|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
1-399 |
0e+00 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 599.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 1 MAENKKKND---DMATVEFESSEEvSIIPTFDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKT 77
Cdd:PTZ00424 1 MATSEQKNQseqVASTGTIESNYD-EIVDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 78 ATFSISVLQSLDTQVRETQALILSPTRELAVQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFD 157
Cdd:PTZ00424 80 ATFVIAALQLIDYDLNACQALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 158 MIRRRNLRTRAIKLLVLDEADEMLNKGFKEQLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRILVKRDELTLE 237
Cdd:PTZ00424 160 MIDKRHLRVDDLKLFILDEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 238 GIKQFFVAVDREEWKFDTLIDLYDTLTITQAVLFCNTRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGTTR 317
Cdd:PTZ00424 240 GIRQFYVAVEKEEWKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 318 VLISTDVWARGLDVPQVSLVINYDLPNNRELYIHRIGRSGRFGRKGVAINFVKQDDVRILRDIEQYYSTQIDEMPMNIAD 397
Cdd:PTZ00424 320 VLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEVAD 399
|
..
gi 1845969787 398 II 399
Cdd:PTZ00424 400 YL 401
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
25-393 |
3.09e-161 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 459.61 E-value: 3.09e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 25 IPTFDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQV-RETQALILSPT 103
Cdd:COG0513 1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRpRAPQALILAPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 104 RELAVQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNK 183
Cdd:COG0513 81 RELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 184 GFKEQLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRILVKRDELTLEGIKQFFVAVDREEwKFDTLIDLYDTL 263
Cdd:COG0513 161 GFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRD-KLELLRRLLRDE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 264 TITQAVLFCNTRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGTTRVLISTDVWARGLDVPQVSLVINYDLP 343
Cdd:COG0513 240 DPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLP 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1845969787 344 NNRELYIHRIGRSGRFGRKGVAINFVKQDDVRILRDIEQYYSTQIDEMPM 393
Cdd:COG0513 320 EDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEEL 369
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
28-228 |
1.36e-134 |
|
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: 383.36 E-value: 1.36e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 28 FDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRETQALILSPTRELA 107
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 108 VQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKGFKE 187
Cdd:cd18045 81 VQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1845969787 188 QLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRIL 228
Cdd:cd18045 161 QIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRIL 201
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
31-228 |
7.73e-124 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation factor-4A (eIF4A) family consists of 3 proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA. EIF4A proteins are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350697 [Multi-domain] Cd Length: 199 Bit Score: 355.86 E-value: 7.73e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 31 MGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRETQALILSPTRELAVQI 110
Cdd:cd17939 2 MGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 111 QKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKGFKEQLY 190
Cdd:cd17939 82 QKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQIY 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 1845969787 191 DIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRIL 228
Cdd:cd17939 162 DIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRIL 199
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
28-228 |
5.89e-122 |
|
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: 351.36 E-value: 5.89e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 28 FDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRETQALILSPTRELA 107
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 108 VQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKGFKE 187
Cdd:cd18046 81 QQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1845969787 188 QLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRIL 228
Cdd:cd18046 161 QIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRIL 201
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
28-389 |
2.41e-110 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 331.38 E-value: 2.41e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 28 FDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRETQALILSPTRELA 107
Cdd:PRK11776 6 FSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTRELA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 108 VQIQKVVLALGDYM-NVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKGFK 186
Cdd:PRK11776 86 DQVAKEIRRLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMGFQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 187 EQLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRILV--KRDELTlegIKQFFVAVDREEwKFDTLIDLYDTLT 264
Cdd:PRK11776 166 DAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVesTHDLPA---IEQRFYEVSPDE-RLPALQRLLLHHQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 265 ITQAVLFCNTRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGTTRVLISTDVWARGLDVPQVSLVINYDLPN 344
Cdd:PRK11776 242 PESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELAR 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1845969787 345 NRELYIHRIGRSGRFGRKGVAINFVKQDDVRILRDIEQYYSTQID 389
Cdd:PRK11776 322 DPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLN 366
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
27-399 |
3.79e-86 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 274.03 E-value: 3.79e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 27 TFDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRETQALILSPTREL 106
Cdd:PRK11634 7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 107 AVQIQKVVLALGDYMN-VQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKGF 185
Cdd:PRK11634 87 AVQVAEAMTDFSKHMRgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 186 KEQLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRILVKRDELTLEGIKQFFVAVDREEwKFDTLIDLYDTLTI 265
Cdd:PRK11634 167 IEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMR-KNEALVRFLEAEDF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 266 TQAVLFCNTRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGTTRVLISTDVWARGLDVPQVSLVINYDLPNN 345
Cdd:PRK11634 246 DAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMD 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1845969787 346 RELYIHRIGRSGRFGRKGVAINFVKQDDVRILRDIEQYYSTQIDEMPMNIADII 399
Cdd:PRK11634 326 SESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAELL 379
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
26-383 |
5.29e-86 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 267.96 E-value: 5.29e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 26 PTFDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRE----TQALILS 101
Cdd:PRK11192 1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRksgpPRILILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 102 PTRELAVQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEML 181
Cdd:PRK11192 81 PTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 182 NKGFKEQLYDI-----YRylppgAQVVLLSATLPHE-ILEMTSKFMTDPIRILVKRDELTLEGIKQFFVAVDREEWKFDT 255
Cdd:PRK11192 161 DMGFAQDIETIaaetrWR-----KQTLLFSATLEGDaVQDFAERLLNDPVEVEAEPSRRERKKIHQWYYRADDLEHKTAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 256 LIDLYDTLTITQAVLFCNTRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGTTRVLISTDVWARGLDVPQVS 335
Cdd:PRK11192 236 LCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVS 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1845969787 336 LVINYDLPNNRELYIHRIGRSGRFGRKGVAINFVKQDDVRILRDIEQY 383
Cdd:PRK11192 316 HVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERY 363
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
37-227 |
9.64e-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: 256.21 E-value: 9.64e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 37 LLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQ----VRETQALILSPTRELAVQIQK 112
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEpkkkGRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 113 VVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKGFKEQLYDI 192
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1845969787 193 YRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRI 227
Cdd:cd00268 161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
27-391 |
2.39e-82 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 259.36 E-value: 2.39e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 27 TFDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQV------RETQALIL 100
Cdd:PRK10590 2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQphakgrRPVRALIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 101 SPTRELAVQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEM 180
Cdd:PRK10590 82 TPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 181 LNKGFkeqLYDIYRY---LPPGAQVVLLSATLPHEILEMTSKFMTDPIRILVKRDELTLEGIKQFFVAVDREEwKFDTLI 257
Cdd:PRK10590 162 LDMGF---IHDIRRVlakLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKR-KRELLS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 258 DLYDTLTITQAVLFCNTRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGTTRVLISTDVWARGLDVPQVSLV 337
Cdd:PRK10590 238 QMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHV 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1845969787 338 INYDLPNNRELYIHRIGRSGRFGRKGVAINFVKQDDVRILRDIEQYYSTQIDEM 391
Cdd:PRK10590 318 VNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRI 371
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
28-392 |
2.67e-74 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 239.04 E-value: 2.67e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 28 FDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVL-QSLDTQVR------ETQALIL 100
Cdd:PRK01297 89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIInQLLQTPPPkerymgEPRALII 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 101 SPTRELAVQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDyGQH--VVSGTPGRVFDMIRRRNLRTRAIKLLVLDEAD 178
Cdd:PRK01297 169 APTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLE-ARFcdILVATPGRLLDFNQRGEVHLDMVEVMVLDEAD 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 179 EMLNKGFKEQLYDIYRYLPPGA--QVVLLSATLPHEILEMTSKFMTDPIRILVKRDELTLEGIKQFFVAVDREEwKFDTL 256
Cdd:PRK01297 248 RMLDMGFIPQVRQIIRQTPRKEerQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSD-KYKLL 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 257 IDLYDTLTITQAVLFCNTRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGTTRVLISTDVWARGLDVPQVSL 336
Cdd:PRK01297 327 YNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISH 406
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1845969787 337 VINYDLPNNRELYIHRIGRSGRFGRKGVAINFVKQDDVRILRDIEQYYSTQID-EMP 392
Cdd:PRK01297 407 VINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKIScEMP 463
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
33-227 |
1.98e-71 |
|
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: 222.45 E-value: 1.98e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 33 LREDLLRGIYAYGFEKPSAIQQRAIPAILKA--RDVIAQAQSGTGKTATFSISVLQSLDTQVRETQALILSPTRELAVQI 110
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 111 QKVVLALGDYMNVQCHACIGGTNL--GEDIRkldygQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLN-KGFKE 187
Cdd:cd17963 81 GEVVEKMGKFTGVKVALAVPGNDVprGKKIT-----AQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDtQGHGD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1845969787 188 QLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRI 227
Cdd:cd17963 156 QSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
27-393 |
2.18e-70 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 231.38 E-value: 2.18e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 27 TFDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSL-------DTQVRETQALI 99
Cdd:PRK04537 10 TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlsrpalaDRKPEDPRALI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 100 LSPTRELAVQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRT-RAIKLLVLDEAD 178
Cdd:PRK04537 90 LAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVVSlHACEICVLDEAD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 179 EMLNKGFKEQLYDIYRYLPPGA--QVVLLSATLPHEILEMTSKFMTDPIRILVKRDELTLEGIKQ--FFVAvdrEEWKFD 254
Cdd:PRK04537 170 RMFDLGFIKDIRFLLRRMPERGtrQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQriYFPA---DEEKQT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 255 TLIDLYDTLTITQAVLFCNTRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGTTRVLISTDVWARGLDVPQV 334
Cdd:PRK04537 247 LLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGV 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1845969787 335 SLVINYDLPNNRELYIHRIGRSGRFGRKGVAINFVKQDDVRILRDIEQYYSTQIDEMPM 393
Cdd:PRK04537 327 KYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKIPVEPV 385
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
28-227 |
5.41e-69 |
|
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or p54) participates in mRNA regulation mediated by miRNA-mediated silencing. It also plays a role in global and transcript-specific messenger RNA (mRNA) storage, translational repression, and decay. It is a member of the DEAD-box helicase family, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350698 [Multi-domain] Cd Length: 201 Bit Score: 216.40 E-value: 5.41e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 28 FDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRETQALILSPTRELA 107
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 108 VQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKGFKE 187
Cdd:cd17940 81 LQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1845969787 188 QLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRI 227
Cdd:cd17940 161 IIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
25-382 |
4.03e-67 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 221.96 E-value: 4.03e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 25 IPTFDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRETQA-----LI 99
Cdd:PTZ00110 129 VVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGdgpivLV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 100 LSPTRELAVQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADE 179
Cdd:PTZ00110 209 LAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADR 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 180 MLNKGFKEQLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTD-PIRILVKRDELTL-EGIKQFFVAVDREEwKFDTLI 257
Cdd:PTZ00110 289 MLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDLTAcHNIKQEVFVVEEHE-KRGKLK 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 258 DLYDTLTI--TQAVLFCNTRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGTTRVLISTDVWARGLDVPQVS 335
Cdd:PTZ00110 368 MLLQRIMRdgDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVK 447
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1845969787 336 LVINYDLPNNRELYIHRIGRSGRFGRKGVAINFVKQDD-------VRILRDIEQ 382
Cdd:PTZ00110 448 YVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKyrlardlVKVLREAKQ 501
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
28-388 |
1.28e-66 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 217.53 E-value: 1.28e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 28 FDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSL-------DTQVRETQALIL 100
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLlshpapeDRKVNQPRALIM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 101 SPTRELAVQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEM 180
Cdd:PRK04837 90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 181 LNKGFKEQLYDIYRYLPPGAQ--VVLLSATLPHEILEMTSKFMTDPIRILVKRDELTLEGIKQ-FFVAVDREewKFDTLI 257
Cdd:PRK04837 170 FDLGFIKDIRWLFRRMPPANQrlNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEeLFYPSNEE--KMRLLQ 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 258 DLYDTLTITQAVLFCNTRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGTTRVLISTDVWARGLDVPQVSLV 337
Cdd:PRK04837 248 TLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHV 327
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1845969787 338 INYDLPNNRELYIHRIGRSGRFGRKGVAINFVKQDDVRILRDIEQYYSTQI 388
Cdd:PRK04837 328 FNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIGHSI 378
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
25-382 |
1.70e-66 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 219.66 E-value: 1.70e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 25 IPTFDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVL--------QSLDTQvRETQ 96
Cdd:PLN00206 120 ILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIIsrcctirsGHPSEQ-RNPL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 97 ALILSPTRELAVQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDE 176
Cdd:PLN00206 199 AMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDE 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 177 ADEMLNKGFKEQLYDIYRYLPPgAQVVLLSATLPHEILEMTSKFMTDPIRILVKRDELTLEGIKQFFVAVDREEWKfdtl 256
Cdd:PLN00206 279 VDCMLERGFRDQVMQIFQALSQ-PQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKK---- 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 257 IDLYDTLTITQ-----AVLFCNTRRKVDWLTDKMKEAN-FTVSSMHGDMEQKDRDEVMKEFRAGTTRVLISTDVWARGLD 330
Cdd:PLN00206 354 QKLFDILKSKQhfkppAVVFVSSRLGADLLANAITVVTgLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVD 433
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1845969787 331 VPQVSLVINYDLPNNRELYIHRIGRSGRFGRKGVAINFVKQDDVRILRDIEQ 382
Cdd:PLN00206 434 LLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVA 485
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
37-227 |
2.64e-62 |
|
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: 198.64 E-value: 2.64e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 37 LLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRETQALILSPTRELAVQIQKVVLA 116
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 117 LGDYM-NVQCHACIGGTNLGEDIRKLDyGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKGFKEQLYDIYRY 195
Cdd:cd17943 81 IGKKLeGLKCEVFIGGTPVKEDKKKLK-GCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSS 159
|
170 180 190
....*....|....*....|....*....|..
gi 1845969787 196 LPPGAQVVLLSATLPHEILEMTSKFMTDPIRI 227
Cdd:cd17943 160 LPKNKQVIAFSATYPKNLDNLLARYMRKPVLV 191
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
239-369 |
4.67e-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: 193.49 E-value: 4.67e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 239 IKQFFVAVDREEWKFDTLIDLYDTLTITQAVLFCNTRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGTTRV 318
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1845969787 319 LISTDVWARGLDVPQVSLVINYDLPNNRELYIHRIGRSGRFGRKGVAINFV 369
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
50-215 |
7.11e-57 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 183.98 E-value: 7.11e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 50 SAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRETQALILSPTRELAVQIQKVVLALGDYMNVQCHACI 129
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 130 GGTNLGEDIRKLDyGQHVVSGTPGRVFDMIRRRNlRTRAIKLLVLDEADEMLNKGFKEQLYDIYRYLPPGAQVVLLSATL 209
Cdd:pfam00270 81 GGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATL 158
|
....*.
gi 1845969787 210 PHEILE 215
Cdd:pfam00270 159 PRNLED 164
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
41-242 |
1.06e-54 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 179.61 E-value: 1.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 41 IYAYGFEKPSAIQQRAIPAILK-ARDVIAQAQSGTGKTATFSISVLQSLDTQvRETQALILSPTRELAVQIQKVVLALGD 119
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSgLRDVILAAPTGSGKTLAALLPALEALKRG-KGGRVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 120 YMNVQCHACIGGTNLGEDIRKLDYGQ-HVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKGFKEQLYDIYRYLPP 198
Cdd:smart00487 80 SLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1845969787 199 GAQVVLLSATLPHEILEMTSKFMTDPIRILVKRdeLTLEGIKQF 242
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
27-227 |
1.71e-53 |
|
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: 176.34 E-value: 1.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 27 TFDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLdtQVRETQ----ALILSP 102
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKL--KAHSPTvgarALILSP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 103 TRELAVQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLN 182
Cdd:cd17959 80 TRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1845969787 183 KGFKEQLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRI 227
Cdd:cd17959 160 MGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
28-229 |
6.72e-53 |
|
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: 175.23 E-value: 6.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 28 FDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRETQALILSPTRELA 107
Cdd:cd17950 4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRELA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 108 VQIQKVVLALGDYM-NVQCHACIGGTNLGEDIRKL-DYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNK-G 184
Cdd:cd17950 84 FQISNEYERFSKYMpNVKTAVFFGGVPIKKDIEVLkNKCPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLEQlD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1845969787 185 FKEQLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRILV 229
Cdd:cd17950 164 MRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
28-224 |
3.81e-52 |
|
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350713 [Multi-domain] Cd Length: 204 Bit Score: 172.79 E-value: 3.81e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 28 FDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRETQALILSPTRELA 107
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 108 VQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRT---RAIKLLVLDEADEMLNKG 184
Cdd:cd17955 81 YQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDTTkvlSRVKFLVLDEADRLLTGS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1845969787 185 FKEQLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDP 224
Cdd:cd17955 161 FEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
37-227 |
1.41e-50 |
|
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: 168.59 E-value: 1.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 37 LLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSL---DTQVRETQALILSPTRELAVQIQKV 113
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLlyrPKKKAATRVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 114 VLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRR-RNLRTRAIKLLVLDEADEMLNKGFKEQLYDI 192
Cdd:cd17947 81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNsPSFDLDSIEILVLDEADRMLEEGFADELKEI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1845969787 193 YRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRI 227
Cdd:cd17947 161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
27-227 |
1.15e-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: 166.34 E-value: 1.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 27 TFDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRETQALILSPTREL 106
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 107 AVQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRN-LRTRAIKLLVLDEADEMLNKGF 185
Cdd:cd17954 81 AQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLKFLVMDEADRLLNMDF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1845969787 186 KEQLYDIYRYLPPGAQVVLLSATlpheileMTSKF-------MTDPIRI 227
Cdd:cd17954 161 EPEIDKILKVIPRERTTYLFSAT-------MTTKVaklqrasLKNPVKI 202
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
27-231 |
9.80e-48 |
|
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes Drosophila melanogaster Vasa, which is essential for development. DEAD box protein 3 (DDX3) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DDX3 and DDX4 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350725 [Multi-domain] Cd Length: 221 Bit Score: 161.89 E-value: 9.80e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 27 TFDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSL----------DTQVRETQ 96
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLledgppsvgrGRRKAYPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 97 ALILSPTRELAVQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDE 176
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1845969787 177 ADEMLNKGFKEQLYDIYRY--LPPGA--QVVLLSATLPHEILEMTSKFMTDPIRILVKR 231
Cdd:cd17967 161 ADRMLDMGFEPQIRKIVEHpdMPPKGerQTLMFSATFPREIQRLAADFLKNYIFLTVGR 219
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
4-221 |
1.91e-46 |
|
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DEAD-box helicases are a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350810 [Multi-domain] Cd Length: 264 Bit Score: 160.13 E-value: 1.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 4 NKKKNDDMAtVEFESSEEVSIIPTFDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSIS 83
Cdd:cd18052 22 NFDKYDEIP-VEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 84 VLQSLDTQ---------VRETQALILSPTRELAVQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGR 154
Cdd:cd18052 101 VLTGMMKEgltassfseVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGR 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1845969787 155 VFDMIRRRNLRTRAIKLLVLDEADEMLNKGFKEQLYDIYRYL--PPGA--QVVLLSATLPHEILEMTSKFM 221
Cdd:cd18052 181 LLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPgmPSKEdrQTLMFSATFPEEIQRLAAEFL 251
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
37-221 |
9.04e-45 |
|
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350722 [Multi-domain] Cd Length: 211 Bit Score: 153.89 E-value: 9.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 37 LLRGIYAYGFEKPSAIQQRAIPAILKAR-DVIAQAQSGTGKTATFSISVLQSL-----DTQVRETQALILSPTRELAVQI 110
Cdd:cd17964 5 LLKALTRMGFETMTPVQQKTLKPILSTGdDVLARAKTGTGKTLAFLLPAIQSLlntkpAGRRSGVSALIISPTRELALQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 111 QKVVLALGDYM-NVQCHACIGGTNLGEDIRKL-DYGQHVVSGTPGRVFDMIRRRNLRTRA--IKLLVLDEADEMLNKGFK 186
Cdd:cd17964 85 AAEAKKLLQGLrKLRVQSAVGGTSRRAELNRLrRGRPDILVATPGRLIDHLENPGVAKAFtdLDYLVLDEADRLLDMGFR 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 1845969787 187 EQLYDIYRYLPPGA----QVVLLSATLPHEILEMTSKFM 221
Cdd:cd17964 165 PDLEQILRHLPEKNadprQTLLFSATVPDEVQQIARLTL 203
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
25-235 |
2.78e-44 |
|
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: 153.25 E-value: 2.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 25 IPTFDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILK--ARDVIAQAQSGTGKTATFSISVLQSLDTQVRETQALILSP 102
Cdd:cd18048 17 VKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLAdpPQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLSP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 103 TRELAVQIQKVVLALGDYMN-VQCHACIGGTNLGediRKLDYGQHVVSGTPGRVFD-MIRRRNLRTRAIKLLVLDEADEM 180
Cdd:cd18048 97 TFELALQTGKVVEEMGKFCVgIQVIYAIRGNRPG---KGTDIEAQIVIGTPGTVLDwCFKLRLIDVTNISVFVLDEADVM 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1845969787 181 LN-KGFKEQLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRILVKRDELT 235
Cdd:cd18048 174 INvQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
25-227 |
2.22e-43 |
|
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: 150.61 E-value: 2.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 25 IPTFDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQ--VRETQ---ALI 99
Cdd:cd17953 11 IQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQrpVKPGEgpiGLI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 100 LSPTRELAVQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMI---RRRNLRTRAIKLLVLDE 176
Cdd:cd17953 91 MAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtanNGRVTNLRRVTYVVLDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1845969787 177 ADEMLNKGFKEQLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRI 227
Cdd:cd17953 171 ADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
37-227 |
2.63e-43 |
|
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: 149.62 E-value: 2.63e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 37 LLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRETQALILSPTRELAVQIQKVVLA 116
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 117 LGD-YMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKGFKEQLYDIYRY 195
Cdd:cd17962 81 LMKgLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILEN 160
|
170 180 190
....*....|....*....|....*....|..
gi 1845969787 196 LPPGAQVVLLSATLPHEILEMTSKFMTDPIRI 227
Cdd:cd17962 161 ISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
37-229 |
3.20e-43 |
|
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: 149.66 E-value: 3.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 37 LLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRET--QALILSPTRELAVQIQKVV 114
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKKglRALILAPTRELASQIYREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 115 LALGDYMNVQCHACIGGTNLG-----EDIRKLDygqhVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKGFKEQL 189
Cdd:cd17957 81 LKLSKGTGLRIVLLSKSLEAKakdgpKSITKYD----ILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQT 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1845969787 190 YDIYRYLP-PGAQVVLLSATLPHEILEMTSKFMTDPIRILV 229
Cdd:cd17957 157 DEILAACTnPNLQRSLFSATIPSEVEELARSVMKDPIRIIV 197
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
28-224 |
4.21e-43 |
|
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350696 [Multi-domain] Cd Length: 204 Bit Score: 149.39 E-value: 4.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 28 FDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSldtqvreTQALILSPTRELA 107
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQI-------VVALILEPSRELA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 108 VQIQKVVLALGDYMN---VQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKG 184
Cdd:cd17938 74 EQTYNCIENFKKYLDnpkLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1845969787 185 FKEQLYDIYRYLPPGA------QVVLLSATLpH--EILEMTSKFMTDP 224
Cdd:cd17938 154 NLETINRIYNRIPKITsdgkrlQVIVCSATL-HsfEVKKLADKIMHFP 200
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
37-227 |
1.30e-42 |
|
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor 3B-Associated 125 kDa Protein, RHELP, or RNAHP) is an NTPase with a preference for ATP, the hydrolysis of which is enhanced by various RNA substrates. It acts as a non-processive RNA helicase with protein displacement and RNA annealing activities. DDX42 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350710 [Multi-domain] Cd Length: 197 Bit Score: 147.95 E-value: 1.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 37 LLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQvRETQ------ALILSPTRELAVQI 110
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQ-RELEkgegpiAVIVAPTRELAQQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 111 QKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKGFKEQLY 190
Cdd:cd17952 80 YLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 1845969787 191 DIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRI 227
Cdd:cd17952 160 SIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
37-225 |
1.37e-42 |
|
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: 148.12 E-value: 1.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 37 LLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSL------DTQVRETQALILSPTRELAVQI 110
Cdd:cd17961 5 LLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlkakaeSGEEQGTRALILVPTRELAQQV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 111 QKVVLALGDYMN--VQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRA-IKLLVLDEADEMLNKGFKE 187
Cdd:cd17961 85 SKVLEQLTAYCRkdVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLLStLKYLVIDEADLVLSYGYEE 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 1845969787 188 QLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPI 225
Cdd:cd17961 165 DLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
37-227 |
4.20e-42 |
|
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: 146.36 E-value: 4.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 37 LLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRETQ-----ALILSPTRELAVQIQ 111
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERgdgpiVLVLAPTRELAQQIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 112 KVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKGFKEQLYD 191
Cdd:cd17966 81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1845969787 192 IYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRI 227
Cdd:cd17966 161 IVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
37-227 |
3.47e-40 |
|
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350718 [Multi-domain] Cd Length: 202 Bit Score: 141.56 E-value: 3.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 37 LLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSL---DTQVRETQ--ALILSPTRELAVQIQ 111
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrKANLKKGQvgALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 112 KVVLALGDYM--NVQCHACIGGTNLGEDIRKLD-YGQHVVSGTPGRVFDMIRRRN--LRTRAIKLLVLDEADEMLNKGFK 186
Cdd:cd17960 81 EVLQSFLEHHlpKLKCQLLIGGTNVEEDVKKFKrNGPNILVGTPGRLEELLSRKAdkVKVKSLEVLVLDEADRLLDLGFE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1845969787 187 EQLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRI 227
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
37-227 |
9.93e-40 |
|
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: 140.92 E-value: 9.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 37 LLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRET--------QALILSPTRELAV 108
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDeetkddgpYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 109 QIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKGFKEQ 188
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1845969787 189 LYDIYRYLPPGA--------------------QVVLLSATLPHEILEMTSKFMTDPIRI 227
Cdd:cd17945 161 VTKILDAMPVSNkkpdteeaeklaasgkhryrQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
38-229 |
4.29e-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: 138.58 E-value: 4.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 38 LRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLdtqVRE-------TQALILSPTRELAVQI 110
Cdd:cd17941 2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKL---YRErwtpedgLGALIISPTRELAMQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 111 QKVVLALGDYMNVQCHACIGGTNLGEDIRKLDyGQHVVSGTPGRVFD-MIRRRNLRTRAIKLLVLDEADEMLNKGFKEQL 189
Cdd:cd17941 79 FEVLRKVGKYHSFSAGLIIGGKDVKEEKERIN-RMNILVCTPGRLLQhMDETPGFDTSNLQMLVLDEADRILDMGFKETL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1845969787 190 YDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRILV 229
Cdd:cd17941 158 DAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
25-231 |
8.53e-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: 139.40 E-value: 8.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 25 IPTFDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQ------------- 91
Cdd:cd18051 20 IETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQgpgeslpsesgyy 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 92 VRETQ---ALILSPTRELAVQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRA 168
Cdd:cd18051 100 GRRKQyplALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDY 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1845969787 169 IKLLVLDEADEMLNKGFKEQLYDIYRY--LPPGA--QVVLLSATLPHEILEMTSKFMTDPIRILVKR 231
Cdd:cd18051 180 CKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPTGerQTLMFSATFPKEIQMLARDFLDNYIFLAVGR 246
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
27-224 |
2.94e-38 |
|
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: 136.77 E-value: 2.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 27 TFDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILK--ARDVIAQAQSGTGKTATFSISVLQSLDTQVRETQALILSPTR 104
Cdd:cd18047 2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAepPQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 105 ELAVQIQKVVLALGD-YMNVQCHACIGGTNLGEDIRKLDygqHVVSGTPGRVFD-MIRRRNLRTRAIKLLVLDEADEML- 181
Cdd:cd18047 82 ELALQTGKVIEQMGKfYPELKLAYAVRGNKLERGQKISE---QIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADVMIa 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1845969787 182 NKGFKEQLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDP 224
Cdd:cd18047 159 TQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
38-208 |
3.38e-38 |
|
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: 136.34 E-value: 3.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 38 LRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATF---SISVLQSLDTQVRE-TQALILSPTRELAVQIQKV 113
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFlipAIELLYKLKFKPRNgTGVIIISPTRELALQIYGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 114 VLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIR-RRNLRTRAIKLLVLDEADEMLNKGFKEQLYDI 192
Cdd:cd17942 82 AKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQnTKGFLYKNLQCLIIDEADRILEIGFEEEMRQI 161
|
170
....*....|....*.
gi 1845969787 193 YRYLPPGAQVVLLSAT 208
Cdd:cd17942 162 IKLLPKRRQTMLFSAT 177
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
37-227 |
3.29e-37 |
|
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: 134.00 E-value: 3.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 37 LLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSIS-VLQSLDTQVR-------ETQALILSPTRELAV 108
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPlIMFALEQEKKlpfikgeGPYGLIVCPSRELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 109 QIQKVV------LALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLN 182
Cdd:cd17951 81 QTHEVIeyyckaLQEGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1845969787 183 KGFKEQLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRI 227
Cdd:cd17951 161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
251-360 |
6.81e-37 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 129.64 E-value: 6.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 251 WKFDTLIDLYDTLTITQAVLFCNTRRKVDwlTDKMKEA-NFTVSSMHGDMEQKDRDEVMKEFRAGTTRVLISTDVWARGL 329
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLE--AELLLEKeGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
|
90 100 110
....*....|....*....|....*....|.
gi 1845969787 330 DVPQVSLVINYDLPNNRELYIHRIGRSGRFG 360
Cdd:pfam00271 79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
37-227 |
5.43e-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: 130.28 E-value: 5.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 37 LLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQV--RETQ----ALILSPTRELAVQI 110
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPipREQRngpgVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 111 QKVVLALgDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKGFKEQLY 190
Cdd:cd17958 81 EAECSKY-SYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 1845969787 191 DIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRI 227
Cdd:cd17958 160 KILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
45-227 |
1.23e-34 |
|
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1. DDX31 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350707 [Multi-domain] Cd Length: 214 Bit Score: 127.32 E-value: 1.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 45 GFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFS---ISVLQSLDTQVRETQ---ALILSPTRELAVQIQKVVLALG 118
Cdd:cd17949 10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLlpiIQRLLSLEPRVDRSDgtlALVLVPTRELALQIYEVLEKLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 119 DYM-NVQCHACIGGTNLGED---IRKldyGQHVVSGTPGRVFDMIRR-RNLRTRAIKLLVLDEADEMLNKGFKEQLYDIY 193
Cdd:cd17949 90 KPFhWIVPGYLIGGEKRKSEkarLRK---GVNILIATPGRLLDHLKNtQSFDVSNLRWLVLDEADRLLDMGFEKDITKIL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1845969787 194 RYL-------------PPGAQVVLLSATLPHEILEMTSKFMTDPIRI 227
Cdd:cd17949 167 ELLddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
37-209 |
4.59e-34 |
|
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: 126.58 E-value: 4.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 37 LLRGIYAYGFEKPSAIQQRAIPAILKAR-DVIAQAQSGTGKTATFSISVLQSLDTQVRET---------QALILSPTREL 106
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRDGkDVIGAAETGSGKTLAFGIPILERLLSQKSSNgvggkqkplRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 107 AVQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNL---RTRAIKLLVLDEADEMLNK 183
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEhlaNLKSLRFLVLDEADRMLEK 160
|
170 180 190
....*....|....*....|....*....|...
gi 1845969787 184 G-FKE--QLYDIYRYLPPGA----QVVLLSATL 209
Cdd:cd17946 161 GhFAEleKILELLNKDRAGKkrkrQTFVFSATL 193
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
46-227 |
2.05e-31 |
|
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: 120.50 E-value: 2.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 46 FEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRETQA-----LILSPTRELAVQIQKVVLALGDY 120
Cdd:cd18050 82 FKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGdgpicLVLAPTRELAQQVQQVADDYGKS 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 121 MNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKGFKEQLYDIYRYLPPGA 200
Cdd:cd18050 162 SRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDR 241
|
170 180
....*....|....*....|....*..
gi 1845969787 201 QVVLLSATLPHEILEMTSKFMTDPIRI 227
Cdd:cd18050 242 QTLMWSATWPKEVRQLAEDFLRDYVQI 268
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
15-227 |
2.70e-31 |
|
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: 118.96 E-value: 2.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 15 EFESSEEVSI--------IPTFDKMGLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQ 86
Cdd:cd18049 5 QYRRSKEITVrghncpkpVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 87 SLDTQVRETQA-----LILSPTRELAVQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRR 161
Cdd:cd18049 85 HINHQPFLERGdgpicLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1845969787 162 RNLRTRAIKLLVLDEADEMLNKGFKEQLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRI 227
Cdd:cd18049 165 GKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHI 230
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
279-360 |
1.21e-30 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 112.31 E-value: 1.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 279 DWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGTTRVLISTDVWARGLDVPQVSLVINYDLPNNRELYIHRIGRSGR 358
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 1845969787 359 FG 360
Cdd:smart00490 81 AG 82
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
52-221 |
3.58e-29 |
|
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: 112.25 E-value: 3.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 52 IQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLDTQV------RETQALILSPTRELAVQIQKVVLALGDYMNVQC 125
Cdd:cd17944 16 IQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQqprkrgRAPKVLVLAPTRELANQVTKDFKDITRKLSVAC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 126 HacIGGTNLGEDIRKLDYGQHVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKGFKEQLYDI----YRYLPP-GA 200
Cdd:cd17944 96 F--YGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEIlsvsYKKDSEdNP 173
|
170 180
....*....|....*....|.
gi 1845969787 201 QVVLLSATLPHEILEMTSKFM 221
Cdd:cd17944 174 QTLLFSATCPDWVYNVAKKYM 194
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
37-219 |
1.41e-28 |
|
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350706 [Multi-domain] Cd Length: 231 Bit Score: 111.69 E-value: 1.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 37 LLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSL-------DTQVRETQALILSPTRELAVQ 109
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLlrykllaEGPFNAPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 110 IQKVVLALGDYMNVQCHaCIGGTNLGEDIRKLDYGQ-HVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEADEMLNKGFKEQ 188
Cdd:cd17948 81 IGSVAQSLTEGLGLKVK-VITGGRTKRQIRNPHFEEvDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1845969787 189 LYDIYRYLP-------------PGAQVVLLSATLPHEILEMTSK 219
Cdd:cd17948 160 LSHFLRRFPlasrrsentdgldPGTQLVLVSATMPSGVGEVLSK 203
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
65-208 |
1.16e-21 |
|
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: 90.16 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 65 DVIAQAQSGTGKTATFSISVLQSLDTQvrETQALILSPTRELAVQIQKVVLALGDyMNVQCHACIGGTNLGEDIRKLDYG 144
Cdd:cd00046 3 NVLITAPTGSGKTLAALLAALLLLLKK--GKKVLVLVPTKALALQTAERLRELFG-PGIRVAVLVGGSSAEEREKNKLGD 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1845969787 145 QHVVSGTPGRVFDMIRR-RNLRTRAIKLLVLDEADEMLNKGFKEQLYD--IYRYLPPGAQVVLLSAT 208
Cdd:cd00046 80 ADIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLIDSRGALILDlaVRKAGLKNAQVILLSAT 146
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
37-209 |
2.11e-21 |
|
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: 91.92 E-value: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 37 LLRGIYAYGFEKPSAIQQRAIPAILKA---------RDVIAQAQSGTGKTATFSISVLQSL-DTQVRETQALILSPTREL 106
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALsKRVVPRLRALIVVPTKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 107 AVQIQKVVLALGDYMNVQCHACIGGTNLGEDIRKLDYGQH---------VVSgTPGRVFDMIRR------RNLRtraikL 171
Cdd:cd17956 81 VQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTSgrylsrvdiLVA-TPGRLVDHLNStpgftlKHLR-----F 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1845969787 172 LVLDEADEMLNKGFKEQLYDIYRYL--------------------PPGAQVVLLSATL 209
Cdd:cd17956 155 LVIDEADRLLNQSFQDWLETVMKALgrptapdlgsfgdanllersVRPLQKLLFSATL 212
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
267-366 |
1.25e-14 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 75.54 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 267 QAVLFCNTRRKVDWLTDKMKEANFTV------SSMHGD--MEQKDRDEVMKEFRAGTTRVLISTDVWARGLDVPQVSLVI 338
Cdd:COG1111 355 RIIVFTQYRDTAEMIVEFLSEPGIKAgrfvgqASKEGDkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVI 434
|
90 100 110
....*....|....*....|....*....|
gi 1845969787 339 NYDL-PNnrEL-YIHRIGRSGRFGRKGVAI 366
Cdd:COG1111 435 FYEPvPS--EIrSIQRKGRTGRKREGRVVV 462
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
32-384 |
2.08e-14 |
|
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: 74.87 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 32 GLREDLLRGIYAYGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLdTQVRETQALILSPTRELAV-QI 110
Cdd:COG1205 40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEAL-LEDPGATALYLYPTKALARdQL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 111 QKVV-LALGDYMNVQCHACIGGTNLGE--DIRklDYGQHVVSgTPgrvfDMI-----------RR--RNLRtraikLLVL 174
Cdd:COG1205 119 RRLReLAEALGLGVRVATYDGDTPPEErrWIR--EHPDIVLT-NP----DMLhygllphhtrwARffRNLR-----YVVI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 175 DEAdemlnkgfkeQLYD----------------IYRYLPPGAQVVLLSATL--PHEILE-MTSK---------------- 219
Cdd:COG1205 187 DEA----------HTYRgvfgshvanvlrrlrrICRHYGSDPQFILASATIgnPAEHAErLTGRpvtvvdedgsprgert 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 220 --FMTDPIRILVKRDELTLEGIKQFFVAVDREewkfdtlidlydtltiTQAVLFCNTRRKV----DWLTDKMKEANFT-- 291
Cdd:COG1205 257 fvLWNPPLVDDGIRRSALAEAARLLADLVREG----------------LRTLVFTRSRRGAellaRYARRALREPDLAdr 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 292 VSSMHGDMEQKDRDEVMKEFRAGTTRVLISTDVWARGLDVPQVSLVINYDLPNNRELYIHRIGRSGRFGRKGVAInFVKQ 371
Cdd:COG1205 321 VAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV-LVAG 399
|
410
....*....|...
gi 1845969787 372 DDVrilrdIEQYY 384
Cdd:COG1205 400 DDP-----LDQYY 407
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
253-355 |
3.01e-14 |
|
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: 69.54 E-value: 3.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 253 FDTLIDLYDTLTITQAVLFCNTRRKVDWLTDKMKE-----ANFTVSSMHG----------DMEQKDRDEVMKEFRAGTTR 317
Cdd:cd18802 13 IEILREYFPKTPDFRGIIFVERRATAVVLSRLLKEhpstlAFIRCGFLIGrgnssqrkrsLMTQRKQKETLDKFRDGELN 92
|
90 100 110
....*....|....*....|....*....|....*...
gi 1845969787 318 VLISTDVWARGLDVPQVSLVINYDLPNNRELYIHRIGR 355
Cdd:cd18802 93 LLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR 130
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
48-227 |
3.04e-13 |
|
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 (MRH4) plays an essential role during the late stages of mitochondrial ribosome or mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions. MRH4 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350723 [Multi-domain] Cd Length: 251 Bit Score: 68.94 E-value: 3.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 48 KPSAIQQRAIPAILKARD-----------------VIAqAQSGTGKTATFSISVLQSLDTQVRET--------------- 95
Cdd:cd17965 30 KPSPIQTLAIKKLLKTLMrkvtkqtsneepklevfLLA-AETGSGKTLAYLAPLLDYLKRQEQEPfeeaeeeyesakdtg 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 96 --QALILSPTRELAVQIQKVVLALGDYMNVQCH---ACIGGTNlgedIRKLDYGQH---VVSGTPGRVFDMIRRRNLRTR 167
Cdd:cd17965 109 rpRSVILVPTHELVEQVYSVLKKLSHTVKLGIKtfsSGFGPSY----QRLQLAFKGridILVTTPGKLASLAKSRPKILS 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 168 AIKLLVLDEADEMLNKGFKEQLYDIYRYLPPGAQVVLLSATLPHEILEMTSKFMTDPIRI 227
Cdd:cd17965 185 RVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLRKLFPDVVRI 244
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
53-355 |
3.19e-13 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 71.21 E-value: 3.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 53 QQRAIPAILKA-----RDVIAQAQSGTGKTaTFSISVLQSLDTQVRetqALILSPTRELAVQIQKVVLALgdymnvqcha 127
Cdd:COG1061 85 QQEALEALLAAlerggGRGLVVAPTGTGKT-VLALALAAELLRGKR---VLVLVPRRELLEQWAEELRRF---------- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 128 cIGGTNLGEDIRKLDYgqHVVSGTPGRVFDMIRRRNLRtRAIKLLVLDEADEMLNKGFKEqlydIYRYLPPgAQVVLLSA 207
Cdd:COG1061 151 -LGDPLAGGGKKDSDA--PITVATYQSLARRAHLDELG-DRFGLVIIDEAHHAGAPSYRR----ILEAFPA-AYRLGLTA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 208 T-------------LPHEILEMTSKFMTD-----PIRILVKRDELTLEG-----IKQFFVA--VDREEWKFDTLIDLYDT 262
Cdd:COG1061 222 TpfrsdgreillflFDGIVYEYSLKEAIEdgylaPPEYYGIRVDLTDERaeydaLSERLREalAADAERKDKILRELLRE 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 263 LTITQAVL-FCNTRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGTTRVLISTDVWARGLDVPQVSLVINYD 341
Cdd:COG1061 302 HPDDRKTLvFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLR 381
|
330
....*....|....
gi 1845969787 342 LPNNRELYIHRIGR 355
Cdd:COG1061 382 PTGSPREFIQRLGR 395
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
271-368 |
1.35e-12 |
|
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: 64.54 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 271 FCNTRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGTTRVLISTDVWARGLDVPQVSLVINYDLPNNRELYI 350
Cdd:cd18794 36 YCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYY 115
|
90
....*....|....*...
gi 1845969787 351 HRIGRSGRFGRKGVAINF 368
Cdd:cd18794 116 QESGRAGRDGLPSECILF 133
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
272-378 |
2.36e-12 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 68.24 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 272 CNTRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGTTRVLISTDVWARGLDVPQVSLVINYDLPNNRELYIH 351
Cdd:COG0514 237 CLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQ 316
|
90 100
....*....|....*....|....*..
gi 1845969787 352 RIGRSGRFGRKGVAINFVKQDDVRILR 378
Cdd:COG0514 317 EIGRAGRDGLPAEALLLYGPEDVAIQR 343
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
252-354 |
2.84e-11 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 60.57 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 252 KFDTLIDLYDTLTITQ--AVLFCNTRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRA--GTTRVLISTDVWAR 327
Cdd:cd18793 12 KLEALLELLEELREPGekVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEdpDIRVFLLSTKAGGV 91
|
90 100 110
....*....|....*....|....*....|....*.
gi 1845969787 328 GLDVPQVSLVINYDLPNN---------RelyIHRIG 354
Cdd:cd18793 92 GLNLTAANRVILYDPWWNpaveeqaidR---AHRIG 124
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
269-378 |
8.36e-11 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 63.58 E-value: 8.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 269 VLFCNTRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGTTRVLISTDVWARGLDVPQVSLVINYDLPNNREL 348
Cdd:PRK11057 240 IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIES 319
|
90 100 110
....*....|....*....|....*....|
gi 1845969787 349 YIHRIGRSGRFGRKGVAINFVKQDDVRILR 378
Cdd:PRK11057 320 YYQETGRAGRDGLPAEAMLFYDPADMAWLR 349
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
220-365 |
1.43e-10 |
|
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: 59.28 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 220 FMTDPIRILVKRDELTLEGIKQFFVAvdreewkfdTLIDLYDTLTITQAVLFCNtrrkvdWLTDKMKeANFTVSSMHGDM 299
Cdd:cd18811 8 FHTRLDKVYEFVREEIAKGRQAYVIY---------PLIEESEKLDLKAAVAMYE------YLKERFR-PELNVGLLHGRL 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1845969787 300 EQKDRDEVMKEFRAGTTRVLISTDVWARGLDVPQVSLVINYDlpnnrelyIHRIGRS------GRFGRKGVA 365
Cdd:cd18811 72 KSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIED--------AERFGLSqlhqlrGRVGRGDHQ 135
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
299-363 |
1.58e-10 |
|
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: 58.91 E-value: 1.58e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1845969787 299 MEQKDRDEVMKEFRAGTTRVLISTDVWARGLDVPQVSLVINYDlPNNREL-YIHRIGRSGRfGRKG 363
Cdd:cd18801 74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYD-ASPSPIrMIQRMGRTGR-KRQG 137
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
170-322 |
3.81e-10 |
|
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: 61.25 E-value: 3.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 170 KLLVLDEAD----EMLnKGFKEQLYDIYRYlppGAQVVLLSATLPHEILEmtskFMTDPIRILVKRDELTLEGIKQFF-- 243
Cdd:COG1203 270 SVIILDEVQayppYML-ALLLRLLEWLKNL---GGSVILMTATLPPLLRE----ELLEAYELIPDEPEELPEYFRAFVrk 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 244 -VAVDREEWKFDTLID-LYDTLTITQAVLF-CNTRRKVDWLTDKMKEANFTVSSM--HGDMEQKDR----DEVMKEFRAG 314
Cdd:COG1203 342 rVELKEGPLSDEELAElILEALHKGKSVLViVNTVKDAQELYEALKEKLPDEEVYllHSRFCPADRseieKEIKERLERG 421
|
....*...
gi 1845969787 315 TTRVLIST 322
Cdd:COG1203 422 KPCILVST 429
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
53-390 |
4.27e-10 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 61.45 E-value: 4.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 53 QQRAIPA-ILKARDVIAQAQSGTGKTATFSISVLQSLDTQVRetqALILSPTRELAVQI------------QKVVLALGD 119
Cdd:COG1204 27 QAEALEAgLLEGKNLVVSAPTASGKTLIAELAILKALLNGGK---ALYIVPLRALASEKyrefkrdfeelgIKVGVSTGD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 120 YMnvqchaciggtnlgEDIRKLDYGQHVVSgTPGRVFDMIRRRNLRTRAIKLLVLDEA----DEmlNKGFK-EQLYDIYR 194
Cdd:COG1204 104 YD--------------SDDEWLGRYDILVA-TPEKLDSLLRNGPSWLRDVDLVVVDEAhlidDE--SRGPTlEVLLARLR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 195 YLPPGAQVVLLSATL--PHEILE-MTSKFMTDPIRIlVKRDELTL-EGIKQFfvaVDREEWKFDTLIDL-YDTLTI-TQA 268
Cdd:COG1204 167 RLNPEAQIVALSATIgnAEEIAEwLDAELVKSDWRP-VPLNEGVLyDGVLRF---DDGSRRSKDPTLALaLDLLEEgGQV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 269 VLFCNTRRKV----DWLTDKMK-------------------------EANFTVSSM--------HGDMEQKDRDEVMKEF 311
Cdd:COG1204 243 LVFVSSRRDAeslaKKLADELKrrltpeereeleelaeellevseetHTNEKLADClekgvafhHAGLPSELRRLVEDAF 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 312 RAGTTRVLISTDVWARGLDVPQVSLVI-NYDLPNNREL----YIHRIGRSGRFGR--KGVAInFVKQDDVRILRDIEQYY 384
Cdd:COG1204 323 REGLIKVLVATPTLAAGVNLPARRVIIrDTKRGGMVPIpvleFKQMAGRAGRPGYdpYGEAI-LVAKSSDEADELFERYI 401
|
....*.
gi 1845969787 385 STQIDE 390
Cdd:COG1204 402 LGEPEP 407
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
252-378 |
6.68e-10 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 61.01 E-value: 6.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 252 KFDTLIDLYDTLTITQ--AVLFCNTRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAG--TTRVLISTDVWAR 327
Cdd:COG0553 534 KLEALLELLEELLAEGekVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGpeAPVFLISLKAGGE 613
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1845969787 328 GLDVPQVSLVINYDLPNNRELYIHRIGRSGRFG-RKGV-AINFVKQD--DVRILR 378
Cdd:COG0553 614 GLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGqTRDVqVYKLVAEGtiEEKILE 668
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
252-393 |
1.09e-09 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 60.27 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 252 KFDTLIDLY-DTLTI---TQAVLFCNTRRKVDWLTDKMKEANFTV------SSMHGD--MEQKDRDEVMKEFRAGTTRVL 319
Cdd:PRK13766 348 KLEKLREIVkEQLGKnpdSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDkgMSQKEQIEILDKFRAGEFNVL 427
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1845969787 320 ISTDVWARGLDVPQVSLVINYDlPNNREL-YIHRIGRSGRfGRKGVAINFVKQDDvrilRDIEQYYSTQIDEMPM 393
Cdd:PRK13766 428 VSTSVAEEGLDIPSVDLVIFYE-PVPSEIrSIQRKGRTGR-QEEGRVVVLIAKGT----RDEAYYWSSRRKEKKM 496
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
171-362 |
2.46e-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: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 171 LLVLDEAD--EMLNKGFKEQLYDIYRYLppGAQVVLLSATLPHEILEMTSKfmtdpIRILVKRDELTLEGIKQFFVAVDR 248
Cdd:cd09639 126 LLIFDEVHfyDEYTLALILAVLEVLKDN--DVPILLMSATLPKFLKEYAEK-----IGYVEENEPLDLKPNERAPFIKIE 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 249 EEWKFD-----TLIDLYDTLTitQAVLFCNTRRKVDWLTDKMKEANFTVSSM--HGDMEQKDR----DEVMKEFRAGTTR 317
Cdd:cd09639 199 SDKVGEissleRLLEFIKKGG--SVAIIVNTVDRAQEFYQQLKEKGPEEEIMliHSRFTEKDRakkeAELLLEFKKSEKF 276
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1845969787 318 VLISTDVWARGLDVpQVSLVINYDLPNNRelYIHRIGRSGRFGRK 362
Cdd:cd09639 277 VIVATQVIEASLDI-SVDVMITELAPIDS--LIQRLGRLHRYGEK 318
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
263-369 |
1.26e-07 |
|
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: 48.47 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 263 LTITQAVLFCNTRRKVDWLTDKMKeanftvssmhgdmeqkdrdevmkefragttrVLISTDVWARGLDVPQVSLVINYDL 342
Cdd:cd18785 1 VMVVKIIVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDP 49
|
90 100
....*....|....*....|....*...
gi 1845969787 343 PNNRELYIHRIGRSGRFG-RKGVAINFV 369
Cdd:cd18785 50 PSSAASYIQRVGRAGRGGkDEGEVILFV 77
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
284-366 |
2.75e-07 |
|
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: 49.96 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 284 KMKEANFTVSSMHGDMEQKDRDEVMKEFRAGTTRVLISTDVWARGLDVPQVSLVINYDlPNN---RELYIHRiGRSGRFG 360
Cdd:cd18792 55 KELVPEARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIED-ADRfglSQLHQLR-GRVGRGK 132
|
....*.
gi 1845969787 361 RKGVAI 366
Cdd:cd18792 133 HQSYCY 138
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
53-369 |
4.64e-07 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 51.81 E-value: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 53 QQRAIPAILKARDVIAQAQSGTGKTAtfsISVLQSLDTQVRETQALILSPTRELAVQIQKVVLALGDyMNVQCHACIGGT 132
Cdd:PRK01172 27 QRMAIEQLRKGENVIVSVPTAAGKTL---IAYSAIYETFLAGLKSIYIVPLRSLAMEKYEELSRLRS-LGMRVKISIGDY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 133 NLGED-IRKLDygqhVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEAdEMLNKGFK----EQLYDIYRYLPPGAQVVLLSA 207
Cdd:PRK01172 103 DDPPDfIKRYD----VVILTSEKADSLIHHDPYIINDVGLIVADEI-HIIGDEDRgptlETVLSSARYVNPDARILALSA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 208 TLPH--EILE------MTSKFMTDPIRI-LVKRDELTLEGikqffvavdREEWKFDTLIDLYDTLTIT-QAVLFCNTRRK 277
Cdd:PRK01172 178 TVSNanELAQwlnaslIKSNFRPVPLKLgILYRKRLILDG---------YERSQVDINSLIKETVNDGgQVLVFVSSRKN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 278 VDWLTDKMKE-----ANFTVSSM--------------------HGDMEQKDRDEVMKEFRAGTTRVLISTDVWARGLDVP 332
Cdd:PRK01172 249 AEDYAEMLIQhfpefNDFKVSSEnnnvyddslnemlphgvafhHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLP 328
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1845969787 333 qVSLVINYDLPNNRELYI---------HRIGRSGRFGRKGVAINFV 369
Cdd:PRK01172 329 -ARLVIVRDITRYGNGGIrylsnmeikQMIGRAGRPGYDQYGIGYI 373
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
274-358 |
6.87e-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: 48.78 E-value: 6.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 274 TRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGTTRVLISTDVWARGLDVPQVSLVINYD------LPNNRE 347
Cdd:cd18790 36 TKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDadkegfLRSETS 115
|
90
....*....|.
gi 1845969787 348 LyIHRIGRSGR 358
Cdd:cd18790 116 L-IQTIGRAAR 125
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
269-393 |
8.06e-07 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 51.44 E-value: 8.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 269 VLFCNTRRKVDWLTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGTTRVLISTDVWARGLDVPQVSLVINYDLPNNREL 348
Cdd:PLN03137 684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEG 763
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1845969787 349 YIHRIGRSGRFG-RKGVAINFVKQDDVRILRDIEQyysTQIDEMPM 393
Cdd:PLN03137 764 YHQECGRAGRDGqRSSCVLYYSYSDYIRVKHMISQ---GGVEQSPM 806
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
270-358 |
1.55e-06 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 47.64 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 270 LFCNTRRKVDWLTDKMKEA------NFTVSSMHGDMEQKDRDEVMKEFRAGTTRVLISTDVWARGLDVPQVSLVINYDLP 343
Cdd:cd18796 43 VFTNTRSQAERLAQRLRELcpdrvpPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSP 122
|
90
....*....|....*
gi 1845969787 344 NNRELYIHRIGRSGR 358
Cdd:cd18796 123 KSVARLLQRLGRSGH 137
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
295-338 |
4.32e-06 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 48.99 E-value: 4.32e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1845969787 295 MHGDMEQKDRDEVMKEFRAGTTRVLISTDVWARGLDVPQVSL-VI 338
Cdd:PRK10917 511 LHGRMKPAEKDAVMAAFKAGEIDILVATTVIEVGVDVPNATVmVI 555
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
52-210 |
8.81e-06 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 45.72 E-value: 8.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 52 IQQRAIPAILKARD-VIAQAQSGTGKTATFSISVLQSLDTQvrETQALILSPTRELAVQI------------QKVVLALG 118
Cdd:cd17921 5 IQREALRALYLSGDsVLVSAPTSSGKTLIAELAILRALATS--GGKAVYIAPTRALVNQKeadlrerfgplgKNVGLLTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 119 DYmnvqchaciggTNLGEDIRKLDygqhVVSGTPGRVFDMIRR-RNLRTRAIKLLVLDEAdEMLNKGFK----EQLYDIY 193
Cdd:cd17921 83 DP-----------SVNKLLLAEAD----ILVATPEKLDLLLRNgGERLIQDVRLVVVDEA-HLIGDGERgvvlELLLSRL 146
|
170
....*....|....*..
gi 1845969787 194 RYLPPGAQVVLLSATLP 210
Cdd:cd17921 147 LRINKNARFVGLSATLP 163
|
|
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
288-338 |
1.54e-05 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 46.97 E-value: 1.54e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1845969787 288 ANFTVSSMHGDMEQKDRDEVMKEFRAGTTRVLISTDVWARGLDVPQVSL-VI 338
Cdd:COG1200 502 PGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTVIEVGVDVPNATVmVI 553
|
|
| SF2_C_priA |
cd18804 |
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ... |
301-366 |
5.23e-05 |
|
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350191 [Multi-domain] Cd Length: 238 Bit Score: 44.16 E-value: 5.23e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1845969787 301 QKDRDEVMKEFRAGTTRVLISTDVWARGLDVPQVSLV--INYD----LPNNR------ELYIHRIGRSGRFGRKGVAI 366
Cdd:cd18804 130 KGALEKLLDQFERGEIDILIGTQMIAKGLDFPNVTLVgiLNADsglnSPDFRaserafQLLTQVSGRAGRGDKPGKVI 207
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
35-216 |
1.07e-04 |
|
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: 42.91 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 35 EDLLRGIYayGFEKPSAIQQRAIPAILKARDVIAQAQSGTGKTATFSISVLqsldtqVRETQALILSPTRELavqIQKVV 114
Cdd:cd17920 1 EQILKEVF--GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPAL------LLDGVTLVVSPLISL---MQDQV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 115 LALGDyMNVQChACIGGTNLGEDIR----KLDYGQ-HVVSGTP-----GRVFDMIRRRNLRTRaIKLLVLDEA------- 177
Cdd:cd17920 70 DRLQQ-LGIRA-AALNSTLSPEEKRevllRIKNGQyKLLYVTPerllsPDFLELLQRLPERKR-LALIVVDEAhcvsqwg 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1845969787 178 ----DEMLNKG-FKEQLYDIyrylppgaQVVLLSATLP----HEILEM 216
Cdd:cd17920 147 hdfrPDYLRLGrLRRALPGV--------PILALTATATpevrEDILKR 186
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
267-366 |
1.35e-04 |
|
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: 41.77 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 267 QAVLFCNTRRKVDWLTDKMKEANFtvssMHGDMEQKDRDEVMKEFRAGTTRVLISTDVWARGLDVPQVSLVIN----YDL 342
Cdd:cd18795 45 PVLVFCSSRKECEKTAKDLAGIAF----HHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKgtqrYDG 120
|
90 100 110
....*....|....*....|....*....|
gi 1845969787 343 PNNREL----YIHRIGRSGR--FGRKGVAI 366
Cdd:cd18795 121 KGYRELspleYLQMIGRAGRpgFDTRGEAI 150
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
53-209 |
1.41e-04 |
|
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: 42.19 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 53 QQRAIPAILKARDVIAQAQSGTGKTATFSISVLQSLdTQVRETQALILSPTRELAvQIQKVVL-ALGDYM--NVQCHACI 129
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEAL-LRDPGSRALYLYPTKALA-QDQLRSLrELLEQLglGIRVATYD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 130 GGTNLGEDIRKLDYGQHVVSGTPgrvfDMI----------RRRNLRTraIKLLVLDEAdEMLNKGFK-------EQLYDI 192
Cdd:cd17923 83 GDTPREERRAIIRNPPRILLTNP----DMLhyallphhdrWARFLRN--LRYVVLDEA-HTYRGVFGshvalllRRLRRL 155
|
170
....*....|....*..
gi 1845969787 193 YRYLPPGAQVVLLSATL 209
Cdd:cd17923 156 CRRYGADPQFILTSATI 172
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
296-365 |
2.47e-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: 41.18 E-value: 2.47e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1845969787 296 HGDMEQKDRDEVMKEFRAGTTRVLISTDVWARGLDVPQVSLVI--NYDLPNNRELYIHRiGRSGRFGRKGVA 365
Cdd:cd18810 58 HGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIieRADKFGLAQLYQLR-GRVGRSKERAYA 128
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
267-366 |
5.16e-04 |
|
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: 39.93 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 267 QAVLFCNTRRKVD----WLTDKMKEANF---TVSSMHGDMEQKDRDEVMKEFRAGTTRVLISTDVWARGLDVPQVSLVIN 339
Cdd:cd18797 37 KTIVFCRSRKLAElllrYLKARLVEEGPlasKVASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVL 116
|
90 100
....*....|....*....|....*..
gi 1845969787 340 YDLPNNRELYIHRIGRSGRFGRKGVAI 366
Cdd:cd18797 117 AGYPGSLASLWQQAGRAGRRGKDSLVI 143
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
48-124 |
6.81e-04 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 40.48 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 48 KPSAIQQRAIPAILK------ARDVIAQAQSGTGKTATFSISVLQSLDtqvRETQALILSPTRELAVQIQKVVLALGDYM 121
Cdd:cd17918 15 SLTKDQAQAIKDIEKdlhspePMDRLLSGDVGSGKTLVALGAALLAYK---NGKQVAILVPTEILAHQHYEEARKFLPFI 91
|
...
gi 1845969787 122 NVQ 124
Cdd:cd17918 92 NVE 94
|
|
| PRK05298 |
PRK05298 |
excinuclease ABC subunit UvrB; |
281-358 |
7.34e-04 |
|
excinuclease ABC subunit UvrB;
Pssm-ID: 235395 [Multi-domain] Cd Length: 652 Bit Score: 41.57 E-value: 7.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 281 LTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGTTRVLISTDVWARGLDVPQVSLVINYD------LPNNRELyIHRIG 354
Cdd:PRK05298 462 LTDYLKELGIKVRYLHSDIDTLERVEIIRDLRLGEFDVLVGINLLREGLDIPEVSLVAILDadkegfLRSERSL-IQTIG 540
|
....
gi 1845969787 355 RSGR 358
Cdd:PRK05298 541 RAAR 544
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
62-177 |
1.41e-03 |
|
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: 39.56 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969787 62 KARDVIAQAQSGTGKTAtfsISVL-------QSLDTQVRETQALILSPTRELAVQIQKvvlALGDYMNVQCHACIGGTNL 134
Cdd:cd18034 15 LKRNTIVVLPTGSGKTL---IAVMlikemgeLNRKEKNPKKRAVFLVPTVPLVAQQAE---AIRSHTDLKVGEYSGEMGV 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1845969787 135 G--------EDIRKLDygqhVVSGTPGRVFDMIRRRNLRTRAIKLLVLDEA 177
Cdd:cd18034 89 DkwtkerwkEELEKYD----VLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
290-357 |
5.70e-03 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 39.14 E-value: 5.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1845969787 290 FTVSSMHGDMEQKDRDEVMKEFRAGTTRVLISTDVWARGLDVPQVSLVINYDLPNNRELYIHRIGRSG 357
Cdd:PRK09751 302 FIARSHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
|
|
| UvrB |
COG0556 |
Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair]; |
281-337 |
8.22e-03 |
|
Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair];
Pssm-ID: 440322 [Multi-domain] Cd Length: 657 Bit Score: 38.45 E-value: 8.22e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1845969787 281 LTDKMKEANFTVSSMHGDMEQKDRDEVMKEFRAGTTRVLISTDVWARGLDVPQVSLV 337
Cdd:COG0556 459 LTDYLKELGIKVRYLHSDIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLV 515
|
|
| |
