|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
5-402 |
0e+00 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 622.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 5 KNDVNVSSVVDADGLIEGNYDQVVESFDDMELKEELLRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFS 84
Cdd:PTZ00424 4 SEQKNQSEQVASTGTIESNYDEIVDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 85 VSILQRIDHEDPHVQALVMAPTRELAQQIQKVMSALGEYLNVNILPCIGGTSVRDDQRKLEAGIHVVVGTPGRVGDMINR 164
Cdd:PTZ00424 84 IAALQLIDYDLNACQALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 165 NALDTSRIKMFVLDEADEMLSRGFKDQIYEVFRSMPQDVQVVLLSATMPSEVLDVTNRFMRNPIRILVKKDELTLEGIRQ 244
Cdd:PTZ00424 164 RHLRVDDLKLFILDEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 245 FYINVQKDEWKFDCLCDLYNVVNVTQAVIFCNTRRKVDTLTEKMTENQFTVSCLHGDMDQAERDTIMREFRSGSSRVLIT 324
Cdd:PTZ00424 244 FYVAVEKEEWKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLIT 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71987143 325 TDILARGIDVQQVSLVINYDLPSNRENYIHRIGRSGRFGRKGVAINFVTENDARQLKEIESYYTTQIEEMPESIADLI 402
Cdd:PTZ00424 324 TDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEVADYL 401
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
30-395 |
5.35e-168 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 476.56 E-value: 5.35e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 30 SFDDMELKEELLRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQRIDHEDP-HVQALVMAPTRE 108
Cdd:COG0513 3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPrAPQALILAPTRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 109 LAQQIQKVMSALGEYLNVNILPCIGGTSVRDDQRKLEAGIHVVVGTPGRVGDMINRNALDTSRIKMFVLDEADEMLSRGF 188
Cdd:COG0513 83 LALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 189 KDQIYEVFRSMPQDVQVVLLSATMPSEVLDVTNRFMRNPIRILVKKDELTLEGIRQFYINVQKDEwKFDCLCDLYNVVNV 268
Cdd:COG0513 163 IEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRD-KLELLRRLLRDEDP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 269 TQAVIFCNTRRKVDTLTEKMTENQFTVSCLHGDMDQAERDTIMREFRSGSSRVLITTDILARGIDVQQVSLVINYDLPSN 348
Cdd:COG0513 242 ERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPED 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 71987143 349 RENYIHRIGRSGRFGRKGVAINFVTENDARQLKEIESYYTTQIEEMP 395
Cdd:COG0513 322 PEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEE 368
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
31-231 |
4.12e-141 |
|
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: 399.90 E-value: 4.12e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 31 FDDMELKEELLRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQRIDHEDPHVQALVMAPTRELA 110
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 111 QQIQKVMSALGEYLNVNILPCIGGTSVRDDQRKLEAGIHVVVGTPGRVGDMINRNALDTSRIKMFVLDEADEMLSRGFKD 190
Cdd:cd18046 81 QQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 71987143 191 QIYEVFRSMPQDVQVVLLSATMPSEVLDVTNRFMRNPIRIL 231
Cdd:cd18046 161 QIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRIL 201
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
33-231 |
3.45e-120 |
|
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: 347.00 E-value: 3.45e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 33 DMELKEELLRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQRIDHEDPHVQALVMAPTRELAQQ 112
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 113 IQKVMSALGEYLNVNILPCIGGTSVRDDQRKLEAGIHVVVGTPGRVGDMINRNALDTSRIKMFVLDEADEMLSRGFKDQI 192
Cdd:cd17939 81 IQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQI 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 71987143 193 YEVFRSMPQDVQVVLLSATMPSEVLDVTNRFMRNPIRIL 231
Cdd:cd17939 161 YDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRIL 199
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
30-392 |
3.69e-107 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 323.29 E-value: 3.69e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 30 SFDDMELKEELLRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQRIDHEDPHVQALVMAPTREL 109
Cdd:PRK11776 5 AFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTREL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 110 AQQIQKVMSALGEYL-NVNILPCIGGTSVRDDQRKLEAGIHVVVGTPGRVGDMINRNALDTSRIKMFVLDEADEMLSRGF 188
Cdd:PRK11776 85 ADQVAKEIRRLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMGF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 189 KDQIYEVFRSMPQDVQVVLLSATMPSEVLDVTNRFMRNPIRILV--KKDELTlegIRQFYINVQKDEwKFDCLCDLYNVV 266
Cdd:PRK11776 165 QDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVesTHDLPA---IEQRFYEVSPDE-RLPALQRLLLHH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 267 NVTQAVIFCNTRRKVDTLTEKMTENQFTVSCLHGDMDQAERDTIMREFRSGSSRVLITTDILARGIDVQQVSLVINYDLP 346
Cdd:PRK11776 241 QPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELA 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 71987143 347 SNRENYIHRIGRSGRFGRKGVAINFVTENDARQLKEIESYYTTQIE 392
Cdd:PRK11776 321 RDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLN 366
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
31-231 |
2.30e-100 |
|
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: 296.69 E-value: 2.30e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 31 FDDMELKEELLRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQRIDHEDPHVQALVMAPTRELA 110
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 111 QQIQKVMSALGEYLNVNILPCIGGTSVRDDQRKLEAGIHVVVGTPGRVGDMINRNALDTSRIKMFVLDEADEMLSRGFKD 190
Cdd:cd18045 81 VQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 71987143 191 QIYEVFRSMPQDVQVVLLSATMPSEVLDVTNRFMRNPIRIL 231
Cdd:cd18045 161 QIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRIL 201
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
30-402 |
3.62e-87 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 276.73 E-value: 3.62e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 30 SFDDMELKEELLRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQRIDHEDPHVQALVMAPTREL 109
Cdd:PRK11634 7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 110 AQQIQKVMSALGEYLN-VNILPCIGGTSVRDDQRKLEAGIHVVVGTPGRVGDMINRNALDTSRIKMFVLDEADEMLSRGF 188
Cdd:PRK11634 87 AVQVAEAMTDFSKHMRgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 189 KDQIYEVFRSMPQDVQVVLLSATMPSEVLDVTNRFMRNPIRILVKKDELTLEGIRQFYINVQKDEwKFDCLCDLYNVVNV 268
Cdd:PRK11634 167 IEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMR-KNEALVRFLEAEDF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 269 TQAVIFCNTRRKVDTLTEKMTENQFTVSCLHGDMDQAERDTIMREFRSGSSRVLITTDILARGIDVQQVSLVINYDLPSN 348
Cdd:PRK11634 246 DAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMD 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 71987143 349 RENYIHRIGRSGRFGRKGVAINFVTENDARQLKEIESYYTTQIEEMPESIADLI 402
Cdd:PRK11634 326 SESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAELL 379
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
40-230 |
4.40e-85 |
|
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350669 [Multi-domain] Cd Length: 196 Bit Score: 257.37 E-value: 4.40e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 40 LLRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQRIDHED----PHVQALVMAPTRELAQQIQK 115
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPkkkgRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 116 VMSALGEYLNVNILPCIGGTSVRDDQRKLEAGIHVVVGTPGRVGDMINRNALDTSRIKMFVLDEADEMLSRGFKDQIYEV 195
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 71987143 196 FRSMPQDVQVVLLSATMPSEVLDVTNRFMRNPIRI 230
Cdd:cd00268 161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
30-394 |
1.53e-83 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 262.44 E-value: 1.53e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 30 SFDDMELKEELLRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQRIDHEDPH------VQALVM 103
Cdd:PRK10590 2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHakgrrpVRALIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 104 APTRELAQQIQKVMSALGEYLNVNILPCIGGTSVRDDQRKLEAGIHVVVGTPGRVGDMINRNALDTSRIKMFVLDEADEM 183
Cdd:PRK10590 82 TPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 184 LSRGFKDQIYEVFRSMPQDVQVVLLSATMPSEVLDVTNRFMRNPIRILVKKDELTLEGIRQFYINVQKDEwKFDCLCDLY 263
Cdd:PRK10590 162 LDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKR-KRELLSQMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 264 NVVNVTQAVIFCNTRRKVDTLTEKMTENQFTVSCLHGDMDQAERDTIMREFRSGSSRVLITTDILARGIDVQQVSLVINY 343
Cdd:PRK10590 241 GKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNY 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 71987143 344 DLPSNRENYIHRIGRSGRFGRKGVAINFVTENDARQLKEIESYYTTQIEEM 394
Cdd:PRK10590 321 ELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRI 371
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
31-393 |
3.59e-81 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 255.64 E-value: 3.59e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 31 FDDMELKEELLRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQ------RIDHEDPHVqaLVMA 104
Cdd:PRK11192 3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQhlldfpRRKSGPPRI--LILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 105 PTRELAQQIQKVMSALGEYLNVNILPCIGGTSVRDDQRKLEAGIHVVVGTPGRVGDMINRNALDTSRIKMFVLDEADEML 184
Cdd:PRK11192 81 PTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 185 SRGFKdqiyevfrsmpQDV-----------QVVLLSATMPSE-VLDVTNRFMRNPIRILVKKDELTLEGIRQFYINVQKD 252
Cdd:PRK11192 161 DMGFA-----------QDIetiaaetrwrkQTLLFSATLEGDaVQDFAERLLNDPVEVEAEPSRRERKKIHQWYYRADDL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 253 EWKFDCLCDLYNVVNVTQAVIFCNTRRKVDTLTEKMTENQFTVSCLHGDMDQAERDTIMREFRSGSSRVLITTDILARGI 332
Cdd:PRK11192 230 EHKTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGI 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71987143 333 DVQQVSLVINYDLPSNRENYIHRIGRSGRFGRKGVAINFVTENDARQLKEIESYyttqIEE 393
Cdd:PRK11192 310 DIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERY----IEE 366
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
31-395 |
8.19e-78 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 248.29 E-value: 8.19e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 31 FDDMELKEELLRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQRIDHEDPHVQ-------ALVM 103
Cdd:PRK01297 89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKErymgeprALII 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 104 APTRELAQQIQKVMSALGEYLNVNILPCIGGTSVRDDQRKLEAG-IHVVVGTPGRVGDMINRNALDTSRIKMFVLDEADE 182
Cdd:PRK01297 169 APTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEADR 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 183 MLSRGFKDQIYEVFRSMP--QDVQVVLLSATMPSEVLDVTNRFMRNPIRILVKKDELTLEGIRQ-FYINVQKDEWKFdcl 259
Cdd:PRK01297 249 MLDMGFIPQVRQIIRQTPrkEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQhVYAVAGSDKYKL--- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 260 cdLYNVV---NVTQAVIFCNTRRKVDTLTEKMTENQFTVSCLHGDMDQAERDTIMREFRSGSSRVLITTDILARGIDVQQ 336
Cdd:PRK01297 326 --LYNLVtqnPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDG 403
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 337 VSLVINYDLPSNRENYIHRIGRSGRFGRKGVAINFVTENDARQLKEIESYYTTQIE-EMP 395
Cdd:PRK01297 404 ISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKIScEMP 463
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
31-230 |
1.71e-74 |
|
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: 230.65 E-value: 1.71e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 31 FDDMELKEELLRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQRIDHEDPHVQALVMAPTRELA 110
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 111 QQIQKVMSALGEYLNVNILPCIGGTSVRDDQRKLEAGIHVVVGTPGRVGDMINRNALDTSRIKMFVLDEADEMLSRGFKD 190
Cdd:cd17940 81 LQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 71987143 191 QIYEVFRSMPQDVQVVLLSATMPSEVLDVTNRFMRNPIRI 230
Cdd:cd17940 161 IIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
30-395 |
3.84e-71 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 233.69 E-value: 3.84e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 30 SFDDMELKEELLRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQRI---------DHEDPhvQA 100
Cdd:PRK04537 10 TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlsrpaladrKPEDP--RA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 101 LVMAPTRELAQQIQKVMSALGEYLNVNILPCIGGTSVrDDQRK-LEAGIHVVVGTPGRVGDMINRNALDTSRI-KMFVLD 178
Cdd:PRK04537 88 LILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDY-DKQRElLQQGVDVIIATPGRLIDYVKQHKVVSLHAcEICVLD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 179 EADEMLSRGFKDQIYEVFRSMPQDV--QVVLLSATMPSEVLDVTNRFMRNPIRILVKKDELTLEGIRQfYINVQKDEWKF 256
Cdd:PRK04537 167 EADRMFDLGFIKDIRFLLRRMPERGtrQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQ-RIYFPADEEKQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 257 DCLCDLYNVVNVTQAVIFCNTRRKVDTLTEKMTENQFTVSCLHGDMDQAERDTIMREFRSGSSRVLITTDILARGIDVQQ 336
Cdd:PRK04537 246 TLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDG 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 71987143 337 VSLVINYDLPSNRENYIHRIGRSGRFGRKGVAINFVTENDARQLKEIESYYTTQIEEMP 395
Cdd:PRK04537 326 VKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKIPVEP 384
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
19-383 |
2.90e-70 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 230.43 E-value: 2.90e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 19 LIEG-NYDQVVESFDDMELKEELLRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFsvsILQRIDH---- 93
Cdd:PTZ00110 119 IIAGeNVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAF---LLPAIVHinaq 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 94 ------EDPHVqaLVMAPTRELAQQIQKVMSALGEYLNVNILPCIGGTSVRDDQRKLEAGIHVVVGTPGRVGDMINRNAL 167
Cdd:PTZ00110 196 pllrygDGPIV--LVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVT 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 168 DTSRIKMFVLDEADEMLSRGFKDQIYEVFRSMPQDVQVVLLSATMPSEVLDVTNRFMRN-PIRILVKKDELTL-EGIRQf 245
Cdd:PTZ00110 274 NLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDLTAcHNIKQ- 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 246 YINVQKDEWKFDCLCDLYNVVNV--TQAVIFCNTRRKVDTLTEKMTENQFTVSCLHGDMDQAERDTIMREFRSGSSRVLI 323
Cdd:PTZ00110 353 EVFVVEEHEKRGKLKMLLQRIMRdgDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMI 432
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 324 TTDILARGIDVQQVSLVINYDLPSNRENYIHRIGRSGRFGRKGVAINFVTENDARQLKEI 383
Cdd:PTZ00110 433 ATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDL 492
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
31-391 |
6.97e-70 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 226.01 E-value: 6.97e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 31 FDDMELKEELLRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVS----ILQRIDHEDPHV---QALVM 103
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTAtfhyLLSHPAPEDRKVnqpRALIM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 104 APTRELAQQIQKVMSALGEYLNVNILPCIGGTSVrDDQRK-LEAGIHVVVGTPGRVGDMINRNALDTSRIKMFVLDEADE 182
Cdd:PRK04837 90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGY-DKQLKvLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 183 MLSRGFKDQIYEVFRSMPQDVQ--VVLLSATMPSEVLDVTNRFMRNPIRILVKKDELTLEGIRQ--FYinvQKDEWKFDC 258
Cdd:PRK04837 169 MFDLGFIKDIRWLFRRMPPANQrlNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEelFY---PSNEEKMRL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 259 LCDLYNVVNVTQAVIFCNTRRKVDTLTEKMTENQFTVSCLHGDMDQAERDTIMREFRSGSSRVLITTDILARGIDVQQVS 338
Cdd:PRK04837 246 LQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVT 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 71987143 339 LVINYDLPSNRENYIHRIGRSGRFGRKGVAINFVTENDARQLKEIESYYTTQI 391
Cdd:PRK04837 326 HVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIGHSI 378
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
36-230 |
5.05e-68 |
|
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: 213.59 E-value: 5.05e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 36 LKEELLRGIYGFGFEKPSAIQKRAI------VPcttgKDVIAQAQSGTGKTATFSVSILQRIDHEDPHVQALVMAPTREL 109
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALplilsdPP----ENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTREL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 110 AQQIQKVMSALGEYLNVNILPCIGGTSVRDDqRKLEAgiHVVVGTPGRVGDMINRNALDTSRIKMFVLDEADEML-SRGF 188
Cdd:cd17963 77 ARQIGEVVEKMGKFTGVKVALAVPGNDVPRG-KKITA--QIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLdTQGH 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 71987143 189 KDQIYEVFRSMPQDVQVVLLSATMPSEVLDVTNRFMRNPIRI 230
Cdd:cd17963 154 GDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
30-383 |
2.58e-66 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 219.27 E-value: 2.58e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 30 SFDDMELKEELLRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQR---IDHEDPHVQ----ALV 102
Cdd:PLN00206 122 SFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRcctIRSGHPSEQrnplAMV 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 103 MAPTRELAQQIQKVMSALGEYLNVNILPCIGGTSVRDDQRKLEAGIHVVVGTPGRVGDMINRNALDTSRIKMFVLDEADE 182
Cdd:PLN00206 202 LTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDC 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 183 MLSRGFKDQIYEVFRSMPQDvQVVLLSATMPSEVLDVTNRFMRNPIRILVKKDELTLEGIRQFYINV---QKDEWKFDCL 259
Cdd:PLN00206 282 MLERGFRDQVMQIFQALSQP-QVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVetkQKKQKLFDIL 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 260 cdLYNVVNVTQAVIFCNTRRKVDTLTEKMTE-NQFTVSCLHGDMDQAERDTIMREFRSGSSRVLITTDILARGIDVQQVS 338
Cdd:PLN00206 361 --KSKQHFKPPAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVR 438
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 71987143 339 LVINYDLPSNRENYIHRIGRSGRFGRKGVAINFVTENDARQLKEI 383
Cdd:PLN00206 439 QVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPEL 483
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
30-232 |
6.79e-64 |
|
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: 203.73 E-value: 6.79e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 30 SFDDMELKEELLRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQRIDHEDPHVQALVMAPTREL 109
Cdd:cd17950 3 GFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTREL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 110 AQQIQKVMSALGEYL-NVNILPCIGGTSVRDDQRKLEAGI-HVVVGTPGRVGDMINRNALDTSRIKMFVLDEADEML-SR 186
Cdd:cd17950 83 AFQISNEYERFSKYMpNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLeQL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 71987143 187 GFKDQIYEVFRSMPQDVQVVLLSATMPSEVLDVTNRFMRNPIRILV 232
Cdd:cd17950 163 DMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
242-372 |
1.02e-61 |
|
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350174 [Multi-domain] Cd Length: 131 Bit Score: 195.03 E-value: 1.02e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 242 IRQFYINVQKDEWKFDCLCDLYNVVNVTQAVIFCNTRRKVDTLTEKMTENQFTVSCLHGDMDQAERDTIMREFRSGSSRV 321
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 71987143 322 LITTDILARGIDVQQVSLVINYDLPSNRENYIHRIGRSGRFGRKGVAINFV 372
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
53-219 |
2.88e-60 |
|
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: 192.46 E-value: 2.88e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 53 SAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQRIDHEDPHVQALVMAPTRELAQQIQKVMSALGEYLNVNILPCI 132
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 133 GGTSVRDDQRKLeAGIHVVVGTPGRVGDMINRNALdTSRIKMFVLDEADEMLSRGFKDQIYEVFRSMPQDVQVVLLSATM 212
Cdd:pfam00270 81 GGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATL 158
|
....*..
gi 71987143 213 PSEVLDV 219
Cdd:pfam00270 159 PRNLEDL 165
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
40-230 |
2.23e-59 |
|
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, Component Of Gems 3, Gemin-3, and SMN-Interacting Protein) interacts directly with SMN (survival of motor neurons), the spinal muscular atrophy gene product, and may play a catalytic role in the function of the SMN complex on ribonucleoproteins. Diseases associated with DDX20 include spinal muscular atrophy and muscular atrophy. DDX20 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350701 [Multi-domain] Cd Length: 192 Bit Score: 191.32 E-value: 2.23e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 40 LLRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQRIDHEDPHVQALVMAPTRELAQQIQKVMSA 119
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 120 LGEYLNVniLPC---IGGTSVRDDQRKLeAGIHVVVGTPGRVGDMINRNALDTSRIKMFVLDEADEMLSRGFKDQIYEVF 196
Cdd:cd17943 81 IGKKLEG--LKCevfIGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIF 157
|
170 180 190
....*....|....*....|....*....|....
gi 71987143 197 RSMPQDVQVVLLSATMPSEVLDVTNRFMRNPIRI 230
Cdd:cd17943 158 SSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLV 191
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
44-245 |
1.84e-54 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 178.84 E-value: 1.84e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 44 IYGFGFEKPSAIQKRAIVPCTTG-KDVIAQAQSGTGKTATFSVSILQRIdHEDPHVQALVMAPTRELAQQIQKVMSALGE 122
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAL-KRGKGGRVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 123 YLNVNILPCIGGTSVRDDQRKLEAG-IHVVVGTPGRVGDMINRNALDTSRIKMFVLDEADEMLSRGFKDQIYEVFRSMPQ 201
Cdd:smart00487 80 SLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 71987143 202 DVQVVLLSATMPSEVLDVTNRFMRNPIRILVKkdELTLEGIRQF 245
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFIDVG--FTPLEPIEQF 201
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
40-230 |
5.22e-53 |
|
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: 175.14 E-value: 5.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 40 LLRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQRIDHEDPHVQ---ALVMAPTRELAQQIQKV 116
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAatrVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 117 MSALGEYLNVNILPCIGGTSVRDDQRKLEAGIHVVVGTPGRVGDMI-NRNALDTSRIKMFVLDEADEMLSRGFKDQIYEV 195
Cdd:cd17947 81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLrNSPSFDLDSIEILVLDEADRMLEEGFADELKEI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 71987143 196 FRSMPQDVQVVLLSATMPSEVLDVTNRFMRNPIRI 230
Cdd:cd17947 161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
31-227 |
2.17e-51 |
|
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: 170.87 E-value: 2.17e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 31 FDDMELKEELLRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQRIDhEDPH-VQALVMAPTREL 109
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLS-EDPYgIFALVLTPTREL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 110 AQQIQKVMSALGEYLNVNILPCIGGTSVRDDQRKLEAGIHVVVGTPGRVGDMInRNALDT----SRIKMFVLDEADEMLS 185
Cdd:cd17955 80 AYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHL-RSSDDTtkvlSRVKFLVLDEADRLLT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 71987143 186 RGFKDQIYEVFRSMPQDVQVVLLSATMPSEVLDVTNRFMRNP 227
Cdd:cd17955 159 GSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
30-226 |
4.64e-50 |
|
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: 168.05 E-value: 4.64e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 30 SFDDMELKEELLRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQRIDHEDPHV----------Q 99
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSvgrgrrkaypS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 100 ALVMAPTRELAQQIQKVMSALGEYLNVNILPCIGGTSVRDDQRKLEAGIHVVVGTPGRVGDMINRNALDTSRIKMFVLDE 179
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 71987143 180 ADEMLSRGFKDQIYEVFR--SMPQ--DVQVVLLSATMPSEVLDVTNRFMRN 226
Cdd:cd17967 161 ADRMLDMGFEPQIRKIVEhpDMPPkgERQTLMFSATFPREIQRLAADFLKN 211
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
30-230 |
7.11e-49 |
|
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: 164.41 E-value: 7.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 30 SFDDMELKEELLRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQRIDHEDPHVQALVMAPTREL 109
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 110 AQQIQKVMSALGEYLNVNILPCIGGTSVRDDQRKLEAGIHVVVGTPGRVGDMI-NRNALDTSRIKMFVLDEADEMLSRGF 188
Cdd:cd17954 81 AQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLeNTKGFSLKSLKFLVMDEADRLLNMDF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 71987143 189 KDQIYEVFRSMPQDVQVVLLSATMPSEVLDVTNRFMRNPIRI 230
Cdd:cd17954 161 EPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
36-225 |
3.81e-47 |
|
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: 160.06 E-value: 3.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 36 LKEELLRGIYGFGFEKPSAIQKRAIVPC-TTGKDVIAQAQSGTGKTATFSVSILQRI-----DHEDPHVQALVMAPTREL 109
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPIlSTGDDVLARAKTGTGKTLAFLLPAIQSLlntkpAGRRSGVSALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 110 AQQIQKVMSALGEYL-NVNILPCIGGTSVRDDQRKLE-AGIHVVVGTPGRVGDMIN--RNALDTSRIKMFVLDEADEMLS 185
Cdd:cd17964 81 ALQIAAEAKKLLQGLrKLRVQSAVGGTSRRAELNRLRrGRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRLLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 71987143 186 RGFKDQIYEVFRSMPQ----DVQVVLLSATMPSEVLDVTNRFMR 225
Cdd:cd17964 161 MGFRPDLEQILRHLPEknadPRQTLLFSATVPDEVQQIARLTLK 204
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
36-228 |
1.35e-46 |
|
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: 158.52 E-value: 1.35e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 36 LKEELLRGIYGFGFEKPSAIQKRAIvPCT-TGKDVIAQAQSGTGKTATFSVSILQRI------DHEDPHVQALVMAPTRE 108
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAI-PLAlEGKDILARARTGSGKTAAYALPIIQKIlkakaeSGEEQGTRALILVPTRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 109 LAQQIQKVMSALGEYLNVNI-LPCIGGTSVRDDQRKLEAGI-HVVVGTPGRVGDMINRNAL-DTSRIKMFVLDEADEMLS 185
Cdd:cd17961 80 LAQQVSKVLEQLTAYCRKDVrVVNLSASSSDSVQRALLAEKpDIVVSTPARLLSHLESGSLlLLSTLKYLVIDEADLVLS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 71987143 186 RGFKDQIYEVFRSMPQDVQVVLLSATMPSEVLDVTNRFMRNPI 228
Cdd:cd17961 160 YGYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
28-238 |
8.78e-46 |
|
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: 157.49 E-value: 8.78e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 28 VESFDDMELKEELLRGIYGFGFEKPSAIQKRAIvPCTTG---KDVIAQAQSGTGKTATFSVSILQRIDHEDPHVQALVMA 104
Cdd:cd18048 17 VKSFEELHLKEELLRGIYAMGFNRPSKIQENAL-PMMLAdppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 105 PTRELAQQIQKVMSALGEYLN-VNILPCIGGTSVRDDQRkLEAgiHVVVGTPGRVGDMINRNAL-DTSRIKMFVLDEADE 182
Cdd:cd18048 96 PTFELALQTGKVVEEMGKFCVgIQVIYAIRGNRPGKGTD-IEA--QIVIGTPGTVLDWCFKLRLiDVTNISVFVLDEADV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 71987143 183 MLS-RGFKDQIYEVFRSMPQDVQVVLLSATMPSEVLDVTNRFMRNPIRILVKKDELT 238
Cdd:cd18048 173 MINvQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
31-227 |
1.16e-45 |
|
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: 156.33 E-value: 1.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 31 FDDMELKEELLRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQRidhedphVQALVMAPTRELA 110
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQI-------VVALILEPSRELA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 111 QQIQKVMSALGEYLN---VNILPCIGGTSVRDDQRKLEAGIHVVVGTPGRVGDMINRNALDTSRIKMFVLDEADEMLSRG 187
Cdd:cd17938 74 EQTYNCIENFKKYLDnpkLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 71987143 188 FKDQIYEVFRSMPQ------DVQVVLLSATMPS-EVLDVTNRFMRNP 227
Cdd:cd17938 154 NLETINRIYNRIPKitsdgkRLQVIVCSATLHSfEVKKLADKIMHFP 200
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
40-230 |
1.05e-44 |
|
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: 154.01 E-value: 1.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 40 LLRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQRIDHEdPHV---------QALVMAPTRELA 110
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRL-PPLdeetkddgpYALILAPTRELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 111 QQIQKVMSALGEYLNVNILPCIGGTSVRDDQRKLEAGIHVVVGTPGRVGDMINRNALDTSRIKMFVLDEADEMLSRGFKD 190
Cdd:cd17945 80 QQIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 191 QIYEVFRSMPQDV--------------------QVVLLSATMPSEVLDVTNRFMRNPIRI 230
Cdd:cd17945 160 QVTKILDAMPVSNkkpdteeaeklaasgkhryrQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
30-230 |
1.53e-44 |
|
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: 153.23 E-value: 1.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 30 SFDDMELKEELLRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQRIDHEDPHV--QALVMAPTR 107
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVgaRALILSPTR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 108 ELAQQIQKVMSALGEYLNVNILPCIGGTSVRDDQRKLEAGIHVVVGTPGRVGDMINRNALDTSRIKMFVLDEADEMLSRG 187
Cdd:cd17959 82 ELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 71987143 188 FKDQIYEVFRSMPQDVQVVLLSATMPSEVLDVTNRFMRNPIRI 230
Cdd:cd17959 162 FAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
40-230 |
2.48e-44 |
|
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: 152.32 E-value: 2.48e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 40 LLRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQRIDHEDPHVQALVMAPTRELAQQIQKVMSA 119
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 120 LGE-YLNVNILPCIGGTSVRDDQRKLEAGIHVVVGTPGRVGDMINRNALDTSRIKMFVLDEADEMLSRGFKDQIYEVFRS 198
Cdd:cd17962 81 LMKgLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILEN 160
|
170 180 190
....*....|....*....|....*....|..
gi 71987143 199 MPQDVQVVLLSATMPSEVLDVTNRFMRNPIRI 230
Cdd:cd17962 161 ISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
40-230 |
2.75e-44 |
|
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350718 [Multi-domain] Cd Length: 202 Bit Score: 152.34 E-value: 2.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 40 LLRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQRI-----DHEDPHVQALVMAPTRELAQQIQ 114
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrkaNLKKGQVGALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 115 KVMSALGEY--LNVNILPCIGGTSV-RDDQRKLEAGIHVVVGTPGRVGDMINRNA--LDTSRIKMFVLDEADEMLSRGFK 189
Cdd:cd17960 81 EVLQSFLEHhlPKLKCQLLIGGTNVeEDVKKFKRNGPNILVGTPGRLEELLSRKAdkVKVKSLEVLVLDEADRLLDLGFE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 71987143 190 DQIYEVFRSMPQDVQVVLLSATMPSEVLDVTNRFMRNPIRI 230
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
36-230 |
3.42e-44 |
|
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: 152.92 E-value: 3.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 36 LKEELLRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQRIDHEDPHVQ-----ALVMAPTRELA 110
Cdd:cd17953 19 LSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVKPgegpiGLIMAPTRELA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 111 QQIQKVMSALGEYLNVNILPCIGGTSVRDDQRKLEAGIHVVVGTPGRVGDMINRNA---LDTSRIKMFVLDEADEMLSRG 187
Cdd:cd17953 99 LQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNgrvTNLRRVTYVVLDEADRMFDMG 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 71987143 188 FKDQIYEVFRSMPQDVQVVLLSATMPSEVLDVTNRFMRNPIRI 230
Cdd:cd17953 179 FEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
40-232 |
8.81e-44 |
|
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: 151.20 E-value: 8.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 40 LLRGIYGFGFEKPSAIQKRAIvPCTT-GKDVIAQAQSGTGKTATFSVSILQRI--DHEDPHVQALVMAPTRELAQQIQKV 116
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAI-PILLhGRDLLACAPTGSGKTLAFLIPILQKLgkPRKKKGLRALILAPTRELASQIYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 117 MSALGEYLNVNIlpCI---GGTSVRDDQRKLEAGIHVVVGTPGRVGDMINRNALDTSRIKMFVLDEADEMLSRGFKDQIY 193
Cdd:cd17957 80 LLKLSKGTGLRI--VLlskSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 71987143 194 EVFRSMPQ-DVQVVLLSATMPSEVLDVTNRFMRNPIRILV 232
Cdd:cd17957 158 EILAACTNpNLQRSLFSATIPSEVEELARSVMKDPIRIIV 197
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
28-225 |
2.32e-41 |
|
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: 146.65 E-value: 2.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 28 VESFDDMELKEELLRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQRIDHED---------PHV 98
Cdd:cd18052 42 ILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEGltassfsevQEP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 99 QALVMAPTRELAQQIQKvmSALGEYLNVNILPCI--GGTSVRDDQRKLEAGIHVVVGTPGRVGDMINRNALDTSRIKMFV 176
Cdd:cd18052 122 QALIVAPTRELANQIFL--EARKFSYGTCIRPVVvyGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLI 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 71987143 177 LDEADEMLSRGFKDQIYEV--FRSMP--QDVQVVLLSATMPSEVLDVTNRFMR 225
Cdd:cd18052 200 LDEADRMLDMGFGPEIRKLvsEPGMPskEDRQTLMFSATFPEEIQRLAAEFLK 252
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
40-236 |
7.69e-41 |
|
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: 144.69 E-value: 7.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 40 LLRGIYGFGFEKPSAIQKRAI-VPCTTGKDVIAQAQSGTGKTATFSVSILQRI---------DHEDPHVQALVMAPTREL 109
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALpAAIRDGKDVIGAAETGSGKTLAFGIPILERLlsqkssngvGGKQKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 110 AQQIQKVMSALGEYLNVNILPCIGGTSVRDDQRKLEAGIHVVVGTPGRVGDMI-NRNALDTS--RIKMFVLDEADEMLSR 186
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIqEGNEHLANlkSLRFLVLDEADRMLEK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 71987143 187 G-FKD--QIYEVFRSMPQDV----QVVLLSATMpSEVLDVTNRFMRNPIRILVKKDE 236
Cdd:cd17946 161 GhFAEleKILELLNKDRAGKkrkrQTFVFSATL-TLDHQLPLKLNSKKKKKKKEKKQ 216
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
40-230 |
1.19e-39 |
|
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: 140.20 E-value: 1.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 40 LLRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQRIDHEdPHVQ------ALVMAPTRELAQQI 113
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQ-PPLErgdgpiVLVLAPTRELAQQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 114 QKVMSALGEYLNVNILPCIGGTSVRDDQRKLEAGIHVVVGTPGRVGDMINRNALDTSRIKMFVLDEADEMLSRGFKDQIY 193
Cdd:cd17966 80 QQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 71987143 194 EVFRSMPQDVQVVLLSATMPSEVLDVTNRFMRNPIRI 230
Cdd:cd17966 160 KIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
40-230 |
1.77e-39 |
|
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor 3B-Associated 125 kDa Protein, RHELP, or RNAHP) is an NTPase with a preference for ATP, the hydrolysis of which is enhanced by various RNA substrates. It acts as a non-processive RNA helicase with protein displacement and RNA annealing activities. DDX42 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350710 [Multi-domain] Cd Length: 197 Bit Score: 139.86 E-value: 1.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 40 LLRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQRIdHEDPHVQ------ALVMAPTRELAQQI 113
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHI-MDQRELEkgegpiAVIVAPTRELAQQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 114 QKVMSALGEYLNVNILPCIGGTSVRDDQRKLEAGIHVVVGTPGRVGDMINRNALDTSRIKMFVLDEADEMLSRGFKDQIY 193
Cdd:cd17952 80 YLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 71987143 194 EVFRSMPQDVQVVLLSATMPSEVLDVTNRFMRNPIRI 230
Cdd:cd17952 160 SIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
28-228 |
2.33e-39 |
|
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: 140.95 E-value: 2.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 28 VESFDDMELKEELLRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQRIDHEDP----------- 96
Cdd:cd18051 20 IETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQGPgeslpsesgyy 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 97 -----HVQALVMAPTRELAQQIQKvmSALGEYLNVNILPCI--GGTSVRDDQRKLEAGIHVVVGTPGRVGDMINRNALDT 169
Cdd:cd18051 100 grrkqYPLALVLAPTRELASQIYD--EARKFAYRSRVRPCVvyGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71987143 170 SRIKMFVLDEADEMLSRGFKDQIYEVFR--SMPQ--DVQVVLLSATMPSEVLDVTNRFMRNPI 228
Cdd:cd18051 178 DYCKYLVLDEADRMLDMGFEPQIRRIVEqdTMPPtgERQTLMFSATFPKEIQMLARDFLDNYI 240
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
47-230 |
3.50e-39 |
|
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: 139.64 E-value: 3.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 47 FGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQRIDHEDPHVQ------ALVMAPTRELAQQIQKVMSAL 120
Cdd:cd17949 9 MGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDrsdgtlALVLVPTRELALQIYEVLEKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 121 GEYLnVNILPC--IGGTSVRDDQRKLEAGIHVVVGTPGRVGDMI-NRNALDTSRIKMFVLDEADEMLSRGFKDQIYEVFR 197
Cdd:cd17949 89 LKPF-HWIVPGylIGGEKRKSEKARLRKGVNILIATPGRLLDHLkNTQSFDVSNLRWLVLDEADRLLDMGFEKDITKILE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 71987143 198 -------------SMPQDVQVVLLSATMPSEVLDVTNRFMRNPIRI 230
Cdd:cd17949 168 llddkrskaggekSKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
41-232 |
9.02e-39 |
|
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin gene, NUP98, by inversion 11 (p15q22) chromosome translocation is found in the patients with de novo or therapy-related myeloid malignancies. Diseases associated with DDX10 (also known as DDX10-NUP98 Fusion Protein Type 2) include myelodysplastic syndrome and leukemia, acute myeloid. DDX10 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350699 [Multi-domain] Cd Length: 198 Bit Score: 137.81 E-value: 9.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 41 LRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQRIDHE----DPHVQALVMAPTRELAQQIQKV 116
Cdd:cd17941 2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRErwtpEDGLGALIISPTRELAMQIFEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 117 MSALGEYLNVNILPCIGGTSVRDDQRKLeAGIHVVVGTPGRVGDMINRNA-LDTSRIKMFVLDEADEMLSRGFKDQIYEV 195
Cdd:cd17941 82 LRKVGKYHSFSAGLIIGGKDVKEEKERI-NRMNILVCTPGRLLQHMDETPgFDTSNLQMLVLDEADRILDMGFKETLDAI 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 71987143 196 FRSMPQDVQVVLLSATMPSEVLDVTNRFMRNPIRILV 232
Cdd:cd17941 161 VENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
254-363 |
4.02e-38 |
|
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: 133.10 E-value: 4.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 254 WKFDCLCDLYNVVNVTQAVIFCNTRRKVDTltEKMTE-NQFTVSCLHGDMDQAERDTIMREFRSGSSRVLITTDILARGI 332
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLEA--ELLLEkEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
|
90 100 110
....*....|....*....|....*....|.
gi 71987143 333 DVQQVSLVINYDLPSNRENYIHRIGRSGRFG 363
Cdd:pfam00271 79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
55-225 |
2.27e-36 |
|
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: 131.89 E-value: 2.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 55 IQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQRIDHEDPHV------QALVMAPTRELAQQIQKVMSALGEYLNVNI 128
Cdd:cd17944 16 IQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRkrgrapKVLVLAPTRELANQVTKDFKDITRKLSVAC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 129 LpcIGGTSVRDDQRKLEAGIHVVVGTPGRVGDMINRNALDTSRIKMFVLDEADEMLSRGFKDQIYEV----FRSMPQD-V 203
Cdd:cd17944 96 F--YGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEIlsvsYKKDSEDnP 173
|
170 180
....*....|....*....|..
gi 71987143 204 QVVLLSATMPSEVLDVTNRFMR 225
Cdd:cd17944 174 QTLLFSATCPDWVYNVAKKYMK 195
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
40-230 |
3.37e-36 |
|
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: 131.05 E-value: 3.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 40 LLRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSIL--------QRIDHEDPHVqaLVMAPTRELAQ 111
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFihldlqpiPREQRNGPGV--LVLTPTRELAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 112 QIQKVMSalgEYLNVNILP-CIGGTSVRDDQ-RKLEAGIHVVVGTPGRVGDMINRNALDTSRIKMFVLDEADEMLSRGFK 189
Cdd:cd17958 79 QIEAECS---KYSYKGLKSvCVYGGGNRNEQiEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 71987143 190 DQIYEVFRSMPQDVQVVLLSATMPSEVLDVTNRFMRNPIRI 230
Cdd:cd17958 156 PQIRKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
29-227 |
2.19e-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: 129.07 E-value: 2.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 29 ESFDDMELKEELLRGIYGFGFEKPSAIQKRAI--VPCTTGKDVIAQAQSGTGKTATFSVSILQRIDHEDPHVQALVMAPT 106
Cdd:cd18047 1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALplMLAEPPQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 107 RELAQQIQKVMSALGE-YLNVNILPCIGGTSVrddQRKLEAGIHVVVGTPGRVGD-MINRNALDTSRIKMFVLDEADEML 184
Cdd:cd18047 81 YELALQTGKVIEQMGKfYPELKLAYAVRGNKL---ERGQKISEQIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADVMI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 71987143 185 -SRGFKDQIYEVFRSMPQDVQVVLLSATMPSEVLDVTNRFMRNP 227
Cdd:cd18047 158 aTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
40-230 |
1.14e-33 |
|
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts with several spliceosomal proteins and may recognize the bacterial second messengers cyclic di-GMP and cyclic di-AMP, resulting in the induction of genes involved in the innate immune response. Diseases associated with DDX41 include "myeloproliferative/lymphoproliferative neoplasms, familial" and "Ddx41-related susceptibility to familial myeloproliferative/lymphoproliferative neoplasms". DDX41 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350709 [Multi-domain] Cd Length: 206 Bit Score: 124.76 E-value: 1.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 40 LLRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVS-ILQRIDHED--PHVQ-----ALVMAPTRELAQ 111
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPlIMFALEQEKklPFIKgegpyGLIVCPSRELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 112 QIQKVMSALGEYLNVNILP------CIGGTSVRDDQRKLEAGIHVVVGTPGRVGDMINRNALDTSRIKMFVLDEADEMLS 185
Cdd:cd17951 81 QTHEVIEYYCKALQEGGYPqlrcllCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 71987143 186 RGFKDQIYEVFRSMPQDVQVVLLSATMPSEVLDVTNRFMRNPIRI 230
Cdd:cd17951 161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
41-218 |
2.18e-33 |
|
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: 123.62 E-value: 2.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 41 LRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATF---SVSILQRIDHEDPH-VQALVMAPTRELAQQIQKV 116
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFlipAIELLYKLKFKPRNgTGVIIISPTRELALQIYGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 117 MSALGEYLNVNILPCIGGTSVRDDQRKLEAGIHVVVGTPGRVGD-MINRNALDTSRIKMFVLDEADEMLSRGFKDQIYEV 195
Cdd:cd17942 82 AKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDhLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQI 161
|
170 180
....*....|....*....|...
gi 71987143 196 FRSMPQDVQVVLLSATMPSEVLD 218
Cdd:cd17942 162 IKLLPKRRQTMLFSATQTRKVED 184
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
49-230 |
5.74e-33 |
|
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: 123.58 E-value: 5.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 49 FEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQRIDHEdPHVQ------ALVMAPTRELAQQIQKVMSALGE 122
Cdd:cd18049 44 FTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQ-PFLErgdgpiCLVLAPTRELAQQVQQVAAEYGR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 123 YLNVNIlPCIGGTSVRDDQ-RKLEAGIHVVVGTPGRVGDMINRNALDTSRIKMFVLDEADEMLSRGFKDQIYEVFRSMPQ 201
Cdd:cd18049 123 ACRLKS-TCIYGGAPKGPQiRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRP 201
|
170 180
....*....|....*....|....*....
gi 71987143 202 DVQVVLLSATMPSEVLDVTNRFMRNPIRI 230
Cdd:cd18049 202 DRQTLMWSATWPKEVRQLAEDFLKDYIHI 230
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
49-230 |
4.77e-32 |
|
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: 122.04 E-value: 4.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 49 FEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQRIDHEdPHVQ------ALVMAPTRELAQQIQKVMSALGE 122
Cdd:cd18050 82 FKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQ-PYLErgdgpiCLVLAPTRELAQQVQQVADDYGK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 123 YLNVNILPCIGGTSVRDDQRKLEAGIHVVVGTPGRVGDMINRNALDTSRIKMFVLDEADEMLSRGFKDQIYEVFRSMPQD 202
Cdd:cd18050 161 SSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPD 240
|
170 180
....*....|....*....|....*...
gi 71987143 203 VQVVLLSATMPSEVLDVTNRFMRNPIRI 230
Cdd:cd18050 241 RQTLMWSATWPKEVRQLAEDFLRDYVQI 268
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
282-363 |
1.46e-30 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 112.31 E-value: 1.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 282 DTLTEKMTENQFTVSCLHGDMDQAERDTIMREFRSGSSRVLITTDILARGIDVQQVSLVINYDLPSNRENYIHRIGRSGR 361
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 71987143 362 FG 363
Cdd:smart00490 81 AG 82
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
40-222 |
1.81e-25 |
|
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: 103.22 E-value: 1.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 40 LLRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQRIdHEDPHV--------QALVMAPTRELAQ 111
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRL-LRYKLLaegpfnapRGLVITPSRELAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 112 QIQKVMSALGEYLNVNILPCIGGTSVRDDQRKLEAGIHVVVGTPGRVGDMINRNALDTSRIKMFVLDEADEMLSRGFKDQ 191
Cdd:cd17948 80 QIGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 71987143 192 IYEVFRSMP-------------QDVQVVLLSATMPSEVLDVTNR 222
Cdd:cd17948 160 LSHFLRRFPlasrrsentdgldPGTQLVLVSATMPSGVGEVLSK 203
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
66-211 |
1.55e-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: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 66 GKDVIAQAQSGTGKTATFSVSILQRIDheDPHVQALVMAPTRELAQQIQKVMSALGEyLNVNILPCIGGTSVRDDQRKLE 145
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLL--KKGKKVLVLVPTKALALQTAERLRELFG-PGIRVAVLVGGSSAEEREKNKL 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71987143 146 AGIHVVVGTPGRVGDMINRNA-LDTSRIKMFVLDEADEMLSRGFKDQIYE--VFRSMPQDVQVVLLSAT 211
Cdd:cd00046 78 GDADIIIATPDMLLNLLLREDrLFLKDLKLIIVDEAHALLIDSRGALILDlaVRKAGLKNAQVILLSAT 146
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
47-212 |
1.01e-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: 87.30 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 47 FGFEKPSAIQKrAIVP-------CTTG---KDVIAQAQSGTGKTATFSVSILQRI-DHEDPHVQALVMAPTRELAQQIQK 115
Cdd:cd17956 8 NGITSAFPVQA-AVIPwllpsskSTPPyrpGDLCVSAPTGSGKTLAYVLPIVQALsKRVVPRLRALIVVPTKELVQQVYK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 116 VMSALGEYLNVNILPCIGGTSVRDDQRKLEAGIH--------VVVGTPGRVGDMINRNA-LDTSRIKMFVLDEADEMLSR 186
Cdd:cd17956 87 VFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTSgrylsrvdILVATPGRLVDHLNSTPgFTLKHLRFLVIDEADRLLNQ 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 71987143 187 GFKD----QIYEVFRSMPQD----------------VQVVLLSATM 212
Cdd:cd17956 167 SFQDwletVMKALGRPTAPDlgsfgdanllersvrpLQKLLFSATL 212
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
27-387 |
3.80e-19 |
|
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: 89.51 E-value: 3.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 27 VVESFDDmELKEELLRGIYGFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQRIdHEDPHVQALVMAPT 106
Cdd:COG1205 33 RYAPWPD-WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEAL-LEDPGATALYLYPT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 107 RELAQ-QIQKvMSALGEYLNVNILPCI--GGTSvRDDQRKLEAGIHVVVGTPgrvgDMINRNALDT--------SRIKMF 175
Cdd:COG1205 111 KALARdQLRR-LRELAEALGLGVRVATydGDTP-PEERRWIREHPDIVLTNP----DMLHYGLLPHhtrwarffRNLRYV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 176 VLDEADEMlsRG-FKDQIYEVFR----------SMPqdvQVVLLSATM--PSEV------LDVTnrfmrnpiriLVKKD- 235
Cdd:COG1205 185 VIDEAHTY--RGvFGSHVANVLRrlrricrhygSDP---QFILASATIgnPAEHaerltgRPVT----------VVDEDg 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 236 -------------ELTLEGIRQFYINvqkdEWKfDCLCDLynVVNVTQAVIFCNTRRKVDTLTeKMTENQFTVSCL---- 298
Cdd:COG1205 250 sprgertfvlwnpPLVDDGIRRSALA----EAA-RLLADL--VREGLRTLVFTRSRRGAELLA-RYARRALREPDLadrv 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 299 ---HGDMDQAERDTIMREFRSGSSRVLITTDILARGIDVQQVSLVINYDLPSNRENYIHRIGRSGRFGRKGVAInFVTEN 375
Cdd:COG1205 322 aayRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV-LVAGD 400
|
410
....*....|..
gi 71987143 376 DArqlkeIESYY 387
Cdd:COG1205 401 DP-----LDQYY 407
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
31-230 |
3.92e-18 |
|
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 (MRH4) plays an essential role during the late stages of mitochondrial ribosome or mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions. MRH4 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350723 [Multi-domain] Cd Length: 251 Bit Score: 83.19 E-value: 3.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 31 FDDMEL--------KEELLRGIYGFGFE-KPSAIQKRAI----------VPCTTGKD-------VIAqAQSGTGKTATF- 83
Cdd:cd17965 1 FDQLKLlpsvreaiIKEILKGSNKTDEEiKPSPIQTLAIkkllktlmrkVTKQTSNEepklevfLLA-AETGSGKTLAYl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 84 --SVSILQRIDHEDPH--------------VQALVMAPTRELAQQIQKVMSALGEY--LNVNILPCIGGTSVRDDQRKLE 145
Cdd:cd17965 80 apLLDYLKRQEQEPFEeaeeeyesakdtgrPRSVILVPTHELVEQVYSVLKKLSHTvkLGIKTFSSGFGPSYQRLQLAFK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 146 AGIHVVVGTPGRVGDMINRNALDTSRIKMFVLDEADEMLSRGFKDQIYEVFRSMPQDVQVVLLSATMPSEVLDVTNRFMR 225
Cdd:cd17965 160 GRIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLRKLFP 239
|
....*
gi 71987143 226 NPIRI 230
Cdd:cd17965 240 DVVRI 244
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
76-383 |
1.39e-15 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 78.53 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 76 GTGKTaTFSVSILQRIDHEDPhvqALVMAPTRELAQQIQKvmsalgEYLNVNILPCIGGtsvrddqRKLEAGIHVVVGTP 155
Cdd:COG1061 110 GTGKT-VLALALAAELLRGKR---VLVLVPRRELLEQWAE------ELRRFLGDPLAGG-------GKKDSDAPITVATY 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 156 GRVGDMINRNALDtSRIKMFVLDEADEMLSRGFKdqiyEVFRSMPqDVQVVLLSATmPsEVLDVTNRFMRN--------- 226
Cdd:COG1061 173 QSLARRAHLDELG-DRFGLVIIDEAHHAGAPSYR----RILEAFP-AAYRLGLTAT-P-FRSDGREILLFLfdgivyeys 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 227 -----------PIRILVKKDELTLEGIRQFYIN-------VQKDEWKFDCLCDLYN-VVNVTQAVIFCNTRRKVDTLTEK 287
Cdd:COG1061 245 lkeaiedgylaPPEYYGIRVDLTDERAEYDALSerlrealAADAERKDKILRELLReHPDDRKTLVFCSSVDHAEALAEL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 288 MTENQFTVSCLHGDMDQAERDTIMREFRSGSSRVLITTDILARGIDVQQVSLVINYDLPSNRENYIHRIGR---SGRFGR 364
Cdd:COG1061 325 LNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRglrPAPGKE 404
|
330
....*....|....*....
gi 71987143 365 KGVAINFVTeNDARQLKEI 383
Cdd:COG1061 405 DALVYDFVG-NDVPVLEEL 422
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
164-381 |
4.58e-15 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 76.72 E-value: 4.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 164 RNALDTSRIKMFVLDEA--------D---EMLsrgfkdQIYEVFRSMPqDVQVVLLSATMPSEV-LDVTNRF-MRNP--- 227
Cdd:COG0514 124 LELLRRLKISLFAIDEAhcisqwghDfrpDYR------RLGELRERLP-NVPVLALTATATPRVrADIAEQLgLEDPrvf 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 228 ----------IRILVKKDELTLEGIRQFyINVQKDEwkfdclcdlynvvnvtQAVIFCNTRRKVDTLTEKMTENQFTVSC 297
Cdd:COG0514 197 vgsfdrpnlrLEVVPKPPDDKLAQLLDF-LKEHPGG----------------SGIVYCLSRKKVEELAEWLREAGIRAAA 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 298 LHGDMDQAERDTIMREFRSGSSRVLITTDILARGIDVQQVSLVINYDLPSNRENYIHRIGRSGRFGRKGVAINFVTENDA 377
Cdd:COG0514 260 YHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDV 339
|
....
gi 71987143 378 RQLK 381
Cdd:COG0514 340 AIQR 343
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
271-357 |
3.09e-13 |
|
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: 66.35 E-value: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 271 AVIFCNTRRKVDTLTEKMTENQFTVSCLHGDMDQAERDTIMREFRSGSS--RVLITTDILARGIDVQQVSLVINYDLPSN 348
Cdd:cd18793 30 VLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDirVFLLSTKAGGVGLNLTAANRVILYDPWWN 109
|
90
....*....|....*
gi 71987143 349 ------RENYIHRIG 357
Cdd:cd18793 110 paveeqAIDRAHRIG 124
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
271-375 |
4.05e-13 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 71.02 E-value: 4.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 271 AVIFCNTRRKVDTLTEKMTENQFTVSCLHGDMDQAERDTIMREFRSGSS--RVLITTDILARGIDVQQVSLVINYDLPSN 348
Cdd:COG0553 552 VLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEapVFLISLKAGGEGLNLTAADHVIHYDLWWN 631
|
90 100 110
....*....|....*....|....*....|.
gi 71987143 349 --RENyiHRIGRSGRFG-RKGV-AINFVTEN 375
Cdd:COG0553 632 paVEE--QAIDRAHRIGqTRDVqVYKLVAEG 660
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
255-358 |
4.20e-13 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350189 [Multi-domain] Cd Length: 142 Bit Score: 66.08 E-value: 4.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 255 KFDCLCDL----YNVVNVTQAVIFCNTRRKVDTLTEKMTENQ-----FTVSCLHG----------DMDQAERDTIMREFR 315
Cdd:cd18802 8 KLQKLIEIlreyFPKTPDFRGIIFVERRATAVVLSRLLKEHPstlafIRCGFLIGrgnssqrkrsLMTQRKQKETLDKFR 87
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 71987143 316 SGSSRVLITTDILARGIDVQQVSLVINYDLPSNRENYIHRIGR 358
Cdd:cd18802 88 DGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR 130
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
28-398 |
1.73e-12 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 68.77 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 28 VESFDDMELKEELLRgiygFGFEK--PSaiQKRAIVPC-TTGKDVIAQAQSGTGKTATFSVSILQRIDHedpHVQALVMA 104
Cdd:COG1204 3 VAELPLEKVIEFLKE----RGIEElyPP--QAEALEAGlLEGKNLVVSAPTASGKTLIAELAILKALLN---GGKALYIV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 105 PTRELAQQI-QKVMSALGEY-LNVNILpciggTSVRDDQRKLEAGIHVVVGTPGRVGDMINRNALDTSRIKMFVLDEA-- 180
Cdd:COG1204 74 PLRALASEKyREFKRDFEELgIKVGVS-----TGDYDSDDEWLGRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAhl 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 181 --DEmlSRGFkdqIYEV----FRSMPQDVQVVLLSATMP-----SEVLD---VTNRFMRNPIRILVKKDeltleGIRQFy 246
Cdd:COG1204 149 idDE--SRGP---TLEVllarLRRLNPEAQIVALSATIGnaeeiAEWLDaelVKSDWRPVPLNEGVLYD-----GVLRF- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 247 invqKDEwKFDCLCDLYNVVNVT-----QAVIFCNTRRKVDTLTEKM-----------------------------TENQ 292
Cdd:COG1204 218 ----DDG-SRRSKDPTLALALDLleeggQVLVFVSSRRDAESLAKKLadelkrrltpeereeleelaeellevseeTHTN 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 293 FT-VSCL-------HGDMDQAERDTIMREFRSGSSRVLITTDILARGidvqqvslvINydLPSNR---ENYiHRIGR--- 358
Cdd:COG1204 293 EKlADCLekgvafhHAGLPSELRRLVEDAFREGLIKVLVATPTLAAG---------VN--LPARRviiRDT-KRGGMvpi 360
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 71987143 359 --------SGRFGR-----KGVAInfVTENDARQLKEIESYYttqIEEMPESI 398
Cdd:COG1204 361 pvlefkqmAGRAGRpgydpYGEAI--LVAKSSDEADELFERY---ILGEPEPI 408
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
272-386 |
3.46e-12 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 67.82 E-value: 3.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 272 VIFCNTRRKVDTLTEKMTENQFTVSCLHGDMDQAERDTIMREFRSGSSRVLITTDILARGIDVQQVSLVINYDLPSNREN 351
Cdd:PRK11057 240 IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIES 319
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 71987143 352 YIHRIGRSGRFGRKGVAINF------------VTENDARQLKEIESY 386
Cdd:PRK11057 320 YYQETGRAGRDGLPAEAMLFydpadmawlrrcLEEKPAGQQQDIERH 366
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
271-371 |
1.25e-11 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350181 [Multi-domain] Cd Length: 134 Bit Score: 61.84 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 271 AVIFCNTRRKVDTLTEKMTENQFTVSCLHGDMDQAERDTIMREFRSGSSRVLITTDILARGIDVQQVSLVINYDLPSNRE 350
Cdd:cd18794 33 GIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSME 112
|
90 100
....*....|....*....|.
gi 71987143 351 NYIHRIGRSGRFGRKGVAINF 371
Cdd:cd18794 113 SYYQESGRAGRDGLPSECILF 133
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
270-375 |
4.75e-10 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 61.28 E-value: 4.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 270 QAVIFCNTRRKVDTLTEKMTENQFTV------SCLHGD--MDQAERDTIMREFRSGSSRVLITTDILARGIDVQQVSLVI 341
Cdd:COG1111 355 RIIVFTQYRDTAEMIVEFLSEPGIKAgrfvgqASKEGDkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVI 434
|
90 100 110
....*....|....*....|....*....|....*.
gi 71987143 342 NYDL-PSN-RenYIHRIGRSGRFGRKGVAInFVTEN 375
Cdd:COG1111 435 FYEPvPSEiR--SIQRKGRTGRKREGRVVV-LIAKG 467
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
268-372 |
8.04e-10 |
|
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: 55.02 E-value: 8.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 268 VTQAVIFCNTRRKVDTLTEKMTenqftvsclhgdmdqaerdtimrefrsgssrVLITTDILARGIDVQQVSLVINYDLPS 347
Cdd:cd18785 3 VVKIIVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDPPS 51
|
90 100
....*....|....*....|....*.
gi 71987143 348 NRENYIHRIGRSGRFG-RKGVAINFV 372
Cdd:cd18785 52 SAASYIQRVGRAGRGGkDEGEVILFV 77
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
273-361 |
8.36e-10 |
|
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: 56.89 E-value: 8.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 273 IFCNTRRKVDTLT--------EKMTENQFTVSclHGDMDQAERDTIMREFRSGSSRVLITTDILARGIDVQQVSLVINYD 344
Cdd:cd18796 43 VFTNTRSQAERLAqrlrelcpDRVPPDFIALH--HGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIG 120
|
90
....*....|....*..
gi 71987143 345 LPSNRENYIHRIGRSGR 361
Cdd:cd18796 121 SPKSVARLLQRLGRSGH 137
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
56-212 |
8.33e-09 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 54.90 E-value: 8.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 56 QKRAIVPCTTGKDVIAQAQSGTGKTATFSVSILQRIdHEDPHVQALVMAPTRELAQQIQKVMSALGEYL--NVNILPCIG 133
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEAL-LRDPGSRALYLYPTKALAQDQLRSLRELLEQLglGIRVATYDG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 134 GTSVRDDQRKLEAGIHVVVGTPgrvgDMIN----RNALDTSRI----KMFVLDEAD----------EMLSRGFKDqiyeV 195
Cdd:cd17923 84 DTPREERRAIIRNPPRILLTNP----DMLHyallPHHDRWARFlrnlRYVVLDEAHtyrgvfgshvALLLRRLRR----L 155
|
170
....*....|....*..
gi 71987143 196 FRSMPQDVQVVLLSATM 212
Cdd:cd17923 156 CRRYGADPQFILTSATI 172
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
166-365 |
3.10e-08 |
|
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: 55.13 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 166 ALDTSRIkmfVLDEADEMLS--RGFKDQIYEVFRSMpqDVQVVLLSATMPsEVLDVTNRFMRNPIrilvKKDELTLEGIR 243
Cdd:cd09639 121 SIANSLL---IFDEVHFYDEytLALILAVLEVLKDN--DVPILLMSATLP-KFLKEYAEKIGYVE----ENEPLDLKPNE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 244 QFYINVQKDEWKFD-----CLCDLYNvvNVTQAVIFCNTRRKVDTLTEKMTE--NQFTVSCLHG---DMDQAERDT-IMR 312
Cdd:cd09639 191 RAPFIKIESDKVGEissleRLLEFIK--KGGSVAIIVNTVDRAQEFYQQLKEkgPEEEIMLIHSrftEKDRAKKEAeLLL 268
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 71987143 313 EFRSGSSRVLITTDILARGIDVqQVSLVINYDLPSNRenYIHRIGRSGRFGRK 365
Cdd:cd09639 269 EFKKSEKFVIVATQVIEASLDI-SVDVMITELAPIDS--LIQRLGRLHRYGEK 318
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
65-213 |
6.16e-08 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 52.26 E-value: 6.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 65 TGKDVIAQAQSGTGKTATFSVSILQRIDHEDPhvQALVMAPTRELAQQIQKVMSALGEYLNVNILPCIGGTSVRDDQrkl 144
Cdd:cd17921 16 SGDSVLVSAPTSSGKTLIAELAILRALATSGG--KAVYIAPTRALVNQKEADLRERFGPLGKNVGLLTGDPSVNKLL--- 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71987143 145 EAGIHVVVGTPGRVGDMINRNA-LDTSRIKMFVLDEA----DEmlSRGfkdQIYEV----FRSMPQDVQVVLLSATMP 213
Cdd:cd17921 91 LAEADILVATPEKLDLLLRNGGeRLIQDVRLVVVDEAhligDG--ERG---VVLELllsrLLRINKNARFVGLSATLP 163
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
277-392 |
2.04e-07 |
|
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: 50.32 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 277 TRRKVDTLTEKMTENQFTVSCLHGDMDQAERDTIMREFRSGSSRVLITTDILARGIDVQQVSLVINYD-----LPSNREN 351
Cdd:cd18790 36 TKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDadkegFLRSETS 115
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 71987143 352 YIHRIGRSGRfGRKGVAI---NFVTENDARQLKEIESYYTTQIE 392
Cdd:cd18790 116 LIQTIGRAAR-NVNGKVIlyaDKITDSMQKAIEETERRREIQME 158
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
270-369 |
3.06e-07 |
|
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: 49.47 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 270 QAVIFCNTRRKVDTLTEKMTenqfTVSCLHGDMDQAERDTIMREFRSGSSRVLITTDILARGID-----VqqvslVIN-- 342
Cdd:cd18795 45 PVLVFCSSRKECEKTAKDLA----GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNlpartV-----IIKgt 115
|
90 100 110
....*....|....*....|....*....|....*
gi 71987143 343 --YDLPSNRE----NYIHRIGRSGR--FGRKGVAI 369
Cdd:cd18795 116 qrYDGKGYRElsplEYLQMIGRAGRpgFDTRGEAI 150
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
263-369 |
3.14e-07 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 49.56 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 263 YNVVNVTQAVIFCNTRRKVDTLT----EKMTENQFTVSCL---HGDMDQAERDTIMREFRSGSSRVLITTDILARGIDVQ 335
Cdd:cd18797 30 DLVRAGVKTIVFCRSRKLAELLLrylkARLVEEGPLASKVasyRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIG 109
|
90 100 110
....*....|....*....|....*....|....
gi 71987143 336 QVSLVINYDLPSNRENYIHRIGRSGRFGRKGVAI 369
Cdd:cd18797 110 GLDAVVLAGYPGSLASLWQQAGRAGRRGKDSLVI 143
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
302-366 |
7.74e-07 |
|
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: 48.12 E-value: 7.74e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71987143 302 MDQAERDTIMREFRSGSSRVLITTDILARGIDVQQVSLVINYDLPSNRENYIHRIGRSGRfGRKG 366
Cdd:cd18801 74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR-KRQG 137
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
292-368 |
1.03e-06 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 48.11 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 292 QFTVSCLHGDMDQAERDTIMREFRSGSSRVLITTDILARGIDVQQVSLVINYDlpsnrenyIHRIGRS------GRFGRK 365
Cdd:cd18811 61 ELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIED--------AERFGLSqlhqlrGRVGRG 132
|
...
gi 71987143 366 GVA 368
Cdd:cd18811 133 DHQ 135
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
272-365 |
1.04e-06 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 51.05 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 272 VIFCNTRRKVDTLTEKMTENQFTVSCLHGDMDQAERDTIMREFRSGSSRVLITTDILARGIDVQQVSLVINYDLPSNREN 351
Cdd:PLN03137 684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEG 763
|
90
....*....|....
gi 71987143 352 YIHRIGRSGRFGRK 365
Cdd:PLN03137 764 YHQECGRAGRDGQR 777
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
68-154 |
2.64e-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: 47.41 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 68 DVIAQAQSGTGKTATFSVSILqriDHEDPHVQALVMAPTRELAQQIQKVMSALgeYLNVNILPCIGGTsvrddQRKLEAG 147
Cdd:cd17918 38 DRLLSGDVGSGKTLVALGAAL---LAYKNGKQVAILVPTEILAHQHYEEARKF--LPFINVELVTGGT-----KAQILSG 107
|
....*..
gi 71987143 148 IHVVVGT 154
Cdd:cd17918 108 ISLLVGT 114
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
176-325 |
6.08e-06 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 48.15 E-value: 6.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 176 VLDEAD----EMLSrgfkdQIYEVFRSMPQ-DVQVVLLSATMPSEVLDvtnrFMRNPIRILVKKDELTLEGIRQFY---I 247
Cdd:COG1203 273 ILDEVQayppYMLA-----LLLRLLEWLKNlGGSVILMTATLPPLLRE----ELLEAYELIPDEPEELPEYFRAFVrkrV 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 248 NVQKDEWKFDCLCDLY--NVVNVTQAVIFCNTRRKVDTLTEKMTE--NQFTVSCLHGDMDQAER----DTIMREFRSGSS 319
Cdd:COG1203 344 ELKEGPLSDEELAELIleALHKGKSVLVIVNTVKDAQELYEALKEklPDEEVYLLHSRFCPADRseieKEIKERLERGKP 423
|
....*.
gi 71987143 320 RVLITT 325
Cdd:COG1203 424 CILVST 429
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
38-228 |
1.16e-05 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 45.99 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 38 EELLRGIygFGFEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKTATFSV--SILQRIdhedphvqALVMAPTRELAQ-QIQ 114
Cdd:cd17920 1 EQILKEV--FGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLpaLLLDGV--------TLVVSPLISLMQdQVD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 115 KvMSALG---EYLNVNILPciggTSVRDDQRKLEAG-IHVVVGTPGRVGDMINRNALD----TSRIKMFVLDEA------ 180
Cdd:cd17920 71 R-LQQLGiraAALNSTLSP----EEKREVLLRIKNGqYKLLYVTPERLLSPDFLELLQrlpeRKRLALIVVDEAhcvsqw 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 71987143 181 -----DEMLSRGfkdqiyeVFRSMPQDVQVVLLSATMPSEVLD--VTNRFMRNPI 228
Cdd:cd17920 146 ghdfrPDYLRLG-------RLRRALPGVPILALTATATPEVREdiLKRLGLRNPV 193
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
272-387 |
1.56e-05 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 47.18 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 272 VIFCNTRRKVDTLTEKMTENQFTV------SCLHGD--MDQAERDTIMREFRSGSSRVLITTDILARGIDVQQVSLVINY 343
Cdd:PRK13766 369 IVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDkgMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFY 448
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 71987143 344 D-LPSN-RenYIHRIGRSGRfGRKGVAINFVTEnDARQlkeiESYY 387
Cdd:PRK13766 449 EpVPSEiR--SIQRKGRTGR-QEEGRVVVLIAK-GTRD----EAYY 486
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
49-373 |
2.18e-05 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 46.63 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 49 FEKPSAIQKRAIVPCTTGKDVIAQAQSGTGKT-ATFSVSILQRIDHEDPH-----VQALVMAPTRELAQQIQK----VMS 118
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAFLPALDELARRPRPGelpdgLRVLYISPLKALANDIERnlraPLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 119 ALGEYLNVNiLPCI------GGTSVRDDQRKLEAGIHVVVGTPGRVGDMIN-RNALDT-SRIKMFVLDEADEMLS--RGf 188
Cdd:COG1201 102 EIGEAAGLP-LPEIrvgvrtGDTPASERQRQRRRPPHILITTPESLALLLTsPDARELlRGVRTVIVDEIHALAGskRG- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 189 kDQI---YEVFRSM-PQDVQVVLLSATM--PSEVLD-------------VTNRFMRNP-IRILVKKDELTLEGIRQFYIN 248
Cdd:COG1201 180 -VHLalsLERLRALaPRPLQRIGLSATVgpLEEVARflvgyedprpvtiVDAGAGKKPdLEVLVPVEDLIERFPWAGHLW 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 249 VQkdewkfdclcdLYN-VVNVTQA----VIFCNTRRkvdtLTEKMT--------ENQFTVSCLHGDMDQAERDTIMREFR 315
Cdd:COG1201 259 PH-----------LYPrVLDLIEAhrttLVFTNTRS----QAERLFqrlnelnpEDALPIAAHHGSLSREQRLEVEEALK 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 71987143 316 SGSSRVLITTDILARGIDVQQVSLVINYDLPSNRENYIHRIGRSG-RFGRKGVAINFVT 373
Cdd:COG1201 324 AGELRAVVATSSLELGIDIGDVDLVIQVGSPKSVARLLQRIGRAGhRVGEVSKGRLVPT 382
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
292-367 |
3.92e-05 |
|
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: 43.79 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 292 QFTVSCLHGDMDQAERDTIMREFRSGSSRVLITTDILARGIDVQQVSLVINYDlpsnrenyIHRIGRS------GRFGRK 365
Cdd:cd18792 60 EARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIED--------ADRFGLSqlhqlrGRVGRG 131
|
..
gi 71987143 366 GV 367
Cdd:cd18792 132 KH 133
|
|
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
292-325 |
1.38e-04 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 43.89 E-value: 1.38e-04
10 20 30
....*....|....*....|....*....|....
gi 71987143 292 QFTVSCLHGDMDQAERDTIMREFRSGSSRVLITT 325
Cdd:COG1200 503 GLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVAT 536
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
299-360 |
2.65e-04 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 43.37 E-value: 2.65e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71987143 299 HGDMDQAERDTIMREFRSGSSRVLITTDILARGIDVQQVSLVINYDLPSNRENYIHRIGRSG 360
Cdd:PRK09751 308 HGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
|
|
| PRK05298 |
PRK05298 |
excinuclease ABC subunit UvrB; |
281-340 |
5.02e-04 |
|
excinuclease ABC subunit UvrB;
Pssm-ID: 235395 [Multi-domain] Cd Length: 652 Bit Score: 42.34 E-value: 5.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71987143 281 VDTLTEKM--------TENQFTVSCLHGDMDQAERDTIMREFRSGSSRVLITTDILARGIDVQQVSLV 340
Cdd:PRK05298 451 VTTLTKRMaedltdylKELGIKVRYLHSDIDTLERVEIIRDLRLGEFDVLVGINLLREGLDIPEVSLV 518
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
298-358 |
5.03e-04 |
|
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350176 [Multi-domain] Cd Length: 153 Bit Score: 40.31 E-value: 5.03e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71987143 298 LHGDMDQAERDTIMREFRSGSSRVLITTDILARGIDVQQ--VSLVINYDLPSNREnYIHRIGR 358
Cdd:cd18789 74 ITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPEanVAIQISGHGGSRRQ-EAQRLGR 135
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
67-180 |
5.36e-04 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 40.71 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 67 KDVIAQAQSGTGKTAtfsVSI-LQRIDHED------PHVQALVMAPTRELAQQiQkvMSALGEYLNVNILPCIGGTSVRD 139
Cdd:cd18034 17 RNTIVVLPTGSGKTL---IAVmLIKEMGELnrkeknPKKRAVFLVPTVPLVAQ-Q--AEAIRSHTDLKVGEYSGEMGVDK 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 71987143 140 --DQRKLE--AGIHVVVGTPGRVGDMINRNALDTSRIKMFVLDEA 180
Cdd:cd18034 91 wtKERWKEelEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| SF2_C_priA |
cd18804 |
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ... |
306-396 |
5.86e-04 |
|
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350191 [Multi-domain] Cd Length: 238 Bit Score: 41.08 E-value: 5.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 306 ERDTIMREFRSGSSRVLITTDILARGIDVQQVSLV--INYDLPSNRENY---------IHRI-GRSGRFGRKGVAI--NF 371
Cdd:cd18804 132 ALEKLLDQFERGEIDILIGTQMIAKGLDFPNVTLVgiLNADSGLNSPDFraserafqlLTQVsGRAGRGDKPGKVIiqTY 211
|
90 100
....*....|....*....|....*
gi 71987143 372 VTENDARQLKEIESYYTTQIEEMPE 396
Cdd:cd18804 212 NPEHPLIQAAKEEDYEAFYEEELAE 236
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
295-368 |
6.45e-04 |
|
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF 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: 350197 [Multi-domain] Cd Length: 151 Bit Score: 40.02 E-value: 6.45e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71987143 295 VSCLHGDMDQAERDTIMREFRSGSSRVLITTDILARGIDVQQVSLVINYDLPSNRENYIHRI-GRSGRFGRKGVA 368
Cdd:cd18810 54 IAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIERADKFGLAQLYQLrGRVGRSKERAYA 128
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
76-154 |
9.09e-04 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 41.29 E-value: 9.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 76 GTGKTATFSVSILQRIDHedpHVQALVMAPTRELAQQ----IQKVMSALGeyLNVNILpcIGGTSVRDDQRKLEA----G 147
Cdd:PRK10917 292 GSGKTVVAALAALAAIEA---GYQAALMAPTEILAEQhyenLKKLLEPLG--IRVALL--TGSLKGKERREILEAiasgE 364
|
....*..
gi 71987143 148 IHVVVGT 154
Cdd:PRK10917 365 ADIVIGT 371
|
|
| DEXHc_RecG |
cd17992 |
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in ... |
35-154 |
9.46e-04 |
|
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. It is a member 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: 350750 [Multi-domain] Cd Length: 225 Bit Score: 40.21 E-value: 9.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 35 ELKEELLRGiygFGFEKPSAiQKRAIvpcttgkDVIAQAQS-------------GTGKTATFSVSILQRIDHedpHVQAL 101
Cdd:cd17992 33 ELLKKFLEA---LPFELTGA-QKRVI-------DEILRDLAsekpmnrllqgdvGSGKTVVAALAMLAAVEN---GYQVA 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 71987143 102 VMAPTRELAQQIQKVMSALGEYLNVNILPCIGgtSVRDDQRK-----LEAG-IHVVVGT 154
Cdd:cd17992 99 LMAPTEILAEQHYDSLKKLLEPLGIRVALLTG--STKAKEKReilekIASGeIDIVIGT 155
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
271-341 |
1.32e-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: 1.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71987143 271 AVIFCNTRRKVDTLTEKMTENQFTVSCLHGD--MDQAERDTIMR-EFRSGSSRVLITTDILARGIDVQQVSLVI 341
Cdd:cd18799 9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDysDRERGDEALILlFFGELKPPILVTVDLLTTGVDIPEVDNVV 82
|
|
| UvrB |
COG0556 |
Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair]; |
281-340 |
5.16e-03 |
|
Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair];
Pssm-ID: 440322 [Multi-domain] Cd Length: 657 Bit Score: 38.84 E-value: 5.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71987143 281 VDTLTEKM--------TENQFTVSCLHGDMDQAERDTIMREFRSGSSRVLITTDILARGIDVQQVSLV 340
Cdd:COG0556 448 VTTLTKRMaedltdylKELGIKVRYLHSDIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLV 515
|
|
| ComFA |
COG4098 |
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ... |
270-361 |
8.31e-03 |
|
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, recombination and repair];
Pssm-ID: 443274 [Multi-domain] Cd Length: 451 Bit Score: 38.32 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 270 QAVIFCNTRRKVDTLTEKMTE--NQFTVSCLHGDmDQaERDTIMREFRSGSSRVLITTDILARGIDVQQVS-LVINYDlp 346
Cdd:COG4098 321 QLLIFVPTIELLEQLVALLQKlfPEERIAGVHAE-DP-ERKEKVQAFRDGEIPILVTTTILERGVTFPNVDvAVLGAD-- 396
|
90 100
....*....|....*....|....*
gi 71987143 347 snrenyiHRI----------GRSGR 361
Cdd:COG4098 397 -------HPVfteaalvqiaGRVGR 414
|
|
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
76-154 |
8.83e-03 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 38.11 E-value: 8.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 76 GTGKT--ATFSvsILQRIDHedpHVQALVMAPTRELAQQ----IQKVMSALGeyLNVNILpcIGGTSVRDDQRKLEA--- 146
Cdd:COG1200 290 GSGKTvvALLA--MLAAVEA---GYQAALMAPTEILAEQhyrsLSKLLEPLG--IRVALL--TGSTKAKERREILAAlas 360
|
....*....
gi 71987143 147 G-IHVVVGT 154
Cdd:COG1200 361 GeADIVVGT 369
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
103-211 |
9.33e-03 |
|
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350791 [Multi-domain] Cd Length: 182 Bit Score: 36.92 E-value: 9.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987143 103 MAPTREL-AQQIQKVMSALGEYLNVNILpcIGGTSVRDDQRKLEAGIHVVVGTPGRVGDMINRNALDTSRIKMFVLDEAd 181
Cdd:cd18033 52 MAPTKPLvSQQIEACYKITGIPSSQTAE--LTGSVPPTKRAELWASKRVFFLTPQTLENDLKEGDCDPKSIVCLVIDEA- 128
|
90 100 110
....*....|....*....|....*....|....*
gi 71987143 182 emlSRGFKDQIY-----EVFRSMPQdVQVVLLSAT 211
Cdd:cd18033 129 ---HRATGNYAYcqvvrELMRYNSH-FRILALTAT 159
|
|
| |
