|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
1-403 |
0e+00 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 625.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 1 MSKPDDSPAAANNLNiaDGEIESNWETVIDNFDNMELKDELLRGVYAYGFERPSAIQARAILPVIKGHDVIAQAQSGTGK 80
Cdd:PTZ00424 1 MATSEQKNQSEQVAS--TGTIESNYDEIVDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 81 TATFSIAILQRIDPSIQAVQALILAPTRELAQQIQKVVIALGDYMKINCHACIGGTNVREDMAKLNEGAQVVVGTPGRVY 160
Cdd:PTZ00424 79 TATFVIAALQLIDYDLNACQALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 161 DMINRRAFKTDQLKMFCLDEADEMLSRGFKDQMYEVFQLLPQDTQCVLLSATMPHEVLEVTKKFMREPIRILVKRDELTL 240
Cdd:PTZ00424 159 DMIDKRHLRVDDLKLFILDEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 241 EGIKQFYVAVEKEEWKLETLCDLYETVTITQAVIFCNTRRKVDWLTDKLTAREFTVSAMHGDMEQGQREIIMREFRSGSS 320
Cdd:PTZ00424 239 EGIRQFYVAVEKEEWKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGST 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 321 RVLITTDLLARGIDVQQVSLVINYDLPSNRENYIHRIGRGGRFGRKGVAINFVTSDDVRMLRDIEQFYSTQIDEMPLNVA 400
Cdd:PTZ00424 319 RVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEVA 398
|
...
gi 388856094 401 DLI 403
Cdd:PTZ00424 399 DYL 401
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
31-397 |
7.79e-153 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 438.43 E-value: 7.79e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 31 NFDNMELKDELLRGVYAYGFERPSAIQARAILPVIKGHDVIAQAQSGTGKTATFSIAILQRIDPSIQ-AVQALILAPTRE 109
Cdd:COG0513 3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPrAPQALILAPTRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 110 LAQQIQKVVIALGDYMKINCHACIGGTNVREDMAKLNEGAQVVVGTPGRVYDMINRRAFKTDQLKMFCLDEADEMLSRGF 189
Cdd:COG0513 83 LALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 190 KDQMYEVFQLLPQDTQCVLLSATMPHEVLEVTKKFMREPIRILVKRDELTLEGIKQFYVAVEKEEwKLETLCDLYETVTI 269
Cdd:COG0513 163 IEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRD-KLELLRRLLRDEDP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 270 TQAVIFCNTRRKVDWLTDKLTAREFTVSAMHGDMEQGQREIIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPSN 349
Cdd:COG0513 242 ERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPED 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 388856094 350 RENYIHRIgrggrfgrkgVAINFVTSDDVRMLRDIEQFYSTQIDEMPL 397
Cdd:COG0513 322 PEDYVHRIgrtgragaegTAISLVTPDERRLLRAIEKLIGQKIEEEEL 369
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
32-232 |
2.77e-138 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation factor 4A-I (DDX2A) and eukaryotic initiation factor 4A-II (DDX2B) are involved in cap recognition and are required for mRNA binding to ribosome. They are DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350804 [Multi-domain] Cd Length: 201 Bit Score: 392.96 E-value: 2.77e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 32 FDNMELKDELLRGVYAYGFERPSAIQARAILPVIKGHDVIAQAQSGTGKTATFSIAILQRIDPSIQAVQALILAPTRELA 111
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 112 QQIQKVVIALGDYMKINCHACIGGTNVREDMAKLNEGAQVVVGTPGRVYDMINRRAFKTDQLKMFCLDEADEMLSRGFKD 191
Cdd:cd18046 81 QQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 388856094 192 QMYEVFQLLPQDTQCVLLSATMPHEVLEVTKKFMREPIRIL 232
Cdd:cd18046 161 QIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRIL 201
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
35-232 |
4.28e-124 |
|
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: 356.63 E-value: 4.28e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 35 MELKDELLRGVYAYGFERPSAIQARAILPVIKGHDVIAQAQSGTGKTATFSIAILQRIDPSIQAVQALILAPTRELAQQI 114
Cdd:cd17939 2 MGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 115 QKVVIALGDYMKINCHACIGGTNVREDMAKLNEGAQVVVGTPGRVYDMINRRAFKTDQLKMFCLDEADEMLSRGFKDQMY 194
Cdd:cd17939 82 QKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQIY 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 388856094 195 EVFQLLPQDTQCVLLSATMPHEVLEVTKKFMREPIRIL 232
Cdd:cd17939 162 DIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRIL 199
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
32-232 |
8.28e-107 |
|
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: 312.86 E-value: 8.28e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 32 FDNMELKDELLRGVYAYGFERPSAIQARAILPVIKGHDVIAQAQSGTGKTATFSIAILQRIDPSIQAVQALILAPTRELA 111
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 112 QQIQKVVIALGDYMKINCHACIGGTNVREDMAKLNEGAQVVVGTPGRVYDMINRRAFKTDQLKMFCLDEADEMLSRGFKD 191
Cdd:cd18045 81 VQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 388856094 192 QMYEVFQLLPQDTQCVLLSATMPHEVLEVTKKFMREPIRIL 232
Cdd:cd18045 161 QIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRIL 201
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
32-398 |
3.90e-90 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 279.38 E-value: 3.90e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 32 FDNMELKDELLRGVYAYGFERPSAIQARAiLPVI-KGHDVIAQAQSGTGKTATFSIAILQRIDPSIQAVQALILAPTREL 110
Cdd:PRK11776 6 FSTLPLPPALLANLNELGYTEMTPIQAQS-LPAIlAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTREL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 111 AQQIQKVVIALGDYM---KIN--ChaciGGTNVREDMAKLNEGAQVVVGTPGRVYDMINRRAFKTDQLKMFCLDEADEML 185
Cdd:PRK11776 85 ADQVAKEIRRLARFIpniKVLtlC----GGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 186 SRGFKDQMYEVFQLLPQDTQCVLLSATMPHEVLEVTKKFMREPIRILV--KRDELTLEgiKQFYvAVEKEEwKLETLCDL 263
Cdd:PRK11776 161 DMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVesTHDLPAIE--QRFY-EVSPDE-RLPALQRL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 264 YETVTITQAVIFCNTRRKVDWLTDKLTAREFTVSAMHGDMEQGQREIIMREFRSGSSRVLITTDLLARGIDVQQVSLVIN 343
Cdd:PRK11776 237 LLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVIN 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 388856094 344 YDLPSNRENYIHRIGRGGRFGRKGVAINFVTSDDVRMLRDIEQFYSTQIDEMPLN 398
Cdd:PRK11776 317 YELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLP 371
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
41-231 |
7.10e-88 |
|
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: 264.69 E-value: 7.10e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 41 LLRGVYAYGFERPSAIQARAILPVIKGHDVIAQAQSGTGKTATFSIAILQRIDP----SIQAVQALILAPTRELAQQIQK 116
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPepkkKGRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 117 VVIALGDYMKINCHACIGGTNVREDMAKLNEGAQVVVGTPGRVYDMINRRAFKTDQLKMFCLDEADEMLSRGFKDQMYEV 196
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 388856094 197 FQLLPQDTQCVLLSATMPHEVLEVTKKFMREPIRI 231
Cdd:cd00268 161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
32-403 |
4.53e-77 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 250.54 E-value: 4.53e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 32 FDNMELKDELLRGVYAYGFERPSAIQARAILPVIKGHDVIAQAQSGTGKTATFSIAILQRIDPSIQAVQALILAPTRELA 111
Cdd:PRK11634 8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTRELA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 112 QQIQKVVIALGDYMK-INCHACIGGTNVREDMAKLNEGAQVVVGTPGRVYDMINRRAFKTDQLKMFCLDEADEMLSRGFK 190
Cdd:PRK11634 88 VQVAEAMTDFSKHMRgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 191 DQMYEVFQLLPQDTQCVLLSATMPHEVLEVTKKFMREPIRILVKRDELTLEGIKQFYVAVEKEEwKLETLCDLYETVTIT 270
Cdd:PRK11634 168 EDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMR-KNEALVRFLEAEDFD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 271 QAVIFCNTRRKVDWLTDKLTAREFTVSAMHGDMEQGQREIIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPSNR 350
Cdd:PRK11634 247 AAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDS 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 388856094 351 ENYIHRIGRGGRFGRKGVAINFVTSDDVRMLRDIEQFYSTQIDEMPLNVADLI 403
Cdd:PRK11634 327 ESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAELL 379
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
31-397 |
1.32e-74 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 239.32 E-value: 1.32e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 31 NFDNMELKDELLRGVYAYGFERPSAIQARAILPVIKGHDVIAQAQSGTGKTATFSIAILQRI---DPSIQA---VQALIL 104
Cdd:PRK10590 2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLitrQPHAKGrrpVRALIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 105 APTRELAQQIQKVVIALGDYMKINCHACIGGTNVREDMAKLNEGAQVVVGTPGRVYDMINRRAFKTDQLKMFCLDEADEM 184
Cdd:PRK10590 82 TPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 185 LSRGFKDQMYEVFQLLPQDTQCVLLSATMPHEVLEVTKKFMREPIRILVKRDELTLEGIKQFYVAVEKEEwKLETLCDLY 264
Cdd:PRK10590 162 LDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKR-KRELLSQMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 265 ETVTITQAVIFCNTRRKVDWLTDKLTAREFTVSAMHGDMEQGQREIIMREFRSGSSRVLITTDLLARGIDVQQVSLVINY 344
Cdd:PRK10590 241 GKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNY 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 388856094 345 DLPSNRENYIHRIGRGGRFGRKGVAINFVTSDDVRMLRDIEQFYSTQIDEMPL 397
Cdd:PRK10590 321 ELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRIAI 373
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
32-231 |
4.77e-72 |
|
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: 224.10 E-value: 4.77e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 32 FDNMELKDELLRGVYAYGFERPSAIQARAILPVIKGHDVIAQAQSGTGKTATFSIAILQRIDPSIQAVQALILAPTRELA 111
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 112 QQIQKVVIALGDYMKINCHACIGGTNVREDMAKLNEGAQVVVGTPGRVYDMINRRAFKTDQLKMFCLDEADEMLSRGFKD 191
Cdd:cd17940 81 LQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 388856094 192 QMYEVFQLLPQDTQCVLLSATMPHEVLEVTKKFMREPIRI 231
Cdd:cd17940 161 IIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
37-231 |
3.39e-69 |
|
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: 216.67 E-value: 3.39e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 37 LKDELLRGVYAYGFERPSAIQARAiLPVIKG---HDVIAQAQSGTGKTATFSIAILQRIDPSIQAVQALILAPTRELAQQ 113
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETA-LPLILSdppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 114 IQKVVIALGDYMKINCHACIGGTNVRedmAKLNEGAQVVVGTPGRVYDMINRRAFKTDQLKMFCLDEADEML-SRGFKDQ 192
Cdd:cd17963 80 IGEVVEKMGKFTGVKVALAVPGNDVP---RGKKITAQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLdTQGHGDQ 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 388856094 193 MYEVFQLLPQDTQCVLLSATMPHEVLEVTKKFMREPIRI 231
Cdd:cd17963 157 SIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
41-231 |
5.01e-65 |
|
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: 205.96 E-value: 5.01e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 41 LLRGVYAYGFERPSAIQARAIlPVIK-GHDVIAQAQSGTGKTATFSIAILQRIDPSIQAVQALILAPTRELAQQIQKVVI 119
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAI-PLGLaGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 120 ALGDYMK-INCHACIGGTNVREDMAKLNeGAQVVVGTPGRVYDMINRRAFKTDQLKMFCLDEADEMLSRGFKDQMYEVFQ 198
Cdd:cd17943 80 KIGKKLEgLKCEVFIGGTPVKEDKKKLK-GCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFS 158
|
170 180 190
....*....|....*....|....*....|...
gi 388856094 199 LLPQDTQCVLLSATMPHEVLEVTKKFMREPIRI 231
Cdd:cd17943 159 SLPKNKQVIAFSATYPKNLDNLLARYMRKPVLV 191
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
31-387 |
2.50e-64 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 212.11 E-value: 2.50e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 31 NFDNMELKDELLRGVYAYGFERPSAIQARAILPVIKGHDVIAQAQSGTGKTATFSIAILQR-ID-PSIQAVQA--LILAP 106
Cdd:PRK11192 2 TFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHlLDfPRRKSGPPriLILTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 107 TRELAQQIQKVVIALGDYMKINCHACIGGTNVREDMAKLNEGAQVVVGTPGRVYDMINRRAFKTDQLKMFCLDEADEMLS 186
Cdd:PRK11192 82 TRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 187 RGFKdqmyEVFQLLPQDT----QCVLLSATMPHE-VLEVTKKFMREPIRILVK--RDELtlEGIKQFYVAVEKEEWKLET 259
Cdd:PRK11192 162 MGFA----QDIETIAAETrwrkQTLLFSATLEGDaVQDFAERLLNDPVEVEAEpsRRER--KKIHQWYYRADDLEHKTAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 260 LCDLYETVTITQAVIFCNTRRKVDWLTDKLTAREFTVSAMHGDMEQGQREIIMREFRSGSSRVLITTDLLARGIDVQQVS 339
Cdd:PRK11192 236 LCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVS 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 388856094 340 LVINYDLPSNRENYIHRIGRGGRFGRKGVAINFVTSDDVRMLRDIEQF 387
Cdd:PRK11192 316 HVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERY 363
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
32-396 |
5.12e-63 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 209.77 E-value: 5.12e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 32 FDNMELKDELLRGVYAYGFERPSAIQARAILPVIKGHDVIAQAQSGTGKTATFSIAI---LQRIDPSIQ----AVQALIL 104
Cdd:PRK01297 89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIinqLLQTPPPKErymgEPRALII 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 105 APTRELAQQIQKVVIALGDYMKINCHACIGGTNVREDMAKLNEG-AQVVVGTPGRVYDMINRRAFKTDQLKMFCLDEADE 183
Cdd:PRK01297 169 APTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEADR 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 184 MLSRGFKDQMYEVFQLLP--QDTQCVLLSATMPHEVLEVTKKFMREPIRILVKRDELTLEGIKQFYVAVEKEEwKLETLC 261
Cdd:PRK01297 249 MLDMGFIPQVRQIIRQTPrkEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSD-KYKLLY 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 262 DLYETVTITQAVIFCNTRRKVDWLTDKLTAREFTVSAMHGDMEQGQREIIMREFRSGSSRVLITTDLLARGIDVQQVSLV 341
Cdd:PRK01297 328 NLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHV 407
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 388856094 342 INYDLPSNRENYIHRIGRGGRFGRKGVAINFVTSDDVRMLRDIEQFYSTQID-EMP 396
Cdd:PRK01297 408 INFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKIScEMP 463
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
32-233 |
1.66e-60 |
|
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: 194.87 E-value: 1.66e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 32 FDNMELKDELLRGVYAYGFERPSAIQARAILPVIKGHDVIAQAQSGTGKTATFSIAILQRIDPSIQAVQALILAPTRELA 111
Cdd:cd17950 4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRELA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 112 QQIQKVVIALGDYMKINCHACI-GGTNVREDMAKL-NEGAQVVVGTPGRVYDMINRRAFKTDQLKMFCLDEADEML-SRG 188
Cdd:cd17950 84 FQISNEYERFSKYMPNVKTAVFfGGVPIKKDIEVLkNKCPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLeQLD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 388856094 189 FKDQMYEVFQLLPQDTQCVLLSATMPHEVLEVTKKFMREPIRILV 233
Cdd:cd17950 164 MRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
29-384 |
3.74e-59 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 201.16 E-value: 3.74e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 29 IDNFDNMELKDELLRGVYAYGFERPSAIQARAILPVIKGHDVIAQAQSGTGKTATFsiailqrIDPSIQAVQA------- 101
Cdd:PTZ00110 129 VVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAF-------LLPAIVHINAqpllryg 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 102 -----LILAPTRELAQQIQKVVIALGDYMKINCHACIGGTNVREDMAKLNEGAQVVVGTPGRVYDMINRRAFKTDQLKMF 176
Cdd:PTZ00110 202 dgpivLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 177 CLDEADEMLSRGFKDQMYE-VFQLLPqDTQCVLLSATMPHEVLEVTKKFMRE-PIRILVKRDELTL-EGIKQfYVAVEKE 253
Cdd:PTZ00110 282 VLDEADRMLDMGFEPQIRKiVSQIRP-DRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDLTAcHNIKQ-EVFVVEE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 254 EWKLETLCDLYETVTI--TQAVIFCNTRRKVDWLTDKLTAREFTVSAMHGDMEQGQREIIMREFRSGSSRVLITTDLLAR 331
Cdd:PTZ00110 360 HEKRGKLKMLLQRIMRdgDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASR 439
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 388856094 332 GIDVQQVSLVINYDLPSNRENYIHRIGRGGRFGRKGVAINFVTSDDVRMLRDI 384
Cdd:PTZ00110 440 GLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDL 492
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
31-397 |
9.69e-59 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 200.56 E-value: 9.69e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 31 NFDNMELKDELLRGVYAYGFERPSAIQArAILPV-IKGHDVIAQAQSGTGKTATFSIAILQRI-------DPSIQAVQAL 102
Cdd:PRK04537 10 TFSSFDLHPALLAGLESAGFTRCTPIQA-LTLPVaLPGGDVAGQAQTGTGKTLAFLVAVMNRLlsrpalaDRKPEDPRAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 103 ILAPTRELAQQIQKVVIALGDYMKINCHACIGGTNVREDMAKLNEGAQVVVGTPGRVYDMINRRAFKTDQLKMFC-LDEA 181
Cdd:PRK04537 89 ILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVVSLHACEICvLDEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 182 DEMLSRGFKDQMYEVFQLLPQDT--QCVLLSATMPHEVLEVTKKFMREPIRILVKRDELTLEGIKQ-FYVAVEKEewKLE 258
Cdd:PRK04537 169 DRMFDLGFIKDIRFLLRRMPERGtrQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQrIYFPADEE--KQT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 259 TLCDLYETVTITQAVIFCNTRRKVDWLTDKLTAREFTVSAMHGDMEQGQREIIMREFRSGSSRVLITTDLLARGIDVQQV 338
Cdd:PRK04537 247 LLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGV 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 388856094 339 SLVINYDLPSNRENYIHRIGRGGRFGRKGVAINFVTSDDVRMLRDIEQFYSTQIDEMPL 397
Cdd:PRK04537 327 KYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKIPVEPV 385
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
54-220 |
1.23e-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: 185.91 E-value: 1.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 54 SAIQARAILPVIKGHDVIAQAQSGTGKTATFSIAILQRIDPSIQAVQALILAPTRELAQQIQKVVIALGDYMKINCHACI 133
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 134 GGTNVREDMAKLnEGAQVVVGTPGRVYDMINRRaFKTDQLKMFCLDEADEMLSRGFKDQMYEVFQLLPQDTQCVLLSATM 213
Cdd:pfam00270 81 GGDSRKEQLEKL-KGPDILVGTPGRLLDLLQER-KLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATL 158
|
....*..
gi 388856094 214 PHEVLEV 220
Cdd:pfam00270 159 PRNLEDL 165
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
45-246 |
3.28e-53 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 175.76 E-value: 3.28e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 45 VYAYGFERPSAIQARAILPVIKG-HDVIAQAQSGTGKTATFSIAILQRIDPSiQAVQALILAPTRELAQQIQKVVIALGD 123
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRG-KGGRVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 124 YMKINCHACIGGTNVREDMAKLNEG-AQVVVGTPGRVYDMINRRAFKTDQLKMFCLDEADEMLSRGFKDQMYEVFQLLPQ 202
Cdd:smart00487 80 SLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 388856094 203 DTQCVLLSATMPHEVLEVTKKFMREPIRILVKRdeLTLEGIKQF 246
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
41-231 |
2.44e-52 |
|
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: 173.21 E-value: 2.44e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 41 LLRGVYAYGFERPSAIQARAILPVIKGHDVIAQAQSGTGKTATFSIAILQRI---DPSIQAVQALILAPTRELAQQIQKV 117
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLlyrPKKKAATRVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 118 VIALGDYMKINCHACIGGTNVREDMAKLNEGAQVVVGTPGRVYDMI-NRRAFKTDQLKMFCLDEADEMLSRGFKDQMYEV 196
Cdd:cd17947 81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLrNSPSFDLDSIEILVLDEADRMLEEGFADELKEI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 388856094 197 FQLLPQDTQCVLLSATMPHEVLEVTKKFMREPIRI 231
Cdd:cd17947 161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
29-386 |
1.28e-51 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 180.37 E-value: 1.28e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 29 IDNFDNMELKDELLRGVYAYGFERPSAIQARAILPVIKGHDVIAQAQSGTGKTATFSIAILQRI-------DPSIQAVQA 101
Cdd:PLN00206 120 ILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCctirsghPSEQRNPLA 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 102 LILAPTRELAQQIQKVVIALGDYMKINCHACIGGTNVREDMAKLNEGAQVVVGTPGRVYDMINRRAFKTDQLKMFCLDEA 181
Cdd:PLN00206 200 MVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEV 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 182 DEMLSRGFKDQMYEVFQLLPQdTQCVLLSATMPHEVLEVTKKFMREPIRILVKRDELTLEGIKQFYVAVEKEEWKLEtlc 261
Cdd:PLN00206 280 DCMLERGFRDQVMQIFQALSQ-PQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQK--- 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 262 dLYETVTITQ-----AVIFCNTRRKVDWLTDKLT-AREFTVSAMHGDMEQGQREIIMREFRSGSSRVLITTDLLARGIDV 335
Cdd:PLN00206 356 -LFDILKSKQhfkppAVVFVSSRLGADLLANAITvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDL 434
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 388856094 336 QQVSLVINYDLPSNRENYIHRIGRGGRFGRKGVAINFVTSDDVRMLRDIEQ 386
Cdd:PLN00206 435 LRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVA 485
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
32-357 |
1.51e-51 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 178.24 E-value: 1.51e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 32 FDNMELKDELLRGVYAYGFERPSAIQARAILPVIKGHDVIAQAQSGTGKT-----ATFSIAILQRIDPSIQAVQ--ALIL 104
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTmafltATFHYLLSHPAPEDRKVNQprALIM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 105 APTRELAQQIQKVVIALGDYMKINCHACIGGTNVREDMAKLNEGAQVVVGTPGRVYDMINRRAFKTDQLKMFCLDEADEM 184
Cdd:PRK04837 90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 185 LSRGF-KDQMYeVFQLLPQDTQ--CVLLSATMPHEVLEVTKKFMREPIRILVKRDELTLEGIKQ--FYVAVEKeewKLET 259
Cdd:PRK04837 170 FDLGFiKDIRW-LFRRMPPANQrlNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEelFYPSNEE---KMRL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 260 LCDLYETVTITQAVIFCNTRRKVDWLTDKLTAREFTVSAMHGDMEQGQREIIMREFRSGSSRVLITTDLLARGIDVQQVS 339
Cdd:PRK04837 246 LQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVT 325
|
330
....*....|....*...
gi 388856094 340 LVINYDLPSNRENYIHRI 357
Cdd:PRK04837 326 HVFNYDLPDDCEDYVHRI 343
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
37-227 |
2.55e-49 |
|
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: 165.83 E-value: 2.55e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 37 LKDELLRGVYAYGFERPSAIQARAILPVI-KGHDVIAQAQSGTGKTATFSIAILQRI-----DPSIQAVQALILAPTREL 110
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPAIQSLlntkpAGRRSGVSALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 111 AQQIQKVVIALGDYM-KINCHACIGGTNVREDMAKL-NEGAQVVVGTPGRVYDMIN----RRAFKtdQLKMFCLDEADEM 184
Cdd:cd17964 81 ALQIAAEAKKLLQGLrKLRVQSAVGGTSRRAELNRLrRGRPDILVATPGRLIDHLEnpgvAKAFT--DLDYLVLDEADRL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 388856094 185 LSRGFKDQMYEVFQLLPQ----DTQCVLLSATMPHEVLEVTKKFMRE 227
Cdd:cd17964 159 LDMGFRPDLEQILRHLPEknadPRQTLLFSATVPDEVQQIARLTLKK 205
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
37-229 |
5.71e-47 |
|
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: 159.67 E-value: 5.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 37 LKDELLRGVYAYGFERPSAIQARAILPVIKGHDVIAQAQSGTGKTATFSIAILQRI------DPSIQAVQALILAPTREL 110
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlkakaeSGEEQGTRALILVPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 111 AQQIQKVVIALGDYM--KINCHACIGGTNVREDMAKLNEGAQVVVGTPGRVYDMINR-RAFKTDQLKMFCLDEADEMLSR 187
Cdd:cd17961 81 AQQVSKVLEQLTAYCrkDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESgSLLLLSTLKYLVIDEADLVLSY 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 388856094 188 GFKDQMYEVFQLLPQDTQCVLLSATMPHEVLEVTKKFMREPI 229
Cdd:cd17961 161 GYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
31-231 |
1.12e-46 |
|
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350717 [Multi-domain] Cd Length: 205 Bit Score: 159.01 E-value: 1.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 31 NFDNMELKDELLRGVYAYGFERPSAIQARAILPVIKGHDVIAQAQSGTGKTATFSIAILQRIDPS--IQAVQALILAPTR 108
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHspTVGARALILSPTR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 109 ELAQQIQKVVIALGDYMKINCHACIGGTNVREDMAKLNEGAQVVVGTPGRVYDMINRRAFKTDQLKMFCLDEADEMLSRG 188
Cdd:cd17959 82 ELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 388856094 189 FKDQMYEVFQLLPQDTQCVLLSATMPHEVLEVTKKFMREPIRI 231
Cdd:cd17959 162 FAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
243-358 |
3.40e-46 |
|
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: 154.97 E-value: 3.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 243 IKQFYVAVEKEEWKLETLCDLYETVTITQAVIFCNTRRKVDWLTDKLTAREFTVSAMHGDMEQGQREIIMREFRSGSSRV 322
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 388856094 323 LITTDLLARGIDVQQVSLVINYDLPSNRENYIHRIG 358
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIG 116
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
41-231 |
6.52e-46 |
|
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: 156.58 E-value: 6.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 41 LLRGVYAYGFERPSAIQARAILPVIKGHDVIAQAQSGTGKTATFSIAILQRI-----DPSIQAVQALILAPTRELAQQIQ 115
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrkaNLKKGQVGALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 116 KVVIALGDYM--KINCHACIGGTNVREDMAKL-NEGAQVVVGTPGRVYDMINRRA--FKTDQLKMFCLDEADEMLSRGFK 190
Cdd:cd17960 81 EVLQSFLEHHlpKLKCQLLIGGTNVEEDVKKFkRNGPNILVGTPGRLEELLSRKAdkVKVKSLEVLVLDEADRLLDLGFE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 388856094 191 DQMYEVFQLLPQDTQCVLLSATMPHEVLEVTKKFMREPIRI 231
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
32-231 |
1.05e-45 |
|
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: 156.32 E-value: 1.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 32 FDNMELKDELLRGVYAYGFERPSAIQARAILPVIKGHDVIAQAQSGTGKTATFSIAILQRIDPSIQAVQALILAPTRELA 111
Cdd:cd17954 2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTRELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 112 QQIQKVVIALGDYMKINCHACIGGTNVREDMAKLNEGAQVVVGTPGRVYDMI-NRRAFKTDQLKMFCLDEADEMLSRGFK 190
Cdd:cd17954 82 QQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLeNTKGFSLKSLKFLVMDEADRLLNMDFE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 388856094 191 DQMYEVFQLLPQDTQCVLLSATMPHEVLEVTKKFMREPIRI 231
Cdd:cd17954 162 PEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
32-228 |
5.12e-45 |
|
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: 154.30 E-value: 5.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 32 FDNMELKDELLRGVYAYGFERPSAIQARAILPVIKGHDVIAQAQSGTGKTATFSIAILQRI--DPSiqAVQALILAPTRE 109
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLseDPY--GIFALVLTPTRE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 110 LAQQIQKVVIALGDYMKINCHACIGGTNVREDMAKLNEGAQVVVGTPGRVYDMI---NRRAFKTDQLKMFCLDEADEMLS 186
Cdd:cd17955 79 LAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLrssDDTTKVLSRVKFLVLDEADRLLT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 388856094 187 RGFKDQMYEVFQLLPQDTQCVLLSATMPHEVLEVTKKFMREP 228
Cdd:cd17955 159 GSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
41-231 |
1.68e-43 |
|
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: 150.93 E-value: 1.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 41 LLRGVYAYGFERPSAIQARAILPVIKGHDVIAQAQSGTGKTATFSIAILQRID--PSIQAV------QALILAPTRELAQ 112
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISrlPPLDEEtkddgpYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 113 QIQKVVIALGDYMKINCHACIGGTNVREDMAKLNEGAQVVVGTPGRVYDMINRRAFKTDQLKMFCLDEADEMLSRGFKDQ 192
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 388856094 193 MYEVFQLLPQDT--------------------QCVLLSATMPHEVLEVTKKFMREPIRI 231
Cdd:cd17945 161 VTKILDAMPVSNkkpdteeaeklaasgkhryrQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
41-231 |
1.46e-42 |
|
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: 147.95 E-value: 1.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 41 LLRGVYAYGFERPSAIQARAILPVIKGHDVIAQAQSGTGKTATFSIAILQRI--DPSIQAVQ---ALILAPTRELAQQIQ 115
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHImdQRELEKGEgpiAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 116 KVVIALGDYMKINCHACIGGTNVREDMAKLNEGAQVVVGTPGRVYDMINRRAFKTDQLKMFCLDEADEMLSRGFKDQMYE 195
Cdd:cd17952 81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 388856094 196 VFQLLPQDTQCVLLSATMPHEVLEVTKKFMREPIRI 231
Cdd:cd17952 161 IVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
49-231 |
5.99e-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: 147.14 E-value: 5.99e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 49 GFERPSAIQARAILPVIKGHDVIAQAQSGTGKTATFSIAILQRI--DPSIQAVQ---ALILAPTRELAQQIQKVVIALGD 123
Cdd:cd17953 31 GYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIkdQRPVKPGEgpiGLIMAPTRELALQIYVECKKFSK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 124 YMKINCHACIGGTNVREDMAKLNEGAQVVVGTPGRVYDMI---NRRAFKTDQLKMFCLDEADEMLSRGFKDQMYEVFQLL 200
Cdd:cd17953 111 ALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtanNGRVTNLRRVTYVVLDEADRMFDMGFEPQIMKIVNNI 190
|
170 180 190
....*....|....*....|....*....|.
gi 388856094 201 PQDTQCVLLSATMPHEVLEVTKKFMREPIRI 231
Cdd:cd17953 191 RPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
32-228 |
8.66e-42 |
|
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350696 [Multi-domain] Cd Length: 204 Bit Score: 145.93 E-value: 8.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 32 FDNMELKDELLRGVYAYGFERPSAIQARAILPVIKGHDVIAQAQSGTGKTATFSIailqridPSIQAVQALILAPTRELA 111
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCL-------PVLQIVVALILEPSRELA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 112 QQIQKVVIALGDYM---KINCHACIGGTNVREDMAKLNEGAQVVVGTPGRVYDMINRRAFKTDQLKMFCLDEADEMLSRG 188
Cdd:cd17938 74 EQTYNCIENFKKYLdnpKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 388856094 189 FKDQMYEVFQLLPQDT------QCVLLSATMpH--EVLEVTKKFMREP 228
Cdd:cd17938 154 NLETINRIYNRIPKITsdgkrlQVIVCSATL-HsfEVKKLADKIMHFP 200
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
41-231 |
2.19e-41 |
|
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: 144.61 E-value: 2.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 41 LLRGVYAYGFERPSAIQARAILPVIKGHDVIAQAQSGTGKTATFSIAILQRIDPSIQAVQALILAPTRELAQQIQKVVIA 120
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 121 LGD-YMKINCHACIGGTNVREDMAKLNEGAQVVVGTPGRVYDMINRRAFKTDQLKMFCLDEADEMLSRGFKDQMYEVFQL 199
Cdd:cd17962 81 LMKgLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILEN 160
|
170 180 190
....*....|....*....|....*....|..
gi 388856094 200 LPQDTQCVLLSATMPHEVLEVTKKFMREPIRI 231
Cdd:cd17962 161 ISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
29-239 |
2.52e-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: 145.55 E-value: 2.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 29 IDNFDNMELKDELLRGVYAYGFERPSAIQARAiLPVIKGH---DVIAQAQSGTGKTATFSIAILQRIDPSIQAVQALILA 105
Cdd:cd18048 17 VKSFEELHLKEELLRGIYAMGFNRPSKIQENA-LPMMLADppqNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 106 PTRELAQQIQKVVIALGDYmkinchaCIG--------------GTNVRedmaklnegAQVVVGTPGRVYDMINR-RAFKT 170
Cdd:cd18048 96 PTFELALQTGKVVEEMGKF-------CVGiqviyairgnrpgkGTDIE---------AQIVIGTPGTVLDWCFKlRLIDV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 171 DQLKMFCLDEADEMLS-RGFKDQMYEVFQLLPQDTQCVLLSATMPHEVLEVTKKFMREPIRILVKRDELT 239
Cdd:cd18048 160 TNISVFVLDEADVMINvQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
32-235 |
2.61e-40 |
|
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: 142.63 E-value: 2.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 32 FDNMELKDELLRGVYAYGFERPSAIQARAILPVIKGHDVIAQAQSGTGKTATFSIAILQRI--DPSIQAV--------QA 101
Cdd:cd17967 2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLleDGPPSVGrgrrkaypSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 102 LILAPTRELAQQIQKVV--IALGDYMKINChaCIGGTNVREDMAKLNEGAQVVVGTPGRVYDMINRRAFKTDQLKMFCLD 179
Cdd:cd17967 82 LILAPTRELAIQIYEEArkFSYRSGVRSVV--VYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 180 EADEMLSRGFKDQMYEVFQ----LLPQDTQCVLLSATMPHEVLEVTKKFMREPIRILVKR 235
Cdd:cd17967 160 EADRMLDMGFEPQIRKIVEhpdmPPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVGR 219
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
42-231 |
2.87e-40 |
|
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein and is activated by Myc protein. DDX18 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350700 [Multi-domain] Cd Length: 198 Bit Score: 141.73 E-value: 2.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 42 LRGVYAYGFERPSAIQARAILPVIKGHDVIAQAQSGTGKTATFSIAILQ-----RIDPSiQAVQALILAPTRELAQQIQK 116
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIEllyklKFKPR-NGTGVIIISPTRELALQIYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 117 VVIALGDYMKINCHACIGGTNVREDMAKLNEGAQVVVGTPGRVYD-MINRRAFKTDQLKMFCLDEADEMLSRGFKDQMYE 195
Cdd:cd17942 81 VAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDhLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQ 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 388856094 196 VFQLLPQDTQCVLLSATMPHEVLEVTK-KFMREPIRI 231
Cdd:cd17942 161 IIKLLPKRRQTMLFSATQTRKVEDLARiSLKKKPLYV 197
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
29-227 |
4.10e-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: 143.57 E-value: 4.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 29 IDNFDNMELKDELLRGVYAYGFERPSAIQARAILPVIKGHDVIAQAQSGTGKTATFSIAILQR-----IDPS----IQAV 99
Cdd:cd18052 42 ILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGmmkegLTASsfseVQEP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 100 QALILAPTRELAQQIQKvvialgDYMKINCHACI------GGTNVREDMAKLNEGAQVVVGTPGRVYDMINRRAFKTDQL 173
Cdd:cd18052 122 QALIVAPTRELANQIFL------EARKFSYGTCIrpvvvyGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKL 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 388856094 174 KMFCLDEADEMLSRGFKDQMYEVFQLL----PQDTQCVLLSATMPHEVLEVTKKFMRE 227
Cdd:cd18052 196 KYLILDEADRMLDMGFGPEIRKLVSEPgmpsKEDRQTLMFSATFPEEIQRLAAEFLKE 253
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
41-233 |
5.90e-39 |
|
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350715 [Multi-domain] Cd Length: 198 Bit Score: 138.49 E-value: 5.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 41 LLRGVYAYGFERPSAIQARAIlPVI-KGHDVIAQAQSGTGKTATFSIAILQRIDPSIQA--VQALILAPTRELAQQIQKV 117
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAI-PILlHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKkgLRALILAPTRELASQIYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 118 VIALGDYMKINCHACIGGTNVR-EDMAKLNEGAQVVVGTPGRVYDMINRRAFKTDQLKMFCLDEADEMLSRGFKDQMYEV 196
Cdd:cd17957 80 LLKLSKGTGLRIVLLSKSLEAKaKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEI 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 388856094 197 FQLLPQ-DTQCVLLSATMPHEVLEVTKKFMREPIRILV 233
Cdd:cd17957 160 LAACTNpNLQRSLFSATIPSEVEELARSVMKDPIRIIV 197
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
42-233 |
1.43e-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: 134.72 E-value: 1.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 42 LRGVYAYGFERPSAIQARAILPVIKGHDVIAQAQSGTGKTATFSIAILQRID----PSIQAVQALILAPTRELAQQIQKV 117
Cdd:cd17941 2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYrerwTPEDGLGALIISPTRELAMQIFEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 118 VIALGDYMKINCHACIGGTNVREDMAKLNEgAQVVVGTPGRVYDMINRRA-FKTDQLKMFCLDEADEMLSRGFKDQMYEV 196
Cdd:cd17941 82 LRKVGKYHSFSAGLIIGGKDVKEEKERINR-MNILVCTPGRLLQHMDETPgFDTSNLQMLVLDEADRILDMGFKETLDAI 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 388856094 197 FQLLPQDTQCVLLSATMPHEVLEVTKKFMREPIRILV 233
Cdd:cd17941 161 VENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
41-231 |
8.74e-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: 132.49 E-value: 8.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 41 LLRGVYAYGFERPSAIQARAILPVIKGHDVIAQAQSGTGKTATFSI---------AILQRIDPSIqavqALILAPTRELA 111
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLpaivhinaqPPLERGDGPI----VLVLAPTRELA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 112 QQIQKVVIALGDYMKINCHACIGGTNVREDMAKLNEGAQVVVGTPGRVYDMINRRAFKTDQLKMFCLDEADEMLSRGFKD 191
Cdd:cd17966 77 QQIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 388856094 192 QMYEVFQLLPQDTQCVLLSATMPHEVLEVTKKFMREPIRI 231
Cdd:cd17966 157 QIRKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
41-231 |
3.03e-36 |
|
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: 131.31 E-value: 3.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 41 LLRGVYAYGFERPSAIQARAILPVIKGHDVIAQAQSGTGKTATFSI-AILQRID-----PSIQAVQ--ALILAPTRELAQ 112
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLpLIMFALEqekklPFIKGEGpyGLIVCPSRELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 113 QIQKVV------IALGDYMKINCHACIGGTNVREDMAKLNEGAQVVVGTPGRVYDMINRRAFKTDQLKMFCLDEADEMLS 186
Cdd:cd17951 81 QTHEVIeyyckaLQEGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 388856094 187 RGFKDQMYEVFQLLPQDTQCVLLSATMPHEVLEVTKKFMREPIRI 231
Cdd:cd17951 161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
49-231 |
4.38e-36 |
|
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: 131.17 E-value: 4.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 49 GFERPSAIQARAILPVIKGHDVIAQAQSGTGKTATFSIAILQRI---DPSIQ---AVQALILAPTRELAQQIQKVVIALG 122
Cdd:cd17949 10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLlslEPRVDrsdGTLALVLVPTRELALQIYEVLEKLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 123 DYMK-INCHACIGGTNVREDMAKLNEGAQVVVGTPGRVYDMI-NRRAFKTDQLKMFCLDEADEMLSRGFKDQMYEVFQLL 200
Cdd:cd17949 90 KPFHwIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLkNTQSFDVSNLRWLVLDEADRLLDMGFEKDITKILELL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 388856094 201 -------------PQDTQCVLLSATMPHEVLEVTKKFMREPIRI 231
Cdd:cd17949 170 ddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
32-228 |
5.08e-35 |
|
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: 128.30 E-value: 5.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 32 FDNMELKDELLRGVYAYGFERPSAIQARAiLPVIKG---HDVIAQAQSGTGKTATFSIAILQRIDPSIQAVQALILAPTR 108
Cdd:cd18047 3 FEELRLKPQLLQGVYAMGFNRPSKIQENA-LPLMLAeppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 109 ELAQQIQKVVIALGD-YMKINCHACIGGTNVrEDMAKLNEgaQVVVGTPGRVYD-MINRRAFKTDQLKMFCLDEADEML- 185
Cdd:cd18047 82 ELALQTGKVIEQMGKfYPELKLAYAVRGNKL-ERGQKISE--QIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADVMIa 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 388856094 186 SRGFKDQMYEVFQLLPQDTQCVLLSATMPHEVLEVTKKFMREP 228
Cdd:cd18047 159 TQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
2-235 |
1.46e-34 |
|
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: 128.23 E-value: 1.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 2 SKPDDSPAAANNLNIADGeiesnwetvIDNFDNMELKDELLRGVYAYGFERPSAIQARAILPVIKGHDVIAQAQSGTGKT 81
Cdd:cd18051 2 DKYEDIPVEATGENCPPH---------IETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 82 ATFSIAILQRI------DPSIQAVQ----------ALILAPTRELAQQIQKvvialgDYMKINCHACI------GGTNVR 139
Cdd:cd18051 73 AAFLLPILSQIyeqgpgESLPSESGyygrrkqyplALVLAPTRELASQIYD------EARKFAYRSRVrpcvvyGGADIG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 140 EDMAKLNEGAQVVVGTPGRVYDMINRRAFKTDQLKMFCLDEADEMLSRGFKDQMYEVFQllpQDT-------QCVLLSAT 212
Cdd:cd18051 147 QQMRDLERGCHLLVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVE---QDTmpptgerQTLMFSAT 223
|
250 260
....*....|....*....|...
gi 388856094 213 MPHEVLEVTKKFMREPIRILVKR 235
Cdd:cd18051 224 FPKEIQMLARDFLDNYIFLAVGR 246
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
49-231 |
2.72e-34 |
|
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: 126.04 E-value: 2.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 49 GFERPSAIQARAILPVIKGHDVIAQAQSGTGKTATF----SIAILQRIDPSIQAVQA--LILAPTRELAQQIQ-KVVIAL 121
Cdd:cd17958 9 GFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYllpgFIHLDLQPIPREQRNGPgvLVLTPTRELALQIEaECSKYS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 122 GDYMKINChaCIGGTNVREDMAKLNEGAQVVVGTPGRVYDMINRRAFKTDQLKMFCLDEADEMLSRGFKDQMYEVFQLLP 201
Cdd:cd17958 89 YKGLKSVC--VYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIRKILLDIR 166
|
170 180 190
....*....|....*....|....*....|
gi 388856094 202 QDTQCVLLSATMPHEVLEVTKKFMREPIRI 231
Cdd:cd17958 167 PDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
56-226 |
1.58e-33 |
|
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and nucleolar RNA helicase 2) is an RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II. It promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) and binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs. DDX50 (also called Gu-Beta, Nucleolar Protein Gu2, and malignant cell derived RNA helicase). DDX21 and DDX50 have similar genomic structures and are in tandem orientation on chromosome 10, suggesting that the two genes arose by gene duplication in evolution. Diseases associated with DDX21 include stomach disease and cerebral creatine deficiency syndrome 3. Diseases associated with DDX50 include rectal disease. Both are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. Their name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.
Pssm-ID: 350702 [Multi-domain] Cd Length: 202 Bit Score: 124.19 E-value: 1.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 56 IQARAILPVIKGHDVIAQAQSGTGKTATFSIAILQRIDPSIQ------AVQALILAPTRELAQQIQKVVIALGDYMKINC 129
Cdd:cd17944 16 IQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQprkrgrAPKVLVLAPTRELANQVTKDFKDITRKLSVAC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 130 HacIGGTNVREDMAKLNEGAQVVVGTPGRVYDMINRRAFKTDQLKMFCLDEADEMLSRGFKDQMYEVFQLL-----PQDT 204
Cdd:cd17944 96 F--YGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSVSykkdsEDNP 173
|
170 180
....*....|....*....|..
gi 388856094 205 QCVLLSATMPHEVLEVTKKFMR 226
Cdd:cd17944 174 QTLLFSATCPDWVYNVAKKYMK 195
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
41-213 |
1.29e-31 |
|
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: 120.04 E-value: 1.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 41 LLRGVYAYGFERPSAIQARAILPVIK-GHDVIAQAQSGTGKTATFSIAILQRI---------DPSIQAVQALILAPTREL 110
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLlsqkssngvGGKQKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 111 AQQIQKVVIALGDYMKINCHACIGGTNVREDMAKLNEGAQVVVGTPGRVYDMI---NRRAFKTDQLKMFCLDEADEMLSR 187
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIqegNEHLANLKSLRFLVLDEADRMLEK 160
|
170 180 190
....*....|....*....|....*....|...
gi 388856094 188 GFKDQMYEVFQLLPQDT-------QCVLLSATM 213
Cdd:cd17946 161 GHFAELEKILELLNKDRagkkrkrQTFVFSATL 193
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
255-358 |
1.05e-29 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 110.76 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 255 WKLETLCDLYETVTITQAVIFCNTRRKVDwlTDKLTARE-FTVSAMHGDMEQGQREIIMREFRSGSSRVLITTDLLARGI 333
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLE--AELLLEKEgIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
|
90 100
....*....|....*....|....*
gi 388856094 334 DVQQVSLVINYDLPSNRENYIHRIG 358
Cdd:pfam00271 79 DLPDVDLVINYDLPWNPASYIQRIG 103
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
31-231 |
5.88e-29 |
|
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: 112.80 E-value: 5.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 31 NFDNMELKDELLRGVYAYGFERPSAIQARAILPVIKGHDVIAQAQSGTGKTATFSIA---------ILQRIDPSIqavqA 101
Cdd:cd18049 25 NFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPaivhinhqpFLERGDGPI----C 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 102 LILAPTRELAQQIQKVVIALGDYMKINCHACIGGTNVREDMAKLNEGAQVVVGTPGRVYDMINRRAFKTDQLKMFCLDEA 181
Cdd:cd18049 101 LVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 388856094 182 DEMLSRGFKDQMYEVFQLLPQDTQCVLLSATMPHEVLEVTKKFMREPIRI 231
Cdd:cd18049 181 DRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHI 230
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
48-223 |
1.38e-28 |
|
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350706 [Multi-domain] Cd Length: 231 Bit Score: 111.69 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 48 YGFERPSAIQARAILPVIKGHDVIAQAQSGTGKTATFSIAILQRI-------DPSIQAVQALILAPTRELAQQIQKVVIA 120
Cdd:cd17948 8 QGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLlrykllaEGPFNAPRGLVITPSRELAEQIGSVAQS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 121 LGDYMKINCHACIGGTNVREDMAKLNEGAQVVVGTPGRVYDMINRRAFKTDQLKMFCLDEADEMLSRGFKDQM---YEVF 197
Cdd:cd17948 88 LTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKLshfLRRF 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 388856094 198 QL----------LPQDTQCVLLSATMPHEVLEVTKK 223
Cdd:cd17948 168 PLasrrsentdgLDPGTQLVLVSATMPSGVGEVLSK 203
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
50-231 |
8.52e-28 |
|
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: 110.87 E-value: 8.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 50 FERPSAIQARAILPVIKGHDVIAQAQSGTGKTATFSIAILQRID--PSIQAVQA---LILAPTRELAQQIQKVVIALGDY 124
Cdd:cd18050 82 FKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINhqPYLERGDGpicLVLAPTRELAQQVQQVADDYGKS 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 125 MKINCHACIGGTNVREDMAKLNEGAQVVVGTPGRVYDMINRRAFKTDQLKMFCLDEADEMLSRGFKDQMYEVFQLLPQDT 204
Cdd:cd18050 162 SRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDR 241
|
170 180
....*....|....*....|....*..
gi 388856094 205 QCVLLSATMPHEVLEVTKKFMREPIRI 231
Cdd:cd18050 242 QTLMWSATWPKEVRQLAEDFLRDYVQI 268
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
67-212 |
1.33e-23 |
|
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: 95.55 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 67 GHDVIAQAQSGTGKTATFSIAILQRIDPsiQAVQALILAPTRELAQQIQKVVIALGDyMKINCHACIGGTNVREDMAKLN 146
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLK--KGKKVLVLVPTKALALQTAERLRELFG-PGIRVAVLVGGSSAEEREKNKL 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 388856094 147 EGAQVVVGTPGRVYDMINR-RAFKTDQLKMFCLDEADEMLSRGFKDQM--YEVFQLLPQDTQCVLLSAT 212
Cdd:cd00046 78 GDADIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLIDSRGALIldLAVRKAGLKNAQVILLSAT 146
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
283-357 |
1.95e-23 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 93.05 E-value: 1.95e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 388856094 283 DWLTDKLTAREFTVSAMHGDMEQGQREIIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPSNRENYIHRI 357
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRI 75
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
53-213 |
7.46e-19 |
|
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: 84.61 E-value: 7.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 53 PSAIQARAILPVIKGHDVIAQAQSGTGKTATFSIAILQ----RIDPSIQAvqaLILAPTRELAQQIQKVVIALGDYMKIN 128
Cdd:cd17956 22 PWLLPSSKSTPPYRPGDLCVSAPTGSGKTLAYVLPIVQalskRVVPRLRA---LIVVPTKELVQQVYKVFESLCKGTGLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 129 CHACIGGTNVREDMAKLNEG--------AQVVVGTPGRVYDMINR-RAFKTDQLKMFCLDEADEMLSRGFKD----QMYE 195
Cdd:cd17956 99 VVSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRLVDHLNStPGFTLKHLRFLVIDEADRLLNQSFQDwletVMKA 178
|
170 180 190
....*....|....*....|....*....|....
gi 388856094 196 VFQLLPQDTQC----------------VLLSATM 213
Cdd:cd17956 179 LGRPTAPDLGSfgdanllersvrplqkLLFSATL 212
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
37-350 |
1.76e-13 |
|
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: 72.18 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 37 LKDELLRGVYAYGFERPSAIQARAILPVIKGHDVIAQAQSGTGKTATFSIAILQRI--DPSiqaVQALILAPTRELAQ-Q 113
Cdd:COG1205 41 LPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALleDPG---ATALYLYPTKALARdQ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 114 IQKV---VIALGdyMKINCHACIGGTNvREDMAKLNEGAQVVVGTPgrvyDMIN----------RRAFKTdqLKMFCLDE 180
Cdd:COG1205 118 LRRLrelAEALG--LGVRVATYDGDTP-PEERRWIREHPDIVLTNP----DMLHygllphhtrwARFFRN--LRYVVIDE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 181 ADEMlsRG-FKDQMYEVF-------QLLPQDTQCVLLSATM--PHE---------VLEVTKK----------FMREPIRI 231
Cdd:COG1205 189 AHTY--RGvFGSHVANVLrrlrricRHYGSDPQFILASATIgnPAEhaerltgrpVTVVDEDgsprgertfvLWNPPLVD 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 232 LVKRDELTLEGIKQFYVAVEKEewkLETLCdlyetvtitqaviFCNTRRKV----DWLTDKLTAREFT--VSAMHGDMEQ 305
Cdd:COG1205 267 DGIRRSALAEAARLLADLVREG---LRTLV-------------FTRSRRGAellaRYARRALREPDLAdrVAAYRAGYLP 330
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 388856094 306 GQREIIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPSNR 350
Cdd:COG1205 331 EERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTR 375
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
77-342 |
5.15e-13 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 70.44 E-value: 5.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 77 GTGKT--ATFSIAILQRIDPsiqavqALILAPTRELAQQIQKvvialgDYMKINCHACIGGTnvredmaKLNEGAQVVVG 154
Cdd:COG1061 110 GTGKTvlALALAAELLRGKR------VLVLVPRRELLEQWAE------ELRRFLGDPLAGGG-------KKDSDAPITVA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 155 TPGRVYDMINRRAFKtDQLKMFCLDEADEMLSRGFKdqmyEVFQLLPqDTQCVLLSAT--------MPHEVL-----EVT 221
Cdd:COG1061 171 TYQSLARRAHLDELG-DRFGLVIIDEAHHAGAPSYR----RILEAFP-AAYRLGLTATpfrsdgreILLFLFdgivyEYS 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 222 -KKFMRE----PIRILVKRDELTLEG-----IKQFYVA--VEKEEWKLETLCD-LYETVTITQAVIFCNTRRKVDWLTDK 288
Cdd:COG1061 245 lKEAIEDgylaPPEYYGIRVDLTDERaeydaLSERLREalAADAERKDKILRElLREHPDDRKTLVFCSSVDHAEALAEL 324
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 388856094 289 LTAREFTVSAMHGDMEQGQREIIMREFRSGSSRVLITTDLLARGIDVQQVSLVI 342
Cdd:COG1061 325 LNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI 378
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
247-354 |
6.10e-12 |
|
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: 62.99 E-value: 6.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 247 YVAVEKEEWKLETLCDLYETVTITQAVIFCNTR---------------RKVDWLTDKLTAREFTVSAMHGDMEQGQREII 311
Cdd:cd18802 3 IVVIPKLQKLIEILREYFPKTPDFRGIIFVERRatavvlsrllkehpsTLAFIRCGFLIGRGNSSQRKRSLMTQRKQKET 82
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 388856094 312 MREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPSNRENYI 354
Cdd:cd18802 83 LDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYI 125
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
256-349 |
7.09e-11 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 59.41 E-value: 7.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 256 KLETLCDLYETVTITQ--AVIFCNTRRKVDWLTDKLTAREFTVSAMHGDMEQGQREIIMREFRSGSS--RVLITTDLLAR 331
Cdd:cd18793 12 KLEALLELLEELREPGekVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDirVFLLSTKAGGV 91
|
90
....*....|....*...
gi 388856094 332 GIDVQQVSLVINYDLPSN 349
Cdd:cd18793 92 GLNLTAANRVILYDPWWN 109
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
32-231 |
1.91e-10 |
|
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: 60.85 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 32 FDNMEL--------KDELLRGVYAYGFER-PSAIQARAIlPVIKGHDVIAQ-----------------AQSGTGKTATFS 85
Cdd:cd17965 1 FDQLKLlpsvreaiIKEILKGSNKTDEEIkPSPIQTLAI-KKLLKTLMRKVtkqtsneepklevfllaAETGSGKTLAYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 86 IAIL-----QRIDPSIQA------------VQALILAPTRELAQQIQKVVIALGDYMK--INCHACIGGTNVREDMAKLN 146
Cdd:cd17965 80 APLLdylkrQEQEPFEEAeeeyesakdtgrPRSVILVPTHELVEQVYSVLKKLSHTVKlgIKTFSSGFGPSYQRLQLAFK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 147 EGAQVVVGTPGRVYDM--INRRAFKtdQLKMFCLDEADEMLSRGFKDQMYEVFQLLPQDTQCVLLSATMPHEVLEVTKKF 224
Cdd:cd17965 160 GRIDILVTTPGKLASLakSRPKILS--RVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLRKL 237
|
....*..
gi 388856094 225 MREPIRI 231
Cdd:cd17965 238 FPDVVRI 244
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
273-353 |
3.69e-10 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 61.31 E-value: 3.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 273 VIFCNTRRKVDWLTDKLTAREFTVSAMHGDMEQGQREIIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPSNREN 352
Cdd:COG0514 234 IVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEA 313
|
.
gi 388856094 353 Y 353
Cdd:COG0514 314 Y 314
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
272-353 |
4.01e-08 |
|
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: 51.83 E-value: 4.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 272 AVIFCNTRRKVDWLTDKLTAREFTVSAMHGDMEQGQREIIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPSNRE 351
Cdd:cd18794 33 GIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSME 112
|
..
gi 388856094 352 NY 353
Cdd:cd18794 113 SY 114
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
57-333 |
4.06e-08 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 54.90 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 57 QARAI-LPVIKGHDVIAQAQSGTGKTATFSIAILQRIDpsiQAVQALILAPTRELAQQI------------QKVVIALGD 123
Cdd:COG1204 27 QAEALeAGLLEGKNLVVSAPTASGKTLIAELAILKALL---NGGKALYIVPLRALASEKyrefkrdfeelgIKVGVSTGD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 124 YmkinchaciggtnvREDMAKLNEgAQVVVGTPGRVYDMINRRAFKTDQLKMFCLDEA----DEmlSRGFKdqmYEV--- 196
Cdd:COG1204 104 Y--------------DSDDEWLGR-YDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAhlidDE--SRGPT---LEVlla 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 197 -FQLLPQDTQCVLLSATM--PHEVLE-VTKKFMREPIRIlVKRDELTL-EGIKQFyvaVEKEEWKLETLCDL-YETVTI- 269
Cdd:COG1204 164 rLRRLNPEAQIVALSATIgnAEEIAEwLDAELVKSDWRP-VPLNEGVLyDGVLRF---DDGSRRSKDPTLALaLDLLEEg 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 270 TQAVIFCNTRRKV--------DWLTDKLTARE---------------------FTVSAM--------HGDMEQGQREIIM 312
Cdd:COG1204 240 GQVLVFVSSRRDAeslakklaDELKRRLTPEEreeleelaeellevseethtnEKLADClekgvafhHAGLPSELRRLVE 319
|
330 340
....*....|....*....|.
gi 388856094 313 REFRSGSSRVLITTDLLARGI 333
Cdd:COG1204 320 DAFREGLIKVLVATPTLAAGV 340
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
273-353 |
4.49e-08 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 55.10 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 273 VIFCNTRRKVDWLTDKLTAREFTVSAMHGDMEQGQREIIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPSNREN 352
Cdd:PRK11057 240 IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIES 319
|
.
gi 388856094 353 Y 353
Cdd:PRK11057 320 Y 320
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
57-213 |
5.96e-08 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 52.20 E-value: 5.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 57 QARAILPVIKGHDVIAQAQSGTGKTATFSIAILQRI--DPSiqaVQALILAPTRELAQQIQKVVIALGDYM--KINCHAC 132
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALlrDPG---SRALYLYPTKALAQDQLRSLRELLEQLglGIRVATY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 133 IGGT--NVREDMAKlnEGAQVVVGTPgrvyDMIN----------RRAFKTdqLKMFCLDEAD----------EMLSRGFK 190
Cdd:cd17923 82 DGDTprEERRAIIR--NPPRILLTNP----DMLHyallphhdrwARFLRN--LRYVVLDEAHtyrgvfgshvALLLRRLR 153
|
170 180
....*....|....*....|...
gi 388856094 191 DqmyeVFQLLPQDTQCVLLSATM 213
Cdd:cd17923 154 R----LCRRYGADPQFILTSATI 172
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
272-352 |
3.90e-07 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 52.15 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 272 AVIFCNTRRKVDWLTDKLTAREFTVSAMHGDMEQGQREIIMREFRSGSS--RVLITTDLLARGIDVQQVSLVINYDLPSN 349
Cdd:COG0553 552 VLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEapVFLISLKAGGEGLNLTAADHVIHYDLWWN 631
|
....*
gi 388856094 350 --REN 352
Cdd:COG0553 632 paVEE 636
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
271-348 |
1.60e-06 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 50.11 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 271 QAVIFCNTRRKVDWLTDKLTAREFTV------SAMHGD--MEQGQREIIMREFRSGSSRVLITTDLLARGIDVQQVSLVI 342
Cdd:COG1111 355 RIIVFTQYRDTAEMIVEFLSEPGIKAgrfvgqASKEGDkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVI 434
|
....*..
gi 388856094 343 NYDL-PS 348
Cdd:COG1111 435 FYEPvPS 441
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
274-349 |
1.92e-06 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 47.26 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 274 IFCNTRRKVDWLTDKLTAR------EFTVSAMHGDMEQGQREIIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLP 347
Cdd:cd18796 43 VFTNTRSQAERLAQRLRELcpdrvpPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSP 122
|
..
gi 388856094 348 SN 349
Cdd:cd18796 123 KS 124
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
56-214 |
4.04e-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: 46.87 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 56 IQARAILPVI-KGHDVIAQAQSGTGKTATFSIAILQRIDPSIQavQALILAPTRELAQQI-QKVVIALGDYMKiNCHACI 133
Cdd:cd17921 5 IQREALRALYlSGDSVLVSAPTSSGKTLIAELAILRALATSGG--KAVYIAPTRALVNQKeADLRERFGPLGK-NVGLLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 134 GgtNVREDMAKLNEgAQVVVGTPGRVYDMINR-RAFKTDQLKMFCLDEA----DEmlSRGfkdQMYEV----FQLLPQDT 204
Cdd:cd17921 82 G--DPSVNKLLLAE-ADILVATPEKLDLLLRNgGERLIQDVRLVVVDEAhligDG--ERG---VVLELllsrLLRINKNA 153
|
170
....*....|
gi 388856094 205 QCVLLSATMP 214
Cdd:cd17921 154 RFVGLSATLP 163
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
271-333 |
8.15e-06 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350182 [Multi-domain] Cd Length: 154 Bit Score: 45.62 E-value: 8.15e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 388856094 271 QAVIFCNTRRKVdwltdKLTAREFT-VSAMHGDMEQGQREIIMREFRSGSSRVLITTDLLARGI 333
Cdd:cd18795 45 PVLVFCSSRKEC-----EKTAKDLAgIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGV 103
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
52-155 |
9.20e-06 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 45.87 E-value: 9.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 52 RPSAIQARAILPVIKG------HDVIAQAQSGTGKTATFSIAILQRIDpsiQAVQALILAPTRELAQQIQKVVIALgdYM 125
Cdd:cd17918 15 SLTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAALLAYK---NGKQVAILVPTEILAHQHYEEARKF--LP 89
|
90 100 110
....*....|....*....|....*....|
gi 388856094 126 KINCHACIGGTNvredmAKLNEGAQVVVGT 155
Cdd:cd17918 90 FINVELVTGGTK-----AQILSGISLLVGT 114
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
278-345 |
2.85e-05 |
|
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350177 [Multi-domain] Cd Length: 171 Bit Score: 44.16 E-value: 2.85e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 388856094 278 TRRKVDWLTDKLTAREFTVSAMHGDMEQGQREIIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYD 345
Cdd:cd18790 36 TKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILD 103
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
285-345 |
5.17e-05 |
|
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: 43.10 E-value: 5.17e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 388856094 285 LTDKLTArEFTVSAMHGDMEQGQREIIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYD 345
Cdd:cd18811 54 LKERFRP-ELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIED 113
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
207-326 |
2.18e-04 |
|
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: 43.15 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 207 VLLSATMPHEVlevtKKFMREPIRILVKRDELTLEGIKQFY---VAVEKEEWKLETLCDLYETV--TITQAVIFCNTRRK 281
Cdd:COG1203 303 ILMTATLPPLL----REELLEAYELIPDEPEELPEYFRAFVrkrVELKEGPLSDEELAELILEAlhKGKSVLVIVNTVKD 378
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 388856094 282 VDWLTDKLTAREFTVSAM--HGDMEQGQR----EIIMREFRSGSSRVLITT 326
Cdd:COG1203 379 AQELYEALKEKLPDEEVYllHSRFCPADRseieKEIKERLERGKPCILVST 429
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
293-345 |
8.08e-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: 8.08e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 388856094 293 EFTVSAMHGDMEQGQREIIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYD 345
Cdd:cd18792 60 EARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIED 112
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
272-342 |
1.18e-03 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350186 [Multi-domain] Cd Length: 116 Bit Score: 38.31 E-value: 1.18e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 388856094 272 AVIFCNTRRKVDWLTDKLTAREFTVSAMHGD--MEQGQREIIMR-EFRSGSSRVLITTDLLARGIDVQQVSLVI 342
Cdd:cd18799 9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDysDRERGDEALILlFFGELKPPILVTVDLLTTGVDIPEVDNVV 82
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
207-335 |
2.26e-03 |
|
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: 39.72 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 207 VLLSATMPH--------------EVLEVTKKFMREPIRILVKR---DELTLEGIKQFYvaveKEEwkletlcdlyetvti 269
Cdd:cd09639 158 LLMSATLPKflkeyaekigyveeNEPLDLKPNERAPFIKIESDkvgEISSLERLLEFI----KKG--------------- 218
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 388856094 270 TQAVIFCNTRRKV----DWLTDKltAREFTVSAMHGDMEQGQR----EIIMREFRSGSSRVLITTDLLARGIDV 335
Cdd:cd09639 219 GSVAIIVNTVDRAqefyQQLKEK--GPEEEIMLIHSRFTEKDRakkeAELLLEFKKSEKFVIVATQVIEASLDI 290
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
267-358 |
2.40e-03 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 36.53 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 267 VTITQAVIFCNTRRKVDWLTDKLTareftvsamhgdmeqgqreiimrefrsgssrVLITTDLLARGIDVQQVSLVINYDL 346
Cdd:cd18785 1 VMVVKIIVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDP 49
|
90
....*....|..
gi 388856094 347 PSNRENYIHRIG 358
Cdd:cd18785 50 PSSAASYIQRVG 61
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
273-353 |
3.04e-03 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 39.88 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 273 VIFCNTRRKVDWLTDKLtaREFTVSAM--HGDMEQGQREIIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPSNR 350
Cdd:PLN03137 684 IIYCLSRMDCEKVAERL--QEFGHKAAfyHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSI 761
|
...
gi 388856094 351 ENY 353
Cdd:PLN03137 762 EGY 764
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
257-345 |
3.76e-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: 37.72 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 257 LETLCDLYE---TVTITQAVIFCNTRRKVDWLTDKLTAREFTVSAM----HGD------MEQGQREIIMREFRSGSSRVL 323
Cdd:cd18801 15 EEIVKEHFKkkqEGSDTRVIIFSEFRDSAEEIVNFLSKIRPGIRATrfigQASgksskgMSQKEQKEVIEQFRKGGYNVL 94
|
90 100
....*....|....*....|..
gi 388856094 324 ITTDLLARGIDVQQVSLVINYD 345
Cdd:cd18801 95 VATSIGEEGLDIGEVDLIICYD 116
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
46-217 |
3.89e-03 |
|
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also called SKI2 or DHX13) plays a role in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. SKIV2L 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: 350785 [Multi-domain] Cd Length: 179 Bit Score: 38.01 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 46 YAYGFErPSAIQARAILPVIKGHDVIAQAQSGTGKT--ATFSIAILQRidpsiQAVQALILAPTRELA-QQIQKVVIALG 122
Cdd:cd18027 3 FKWPFE-LDVFQKQAILHLEAGDSVFVAAHTSAGKTvvAEYAIALAQK-----HMTRTIYTSPIKALSnQKFRDFKNTFG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 123 DYmkinchACIGGTnvredmAKLNEGAQVVVGTPGRVYDMINRRAFKTDQLKMFCLDEADEM--LSRGFKDQmyEVFQLL 200
Cdd:cd18027 77 DV------GLITGD------VQLNPEASCLIMTTEILRSMLYNGSDVIRDLEWVIFDEVHYIndAERGVVWE--EVLIML 142
|
170
....*....|....*..
gi 388856094 201 PQDTQCVLLSATMPHEV 217
Cdd:cd18027 143 PDHVSIILLSATVPNTV 159
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
274-347 |
8.58e-03 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 38.54 E-value: 8.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388856094 274 IFCNTRRkvdwLTDKLTAR--------EFTVSAMHGDMEQGQREIIMREFRSGSSRVLITT---DLlarGIDVQQVSLVI 342
Cdd:COG1201 277 VFTNTRS----QAERLFQRlnelnpedALPIAAHHGSLSREQRLEVEEALKAGELRAVVATsslEL---GIDIGDVDLVI 349
|
....*
gi 388856094 343 NYDLP 347
Cdd:COG1201 350 QVGSP 354
|
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