|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
20-406 |
0e+00 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 614.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 20 EGVIESNWNEIVDSFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLK 99
Cdd:PTZ00424 16 TGTIESNYDEIVDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 100 ATQALVLAPTRELAQQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMF 179
Cdd:PTZ00424 96 ACQALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLK-AGVHMVVGTPGRVYDMIDKRHLRVDDLKLF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 180 VLDEADEMLSRGFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRILVKKEELTLEGIRQFYINVEREEWK 259
Cdd:PTZ00424 175 ILDEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 260 LDTLCDLYETLTITQAVIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQ 339
Cdd:PTZ00424 255 FDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQ 334
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4503529 340 QVSLVINYDLPTNRENYIHRIGRGGRFGRKGVAINMVTEEDKRTLRDIETFYNTSIEEMPLNVADLI 406
Cdd:PTZ00424 335 QVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEVADYL 401
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
34-235 |
6.42e-149 |
|
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: 419.93 E-value: 6.42e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 34 FDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATQALVLAPTRELA 113
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 114 QQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQMeAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFK 193
Cdd:cd18046 81 QQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQA-GPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 4503529 194 DQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRIL 235
Cdd:cd18046 160 DQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRIL 201
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
33-400 |
5.32e-145 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 418.40 E-value: 5.32e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 33 SFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDL-KATQALVLAPTRE 111
Cdd:COG0513 3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRpRAPQALILAPTRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 112 LAQQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRG 191
Cdd:COG0513 83 LALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALK-RGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 192 FKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRILVKKEELTLEGIRQFYINVEREEwKLDTLCDLYETLT 271
Cdd:COG0513 162 FIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRD-KLELLRRLLRDED 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 272 ITQAVIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPT 351
Cdd:COG0513 241 PERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPE 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 4503529 352 NRENYIHRIgrggrfgrkgVAINMVTEEDKRTLRDIETFYNTSIEEMPL 400
Cdd:COG0513 321 DPEDYVHRIgrtgragaegTAISLVTPDERRLLRAIEKLIGQKIEEEEL 369
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
36-235 |
9.84e-135 |
|
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: 383.98 E-value: 9.84e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 36 DMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATQALVLAPTRELAQQ 115
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 116 IQKVVMALGDYMGASCHACIGGTNVRAEVQKLQMeAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFKDQ 195
Cdd:cd17939 81 IQKVVKALGDYMGVKVHACIGGTSVREDRRKLQY-GPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 4503529 196 IYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRIL 235
Cdd:cd17939 160 IYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRIL 199
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
34-235 |
3.10e-106 |
|
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: 311.71 E-value: 3.10e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 34 FDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATQALVLAPTRELA 113
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 114 QQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFK 193
Cdd:cd18045 81 VQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLD-YGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 4503529 194 DQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRIL 235
Cdd:cd18045 160 EQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRIL 201
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
33-401 |
1.07e-86 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 270.90 E-value: 1.07e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 33 SFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATQALVLAPTREL 112
Cdd:PRK11776 5 AFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTREL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 113 AQQIQKVVMALGDYMG-----ASChaciGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEM 187
Cdd:PRK11776 85 ADQVAKEIRRLARFIPnikvlTLC----GGVPMGPQIDSLE-HGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 188 LSRGFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRILVKKEElTLEGIRQFYINVEREEwKLDTLCDLY 267
Cdd:PRK11776 160 LDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTH-DLPAIEQRFYEVSPDE-RLPALQRLL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 268 ETLTITQAVIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINY 347
Cdd:PRK11776 238 LHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINY 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 4503529 348 DLPTNRENYIHRIGRGGRFGRKGVAINMVTEEDKRTLRDIETFYNTSIEEMPLN 401
Cdd:PRK11776 318 ELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLP 371
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
43-234 |
4.01e-85 |
|
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: 257.76 E-value: 4.01e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 43 LLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDL----KATQALVLAPTRELAQQIQK 118
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPkkkgRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 119 VVMALGDYMGASCHACIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFKDQIYD 198
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALK-KGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 4503529 199 IFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRI 234
Cdd:cd00268 160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
29-406 |
8.61e-77 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 249.77 E-value: 8.61e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 29 EIVDSFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATQALVLAP 108
Cdd:PRK11634 3 EFETTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 109 TRELAQQIQKVVMALGDYM-GASCHACIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEM 187
Cdd:PRK11634 83 TRELAVQVAEAMTDFSKHMrGVNVVALYGGQRYDVQLRALR-QGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 188 LSRGFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRILVKKEELTLEGIRQFYINVEREEwKLDTLCDLY 267
Cdd:PRK11634 162 LRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMR-KNEALVRFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 268 ETLTITQAVIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINY 347
Cdd:PRK11634 241 EAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNY 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 4503529 348 DLPTNRENYIHRIGRGGRFGRKGVAINMVTEEDKRTLRDIETFYNTSIEEMPLNVADLI 406
Cdd:PRK11634 321 DIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAELL 379
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
39-234 |
3.51e-67 |
|
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: 211.67 E-value: 3.51e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 39 LSESLLRGIYAYGFEKPSAIQQRAiLPCIKG---YDVIAQAQSGTGKTATFAISILQQIELDLKATQALVLAPTRELAQQ 115
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETA-LPLILSdppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 116 IQKVVMALGDYMGASCHACIGGTNVRAevqKLQMEApHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEML-SRGFKD 194
Cdd:cd17963 80 IGEVVEKMGKFTGVKVALAVPGNDVPR---GKKITA-QIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLdTQGHGD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 4503529 195 QIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRI 234
Cdd:cd17963 156 QSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
34-234 |
4.16e-64 |
|
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: 204.07 E-value: 4.16e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 34 FDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATQALVLAPTRELA 113
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 114 QQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFK 193
Cdd:cd17940 81 LQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLY-QTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 4503529 194 DQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRI 234
Cdd:cd17940 160 PIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
34-399 |
1.26e-63 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 211.31 E-value: 1.26e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 34 FDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQI-------ELDLKATQALVL 106
Cdd:PRK01297 89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLlqtpppkERYMGEPRALII 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 107 APTRELAQQIQKVVMALGDYMGASCHACIGGTNVraEVQKLQMEAPH--IIVGTPGRVFDMLNRRYLSPKYIKMFVLDEA 184
Cdd:PRK01297 169 APTRELVVQIAKDAAALTKYTGLNVMTFVGGMDF--DKQLKQLEARFcdILVATPGRLLDFNQRGEVHLDMVEVMVLDEA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 185 DEMLSRGFKDQIYDIFQKL--NSNTQVVLLSATMPSDVLEVTKKFMRDPIRILVKKEELTLEGIRQ-FYINVEREEWKLd 261
Cdd:PRK01297 247 DRMLDMGFIPQVRQIIRQTprKEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQhVYAVAGSDKYKL- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 262 tLCDLYETLTITQAVIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQV 341
Cdd:PRK01297 326 -LYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGI 404
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 4503529 342 SLVINYDLPTNRENYIHRIGRGGRFGRKGVAINMVTEEDKRTLRDIETFYNTSIE-EMP 399
Cdd:PRK01297 405 SHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKIScEMP 463
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
33-400 |
1.62e-61 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 205.43 E-value: 1.62e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 33 SFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELD------LKATQALVL 106
Cdd:PRK10590 2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRqphakgRRPVRALIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 107 APTRELAQQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADE 186
Cdd:PRK10590 82 TPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLR-GGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 187 MLSRGFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRILVKKEELTLEGIRQFYINVEREEwKLDTLCDL 266
Cdd:PRK10590 161 MLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKR-KRELLSQM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 267 YETLTITQAVIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVIN 346
Cdd:PRK10590 240 IGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVN 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 4503529 347 YDLPTNRENYIHRIGRGGRFGRKGVAINMVTEEDKRTLRDIETFYNTSIEEMPL 400
Cdd:PRK10590 320 YELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRIAI 373
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
34-388 |
4.37e-61 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 203.64 E-value: 4.37e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 34 FDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIeLDL---KATQA--LVLAP 108
Cdd:PRK11192 3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHL-LDFprrKSGPPriLILTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 109 TRELAQQIQKVVMALGDYMGASCHACIGGTNV--RAEVQKlqmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADE 186
Cdd:PRK11192 82 TRELAMQVADQARELAKHTHLDIATITGGVAYmnHAEVFS---ENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 187 MLSRGFKDQIYDIFQKLNSNTQVVLLSATMPSD-VLEVTKKFMRDPIRILVKKEELTLEGIRQFYINVEREEWKLDTLCD 265
Cdd:PRK11192 159 MLDMGFAQDIETIAAETRWRKQTLLFSATLEGDaVQDFAERLLNDPVEVEAEPSRRERKKIHQWYYRADDLEHKTALLCH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 266 LYETLTITQAVIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVI 345
Cdd:PRK11192 239 LLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVI 318
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 4503529 346 NYDLPTNRENYIHRIGRGGRFGRKGVAINMVTEEDKRTLRDIE 388
Cdd:PRK11192 319 NFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIE 361
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
43-234 |
2.48e-59 |
|
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: 191.32 E-value: 2.48e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 43 LLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATQALVLAPTRELAQQIQKVVMA 122
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 123 LGDYM-GASCHACIGGTNVRAEVQKLQmeAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFKDQIYDIFQ 201
Cdd:cd17943 81 IGKKLeGLKCEVFIGGTPVKEDKKKLK--GCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFS 158
|
170 180 190
....*....|....*....|....*....|...
gi 4503529 202 KLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRI 234
Cdd:cd17943 159 SLPKNKQVIAFSATYPKNLDNLLARYMRKPVLV 191
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
33-236 |
4.39e-58 |
|
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: 188.71 E-value: 4.39e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 33 SFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATQALVLAPTREL 112
Cdd:cd17950 3 GFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTREL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 113 AQQIQKVVMALGDYMGASCHACI-GGTNVRAEVQKLQMEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEML-SR 190
Cdd:cd17950 83 AFQISNEYERFSKYMPNVKTAVFfGGVPIKKDIEVLKNKCPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLeQL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 4503529 191 GFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRILV 236
Cdd:cd17950 163 DMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
33-387 |
1.86e-57 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 196.16 E-value: 1.86e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 33 SFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIEL-------DLKATQALV 105
Cdd:PLN00206 122 SFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTirsghpsEQRNPLAMV 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 106 LAPTRELAQQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEAD 185
Cdd:PLN00206 202 LTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQ-QGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVD 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 186 EMLSRGFKDQIYDIFQKLnSNTQVVLLSATMPSDVLEVTKKFMRDPIRILVKKEELTLEGIRQFYINVEREEWKLDtlcd 265
Cdd:PLN00206 281 CMLERGFRDQVMQIFQAL-SQPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQK---- 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 266 LYETLTITQ-----AVIFINTRRKVDWLTEKMH-ARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQ 339
Cdd:PLN00206 356 LFDILKSKQhfkppAVVFVSSRLGADLLANAITvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLL 435
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 4503529 340 QVSLVINYDLPTNRENYIHRIGRGGRFGRKGVAINMVTEEDKRTLRDI 387
Cdd:PLN00206 436 RVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPEL 483
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
56-223 |
5.50e-57 |
|
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: 184.37 E-value: 5.50e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 56 SAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATQALVLAPTRELAQQIQKVVMALGDYMGASCHACI 135
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 136 GGTNVRAEVQKLQmeAPHIIVGTPGRVFDML-NRRYLspKYIKMFVLDEADEMLSRGFKDQIYDIFQKLNSNTQVVLLSA 214
Cdd:pfam00270 81 GGDSRKEQLEKLK--GPDILVGTPGRLLDLLqERKLL--KNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSA 156
|
....*....
gi 4503529 215 TMPSDVLEV 223
Cdd:pfam00270 157 TLPRNLEDL 165
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
47-249 |
1.10e-55 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 182.31 E-value: 1.10e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 47 IYAYGFEKPSAIQQRAILPCIKGY-DVIAQAQSGTGKTATFAISILQQIeLDLKATQALVLAPTRELAQQIQKVVMALGD 125
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEAL-KRGKGGRVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 126 YMGASCHACIGGTNVRAEVQKLQMEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFKDQIYDIFQKLNS 205
Cdd:smart00487 80 SLGLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 4503529 206 NTQVVLLSATMPSDVLEVTKKFMRDPIRILVkkEELTLEGIRQF 249
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFIDV--GFTPLEPIEQF 201
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
33-400 |
1.87e-53 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 186.69 E-value: 1.87e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 33 SFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQI-------ELDLKATQALV 105
Cdd:PRK04537 10 TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlsrpalaDRKPEDPRALI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 106 LAPTRELAQQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNR-RYLSPKYIKMFVLDEA 184
Cdd:PRK04537 90 LAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQ-QGVDVIIATPGRLIDYVKQhKVVSLHACEICVLDEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 185 DEMLSRGFKDQIYDIFQKLNSNT--QVVLLSATMPSDVLEVTKKFMRDPIRILVKKEELTLEGIRQfYINVEREEWKLDT 262
Cdd:PRK04537 169 DRMFDLGFIKDIRFLLRRMPERGtrQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQ-RIYFPADEEKQTL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 263 LCDLYETLTITQAVIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVS 342
Cdd:PRK04537 248 LLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVK 327
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 4503529 343 LVINYDLPTNRENYIHRIGRGGRFGRKGVAINMVTEEDKRTLRDIETFYNTSIEEMPL 400
Cdd:PRK04537 328 YVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKIPVEPV 385
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
31-360 |
5.04e-53 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 184.98 E-value: 5.04e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 31 VDSFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATF----AISILQQIELDL-KATQALV 105
Cdd:PTZ00110 129 VVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFllpaIVHINAQPLLRYgDGPIVLV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 106 LAPTRELAQQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEAD 185
Cdd:PTZ00110 209 LAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALR-RGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEAD 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 186 EMLSRGFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRD-PIRILVKKEELTL-EGIRQfYINVEREEWKLDTL 263
Cdd:PTZ00110 288 RMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDLTAcHNIKQ-EVFVVEEHEKRGKL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 264 CDLYETLTI--TQAVIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQV 341
Cdd:PTZ00110 367 KMLLQRIMRdgDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDV 446
|
330
....*....|....*....
gi 4503529 342 SLVINYDLPTNRENYIHRI 360
Cdd:PTZ00110 447 KYVINFDFPNQIEDYVHRI 465
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
34-231 |
3.06e-52 |
|
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: 173.56 E-value: 3.06e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 34 FDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATQALVLAPTRELA 113
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 114 QQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKY---IKMFVLDEADEMLSR 190
Cdd:cd17955 81 YQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELS-KRPHIVVATPGRLADHLRSSDDTTKVlsrVKFLVLDEADRLLTG 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 4503529 191 GFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDP 231
Cdd:cd17955 160 SFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
33-234 |
3.52e-52 |
|
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: 173.27 E-value: 3.52e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 33 SFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATQALVLAPTREL 112
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 113 AQQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLqMEAPHIIVGTPGRVFDML-NRRYLSPKYIKMFVLDEADEMLSRG 191
Cdd:cd17954 81 AQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIAL-AKKPHVIVATPGRLVDHLeNTKGFSLKSLKFLVMDEADRLLNMD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 4503529 192 FKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRI 234
Cdd:cd17954 160 FEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
39-229 |
5.61e-51 |
|
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350722 [Multi-domain] Cd Length: 211 Bit Score: 170.46 E-value: 5.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 39 LSESLLRGIYAYGFEKPSAIQQRAILPCI-KGYDVIAQAQSGTGKTATFAISILQQIELDLKATQ-----ALVLAPTREL 112
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRrsgvsALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 113 AQQIQKVVMALGDYM-GASCHACIGGTNVRAEVQKLQMEAPHIIVGTPGRVFDMLnRRYLSPKY---IKMFVLDEADEML 188
Cdd:cd17964 81 ALQIAAEAKKLLQGLrKLRVQSAVGGTSRRAELNRLRRGRPDILVATPGRLIDHL-ENPGVAKAftdLDYLVLDEADRLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 4503529 189 SRGFKDQIYDIFQKLN----SNTQVVLLSATMPSDVLEVTKKFMR 229
Cdd:cd17964 160 DMGFRPDLEQILRHLPeknaDPRQTLLFSATVPDEVQQIARLTLK 204
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
34-395 |
3.96e-50 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 174.39 E-value: 3.96e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 34 FDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKT-----ATFAISILQQIELDLKATQ--ALVL 106
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTmafltATFHYLLSHPAPEDRKVNQprALIM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 107 APTRELAQQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADE 186
Cdd:PRK04837 90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLE-SGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 187 MLSRGFKDQIYDIFQKLNSNTQ--VVLLSATMPSDVLEVTKKFMRDPIRILVKKEELTLEGIRQ--FYINVEReewKLDT 262
Cdd:PRK04837 169 MFDLGFIKDIRWLFRRMPPANQrlNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEelFYPSNEE---KMRL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 263 LCDLYETLTITQAVIFINTRRKV----DWLTEKMHardfTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDV 338
Cdd:PRK04837 246 LQTLIEEEWPDRAIIFANTKHRCeeiwGHLAADGH----RVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHI 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 4503529 339 QQVSLVINYDLPTNRENYIHRIGRGGRFGRKGVAINMVTEEDKRTLRDIETFYNTSI 395
Cdd:PRK04837 322 PAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIGHSI 378
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
43-234 |
1.16e-48 |
|
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: 163.96 E-value: 1.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 43 LLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQI---ELDLKATQALVLAPTRELAQQIQKV 119
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLlyrPKKKAATRVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 120 VMALGDYMGASCHACIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDML-NRRYLSPKYIKMFVLDEADEMLSRGFKDQIYD 198
Cdd:cd17947 81 LQQLAQFTDITFALAVGGLSLKAQEAALR-ARPDIVIATPGRLIDHLrNSPSFDLDSIEILVLDEADRMLEEGFADELKE 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 4503529 199 IFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRI 234
Cdd:cd17947 160 ILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
39-232 |
9.85e-48 |
|
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: 161.60 E-value: 9.85e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 39 LSESLLRGIYAYGFEKPSAIQQRAIlPCI-KGYDVIAQAQSGTGKTATFAISILQQIeLDLKA-------TQALVLAPTR 110
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAI-PLAlEGKDILARARTGSGKTAAYALPIIQKI-LKAKAesgeeqgTRALILVPTR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 111 ELAQQIQKVVMALGDYMGASCHACIGGTNVRAEVQK-LQMEAPHIIVGTPGRVFDMLNRRYLSPK-YIKMFVLDEADEML 188
Cdd:cd17961 79 ELAQQVSKVLEQLTAYCRKDVRVVNLSASSSDSVQRaLLAEKPDIVVSTPARLLSHLESGSLLLLsTLKYLVIDEADLVL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 4503529 189 SRGFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPI 232
Cdd:cd17961 159 SYGYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
33-234 |
1.32e-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: 161.32 E-value: 1.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 33 SFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQieldLKA------TQALVL 106
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEK----LKAhsptvgARALIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 107 APTRELAQQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLqMEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADE 186
Cdd:cd17959 78 SPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEAL-ASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 4503529 187 MLSRGFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRI 234
Cdd:cd17959 157 LFEMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
33-230 |
2.07e-45 |
|
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: 156.11 E-value: 2.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 33 SFDDMNLSESLLRGIYAYGFEKPSAIQQRAIlPCI-KGYDVIAQAQSGTGKTATFAISILQQIELD---------LKAT- 101
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAI-PIIlAGRDLMACAQTGSGKTAAFLLPIISKLLEDgppsvgrgrRKAYp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 102 QALVLAPTRELAQQIQKVVMALGDYMGASCHACIGGTNVRAevQKLQMEAP-HIIVGTPGRVFDMLNRRYLSPKYIKMFV 180
Cdd:cd17967 80 SALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVH--QQLQLLRGcDILVATPGRLVDFIERGRISLSSIKFLV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 4503529 181 LDEADEMLSRGFKDQIYDIFQKLNS----NTQVVLLSATMPSDVLEVTKKFMRD 230
Cdd:cd17967 158 LDEADRMLDMGFEPQIRKIVEHPDMppkgERQTLMFSATFPREIQRLAADFLKN 211
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
246-361 |
4.34e-45 |
|
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: 152.28 E-value: 4.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 246 IRQFYINVEREEWKLDTLCDLYETLTITQAVIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRV 325
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 4503529 326 LITTDLLARGIDVQQVSLVINYDLPTNRENYIHRIG 361
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIG 116
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
43-236 |
6.26e-45 |
|
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: 154.28 E-value: 6.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 43 LLRGIYAYGFEKPSAIQQRAIlPCI-KGYDVIAQAQSGTGKTATFAISILQQIELDLKAT--QALVLAPTRELAQQIQKV 119
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAI-PILlHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKKglRALILAPTRELASQIYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 120 VMALGDYMGASCHACIGGTNVRAEVQKLQMEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFKDQIYDI 199
Cdd:cd17957 80 LLKLSKGTGLRIVLLSKSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEI 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 4503529 200 FQKL-NSNTQVVLLSATMPSDVLEVTKKFMRDPIRILV 236
Cdd:cd17957 160 LAACtNPNLQRSLFSATIPSEVEELARSVMKDPIRIIV 197
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
43-234 |
2.54e-44 |
|
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: 152.73 E-value: 2.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 43 LLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQI-----ELDLKATQALVLAPTRELAQQIQ 117
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrkaNLKKGQVGALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 118 KVVMALGDYMGA--SCHACIGGTNVRAEVQKLQMEAPHIIVGTPGRVFDMLNRRY--LSPKYIKMFVLDEADEMLSRGFK 193
Cdd:cd17960 81 EVLQSFLEHHLPklKCQLLIGGTNVEEDVKKFKRNGPNILVGTPGRLEELLSRKAdkVKVKSLEVLVLDEADRLLDLGFE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 4503529 194 DQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRI 234
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
39-234 |
1.25e-42 |
|
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: 149.06 E-value: 1.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 39 LSESLLRGIYAYGFEKPSAIQQRAIlPCI-KGYDVIAQAQSGTGKTATFAISILQQI--ELDLKATQ---ALVLAPTREL 112
Cdd:cd17953 19 LSEKVLDLIKKLGYEKPTPIQAQAL-PAImSGRDVIGIAKTGSGKTLAFLLPMFRHIkdQRPVKPGEgpiGLIMAPTREL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 113 AQQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQMEApHIIVGTPGRVFDML---NRRYLSPKYIKMFVLDEADEMLS 189
Cdd:cd17953 98 ALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGA-EIVVCTPGRMIDILtanNGRVTNLRRVTYVVLDEADRMFD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 4503529 190 RGFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRI 234
Cdd:cd17953 177 MGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
31-242 |
4.36e-41 |
|
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: 145.16 E-value: 4.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 31 VDSFDDMNLSESLLRGIYAYGFEKPSAIQQRAiLPCIKGY---DVIAQAQSGTGKTATFAISILQQIELDLKATQALVLA 107
Cdd:cd18048 17 VKSFEELHLKEELLRGIYAMGFNRPSKIQENA-LPMMLADppqNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 108 PTRELAQQIQKVVMALGDY-MGASCHACIGGTNVRaevQKLQMEApHIIVGTPGRVFD-MLNRRYLSPKYIKMFVLDEAD 185
Cdd:cd18048 96 PTFELALQTGKVVEEMGKFcVGIQVIYAIRGNRPG---KGTDIEA-QIVIGTPGTVLDwCFKLRLIDVTNISVFVLDEAD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 4503529 186 EMLS-RGFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRILVKKEELT 242
Cdd:cd18048 172 VMINvQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
43-234 |
5.38e-41 |
|
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: 144.38 E-value: 5.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 43 LLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQI----ELDLKATQ----ALVLAPTRELAQ 114
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYIsrlpPLDEETKDdgpyALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 115 QIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQMEApHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFKD 194
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGC-EILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 195 QIYDIFQKLNSNT--------------------QVVLLSATMPSDVLEVTKKFMRDPIRI 234
Cdd:cd17945 160 QVTKILDAMPVSNkkpdteeaeklaasgkhryrQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
33-229 |
8.27e-40 |
|
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: 142.80 E-value: 8.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 33 SFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQ-IELDLKAT--------QA 103
Cdd:cd18052 44 TFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGmMKEGLTASsfsevqepQA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 104 LVLAPTRELAQQIQKVVMALGDymGASCHACI--GGTNVRAEVQKLQMEApHIIVGTPGRVFDMLNRRYLSPKYIKMFVL 181
Cdd:cd18052 124 LIVAPTRELANQIFLEARKFSY--GTCIRPVVvyGGVSVGHQIRQIEKGC-HILVATPGRLLDFIGRGKISLSKLKYLIL 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 4503529 182 DEADEMLSRGFKDQIYDIFQKLNS----NTQVVLLSATMPSDVLEVTKKFMR 229
Cdd:cd18052 201 DEADRMLDMGFGPEIRKLVSEPGMpskeDRQTLMFSATFPEEIQRLAAEFLK 252
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
43-234 |
3.85e-39 |
|
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: 138.84 E-value: 3.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 43 LLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATQALVLAPTRELAQQIQKVVMA 122
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 123 LGDYMGASCHA-CIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFKDQIYDIFQ 201
Cdd:cd17962 81 LMKGLPPMKTAlLVGGLPLPPQLYRLQ-QGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILE 159
|
170 180 190
....*....|....*....|....*....|...
gi 4503529 202 KLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRI 234
Cdd:cd17962 160 NISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
43-234 |
5.72e-39 |
|
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: 138.32 E-value: 5.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 43 LLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIeLDLKATQ------ALVLAPTRELAQQI 116
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHI-MDQRELEkgegpiAVIVAPTRELAQQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 117 QKVVMALGDYMGASCHACIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFKDQI 196
Cdd:cd17952 80 YLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQ-EGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQV 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 4503529 197 YDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRI 234
Cdd:cd17952 159 RSIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
43-234 |
4.01e-37 |
|
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: 133.65 E-value: 4.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 43 LLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIeldlKATQ---------ALVLAPTRELA 113
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHI----NAQPplergdgpiVLVLAPTRELA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 114 QQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFK 193
Cdd:cd17966 77 QQIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLR-RGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 4503529 194 DQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRI 234
Cdd:cd17966 156 PQIRKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
44-236 |
6.35e-37 |
|
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: 133.18 E-value: 6.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 44 LRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQI------ELDlkATQALVLAPTRELAQQIQ 117
Cdd:cd17941 2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLyrerwtPED--GLGALIISPTRELAMQIF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 118 KVVMALGDYMGASCHACIGGTNVRAEvqKLQMEAPHIIVGTPGRVFDMLNRR-YLSPKYIKMFVLDEADEMLSRGFKDQI 196
Cdd:cd17941 80 EVLRKVGKYHSFSAGLIIGGKDVKEE--KERINRMNILVCTPGRLLQHMDETpGFDTSNLQMLVLDEADRILDMGFKETL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 4503529 197 YDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRILV 236
Cdd:cd17941 158 DAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
34-231 |
7.19e-37 |
|
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: 133.22 E-value: 7.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 34 FDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQqieldlkATQALVLAPTRELA 113
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQ-------IVVALILEPSRELA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 114 QQIQKVVMALGDYMGA---SCHACIGGTNVRAEVQKLQMEApHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSR 190
Cdd:cd17938 74 EQTYNCIENFKKYLDNpklRVALLIGGVKAREQLKRLESGV-DIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQ 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 4503529 191 GFKDQIYDIFQKLNSNT------QVVLLSATMPS-DVLEVTKKFMRDP 231
Cdd:cd17938 153 GNLETINRIYNRIPKITsdgkrlQVIVCSATLHSfEVKKLADKIMHFP 200
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
25-232 |
1.02e-36 |
|
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: 134.01 E-value: 1.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 25 SNWNEIVDSFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQI------ELDL 98
Cdd:cd18051 14 ENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIyeqgpgESLP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 99 KATQ----------ALVLAPTRELAQQIqkvvmalgdYMGASCHA-------CI--GGTNVRAEVQKLQmEAPHIIVGTP 159
Cdd:cd18051 94 SESGyygrrkqyplALVLAPTRELASQI---------YDEARKFAyrsrvrpCVvyGGADIGQQMRDLE-RGCHLLVATP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4503529 160 GRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFKDQIYDIFQKLN----SNTQVVLLSATMPSDVLEVTKKFMRDPI 232
Cdd:cd18051 164 GRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTmpptGERQTLMFSATFPKEIQMLARDFLDNYI 240
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
44-234 |
1.21e-36 |
|
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: 132.48 E-value: 1.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 44 LRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISIlqqIELDLK-------ATQALVLAPTRELAQQI 116
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPA---IELLYKlkfkprnGTGVIIISPTRELALQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 117 QKVVMALGDYMGASCHACIGGTNVRAEVQKLQMEAPhIIVGTPGRVFDML-NRRYLSPKYIKMFVLDEADEMLSRGFKDQ 195
Cdd:cd17942 79 YGVAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVN-ILVATPGRLLDHLqNTKGFLYKNLQCLIIDEADRILEIGFEEE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 4503529 196 IYDIFQKLNSNTQVVLLSATMPSDVLEVTK-KFMRDPIRI 234
Cdd:cd17942 158 MRQIIKLLPKRRQTMLFSATQTRKVEDLARiSLKKKPLYV 197
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
43-234 |
2.87e-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: 128.74 E-value: 2.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 43 LLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILqqIELDLKATQ--------ALVLAPTRELAQ 114
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGF--IHLDLQPIPreqrngpgVLVLTPTRELAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 115 QIQKVVMALgDYMGASChACIGGTNVRAEVQKLQMEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFKD 194
Cdd:cd17958 79 QIEAECSKY-SYKGLKS-VCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 4503529 195 QIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRI 234
Cdd:cd17958 157 QIRKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
51-234 |
1.83e-34 |
|
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1. DDX31 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350707 [Multi-domain] Cd Length: 214 Bit Score: 126.93 E-value: 1.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 51 GFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQI-ELDLKATQ-----ALVLAPTRELAQQIQKVVMALg 124
Cdd:cd17949 10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLlSLEPRVDRsdgtlALVLVPTRELALQIYEVLEKL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 125 dymGASCHAC-----IGGTNVRAEVQKLQMEAPhIIVGTPGRVFDML-NRRYLSPKYIKMFVLDEADEMLSRGFKDQIYD 198
Cdd:cd17949 89 ---LKPFHWIvpgylIGGEKRKSEKARLRKGVN-ILIATPGRLLDHLkNTQSFDVSNLRWLVLDEADRLLDMGFEKDITK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 4503529 199 IFQKLNSNT-------------QVVLLSATMPSDVLEVTKKFMRDPIRI 234
Cdd:cd17949 165 ILELLDDKRskaggekskpsrrQTVLVSATLTDGVKRLAGLSLKDPVYI 213
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
43-234 |
3.10e-33 |
|
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: 123.60 E-value: 3.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 43 LLRGIYAYGFEKPSAIQQRAIlPCI-KGYDVIAQAQSGTGKTATFAISIL-----QQIELDLKATQ---ALVLAPTRELA 113
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGL-PTIlSGRDMIGIAFTGSGKTLVFTLPLImfaleQEKKLPFIKGEgpyGLIVCPSRELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 114 QQIQKVV------MALGDYMGASCHACIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEM 187
Cdd:cd17951 80 RQTHEVIeyyckaLQEGGYPQLRCLLCIGGMSVKEQLEVIR-KGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 4503529 188 LSRGFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRI 234
Cdd:cd17951 159 IDMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
33-231 |
1.31e-32 |
|
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: 121.75 E-value: 1.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 33 SFDDMNLSESLLRGIYAYGFEKPSAIQQRAiLPCIKG---YDVIAQAQSGTGKTATFAISILQQIELDLKATQALVLAPT 109
Cdd:cd18047 2 SFEELRLKPQLLQGVYAMGFNRPSKIQENA-LPLMLAeppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 110 RELAQQIQKVVMALGD-YMGASCHACIGGTNVRAEVQKlqmeAPHIIVGTPGRVFD-MLNRRYLSPKYIKMFVLDEADEM 187
Cdd:cd18047 81 YELALQTGKVIEQMGKfYPELKLAYAVRGNKLERGQKI----SEQIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADVM 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 4503529 188 L-SRGFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDP 231
Cdd:cd18047 157 IaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
43-216 |
3.06e-32 |
|
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box protein, which shows little similarity to any of the other known human DEAD box proteins, but shows a high similarity to mouse Ddx24 at the amino acid level. MDM2 mediates nonproteolytic polyubiquitylation of the DEAD-Box RNA helicase DDX24. DDX24 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.
Pssm-ID: 350704 [Multi-domain] Cd Length: 235 Bit Score: 121.58 E-value: 3.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 43 LLRGIYAYGFEKPSAIQQRAILPCIK-GYDVIAQAQSGTGKTATFAISILQQIeLDLKAT----------QALVLAPTRE 111
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERL-LSQKSSngvggkqkplRALILTPTRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 112 LAQQIQKVVMALGDYMGASCHACIGGTNVRAEvQKLQMEAPHIIVGTPGRVFDMLNRR--YL-SPKYIKMFVLDEADEML 188
Cdd:cd17946 80 LAVQVKDHLKAIAKYTNIKIASIVGGLAVQKQ-ERLLKKRPEIVVATPGRLWELIQEGneHLaNLKSLRFLVLDEADRML 158
|
170 180 190
....*....|....*....|....*....|....*
gi 4503529 189 SRGFKDQIYDIFQKLNSNT-------QVVLLSATM 216
Cdd:cd17946 159 EKGHFAELEKILELLNKDRagkkrkrQTFVFSATL 193
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
58-229 |
3.59e-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: 120.72 E-value: 3.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 58 IQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDL------KATQALVLAPTRELAQQIQKVVMALGDYMGASC 131
Cdd:cd17944 16 IQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQqprkrgRAPKVLVLAPTRELANQVTKDFKDITRKLSVAC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 132 HacIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFKDQIYDIFQ---KLNS--N 206
Cdd:cd17944 96 F--YGGTPYQQQIFAIR-NGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSvsyKKDSedN 172
|
170 180
....*....|....*....|...
gi 4503529 207 TQVVLLSATMPSDVLEVTKKFMR 229
Cdd:cd17944 173 PQTLLFSATCPDWVYNVAKKYMK 195
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
43-226 |
4.74e-31 |
|
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: 118.62 E-value: 4.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 43 LLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQI-------ELDLKATQALVLAPTRELAQQ 115
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLlrykllaEGPFNAPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 116 IQKVVMALGDYMGASCHaCIGGTNVRAEVQKLQMEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFKDQ 195
Cdd:cd17948 81 IGSVAQSLTEGLGLKVK-VITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 4503529 196 IYDIFQK-------------LNSNTQVVLLSATMPSDVLEVTKK 226
Cdd:cd17948 160 LSHFLRRfplasrrsentdgLDPGTQLVLVSATMPSGVGEVLSK 203
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
258-361 |
1.08e-28 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 108.07 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 258 WKLDTLCDLYETLTITQAVIFINTRRKVD--WLTEKmhaRDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARG 335
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLEaeLLLEK---EGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77
|
90 100
....*....|....*....|....*.
gi 4503529 336 IDVQQVSLVINYDLPTNRENYIHRIG 361
Cdd:pfam00271 78 LDLPDVDLVINYDLPWNPASYIQRIG 103
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
31-234 |
1.26e-27 |
|
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: 109.33 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 31 VDSFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATQA-----LV 105
Cdd:cd18049 23 VLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGdgpicLV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 106 LAPTRELAQQIQKVVmalGDYmGASCH---ACI-GGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVL 181
Cdd:cd18049 103 LAPTRELAQQVQQVA---AEY-GRACRlksTCIyGGAPKGPQIRDLE-RGVEICIATPGRLIDFLEAGKTNLRRCTYLVL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 4503529 182 DEADEMLSRGFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRI 234
Cdd:cd18049 178 DEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHI 230
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
31-234 |
8.81e-27 |
|
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: 107.79 E-value: 8.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 31 VDSFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATQA-----LV 105
Cdd:cd18050 61 VFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGdgpicLV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 106 LAPTRELAQQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQmEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEAD 185
Cdd:cd18050 141 LAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLE-RGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEAD 219
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 4503529 186 EMLSRGFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRI 234
Cdd:cd18050 220 RMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQI 268
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
69-215 |
1.19e-24 |
|
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: 98.63 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 69 GYDVIAQAQSGTGKTATFAISILQqiELDLKATQALVLAPTRELAQQIQKVVMALGDyMGASCHACIGGTNVRAEVQKLQ 148
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALL--LLLKKGKKVLVLVPTKALALQTAERLRELFG-PGIRVAVLVGGSSAEEREKNKL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 149 MEAPhIIVGTPGRVFDMLNRRYLSPKY-IKMFVLDEADEMLSRGFKDQIYD--IFQKLNSNTQVVLLSAT 215
Cdd:cd00046 78 GDAD-IIIATPDMLLNLLLREDRLFLKdLKLIIVDEAHALLIDSRGALILDlaVRKAGLKNAQVILLSAT 146
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
286-360 |
9.50e-23 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 91.12 E-value: 9.50e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4503529 286 DWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPTNRENYIHRI 360
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRI 75
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
43-220 |
7.46e-20 |
|
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: 87.69 E-value: 7.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 43 LLRGIYAYGFEKPSAIQQR---AILPCIKGY------DVIAQAQSGTGKTATFAISILQQIeLDLKATQ--ALVLAPTRE 111
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAvipWLLPSSKSTppyrpgDLCVSAPTGSGKTLAYVLPIVQAL-SKRVVPRlrALIVVPTKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 112 LAQQIQKVVMALGDYMGASCHACIGGTNVRAEvQKLQMEAPH--------IIVGTPGRVFDMLNR-RYLSPKYIKMFVLD 182
Cdd:cd17956 80 LVQQVYKVFESLCKGTGLKVVSLSGQKSFKKE-QKLLLVDTSgrylsrvdILVATPGRLVDHLNStPGFTLKHLRFLVID 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 4503529 183 EADEMLSRGF--------------KDQIYDIFQKLN------SNTQVVLLSATMPSDV 220
Cdd:cd17956 159 EADRLLNQSFqdwletvmkalgrpTAPDLGSFGDANllersvRPLQKLLFSATLTRDP 216
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
38-350 |
8.83e-15 |
|
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: 76.03 E-value: 8.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 38 NLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATqALVLAPTRELAQ-QI 116
Cdd:COG1205 40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPGAT-ALYLYPTKALARdQL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 117 QKvVMALGDYMGA--SCHACIGGT--NVRAEVQklqmEAPHIIVGTPgrvfDMLNRRYLS--PKYIKMF------VLDEA 184
Cdd:COG1205 119 RR-LRELAEALGLgvRVATYDGDTppEERRWIR----EHPDIVLTNP----DMLHYGLLPhhTRWARFFrnlryvVIDEA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 185 DEMlsRG-FKDQIYDIFQKLN-------SNTQVVLLSATM--PS---------DVLEVTKK----------FMRDPIRIL 235
Cdd:COG1205 190 HTY--RGvFGSHVANVLRRLRricrhygSDPQFILASATIgnPAehaerltgrPVTVVDEDgsprgertfvLWNPPLVDD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 236 VKKEELTLEGIRQFYINVEREewkLDTLCdlyetltitqaviFINTRRKV----DWLTEKMHARDFT--VSAMHGDMDQK 309
Cdd:COG1205 268 GIRRSALAEAARLLADLVREG---LRTLV-------------FTRSRRGAellaRYARRALREPDLAdrVAAYRAGYLPE 331
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 4503529 310 ERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLP 350
Cdd:COG1205 332 ERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYP 372
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
59-345 |
1.31e-13 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 72.36 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 59 QQRAI-----LPCIKGYDVIAQAQSGTGKTaTFAISILQQIELDLKAtqaLVLAPTRELAQQIQKvvmalgdymgaschA 133
Cdd:COG1061 85 QQEALeallaALERGGGRGLVVAPTGTGKT-VLALALAAELLRGKRV---LVLVPRRELLEQWAE--------------E 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 134 CIGGTNVRAEVQKLQMEAPHIIVGTPGRVFDMLNRRYLSPKYiKMFVLDEADEMLSRGFKdQIYDIFQKlnsnTQVVLLS 213
Cdd:COG1061 147 LRRFLGDPLAGGGKKDSDAPITVATYQSLARRAHLDELGDRF-GLVIIDEAHHAGAPSYR-RILEAFPA----AYRLGLT 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 214 ATmP--SD------------VLEVT-KKFMRD----PIRILVKKEELTLEGIRQFYIN-------VEREEWKLDTLCDLY 267
Cdd:COG1061 221 AT-PfrSDgreillflfdgiVYEYSlKEAIEDgylaPPEYYGIRVDLTDERAEYDALSerlrealAADAERKDKILRELL 299
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4503529 268 ETLT-ITQAVIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVI 345
Cdd:COG1061 300 REHPdDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI 378
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
260-357 |
2.09e-11 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350189 [Multi-domain] Cd Length: 142 Bit Score: 61.45 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 260 LDTLCDLYETLTITQAVIFINTRRKV----DWLTEKMHARD-FTVSAMHG----------DMDQKERDVIMREFRSGSSR 324
Cdd:cd18802 13 IEILREYFPKTPDFRGIIFVERRATAvvlsRLLKEHPSTLAfIRCGFLIGrgnssqrkrsLMTQRKQKETLDKFRDGELN 92
|
90 100 110
....*....|....*....|....*....|...
gi 4503529 325 VLITTDLLARGIDVQQVSLVINYDLPTNRENYI 357
Cdd:cd18802 93 LLIATSVLEEGIDVPACNLVIRFDLPKTLRSYI 125
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
259-352 |
1.75e-09 |
|
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: 55.56 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 259 KLDTLCDLYETLTITQ--AVIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSS--RVLITTDLLAR 334
Cdd:cd18793 12 KLEALLELLEELREPGekVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDirVFLLSTKAGGV 91
|
90
....*....|....*...
gi 4503529 335 GIDVQQVSLVINYDLPTN 352
Cdd:cd18793 92 GLNLTAANRVILYDPWWN 109
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
72-234 |
1.77e-09 |
|
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: 57.77 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 72 VIAqAQSGTGKTATFAISILQQI-----------------ELDLKATQALVLAPTRELAQQIQKVVMALGDYMGASCHAC 134
Cdd:cd17965 65 LLA-AETGSGKTLAYLAPLLDYLkrqeqepfeeaeeeyesAKDTGRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 135 IGGTNVRaeVQKLQMEAPH---IIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFKDQIYDIFQKLNSNTQVVL 211
Cdd:cd17965 144 SSGFGPS--YQRLQLAFKGridILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLIL 221
|
170 180
....*....|....*....|...
gi 4503529 212 LSATMPSDVLEVTKKFMRDPIRI 234
Cdd:cd17965 222 CSATIPKEFDKTLRKLFPDVVRI 244
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
59-336 |
2.85e-09 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 58.75 E-value: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 59 QQRAILPCI-KGYDVIAQAQSGTGKTATFAISILQQIELDLKAtqaLVLAPTRELAQQI------------QKVVMALGD 125
Cdd:COG1204 27 QAEALEAGLlEGKNLVVSAPTASGKTLIAELAILKALLNGGKA---LYIVPLRALASEKyrefkrdfeelgIKVGVSTGD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 126 YmgaschaciggTNVRAEVQKlqmeaPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEA----DEmlSRGFK-DQIYDIF 200
Cdd:COG1204 104 Y-----------DSDDEWLGR-----YDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAhlidDE--SRGPTlEVLLARL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 201 QKLNSNTQVVLLSATMPS--DVLE-VTKKFMRDPIRIlVKKEELTLEGIRQFYINVEREEwkLDTLCDL-YETLTI-TQA 275
Cdd:COG1204 166 RRLNPEAQIVALSATIGNaeEIAEwLDAELVKSDWRP-VPLNEGVLYDGVLRFDDGSRRS--KDPTLALaLDLLEEgGQV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 276 VIFINTRRKVDWLTEKMHAR-----------------------------DFTVSAM--------HGDMDQKERDVIMREF 318
Cdd:COG1204 243 LVFVSSRRDAESLAKKLADElkrrltpeereeleelaeellevseethtNEKLADClekgvafhHAGLPSELRRLVEDAF 322
|
330
....*....|....*...
gi 4503529 319 RSGSSRVLITTDLLARGI 336
Cdd:COG1204 323 REGLIKVLVATPTLAAGV 340
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
59-216 |
3.87e-09 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 55.67 E-value: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 59 QQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDlKATQALVLAPTRELAQQIQKVVMALGDYMGASCH-ACIGG 137
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRD-PGSRALYLYPTKALAQDQLRSLRELLEQLGLGIRvATYDG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 138 TNVRAEVQKLQMEAPHIIVGTPgrvfDMLN----------RRYLSP-KYIkmfVLDEAD----------EMLSRGFKdqi 196
Cdd:cd17923 84 DTPREERRAIIRNPPRILLTNP----DMLHyallphhdrwARFLRNlRYV---VLDEAHtyrgvfgshvALLLRRLR--- 153
|
170 180
....*....|....*....|
gi 4503529 197 yDIFQKLNSNTQVVLLSATM 216
Cdd:cd17923 154 -RLCRRYGADPQFILTSATI 172
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
146-329 |
1.27e-07 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 53.55 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 146 KLQMEAPhIIVGTPGRVFDML--NRRYLSPKYIKM----FVLDEAD----EMLSrgfkdQIYDIFQKLNS-NTQVVLLSA 214
Cdd:COG1203 234 KELWDAP-VVVTTIDQLFESLfsNRKGQERRLHNLansvIILDEVQayppYMLA-----LLLRLLEWLKNlGGSVILMTA 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 215 TMPSDVlevtKKFMRDPIRILVKKEELTLEGIRQFY---INVEREEWKLDTLCD-LYETLTITQAVIFI-NTRRKVDWLT 289
Cdd:COG1203 308 TLPPLL----REELLEAYELIPDEPEELPEYFRAFVrkrVELKEGPLSDEELAElILEALHKGKSVLVIvNTVKDAQELY 383
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 4503529 290 EKMHARDFTVSAM--HGDMDQKER----DVIMREFRSGSSRVLITT 329
Cdd:COG1203 384 EALKEKLPDEEVYllHSRFCPADRseieKEIKERLERGKPCILVST 429
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
71-184 |
1.44e-07 |
|
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: 51.50 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 71 DVIAQAQSGTGKTAtfaISIL-------QQIELDLKATQALVLAPTRELAQQiQkvVMALGDYMGASCHACIGGTNV--- 140
Cdd:cd18034 18 NTIVVLPTGSGKTL---IAVMlikemgeLNRKEKNPKKRAVFLVPTVPLVAQ-Q--AEAIRSHTDLKVGEYSGEMGVdkw 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 4503529 141 RAEVQKLQMEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEA 184
Cdd:cd18034 92 TKERWKEELEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
275-355 |
3.44e-07 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 52.53 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 275 AVIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSS--RVLITTDLLARGIDVQQVSLVINYDLPTN 352
Cdd:COG0553 552 VLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEapVFLISLKAGGEGLNLTAADHVIHYDLWWN 631
|
....*
gi 4503529 353 --REN 355
Cdd:COG0553 632 paVEE 636
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
276-356 |
4.57e-07 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 52.02 E-value: 4.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 276 VIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPTNREN 355
Cdd:PRK11057 240 IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIES 319
|
.
gi 4503529 356 Y 356
Cdd:PRK11057 320 Y 320
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
69-223 |
2.04e-06 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 47.58 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 69 GYDVIAQAQSGTGKTATFAISILQQI-ELDLKATQALVLAPTRELAQQIQKVVMALGDYMGAschaciggtNVRAEV--- 144
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLaDEPEKGVQVLYISPLKALINDQERRLEEPLDEIDL---------EIPVAVrhg 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 145 -----QKLQM--EAPHIIVGTPGRVFDMLNRRYLSPKY--IKMFVLDEADEMLS--RG--FKDQIYDIFQKLNSNTQVVL 211
Cdd:cd17922 72 dtsqsEKAKQlkNPPGILITTPESLELLLVNKKLRELFagLRYVVVDEIHALLGskRGvqLELLLERLRKLTGRPLRRIG 151
|
170
....*....|....
gi 4503529 212 LSATM--PSDVLEV 223
Cdd:cd17922 152 LSATLgnLEEAAAF 165
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
288-348 |
4.71e-06 |
|
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: 46.18 E-value: 4.71e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4503529 288 LTEKMHArDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYD 348
Cdd:cd18811 54 LKERFRP-ELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIED 113
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
60-217 |
4.89e-06 |
|
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: 46.49 E-value: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 60 QRAILPCIKGYD--VIAQAQSGTGKT--ATFAI--SILQQIELdlkatqALVLAPTRELAQQI------------QKVVM 121
Cdd:cd17921 6 QREALRALYLSGdsVLVSAPTSSGKTliAELAIlrALATSGGK------AVYIAPTRALVNQKeadlrerfgplgKNVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 122 ALGDYmgaschaciggtnvraEVQKLQMEAPHIIVGTPGRvFDML--NRRYLSPKYIKMFVLDEA----DEmlSRGFK-D 194
Cdd:cd17921 80 LTGDP----------------SVNKLLLAEADILVATPEK-LDLLlrNGGERLIQDVRLVVVDEAhligDG--ERGVVlE 140
|
170 180
....*....|....*....|...
gi 4503529 195 QIYDIFQKLNSNTQVVLLSATMP 217
Cdd:cd17921 141 LLLSRLLRINKNARFVGLSATLP 163
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
265-348 |
8.11e-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: 45.70 E-value: 8.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 265 DLYETLtitQAVIFINTRRKVDWLTEKMhARDFT---------VSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARG 335
Cdd:cd18790 15 DLLGEI---RKRVARGERVLVTTLTKRM-AEDLTeylqelgvkVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREG 90
|
90
....*....|...
gi 4503529 336 IDVQQVSLVINYD 348
Cdd:cd18790 91 LDLPEVSLVAILD 103
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
277-350 |
1.42e-05 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 44.56 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 277 IFINTRRKVDWLTEKMHAR------DFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLP 350
Cdd:cd18796 43 VFTNTRSQAERLAQRLRELcpdrvpPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSP 122
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
276-360 |
1.84e-05 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 46.67 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 276 VIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPTNREN 355
Cdd:COG0514 234 IVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEA 313
|
....*
gi 4503529 356 YIHRI 360
Cdd:COG0514 314 YYQEI 318
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
274-349 |
3.61e-05 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 45.88 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 274 QAVIFINTRRKVDWLTEKMHARDFTV------SAMHGD--MDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVI 345
Cdd:COG1111 355 RIIVFTQYRDTAEMIVEFLSEPGIKAgrfvgqASKEGDkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVI 434
|
....
gi 4503529 346 NYDL 349
Cdd:COG1111 435 FYEP 438
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
274-336 |
6.88e-05 |
|
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: 42.93 E-value: 6.88e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503529 274 QAVIFINTRRKvdwlTEKMhARDFT-VSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGI 336
Cdd:cd18795 45 PVLVFCSSRKE----CEKT-AKDLAgIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGV 103
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
106-225 |
7.18e-05 |
|
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350791 [Multi-domain] Cd Length: 182 Bit Score: 43.08 E-value: 7.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 106 LAPTREL-AQQIQkvvmALGDYMGASCHACIGGT-NVRAEVQKLQMEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDE 183
Cdd:cd18033 52 MAPTKPLvSQQIE----ACYKITGIPSSQTAELTgSVPPTKRAELWASKRVFFLTPQTLENDLKEGDCDPKSIVCLVIDE 127
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 4503529 184 ADEMLSRGFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTK 225
Cdd:cd18033 128 AHRATGNYAYCQVVRELMRYNSHFRILALTATPGSKLEAVQQ 169
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
275-360 |
1.65e-04 |
|
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: 41.43 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 275 AVIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPTNRE 354
Cdd:cd18794 33 GIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSME 112
|
....*.
gi 4503529 355 NYIHRI 360
Cdd:cd18794 113 SYYQES 118
|
|
| PRK05298 |
PRK05298 |
excinuclease ABC subunit UvrB; |
288-344 |
3.70e-04 |
|
excinuclease ABC subunit UvrB;
Pssm-ID: 235395 [Multi-domain] Cd Length: 652 Bit Score: 42.73 E-value: 3.70e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 4503529 288 LTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLV 344
Cdd:PRK05298 462 LTDYLKELGIKVRYLHSDIDTLERVEIIRDLRLGEFDVLVGINLLREGLDIPEVSLV 518
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
206-338 |
4.83e-04 |
|
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: 42.03 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 206 NTQVVLLSATMPsdvlEVTKKFMRDpIRILVKKEELTLEGIRQFYINVEREEWKLD--TLCDLYETLT-ITQAVIFINTR 282
Cdd:cd09639 154 DVPILLMSATLP----KFLKEYAEK-IGYVEENEPLDLKPNERAPFIKIESDKVGEisSLERLLEFIKkGGSVAIIVNTV 228
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503529 283 RKV----DWLTEKMHarDFTVSAMHGDMDQKER----DVIMREFRSGSSRVLITTDLLARGIDV 338
Cdd:cd09639 229 DRAqefyQQLKEKGP--EEEIMLIHSRFTEKDRakkeAELLLEFKKSEKFVIVATQVIEASLDI 290
|
|
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
290-329 |
6.20e-04 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 41.96 E-value: 6.20e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 4503529 290 EKMHAR------DFTVSAMHGDMDQKERDVIMREFRSGSSRVLITT 329
Cdd:COG1200 491 EETYEElreafpGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVAT 536
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
291-348 |
6.62e-04 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350179 [Multi-domain] Cd Length: 160 Bit Score: 39.94 E-value: 6.62e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 4503529 291 KMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYD 348
Cdd:cd18792 55 KELVPEARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIED 112
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| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
51-232 |
1.14e-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: 39.83 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 51 GFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFaisilqQIELDLKATQALVLAPTRELaQQIQkvVMALGDyMGAS 130
Cdd:cd17920 9 GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCY------QLPALLLDGVTLVVSPLISL-MQDQ--VDRLQQ-LGIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503529 131 ChACIGGT----NVRAEVQKLQMEAPHIIVGTP-----GRVFDMLNRRYlSPKYIKMFVLDEA-----------DEMLsr 190
Cdd:cd17920 79 A-AALNSTlspeEKREVLLRIKNGQYKLLYVTPerllsPDFLELLQRLP-ERKRLALIVVDEAhcvsqwghdfrPDYL-- 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 4503529 191 gfkdQIYDIFQKLNsNTQVVLLSATMP----SDVLEVTKkfMRDPI 232
Cdd:cd17920 155 ----RLGRLRRALP-GVPILALTATATpevrEDILKRLG--LRNPV 193
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|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
306-348 |
1.18e-03 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350188 [Multi-domain] Cd Length: 143 Bit Score: 38.88 E-value: 1.18e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 4503529 306 MDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYD 348
Cdd:cd18801 74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYD 116
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
296-338 |
2.40e-03 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 40.13 E-value: 2.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 4503529 296 DFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDV 338
Cdd:PRK10917 505 ELRVGLLHGRMKPAEKDAVMAAFKAGEIDILVATTVIEVGVDV 547
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