33 FEALNLEGDLLRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKI-------DYSLNACQVLLL 105
Cdd:PRK04537 11 FSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlsrpalaDRKPEDPRALIL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 106 APTRELAQQIQKVALALGDYCELRCHACVGGTSVRDDMNKLKSGVHMVVGTPGRVFDMLDKGylRVDNL---KLFILDEA 182
Cdd:PRK04537 91 APTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQH--KVVSLhacEICVLDEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 183 DEMLSRGFKVQIHDIFKKLPQDV--QVALFSATMPNEILHLTTQFMRDPKRILVKQEELTLEGIRQfYVGVEKDEWKMDT 260
Cdd:PRK04537 169 DRMFDLGFIKDIRFLLRRMPERGtrQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQ-RIYFPADEEKQTL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 261 LIDLYETLTIVQAIIYCNTRRRVDQLTKQMRERDFTCSSMHGDMDQKDREVIMRQFRSGSSRVLITTDLLARGIDVQQVS 340
Cdd:PRK04537 248 LLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVK 327
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 126643927 341 LVINYDLPVSPETYIHRIGRSGRFGKKGVSINFVTDDDIVCLRDIERHYNTQIEEMPM 398
Cdd:PRK04537 328 YVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKIPVEPV 385
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
33-393 |
1.01e-64 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 212.91 E-value: 1.01e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 33 FEALNLEGDLLRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKI-------DYSLNACQVLLL 105
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLlshpapeDRKVNQPRALIM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 106 APTRELAQQIQKVALALGDYCELRCHACVGGTSVRDDMNKLKSGVHMVVGTPGRVFDMLDKGYLRVDNLKLFILDEADEM 185
Cdd:PRK04837 90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 186 LSRGFkvqIHDI---FKKLPQDVQ--VALFSATMPNEILHLTTQFMRDPKRILVKQEELTLEGIRQ--FYvgvEKDEWKM 258
Cdd:PRK04837 170 FDLGF---IKDIrwlFRRMPPANQrlNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEelFY---PSNEEKM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 259 DTLIDLYETLTIVQAIIYCNTRRRVDQLTKQMRERDFTCSSMHGDMDQKDREVIMRQFRSGSSRVLITTDLLARGIDVQQ 338
Cdd:PRK04837 244 RLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPA 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 126643927 339 VSLVINYDLPVSPETYIHRIGRSGRFGKKGVSINFVTDDDIVCLRDIERHYNTQI 393
Cdd:PRK04837 324 VTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIGHSI 378
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
244-374 |
5.48e-62 |
|
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: 195.80 E-value: 5.48e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 244 IRQFYVGVEKDEWKMDTLIDLYETLTIVQAIIYCNTRRRVDQLTKQMRERDFTCSSMHGDMDQKDREVIMRQFRSGSSRV 323
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 126643927 324 LITTDLLARGIDVQQVSLVINYDLPVSPETYIHRIGRSGRFGKKGVSINFV 374
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
42-229 |
4.68e-61 |
|
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: 195.56 E-value: 4.68e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 42 LLRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKIDYSLNACQVLLLAPTRELAQQIQKVALA 121
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 122 LGDYCE-LRCHACVGGTSVRDDMNKLKsGVHMVVGTPGRVFDMLDKGYLRVDNLKLFILDEADEMLSRGFKVQIHDIFKK 200
Cdd:cd17943 81 IGKKLEgLKCEVFIGGTPVKEDKKKLK-GCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSS 159
|
170 180
....*....|....*....|....*....
gi 126643927 201 LPQDVQVALFSATMPNEILHLTTQFMRDP 229
Cdd:cd17943 160 LPKNKQVIAFSATYPKNLDNLLARYMRKP 188
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
32-378 |
1.20e-60 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 204.64 E-value: 1.20e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 32 CFEALNLEGDLLRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVI-----AALQKIDYSLNACQVL--L 104
Cdd:PLN00206 122 SFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVpiisrCCTIRSGHPSEQRNPLamV 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 105 LAPTRELAQQIQKVALALGDYCELRCHACVGGTSVRDDMNKLKSGVHMVVGTPGRVFDMLDKGYLRVDNLKLFILDEADE 184
Cdd:PLN00206 202 LTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDC 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 185 MLSRGFKVQIHDIFKKLPQDvQVALFSATMPNEILHLTTQFMRDPKRILVKQEELTLEGIRQFYVGVEKDEWKMDtlidL 264
Cdd:PLN00206 282 MLERGFRDQVMQIFQALSQP-QVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQK----L 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 265 YETLTIVQ-----AIIYCNTRRRVDQLTKQMRE-RDFTCSSMHGDMDQKDREVIMRQFRSGSSRVLITTDLLARGIDVQQ 338
Cdd:PLN00206 357 FDILKSKQhfkppAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLR 436
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 126643927 339 VSLVINYDLPVSPETYIHRIGRSGRFGKKGVSINFVTDDD 378
Cdd:PLN00206 437 VRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEED 476
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
41-232 |
2.05e-60 |
|
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: 194.33 E-value: 2.05e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 41 DLLRGIFAYGFEKPSAIQQRGIKPILDGYDT--IGQAQSGTGKTATFVIAALQKIDYSLNACQVLLLAPTRELAQQIQKV 118
Cdd:cd17963 4 ELLKGLYAMGFNKPSKIQETALPLILSDPPEnlIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQIGEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 119 ALALGDYCELRCHACVGGTSVRDDMnklKSGVHMVVGTPGRVFDMLDKGYLRVDNLKLFILDEADEML-SRGFKVQIHDI 197
Cdd:cd17963 84 VEKMGKFTGVKVALAVPGNDVPRGK---KITAQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLdTQGHGDQSIRI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 126643927 198 FKKLPQDVQVALFSATMPNEILHLTTQFMRDPKRI 232
Cdd:cd17963 161 KRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
55-218 |
4.00e-59 |
|
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: 189.76 E-value: 4.00e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 55 SAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKIDYSLNACQVLLLAPTRELAQQIQKVALALGDYCELRCHACV 134
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 135 GGTSVRDDMNKLKsGVHMVVGTPGRVFDMLDKgYLRVDNLKLFILDEADEMLSRGFKVQIHDIFKKLPQDVQVALFSATM 214
Cdd:pfam00270 81 GGDSRKEQLEKLK-GPDILVGTPGRLLDLLQE-RKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATL 158
|
....
gi 126643927 215 PNEI 218
Cdd:pfam00270 159 PRNL 162
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
46-247 |
2.62e-56 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 183.85 E-value: 2.62e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 46 IFAYGFEKPSAIQQRGIKPILDGY-DTIGQAQSGTGKTATFVIAALQKIdYSLNACQVLLLAPTRELAQQIQKVALALGD 124
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEAL-KRGKGGRVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 125 YCELRCHACVGGTSVRDDMNKLKSGV-HMVVGTPGRVFDMLDKGYLRVDNLKLFILDEADEMLSRGFKVQIHDIFKKLPQ 203
Cdd:smart00487 80 SLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 126643927 204 DVQVALFSATMPNEILHLTTQFMRDPKRILVkqEELTLEGIRQF 247
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFIDV--GFTPLEPIEQF 201
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
33-234 |
1.47e-54 |
|
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: 179.46 E-value: 1.47e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 33 FEALNLEGDLLRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKIDYSLNACQVLLLAPTRELA 112
Cdd:cd17950 4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRELA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 113 QQIQKVALALGDYCELRCHACV-GGTSVRDDMNKLKSGV-HMVVGTPGRVFDMLDKGYLRVDNLKLFILDEADEML-SRG 189
Cdd:cd17950 84 FQISNEYERFSKYMPNVKTAVFfGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLeQLD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 126643927 190 FKVQIHDIFKKLPQDVQVALFSATMPNEILHLTTQFMRDPKRILV 234
Cdd:cd17950 164 MRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
33-232 |
2.08e-48 |
|
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can shuttle between the nucleus and the cytoplasm, and has an RNA-independent ATPase activity. DX47 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350712 [Multi-domain] Cd Length: 203 Bit Score: 163.26 E-value: 2.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 33 FEALNLEGDLLRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKIdysLNACQ---VLLLAPTR 109
Cdd:cd17954 2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQAL---LENPQrffALVLAPTR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 110 ELAQQIQKVALALGDYCELRCHACVGGTSVRDDMNKLKSGVHMVVGTPGRVFDMLD--KGY-LRvdNLKLFILDEADEML 186
Cdd:cd17954 79 ELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLEntKGFsLK--SLKFLVMDEADRLL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 126643927 187 SRGFKVQIHDIFKKLPQDVQVALFSATMPNEILHLTTQFMRDPKRI 232
Cdd:cd17954 157 NMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
33-228 |
1.52e-47 |
|
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: 161.50 E-value: 1.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 33 FEALNLEGDLLRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKI--------DYSLNAC--QV 102
Cdd:cd17967 2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLledgppsvGRGRRKAypSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 103 LLLAPTRELAQQIQKVALALGDYCELRCHACVGGTSVRDDMNKLKSGVHMVVGTPGRVFDMLDKGYLRVDNLKLFILDEA 182
Cdd:cd17967 82 LILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDEA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 126643927 183 DEMLSRGFKVQIHDIFKK----LPQDVQVALFSATMPNEILHLTTQFMRD 228
Cdd:cd17967 162 DRMLDMGFEPQIRKIVEHpdmpPKGERQTLMFSATFPREIQRLAADFLKN 211
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
42-232 |
4.17e-47 |
|
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: 159.73 E-value: 4.17e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 42 LLRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKIDYS---LNACQVLLLAPTRELAQQIQKV 118
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRpkkKAATRVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 119 ALALGDYCELRCHACVGGTSVRDDMNKLKSGVHMVVGTPGRVFDMLDKGY-LRVDNLKLFILDEADEMLSRGFKVQIHDI 197
Cdd:cd17947 81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGFADELKEI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 126643927 198 FKKLPQDVQVALFSATMPNEILHLTTQFMRDPKRI 232
Cdd:cd17947 161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
33-232 |
8.52e-47 |
|
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: 159.39 E-value: 8.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 33 FEALNLEGDLLRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKIDYSL--NACQVLLLAPTRE 110
Cdd:cd17959 3 FQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSptVGARALILSPTRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 111 LAQQIQKVALALGDYCELRCHACVGGTSVRDDMNKLKSGVHMVVGTPGRVFDMLDKGYLRVDNLKLFILDEADEMLSRGF 190
Cdd:cd17959 83 LALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMGF 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 126643927 191 KVQIHDIFKKLPQDVQVALFSATMPNEILHLTTQFMRDPKRI 232
Cdd:cd17959 163 AEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
8-227 |
5.24e-46 |
|
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DEAD-box helicases are a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350810 [Multi-domain] Cd Length: 264 Bit Score: 158.98 E-value: 5.24e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 8 PPSEENVQVASTgeIES-----NYDEI-VEC-----------FEALNLEGDLLRGIFAYGFEKPSAIQQRGIKPILDGYD 70
Cdd:cd18052 5 PPPEDEDEIFAT--IQTginfdKYDEIpVEVtgrnpppailtFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 71 TIGQAQSGTGKTATFVIAALQKI--------DYS-LNACQVLLLAPTRELAQQIQKVALALGDYCELRCHACVGGTSVRD 141
Cdd:cd18052 83 LMACAQTGSGKTAAFLLPVLTGMmkegltasSFSeVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 142 DMNKLKSGVHMVVGTPGRVFDMLDKGYLRVDNLKLFILDEADEMLSRGFKVQIHDIFKKL----PQDVQVALFSATMPNE 217
Cdd:cd18052 163 QIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPgmpsKEDRQTLMFSATFPEE 242
|
250
....*....|
gi 126643927 218 ILHLTTQFMR 227
Cdd:cd18052 243 IQRLAAEFLK 252
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
42-218 |
3.91e-45 |
|
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: 155.05 E-value: 3.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 42 LLRGIFAYGFEKPSAIQQRGIKPIL-DGYDTIGQAQSGTGKTATFVIAALQ-----KIDYSLNACQVLLLAPTRELAQQI 115
Cdd:cd17964 5 LLKALTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPAIQsllntKPAGRRSGVSALIISPTRELALQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 116 QKVALALGDYC-ELRCHACVGGTSVRDDMNKL-KSGVHMVVGTPGRVFDMLDKGYLRVD--NLKLFILDEADEMLSRGFK 191
Cdd:cd17964 85 AAEAKKLLQGLrKLRVQSAVGGTSRRAELNRLrRGRPDILVATPGRLIDHLENPGVAKAftDLDYLVLDEADRLLDMGFR 164
|
170 180 190
....*....|....*....|....*....|.
gi 126643927 192 VQIHDIFKKLPQ----DVQVALFSATMPNEI 218
Cdd:cd17964 165 PDLEQILRHLPEknadPRQTLLFSATVPDEV 195
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
33-229 |
1.35e-44 |
|
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: 153.53 E-value: 1.35e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 33 FEALNLEGDLLRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKIDYSLNACQVLLLAPTRELA 112
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 113 QQIQKVALALGDYCELRCHACVGGTSVRDDMNKLKSGVHMVVGTPGRVFDML---DKGYLRVDNLKLFILDEADEMLSRG 189
Cdd:cd17955 81 YQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLrssDDTTKVLSRVKFLVLDEADRLLTGS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 126643927 190 FKVQIHDIFKKLPQDVQVALFSATMPNEILHLTTQFMRDP 229
Cdd:cd17955 161 FEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
42-232 |
2.17e-44 |
|
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: 152.52 E-value: 2.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 42 LLRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKIdyslNACQ---------VLLLAPTRELA 112
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHI----NAQPplergdgpiVLVLAPTRELA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 113 QQIQKVALALGDYCELRCHACVGGTSVRDDMNKLKSGVHMVVGTPGRVFDMLDKGYLRVDNLKLFILDEADEMLSRGFKV 192
Cdd:cd17966 77 QQIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 126643927 193 QIHDIFKKLPQDVQVALFSATMPNEILHLTTQFMRDPKRI 232
Cdd:cd17966 157 QIRKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
42-232 |
3.63e-42 |
|
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: 146.92 E-value: 3.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 42 LLRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKIDYSLNACQVLLLAPTRELAQQIQKVALA 121
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 122 LGD-YCELRCHACVGGTSVRDDMNKLKSGVHMVVGTPGRVFDMLDKGYLRVDNLKLFILDEADEMLSRGFKVQIHDIFKK 200
Cdd:cd17962 81 LMKgLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILEN 160
|
170 180 190
....*....|....*....|....*....|..
gi 126643927 201 LPQDVQVALFSATMPNEILHLTTQFMRDPKRI 232
Cdd:cd17962 161 ISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
42-229 |
4.25e-42 |
|
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: 147.47 E-value: 4.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 42 LLRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKIDY--------SLNACQVLLLAPTRELAQ 113
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRlppldeetKDDGPYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 114 QIQKVALALGDYCELRCHACVGGTSVRDDMNKLKSGVHMVVGTPGRVFDMLDKGYLRVDNLKLFILDEADEMLSRGFKVQ 193
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 126643927 194 IHDIFKKLPQDV--------------------QVALFSATMPNEILHLTTQFMRDP 229
Cdd:cd17945 161 VTKILDAMPVSNkkpdteeaeklaasgkhryrQTMMFTATMPPAVEKIAKGYLRRP 216
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
42-229 |
2.30e-41 |
|
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: 145.03 E-value: 2.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 42 LLRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKI------DYSLNACQVLLLAPTRELAQQI 115
Cdd:cd17961 5 LLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlkakaeSGEEQGTRALILVPTRELAQQV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 116 QKVALALGDYCE--LRCHACVGGTSVRDDMNKLKSGVHMVVGTPGRVFDMLDKGYLRV-DNLKLFILDEADEMLSRGFKV 192
Cdd:cd17961 85 SKVLEQLTAYCRkdVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLlSTLKYLVIDEADLVLSYGYEE 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 126643927 193 QIHDIFKKLPQDVQVALFSATMPNEILHLTTQFMRDP 229
Cdd:cd17961 165 DLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNP 201
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
42-229 |
8.21e-41 |
|
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts with several spliceosomal proteins and may recognize the bacterial second messengers cyclic di-GMP and cyclic di-AMP, resulting in the induction of genes involved in the innate immune response. Diseases associated with DDX41 include "myeloproliferative/lymphoproliferative neoplasms, familial" and "Ddx41-related susceptibility to familial myeloproliferative/lymphoproliferative neoplasms". DDX41 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350709 [Multi-domain] Cd Length: 206 Bit Score: 143.63 E-value: 8.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 42 LLRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIA----ALQKiDYSLNACQ-----VLLLAPTRELA 112
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPlimfALEQ-EKKLPFIKgegpyGLIVCPSRELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 113 QQIQKV------ALALGDYCELRCHACVGGTSVRDDMNKLKSGVHMVVGTPGRVFDMLDKGYLRVDNLKLFILDEADEML 186
Cdd:cd17951 80 RQTHEVieyyckALQEGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 126643927 187 SRGFKVQIHDIFKKLPQDVQVALFSATMPNEILHLTTQFMRDP 229
Cdd:cd17951 160 DMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKP 202
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
43-213 |
1.13e-40 |
|
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein and is activated by Myc protein. DDX18 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350700 [Multi-domain] Cd Length: 198 Bit Score: 142.88 E-value: 1.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 43 LRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKIdYSL-----NACQVLLLAPTRELAQQIQK 117
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELL-YKLkfkprNGTGVIIISPTRELALQIYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 118 VALALGDYCELRCHACVGGTSVRDDMNKLKSGVHMVVGTPGRVFDMLD--KGYLrVDNLKLFILDEADEMLSRGFKVQIH 195
Cdd:cd17942 81 VAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQntKGFL-YKNLQCLIIDEADRILEIGFEEEMR 159
|
170
....*....|....*...
gi 126643927 196 DIFKKLPQDVQVALFSAT 213
Cdd:cd17942 160 QIIKLLPKRRQTMLFSAT 177
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
36-232 |
3.01e-40 |
|
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: 142.52 E-value: 3.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 36 LNLEGDLLRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKIDYSLNACQ-----VLLLAPTRE 110
Cdd:cd17953 17 CGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVKPgegpiGLIMAPTRE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 111 LAQQIQKVALALGDYCELRCHACVGGTSVRDDMNKLKSGVHMVVGTPGRVFDMLDKGYLRVDNLK---LFILDEADEMLS 187
Cdd:cd17953 97 LALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNGRVTNLRrvtYVVLDEADRMFD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 126643927 188 RGFKVQIHDIFKKLPQDVQVALFSATMPNEILHLTTQFMRDPKRI 232
Cdd:cd17953 177 MGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
42-232 |
4.13e-40 |
|
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: 141.40 E-value: 4.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 42 LLRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAAL-----QKIDYSLNACQVLLLAPTRELAQQIQ 116
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLvhimdQRELEKGEGPIAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 117 KVALALGDYCELRCHACVGGTSVRDDMNKLKSGVHMVVGTPGRVFDMLDKGYLRVDNLKLFILDEADEMLSRGFKVQIHD 196
Cdd:cd17952 81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 126643927 197 IFKKLPQDVQVALFSATMPNEILHLTTQFMRDPKRI 232
Cdd:cd17952 161 IVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
30-240 |
7.68e-40 |
|
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: 141.70 E-value: 7.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 30 VECFEALNLEGDLLRGIFAYGFEKPSAIQQRGIKPILDG--YDTIGQAQSGTGKTATFVIAALQKIDYSLNACQVLLLAP 107
Cdd:cd18048 17 VKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLSP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 108 TRELAQQIQKVALALGDYC-------ELRCHACVGGTSVRddmnklksgVHMVVGTPGRVFDMLDKGYL-RVDNLKLFIL 179
Cdd:cd18048 97 TFELALQTGKVVEEMGKFCvgiqviyAIRGNRPGKGTDIE---------AQIVIGTPGTVLDWCFKLRLiDVTNISVFVL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126643927 180 DEADEMLS-RGFKVQIHDIFKKLPQDVQVALFSATMPNEILHLTTQFMRDPKRILVKQEELT 240
Cdd:cd18048 168 DEADVMINvQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
42-232 |
8.31e-40 |
|
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: 140.79 E-value: 8.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 42 LLRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKI-----DYSLNACQVLLLAPTRELAQQIQ 116
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrkaNLKKGQVGALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 117 KVALALGDYC--ELRCHACVGGTSVRDDMNKLK-SGVHMVVGTPGRVFDMLDKGYLRVD--NLKLFILDEADEMLSRGFK 191
Cdd:cd17960 81 EVLQSFLEHHlpKLKCQLLIGGTNVEEDVKKFKrNGPNILVGTPGRLEELLSRKADKVKvkSLEVLVLDEADRLLDLGFE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 126643927 192 VQIHDIFKKLPQDVQVALFSATMPNEILHLTTQFMRDPKRI 232
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
42-234 |
6.90e-39 |
|
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: 138.11 E-value: 6.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 42 LLRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKIDYSLNAC--QVLLLAPTRELAQQIQKVA 119
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKKglRALILAPTRELASQIYREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 120 LALGDYCELRCHACVGGTSVR-DDMNKLKSGVHMVVGTPGRVFDMLDKGYLRVDNLKLFILDEADEMLSRGFKVQIHDIF 198
Cdd:cd17957 81 LKLSKGTGLRIVLLSKSLEAKaKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEIL 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 126643927 199 KKLPQ-DVQVALFSATMPNEILHLTTQFMRDPKRILV 234
Cdd:cd17957 161 AACTNpNLQRSLFSATIPSEVEELARSVMKDPIRIIV 197
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
29-228 |
1.28e-38 |
|
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, G17P1, or HUMP68) is involved in pathways that include the alteration of RNA structures, plays a role as a coregulator of transcription, a regulator of splicing, and in the processing of small noncoding RNAs. It synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. Dysregulation of this gene may play a role in cancer development. DDX5 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350807 [Multi-domain] Cd Length: 234 Bit Score: 138.60 E-value: 1.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 29 IVECFEAlNLEGDLLRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKIDYSL-----NACQVL 103
Cdd:cd18049 23 VLNFYEA-NFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPflergDGPICL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 104 LLAPTRELAQQIQKVALALGDYCELRCHACVGGTSVRDDMNKLKSGVHMVVGTPGRVFDMLDKGYLRVDNLKLFILDEAD 183
Cdd:cd18049 102 VLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEAD 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 126643927 184 EMLSRGFKVQIHDIFKKLPQDVQVALFSATMPNEILHLTTQFMRD 228
Cdd:cd18049 182 RMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKD 226
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
43-234 |
1.40e-38 |
|
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: 137.42 E-value: 1.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 43 LRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKIdY-----SLNACQVLLLAPTRELAQQIQK 117
Cdd:cd17941 2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKL-YrerwtPEDGLGALIISPTRELAMQIFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 118 VALALGDYCELRCHACVGGTSVRDDMNKLkSGVHMVVGTPGRVFDMLDKG-YLRVDNLKLFILDEADEMLSRGFKVQIHD 196
Cdd:cd17941 81 VLRKVGKYHSFSAGLIIGGKDVKEEKERI-NRMNILVCTPGRLLQHMDETpGFDTSNLQMLVLDEADRILDMGFKETLDA 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 126643927 197 IFKKLPQDVQVALFSATMPNEILHLTTQFMRDPKRILV 234
Cdd:cd17941 160 IVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
33-229 |
2.34e-38 |
|
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350696 [Multi-domain] Cd Length: 204 Bit Score: 137.07 E-value: 2.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 33 FEALNLEGDLLRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKIdyslnacQVLLLAPTRELA 112
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV-------VALILEPSRELA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 113 QQIQKVALALGDYCE---LRCHACVGGTSVRDDMNKLKSGVHMVVGTPGRVFDMLDKGYLRVDNLKLFILDEADEMLSRG 189
Cdd:cd17938 74 EQTYNCIENFKKYLDnpkLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 126643927 190 FKVQIHDIFKKLPQ------DVQVALFSATMPN-EILHLTTQFMRDP 229
Cdd:cd17938 154 NLETINRIYNRIPKitsdgkRLQVIVCSATLHSfEVKKLADKIMHFP 200
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
12-228 |
5.24e-38 |
|
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: 137.48 E-value: 5.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 12 ENVQVASTGEiesNYDEIVECFEALNLeGDLLRG-IFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAAL 90
Cdd:cd18051 5 EDIPVEATGE---NCPPHIETFSDLDL-GEIIRNnIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 91 QKI--------------------DYSLNacqvLLLAPTRELAQQIQKVALALGdYCElRCHACV--GGTSVRDDMNKLKS 148
Cdd:cd18051 81 SQIyeqgpgeslpsesgyygrrkQYPLA----LVLAPTRELASQIYDEARKFA-YRS-RVRPCVvyGGADIGQQMRDLER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 149 GVHMVVGTPGRVFDMLDKGYLRVDNLKLFILDEADEMLSRGFKVQIHDIFKK--LPQ--DVQVALFSATMPNEILHLTTQ 224
Cdd:cd18051 155 GCHLLVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPtgERQTLMFSATFPKEIQMLARD 234
|
....
gi 126643927 225 FMRD 228
Cdd:cd18051 235 FLDN 238
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
256-365 |
8.12e-37 |
|
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: 8.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 256 WKMDTLIDLYETLTIVQAIIYCNTRRRVDqLTKQMRERDFTCSSMHGDMDQKDREVIMRQFRSGSSRVLITTDLLARGID 335
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 126643927 336 VQQVSLVINYDLPVSPETYIHRIGRSGRFG 365
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
42-229 |
1.80e-35 |
|
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: 129.12 E-value: 1.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 42 LLRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKIDYSL------NACQVLLLAPTRELAQQI 115
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPipreqrNGPGVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 116 QkvalalgDYCELRCH-----ACVGGTSVRDD-MNKLKSGVHMVVGTPGRVFDMLDKGYLRVDNLKLFILDEADEMLSRG 189
Cdd:cd17958 81 E-------AECSKYSYkglksVCVYGGGNRNEqIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 126643927 190 FKVQIHDIFKKLPQDVQVALFSATMPNEILHLTTQFMRDP 229
Cdd:cd17958 154 FEPQIRKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDP 193
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
51-232 |
3.00e-35 |
|
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: 130.90 E-value: 3.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 51 FEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKIDYSL-----NACQVLLLAPTRELAQQIQKVALALGDY 125
Cdd:cd18050 82 FKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPylergDGPICLVLAPTRELAQQVQQVADDYGKS 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 126 CELRCHACVGGTSVRDDMNKLKSGVHMVVGTPGRVFDMLDKGYLRVDNLKLFILDEADEMLSRGFKVQIHDIFKKLPQDV 205
Cdd:cd18050 162 SRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDR 241
|
170 180
....*....|....*....|....*..
gi 126643927 206 QVALFSATMPNEILHLTTQFMRDPKRI 232
Cdd:cd18050 242 QTLMWSATWPKEVRQLAEDFLRDYVQI 268
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
57-227 |
1.28e-32 |
|
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and nucleolar RNA helicase 2) is an RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II. It promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) and binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs. DDX50 (also called Gu-Beta, Nucleolar Protein Gu2, and malignant cell derived RNA helicase). DDX21 and DDX50 have similar genomic structures and are in tandem orientation on chromosome 10, suggesting that the two genes arose by gene duplication in evolution. Diseases associated with DDX21 include stomach disease and cerebral creatine deficiency syndrome 3. Diseases associated with DDX50 include rectal disease. Both are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. Their name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.
Pssm-ID: 350702 [Multi-domain] Cd Length: 202 Bit Score: 121.88 E-value: 1.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 57 IQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKIDYSLN------ACQVLLLAPTRELAQQIQKVALALGDYCELRC 130
Cdd:cd17944 16 IQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQprkrgrAPKVLVLAPTRELANQVTKDFKDITRKLSVAC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 131 HacVGGTSVRDDMNKLKSGVHMVVGTPGRVFDMLDKGYLRVDNLKLFILDEADEMLSRGFKVQIHDI----FKKLPQD-V 205
Cdd:cd17944 96 F--YGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEIlsvsYKKDSEDnP 173
|
170 180
....*....|....*....|..
gi 126643927 206 QVALFSATMPNEILHLTTQFMR 227
Cdd:cd17944 174 QTLLFSATCPDWVYNVAKKYMK 195
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
284-365 |
9.17e-31 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 112.69 E-value: 9.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 284 DQLTKQMRERDFTCSSMHGDMDQKDREVIMRQFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPVSPETYIHRIGRSGR 363
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 126643927 364 FG 365
Cdd:smart00490 81 AG 82
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
50-232 |
1.15e-30 |
|
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: 116.92 E-value: 1.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 50 GFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATF---VIAALQKIDYSLN---ACQVLLLAPTRELAQQIQKVALALG 123
Cdd:cd17949 10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYllpIIQRLLSLEPRVDrsdGTLALVLVPTRELALQIYEVLEKLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 124 DYCE-LRCHACVGGTSVRDDMNKLKSGVHMVVGTPGRVFDMLDK-GYLRVDNLKLFILDEADEMLSRGFKVQIHDIFKKL 201
Cdd:cd17949 90 KPFHwIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNtQSFDVSNLRWLVLDEADRLLDMGFEKDITKILELL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 126643927 202 -------------PQDVQVALFSATMPNEILHLTTQFMRDPKRI 232
Cdd:cd17949 170 ddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
42-214 |
2.45e-30 |
|
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: 116.57 E-value: 2.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 42 LLRGIFAYGFEKPSAIQQRGIKP-ILDGYDTIGQAQSGTGKTATFVIAALQKI---------DYSLNACQVLLLAPTREL 111
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAaIRDGKDVIGAAETGSGKTLAFGIPILERLlsqkssngvGGKQKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 112 AQQIQKVALALGDYCELRCHACVGGTSVRDDMNKLKSGVHMVVGTPGRVFDMLDKG--YL-RVDNLKLFILDEADEMLSR 188
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGneHLaNLKSLRFLVLDEADRMLEK 160
|
170 180 190
....*....|....*....|....*....|....
gi 126643927 189 G-FKvQIHDIFKKLP-------QDVQVALFSATM 214
Cdd:cd17946 161 GhFA-ELEKILELLNkdragkkRKRQTFVFSATL 193
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
33-232 |
2.23e-29 |
|
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: 113.28 E-value: 2.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 33 FEALNLEGDLLRGIFAYGFEKPSAIQQRGIKPIL--DGYDTIGQAQSGTGKTATFVIAALQKIDYSLNACQVLLLAPTRE 110
Cdd:cd18047 3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLaePPQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 111 LAQQIQKVALALGDY-------CELRCHACVGGTSVRDdmnklksgvHMVVGTPGRVFDMLDKGYLrVD--NLKLFILDE 181
Cdd:cd18047 83 LALQTGKVIEQMGKFypelklaYAVRGNKLERGQKISE---------QIVIGTPGTVLDWCSKLKF-IDpkKIKVFVLDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 126643927 182 ADEML-SRGFKVQIHDIFKKLPQDVQVALFSATMPNEILHLTTQFMRDPKRI 232
Cdd:cd18047 153 ADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVI 204
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
49-220 |
1.92e-28 |
|
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: 111.30 E-value: 1.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 49 YGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKI-------DYSLNACQVLLLAPTRELAQQIQKVALA 121
Cdd:cd17948 8 QGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLlrykllaEGPFNAPRGLVITPSRELAEQIGSVAQS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 122 LGDYCELRCHACVGGTSVRDDMNKLKSGVHMVVGTPGRVFDMLDKGYLRVDNLKLFILDEADEMLSRGF---------KV 192
Cdd:cd17948 88 LTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFneklshflrRF 167
|
170 180 190
....*....|....*....|....*....|....*
gi 126643927 193 QIH----DIFKKLPQDVQVALFSATMP---NEILH 220
Cdd:cd17948 168 PLAsrrsENTDGLDPGTQLVLVSATMPsgvGEVLS 202
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
68-213 |
1.32e-19 |
|
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: 84.76 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 68 GYDTIGQAQSGTGKTATFVIAALQKIDysLNACQVLLLAPTRELAQQIQKVALALGDYcELRCHACVGGTSVRDDMNKLK 147
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLL--KKGKKVLVLVPTKALALQTAERLRELFGP-GIRVAVLVGGSSAEEREKNKL 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126643927 148 SGVHMVVGTPGRVF-DMLDKGYLRVDNLKLFILDEADEMLSRGFKVQIHD--IFKKLPQDVQVALFSAT 213
Cdd:cd00046 78 GDADIIIATPDMLLnLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDlaVRKAGLKNAQVILLSAT 146
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
37-378 |
6.42e-18 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 86.04 E-value: 6.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 37 NLEGDLLRGIFAYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKIDYSLNACqVLLLAPTRELAQ-QI 115
Cdd:COG1205 40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPGAT-ALYLYPTKALARdQL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 116 QKVAlALGDYCELRCHACV--GGTSvRDDMNKLKSGVHMVVGTPgrvfDMLDKGYLRVD--------NLKLFILDEADEM 185
Cdd:COG1205 119 RRLR-ELAEALGLGVRVATydGDTP-PEERRWIREHPDIVLTNP----DMLHYGLLPHHtrwarffrNLRYVVIDEAHTY 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 186 lsRG-FKVQIHDIFKKLPQ-------DVQVALFSATMPNEILHLTTQFMRD------------PKRILVKQEELTLEGIR 245
Cdd:COG1205 193 --RGvFGSHVANVLRRLRRicrhygsDPQFILASATIGNPAEHAERLTGRPvtvvdedgsprgERTFVLWNPPLVDDGIR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 246 QfYVGVEkdewkmdtLIDLYETLTI--VQAIIYCNTRRRVDQLTKQMRERDFTC------SSMHGDMDQKDREVIMRQFR 317
Cdd:COG1205 271 R-SALAE--------AARLLADLVRegLRTLVFTRSRRGAELLARYARRALREPdladrvAAYRAGYLPEERREIERGLR 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126643927 318 SGSSRVLITTDLLARGIDVQQVSLVINYDLPVSPETYIHRIGRSGRFGKKGVSInFVTDDD 378
Cdd:COG1205 342 SGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV-LVAGDD 401
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
273-373 |
8.31e-17 |
|
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: 76.48 E-value: 8.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 273 AIIYCNTRRRVDQLTKQMRERDFTCSSMHGDMDQKDREVIMRQFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPVSPE 352
Cdd:cd18794 33 GIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSME 112
|
90 100
....*....|....*....|.
gi 126643927 353 TYIHRIGRSGRFGKKGVSINF 373
Cdd:cd18794 113 SYYQESGRAGRDGLPSECILF 133
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
274-383 |
2.94e-16 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 80.18 E-value: 2.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 274 IIYCNTRRRVDQLTKQMRERDFTCSSMHGDMDQKDREVIMRQFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPVSPET 353
Cdd:COG0514 234 IVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEA 313
|
90 100 110
....*....|....*....|....*....|
gi 126643927 354 YIHRIGRSGRFGKKGVSINFVTDDDIVCLR 383
Cdd:COG0514 314 YYQEIGRAGRDGLPAEALLLYGPEDVAIQR 343
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
78-377 |
1.11e-15 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 78.91 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 78 GTGKT--ATFVIAALQKIDyslnacQVLLLAPTRELAQQIQKvalalgDYCELRCHACVGGtsvrddmNKLKSGVHMVVG 155
Cdd:COG1061 110 GTGKTvlALALAAELLRGK------RVLVLVPRRELLEQWAE------ELRRFLGDPLAGG-------GKKDSDAPITVA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 156 TPGRVFDMLDKGYLRvDNLKLFILDEADEMLSRGFKvqihDIFKKLPqdvqvalfsatmPNEILHLT-TQFMRDPKRILV 234
Cdd:COG1061 171 TYQSLARRAHLDELG-DRFGLVIIDEAHHAGAPSYR----RILEAFP------------AAYRLGLTaTPFRSDGREILL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 235 KQE-----ELTL-EGIRQFYVG-----------------------------VEKDEWKMDTLIDLYETLT-IVQAIIYCN 278
Cdd:COG1061 234 FLFdgivyEYSLkEAIEDGYLAppeyygirvdltderaeydalserlrealAADAERKDKILRELLREHPdDRKTLVFCS 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 279 TRRRVDQLTKQMRERDFTCSSMHGDMDQKDREVIMRQFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPVSPETYIHRI 358
Cdd:COG1061 314 SVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRL 393
|
330 340
....*....|....*....|..
gi 126643927 359 GR--SGRFGKKGVSI-NFVTDD 377
Cdd:COG1061 394 GRglRPAPGKEDALVyDFVGND 415
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
54-214 |
3.10e-14 |
|
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: 71.51 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 54 PSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKIdYSLNACQV--LLLAPTRELAQQIQKVALALGDYCELRCH 131
Cdd:cd17956 22 PWLLPSSKSTPPYRPGDLCVSAPTGSGKTLAYVLPIVQAL-SKRVVPRLraLIVVPTKELVQQVYKVFESLCKGTGLKVV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 132 ACVGGTSVRDDMNKLK--------SGVHMVVGTPGRVFDMLD--KGYLrVDNLKLFILDEADEMLSRGF----------- 190
Cdd:cd17956 101 SLSGQKSFKKEQKLLLvdtsgrylSRVDILVATPGRLVDHLNstPGFT-LKHLRFLVIDEADRLLNQSFqdwletvmkal 179
|
170 180 190
....*....|....*....|....*....|...
gi 126643927 191 ---------KVQIHDIFKKLPQDVQVALFSATM 214
Cdd:cd17956 180 grptapdlgSFGDANLLERSVRPLQKLLFSATL 212
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
34-388 |
6.17e-14 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 73.59 E-value: 6.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 34 EALNLEG---DLLRGIFAYGFEKPSaiQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKIDYSLnacqVL--LLAPT 108
Cdd:PRK11057 5 EVLNLESlakQVLQETFGYQQFRPG--QQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTL----VVspLISLM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 109 RELAQQIQKVALALgdycelrchACVGGTSVRDD----MNKLKSG-VHMVVGTPGRVF--DMLDKgyLRVDNLKLFILDE 181
Cdd:PRK11057 79 KDQVDQLLANGVAA---------ACLNSTQTREQqlevMAGCRTGqIKLLYIAPERLMmdNFLEH--LAHWNPALLAVDE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 182 AD-----------EMLSRGfkvQIHDIFKKLPQDVQVALFSATMPNEILHLTTqfMRDPkriLVKQEELTLEGIRqfYVG 250
Cdd:PRK11057 148 AHcisqwghdfrpEYAALG---QLRQRFPTLPFMALTATADDTTRQDIVRLLG--LNDP---LIQISSFDRPNIR--YTL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 251 VEKDEwKMDTLIDLYETLTIVQAIIYCNTRRRVDQLTKQMRERDFTCSSMHGDMDQKDREVIMRQFRSGSSRVLITTDLL 330
Cdd:PRK11057 218 VEKFK-PLDQLMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAF 296
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 331 ARGIDVQQVSLVINYDLPVSPETYIHRIGRSGRFGKKGVSINFVTDDDIVCLR------------DIERH 388
Cdd:PRK11057 297 GMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPADMAWLRrcleekpagqqqDIERH 366
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
75-232 |
4.61e-13 |
|
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: 68.56 E-value: 4.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 75 AQSGTGKTATFVIAAL-----QKIDYSLNACQ------------VLLLAPTRELAQQIQKVALALGDYCELRCH--ACVG 135
Cdd:cd17965 68 AETGSGKTLAYLAPLLdylkrQEQEPFEEAEEeyesakdtgrprSVILVPTHELVEQVYSVLKKLSHTVKLGIKtfSSGF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 136 GTSVRDDMNKLKSGVHMVVGTPGRVFDmldkgyLRVDNLKLF------ILDEADEMLSRGFKVQIHDIFKKLPQDVQVAL 209
Cdd:cd17965 148 GPSYQRLQLAFKGRIDILVTTPGKLAS------LAKSRPKILsrvthlVVDEADTLFDRSFLQDTTSIIKRAPKLKHLIL 221
|
170 180
....*....|....*....|...
gi 126643927 210 FSATMPNEILHLTTQFMRDPKRI 232
Cdd:cd17965 222 CSATIPKEFDKTLRKLFPDVVRI 244
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
259-360 |
5.42e-13 |
|
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: 65.69 E-value: 5.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 259 DTLIDLYETLTIVQAIIYCNTRRRVDQLTKQMRE-----RDFTCSSMHG----------DMDQKDREVIMRQFRSGSSRV 323
Cdd:cd18802 14 EILREYFPKTPDFRGIIFVERRATAVVLSRLLKEhpstlAFIRCGFLIGrgnssqrkrsLMTQRKQKETLDKFRDGELNL 93
|
90 100 110
....*....|....*....|....*....|....*..
gi 126643927 324 LITTDLLARGIDVQQVSLVINYDLPVSPETYIHRIGR 360
Cdd:cd18802 94 LIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR 130
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
257-371 |
1.82e-11 |
|
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: 61.34 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 257 KMDTLIDLYETLTIVQ--AIIYCNTRRRVDQLTKQMRERDFTCSSMHGDMDQKDREVIMRQFRSGSS--RVLITTDLLAR 332
Cdd:cd18793 12 KLEALLELLEELREPGekVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDirVFLLSTKAGGV 91
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 126643927 333 GIDVQQVSLVINYDLPVSPETYIHRIGRSGRFG-KKGVSI 371
Cdd:cd18793 92 GLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGqKKPVVV 131
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
272-369 |
2.83e-10 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 62.05 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 272 QAIIYCNTRRRVDQLTKQMRERDFTC------SSMHGD--MDQKDREVIMRQFRSGSSRVLITTDLLARGIDVQQVSLVI 343
Cdd:COG1111 355 RIIVFTQYRDTAEMIVEFLSEPGIKAgrfvgqASKEGDkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVI 434
|
90 100
....*....|....*....|....*..
gi 126643927 344 NYDlPV-SPETYIHRIGRSGRFGKKGV 369
Cdd:COG1111 435 FYE-PVpSEIRSIQRKGRTGRKREGRV 460
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
257-377 |
1.31e-09 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 59.85 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 257 KMDTLIDLYETLTIVQ--AIIYCNTRRRVDQLTKQMRERDFTCSSMHGDMDQKDREVIMRQFRSGSS--RVLITTDLLAR 332
Cdd:COG0553 534 KLEALLELLEELLAEGekVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEapVFLISLKAGGE 613
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 126643927 333 GIDVQQVSLVINYDLPVSPETYIHRIGRSGRFG-KKGVSI-NFVTDD 377
Cdd:COG0553 614 GLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGqTRDVQVyKLVAEG 660
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
58-389 |
1.62e-09 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 59.52 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 58 QQRGI-KPILDGYDTIGQAQSGTGKTATFVIAALQKIdysLNACQVLLLAPTRELAQQI------------QKVALALGD 124
Cdd:COG1204 27 QAEALeAGLLEGKNLVVSAPTASGKTLIAELAILKAL---LNGGKALYIVPLRALASEKyrefkrdfeelgIKVGVSTGD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 125 YcelrchacvggtsVRDDMNKLKSGVhmVVGTPGRVFDMLDKGYLRVDNLKLFILDEA----DEmlSRGFKVQ-IHDIFK 199
Cdd:COG1204 104 Y-------------DSDDEWLGRYDI--LVATPEKLDSLLRNGPSWLRDVDLVVVDEAhlidDE--SRGPTLEvLLARLR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 200 KLPQDVQVALFSATMPN--EIL------HLTTQFmRDpkrilVKQEELTL-EGIRQFYVGVEKDEwkmDTLIDLyeTLTI 270
Cdd:COG1204 167 RLNPEAQIVALSATIGNaeEIAewldaeLVKSDW-RP-----VPLNEGVLyDGVLRFDDGSRRSK---DPTLAL--ALDL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 271 V----QAIIYCNTRRRVDQLTKQMRER-DFTCSSM------------------------------------HGDMDQKDR 309
Cdd:COG1204 236 LeeggQVLVFVSSRRDAESLAKKLADElKRRLTPEereeleelaeellevseethtnekladclekgvafhHAGLPSELR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 310 EVIMRQFRSGSSRVLITTDLLARGI----------DVQQVSLVinydlPVSPETYIHRIGRSGRFGK--KGVSInfVTDD 377
Cdd:COG1204 316 RLVEDAFREGLIKVLVATPTLAAGVnlparrviirDTKRGGMV-----PIPVLEFKQMAGRAGRPGYdpYGEAI--LVAK 388
|
410
....*....|..
gi 126643927 378 DIVCLRDIERHY 389
Cdd:COG1204 389 SSDEADELFERY 400
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
271-371 |
1.81e-09 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 55.73 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 271 VQAIIYCNTRRRVDQLTKQMRERD-------FTCSSMHGDMDQKDREVIMRQFRSGSSRVLITTDLLARGIDVQQVSLVI 343
Cdd:cd18797 36 VKTIVFCRSRKLAELLLRYLKARLveegplaSKVASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVV 115
|
90 100
....*....|....*....|....*...
gi 126643927 344 NYDLPVSPETYIHRIGRSGRFGKKGVSI 371
Cdd:cd18797 116 LAGYPGSLASLWQQAGRAGRRGKDSLVI 143
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
268-375 |
3.19e-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: 53.09 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 268 LTIVQAIIYCNTRRRVDQLTKQMRerdftcssmhgdmdqkdrevimrqfrsgssrVLITTDLLARGIDVQQVSLVINYDL 347
Cdd:cd18785 1 VMVVKIIVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDP 49
|
90 100
....*....|....*....|....*...
gi 126643927 348 PVSPETYIHRIGRSGRFGKKGVSINFVT 375
Cdd:cd18785 50 PSSAASYIQRVGRAGRGGKDEGEVILFV 77
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
274-363 |
5.25e-09 |
|
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: 54.58 E-value: 5.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 274 IIYCNTRRRVDQLTKQMRERD--------FTCSsmHGDMDQKDREVIMRQFRSGSSRVLITTDLLARGIDVQQVSLVINY 345
Cdd:cd18796 42 LVFTNTRSQAERLAQRLRELCpdrvppdfIALH--HGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQI 119
|
90
....*....|....*...
gi 126643927 346 DLPVSPETYIHRIGRSGR 363
Cdd:cd18796 120 GSPKSVARLLQRLGRSGH 137
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
78-182 |
7.44e-09 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 55.35 E-value: 7.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 78 GTGKT--ATFVIAALQKIDYSL--NACQVLLLAPTRELAQQiQkvALALGDYCELRCHACVGGTSV----RDDMNKLKSG 149
Cdd:cd18034 26 GSGKTliAVMLIKEMGELNRKEknPKKRAVFLVPTVPLVAQ-Q--AEAIRSHTDLKVGEYSGEMGVdkwtKERWKEELEK 102
|
90 100 110
....*....|....*....|....*....|...
gi 126643927 150 VHMVVGTPGRVFDMLDKGYLRVDNLKLFILDEA 182
Cdd:cd18034 103 YDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
304-363 |
1.62e-08 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350188 [Multi-domain] Cd Length: 143 Bit Score: 53.13 E-value: 1.62e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 304 MDQKDREVIMRQFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPVSPETYIHRIGRSGR 363
Cdd:cd18801 74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
58-216 |
4.69e-08 |
|
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: 52.59 E-value: 4.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 58 QQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQKIDYSLNACqVLLLAPTRELAQ-QIQKVAlALGDYCEL--RCHACV 134
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDPGSR-ALYLYPTKALAQdQLRSLR-ELLEQLGLgiRVATYD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 135 GGTSVRDDMNKLKSGVHMVVGTPgrvfDMLDKGYLRVD--------NLKLFILDEAdEMLSRGFKVQIHDIFKKL----- 201
Cdd:cd17923 83 GDTPREERRAIIRNPPRILLTNP----DMLHYALLPHHdrwarflrNLRYVVLDEA-HTYRGVFGSHVALLLRRLrrlcr 157
|
170
....*....|....*..
gi 126643927 202 --PQDVQVALFSATMPN 216
Cdd:cd17923 158 ryGADPQFILTSATIGN 174
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
274-367 |
6.33e-08 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 54.90 E-value: 6.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 274 IIYCNTRRRVDQLTKQMRERDFTCSSMHGDMDQKDREVIMRQFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPVSPET 353
Cdd:PLN03137 684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEG 763
|
90
....*....|....
gi 126643927 354 YIHRIGRSGRFGKK 367
Cdd:PLN03137 764 YHQECGRAGRDGQR 777
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
176-367 |
3.70e-07 |
|
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: 51.66 E-value: 3.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 176 LFILDEADEMLS--RGFKVQIHDIFKKLpqDVQVALFSATMPNEIlhltTQFMRDpKRILVKQEELTLEGIRQFYVGVEK 253
Cdd:cd09639 126 LLIFDEVHFYDEytLALILAVLEVLKDN--DVPILLMSATLPKFL----KEYAEK-IGYVEENEPLDLKPNERAPFIKIE 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 254 DEWK-----MDTLIDLYetLTIVQAIIYCNTRRRVDQLTKQMRERDFTCSSM--HGDMDQKDR----EVIMRQFRSGSSR 322
Cdd:cd09639 199 SDKVgeissLERLLEFI--KKGGSVAIIVNTVDRAQEFYQQLKEKGPEEEIMliHSRFTEKDRakkeAELLLEFKKSEKF 276
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 126643927 323 VLITTdllargiDVQQVSLVINYDLPVS----PETYIHRIGRSGRFGKK 367
Cdd:cd09639 277 VIVAT-------QVIEASLDISVDVMITelapIDSLIQRLGRLHRYGEK 318
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
279-394 |
1.26e-06 |
|
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: 48.01 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 279 TRRRVDQLTKQMRERDFTCSSMHGDMDQKDREVIMRQFRSGSSRVLITTDLLARGIDVQQVSLVINYD-----LPVSPET 353
Cdd:cd18790 36 TKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDadkegFLRSETS 115
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 126643927 354 YIHRIGRSGR--FGKKGVSINFVTDDDIVCLRDIERHYNTQIE 394
Cdd:cd18790 116 LIQTIGRAARnvNGKVILYADKITDSMQKAIEETERRREIQME 158
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
272-376 |
1.56e-06 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350182 [Multi-domain] Cd Length: 154 Bit Score: 47.55 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 272 QAIIYCNTRRRVDQLTKQMRerdftCSSM-HGDMDQKDREVIMRQFRSGSSRVLITTDLLARGI----------DVQQVS 340
Cdd:cd18795 45 PVLVFCSSRKECEKTAKDLA-----GIAFhHAGLTREDRELVEELFREGLIKVLVATSTLAAGVnlpartviikGTQRYD 119
|
90 100 110
....*....|....*....|....*....|....*...
gi 126643927 341 LVINYDLPVSpeTYIHRIGRSGR--FGKKGVSInFVTD 376
Cdd:cd18795 120 GKGYRELSPL--EYLQMIGRAGRpgFDTRGEAI-IMTK 154
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
257-363 |
5.11e-06 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 48.72 E-value: 5.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 257 KMDTLIDLY-ETLTIVQ---AIIYCNTRRRVDQLTKQMRERDFTC------SSMHGD--MDQKDREVIMRQFRSGSSRVL 324
Cdd:PRK13766 348 KLEKLREIVkEQLGKNPdsrIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDkgMSQKEQIEILDKFRAGEFNVL 427
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 126643927 325 ITTDLLARGIDVQQVSLVINYDlPVSPET-YIHRIGRSGR 363
Cdd:PRK13766 428 VSTSVAEEGLDIPSVDLVIFYE-PVPSEIrSIQRKGRTGR 466
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
74-156 |
6.42e-06 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 46.26 E-value: 6.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 74 QAQSGTGKTATFVIAALqkiDYSLNACQVLLLAPTRELAQQIQKVALALgdYCELRCHACVGGTSvrddmNKLKSGVHMV 153
Cdd:cd17918 42 SGDVGSGKTLVALGAAL---LAYKNGKQVAILVPTEILAHQHYEEARKF--LPFINVELVTGGTK-----AQILSGISLL 111
|
...
gi 126643927 154 VGT 156
Cdd:cd17918 112 VGT 114
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
295-362 |
8.18e-06 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 48.38 E-value: 8.18e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126643927 295 FTCSSMHGDMDQKDREVIMRQFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPVSPETYIHRIGRSG 362
Cdd:PRK09751 302 FIARSHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
|
|
| SF2_C_priA |
cd18804 |
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ... |
306-395 |
8.36e-05 |
|
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: 43.77 E-value: 8.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 306 QKDREVIMRQFRSGSSRVLITTDLLARGIDVQQVSLV--------INY-DLPVSPETY--IHRI-GRSGRFGKKGVSI-- 371
Cdd:cd18804 130 KGALEKLLDQFERGEIDILIGTQMIAKGLDFPNVTLVgilnadsgLNSpDFRASERAFqlLTQVsGRAGRGDKPGKVIiq 209
|
90 100
....*....|....*....|....*..
gi 126643927 372 NFVTDDDI---VCLRDIERHYNTQIEE 395
Cdd:cd18804 210 TYNPEHPLiqaAKEEDYEAFYEEELAE 236
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
225-363 |
1.16e-04 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 42.33 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 225 FMRDPKRILVKQEELTLEGiRQFYVgvekdewkMDTLIDLYETLTIVQAIIYCNtrrrvdQLTKQMRErDFTCSSMHGDM 304
Cdd:cd18811 8 FHTRLDKVYEFVREEIAKG-RQAYV--------IYPLIEESEKLDLKAAVAMYE------YLKERFRP-ELNVGLLHGRL 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126643927 305 DQKDREVIMRQFRSGSSRVLITTDLLARGIDVQQVSLVINYDlpvsPETY----IHRI-GRSGR 363
Cdd:cd18811 72 KSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIED----AERFglsqLHQLrGRVGR 131
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
270-360 |
2.20e-04 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350186 [Multi-domain] Cd Length: 116 Bit Score: 40.62 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 270 IVQAIIYCNTRRRVDQLTKQMRERDFTCSSMHGD--MDQKDREVIMRQF-RSGSSRVLITTDLLARGIDVQQVSLVInYD 346
Cdd:cd18799 6 EIKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDysDRERGDEALILLFfGELKPPILVTVDLLTTGVDIPEVDNVV-FL 84
|
90
....*....|....*
gi 126643927 347 LPV-SPETYIHRIGR 360
Cdd:cd18799 85 RPTeSRTLFLQMLGR 99
|
|
| CMS1 |
pfam14617 |
U3-containing 90S pre-ribosomal complex subunit; This is a family of fungal and plant ... |
75-180 |
8.86e-04 |
|
U3-containing 90S pre-ribosomal complex subunit; This is a family of fungal and plant CMS1-like proteins. The family has similarity to the DEAD-box helicases.
Pssm-ID: 373164 Cd Length: 250 Bit Score: 40.62 E-value: 8.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 75 AQSGTGKTATFVIAALQKIDyslnacqvlLLAPTRELAQQIQKVALALGDYCELRCHAcvggTSVRddmnklKSGVHMVV 154
Cdd:pfam14617 120 KSNGSPHTLVLTIAALRAAD---------VLRPLKKLQTKGFKVAKLFAKHIKLEEHI----TYCK------ASRIGIGV 180
|
90 100
....*....|....*....|....*.
gi 126643927 155 GTPGRVFDMLDKGYLRVDNLKLFILD 180
Cdd:pfam14617 181 GTPGRIADLLENESLSVDNLKYIILD 206
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
75-216 |
1.02e-03 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 39.94 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 75 AQSGTGKTATFVIAALQKIdySLNACQVLLLAPTRELAQQI----QKVALALGDYCELrchacVGGTSVRDDMNKLKSGV 150
Cdd:cd17921 24 APTSSGKTLIAELAILRAL--ATSGGKAVYIAPTRALVNQKeadlRERFGPLGKNVGL-----LTGDPSVNKLLLAEADI 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126643927 151 hmVVGTPGRVFDMLDKG-YLRVDNLKLFILDEA----DEmlSRGFKVQihDIFKKLPQ---DVQVALFSATMPN 216
Cdd:cd17921 97 --LVATPEKLDLLLRNGgERLIQDVRLVVVDEAhligDG--ERGVVLE--LLLSRLLRinkNARFVGLSATLPN 164
|
|
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
78-156 |
1.55e-03 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 40.80 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 78 GTGKTATFVIAALQKIDyslNACQVLLLAPTRELAQQ----IQKVALALGdyceLRCHACVGGTSV---RDDMNKLKSG- 149
Cdd:COG1200 290 GSGKTVVALLAMLAAVE---AGYQAALMAPTEILAEQhyrsLSKLLEPLG----IRVALLTGSTKAkerREILAALASGe 362
|
....*..
gi 126643927 150 VHMVVGT 156
Cdd:COG1200 363 ADIVVGT 369
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
78-336 |
1.60e-03 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 40.52 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 78 GTGKTATFVIAALQKIDyslNACQVLLLAPTRELAQQIqkvALALGDYCE---LRCHACVGGTSV--RDDM-NKLKSG-V 150
Cdd:PRK10917 292 GSGKTVVAALAALAAIE---AGYQAALMAPTEILAEQH---YENLKKLLEplgIRVALLTGSLKGkeRREIlEAIASGeA 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 151 HMVVGT-----PGRVFdmldkgylrvDNLKLFILDEademlsrgfkvQiH-------DIFKKLPQDVQVALFSAT----- 213
Cdd:PRK10917 366 DIVIGThaliqDDVEF----------HNLGLVIIDE-----------Q-HrfgveqrLALREKGENPHVLVMTATpiprt 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 214 ----------------MPneilhlttqFMRDP-KRILVKQEELT--LEGI-------RQFYVG---VEKDEwKMD--TLI 262
Cdd:PRK10917 424 lamtaygdldvsvideLP---------PGRKPiTTVVIPDSRRDevYERIreeiakgRQAYVVcplIEESE-KLDlqSAE 493
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126643927 263 DLYETLtivqaiiycntrrrvdqltkQMRERDFTCSSMHGDMDQKDREVIMRQFRSGSSRVLITTDLLARGIDV 336
Cdd:PRK10917 494 ETYEEL--------------------QEAFPELRVGLLHGRMKPAEKDAVMAAFKAGEIDILVATTVIEVGVDV 547
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
274-362 |
2.15e-03 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 40.47 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 274 IIYCNTRRRVDQLTKQMRER--DFTCSSM--HGDMDQKDREVIMRQFRSGSSRVLITT---DLlarGIDVQQVSLVINYD 346
Cdd:COG1201 276 LVFTNTRSQAERLFQRLNELnpEDALPIAahHGSLSREQRLEVEEALKAGELRAVVATsslEL---GIDIGDVDLVIQVG 352
|
90
....*....|....*.
gi 126643927 347 LPVSPETYIHRIGRSG 362
Cdd:COG1201 353 SPKSVARLLQRIGRAG 368
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
41-220 |
4.00e-03 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 38.28 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 41 DLLRGIFayGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALqkidysLNACQVLLLAPTRELAQ-QIQKVA 119
Cdd:cd17920 2 QILKEVF--GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPAL------LLDGVTLVVSPLISLMQdQVDRLQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 120 lALGdyceLRChACVGGTS----VRDDMNKLKSG-VHMVVGTP-----GRVFDMLDKGYLRvDNLKLFILDEA------- 182
Cdd:cd17920 74 -QLG----IRA-AALNSTLspeeKREVLLRIKNGqYKLLYVTPerllsPDFLELLQRLPER-KRLALIVVDEAhcvsqwg 146
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 126643927 183 ----DEMLsrgfkvQIHDIFKKLPqDVQVALFSATMPNEILH 220
Cdd:cd17920 147 hdfrPDYL------RLGRLRRALP-GVPILALTATATPEVRE 181
|
|
| PRK05298 |
PRK05298 |
excinuclease ABC subunit UvrB; |
279-342 |
6.70e-03 |
|
excinuclease ABC subunit UvrB;
Pssm-ID: 235395 [Multi-domain] Cd Length: 652 Bit Score: 38.49 E-value: 6.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126643927 279 TRRRVDQLTKQMRERDFTCSSMHGDMDQKDREVIMRQFRSGSSRVLITTDLLARGIDVQQVSLV 342
Cdd:PRK05298 455 TKRMAEDLTDYLKELGIKVRYLHSDIDTLERVEIIRDLRLGEFDVLVGINLLREGLDIPEVSLV 518
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
300-380 |
8.66e-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: 36.86 E-value: 8.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126643927 300 MHGDMDQKDREVIMRQFRSGSSRVLITTDLLARGIDVQQVSLVINYDlpvsPETY----IHRI-GRSGRFGKKGVSInFV 374
Cdd:cd18792 66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIED----ADRFglsqLHQLrGRVGRGKHQSYCY-LL 140
|
....*.
gi 126643927 375 TDDDIV 380
Cdd:cd18792 141 YPDPKK 146
|
|
| |
