|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
9-394 |
0e+00 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 562.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 9 SSYEISEDY-PLVESFEDLGLKEEILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTVNSNV 87
Cdd:PTZ00424 15 STGTIESNYdEIVDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 88 RETQVLLLSPTRELAEQSQKVCLALGDYCNIEVHCCIGGKKVSDDIKALESGVQIVSGTPGRVNHMITDRHLNTRNIKQL 167
Cdd:PTZ00424 95 NACQALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 168 ILDEADEMLNRGFKEQVYSVYRYLPPTIQVVLVSATLPHDVIEITNKFMNNPFKVLVKRDELTLEGIKQFFISVEKEQWK 247
Cdd:PTZ00424 175 ILDEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 248 FDTLCDLYESLIITQAVIFCNTKEKVDWLAKKMKDGNFEVCKMHGEMSQKERNDIMQRFRKGESRVLISTDLWGRGLDVQ 327
Cdd:PTZ00424 255 FDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQ 334
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71033289 328 QVSLVVNYDLPNSRESYIHRIGRSGRYGRKGVAINFVKDDDIRILRDIEQYYSTQIDEMPMNISELL 394
Cdd:PTZ00424 335 QVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEVADYL 401
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
22-388 |
6.65e-152 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 435.35 E-value: 6.65e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 22 SFEDLGLKEEILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTVNSNV-RETQVLLLSPTRE 100
Cdd:COG0513 3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRpRAPQALILAPTRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 101 LAEQSQKVCLALGDYCNIEVHCCIGGKKVSDDIKALESGVQIVSGTPGRVNHMITDRHLNTRNIKQLILDEADEMLNRGF 180
Cdd:COG0513 83 LALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 181 KEQVYSVYRYLPPTIQVVLVSATLPHDVIEITNKFMNNPFKVLVKRDELTLEGIKQFFISVEKEQwKFDTLCDLYESLII 260
Cdd:COG0513 163 IEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRD-KLELLRRLLRDEDP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 261 TQAVIFCNTKEKVDWLAKKMKDGNFEVCKMHGEMSQKERNDIMQRFRKGESRVLISTDLWGRGLDVQQVSLVVNYDLPNS 340
Cdd:COG0513 242 ERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPED 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 71033289 341 RESYIHRIGRSGRYGRKGVAINFVKDDDIRILRDIEQYYSTQIDEMPM 388
Cdd:COG0513 322 PEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEEL 369
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
23-223 |
2.41e-117 |
|
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: 339.44 E-value: 2.41e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 23 FEDLGLKEEILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTVNSNVRETQVLLLSPTRELA 102
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 103 EQSQKVCLALGDYCNIEVHCCIGGKKVSDDIKALESGVQIVSGTPGRVNHMITDRHLNTRNIKQLILDEADEMLNRGFKE 182
Cdd:cd18045 81 VQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 71033289 183 QVYSVYRYLPPTIQVVLVSATLPHDVIEITNKFMNNPFKVL 223
Cdd:cd18045 161 QIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRIL 201
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
25-223 |
7.69e-110 |
|
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: 320.43 E-value: 7.69e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 25 DLGLKEEILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTVNSNVRETQVLLLSPTRELAEQ 104
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 105 SQKVCLALGDYCNIEVHCCIGGKKVSDDIKALESGVQIVSGTPGRVNHMITDRHLNTRNIKQLILDEADEMLNRGFKEQV 184
Cdd:cd17939 81 IQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQI 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 71033289 185 YSVYRYLPPTIQVVLVSATLPHDVIEITNKFMNNPFKVL 223
Cdd:cd17939 161 YDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRIL 199
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
23-223 |
1.56e-105 |
|
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: 309.38 E-value: 1.56e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 23 FEDLGLKEEILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTVNSNVRETQVLLLSPTRELA 102
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 103 EQSQKVCLALGDYCNIEVHCCIGGKKVSDDIKALESGVQIVSGTPGRVNHMITDRHLNTRNIKQLILDEADEMLNRGFKE 182
Cdd:cd18046 81 QQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 71033289 183 QVYSVYRYLPPTIQVVLVSATLPHDVIEITNKFMNNPFKVL 223
Cdd:cd18046 161 QIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRIL 201
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
22-394 |
9.98e-89 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 280.58 E-value: 9.98e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 22 SFEDLGLKEEILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTVNSNVRETQVLLLSPTREL 101
Cdd:PRK11634 7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 102 AEQsqkVCLALGDYC----NIEVHCCIGGKKVSDDIKALESGVQIVSGTPGRVNHMITDRHLNTRNIKQLILDEADEMLN 177
Cdd:PRK11634 87 AVQ---VAEAMTDFSkhmrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 178 RGFKEQVYSVYRYLPPTIQVVLVSATLPHDVIEITNKFMNNPFKVLVKRDELTLEGIKQFFISVEKEQwKFDTLCDLYES 257
Cdd:PRK11634 164 MGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMR-KNEALVRFLEA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 258 LIITQAVIFCNTKEKVDWLAKKMKDGNFEVCKMHGEMSQKERNDIMQRFRKGESRVLISTDLWGRGLDVQQVSLVVNYDL 337
Cdd:PRK11634 243 EDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDI 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 71033289 338 PNSRESYIHRIGRSGRYGRKGVAINFVKDDDIRILRDIEQYYSTQIDEMPMNISELL 394
Cdd:PRK11634 323 PMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAELL 379
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
22-384 |
1.98e-88 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 274.76 E-value: 1.98e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 22 SFEDLGLKEEILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTVNSNVRETQVLLLSPTREL 101
Cdd:PRK11776 5 AFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTREL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 102 AEQSQKVC--LALGDYcNIEVHCCIGGKKVSDDIKALESGVQIVSGTPGRVNHMITDRHLNTRNIKQLILDEADEMLNRG 179
Cdd:PRK11776 85 ADQVAKEIrrLARFIP-NIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 180 FKEQVYSVYRYLPPTIQVVLVSATLPHDVIEITNKFMNNPfkVLVKRDELTLEG-IKQFFISVEKEQwKFDTLCDLY--- 255
Cdd:PRK11776 164 FQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDP--VEVKVESTHDLPaIEQRFYEVSPDE-RLPALQRLLlhh 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 256 --ESliitqAVIFCNTKEKVDWLAKKMKDGNFEVCKMHGEMSQKERNDIMQRFRKGESRVLISTDLWGRGLDVQQVSLVV 333
Cdd:PRK11776 241 qpES-----CVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVI 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 71033289 334 NYDLPNSRESYIHRIGRSGRYGRKGVAINFVKDDDIRILRDIEQYYSTQID 384
Cdd:PRK11776 316 NYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLN 366
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
23-378 |
5.39e-82 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 257.56 E-value: 5.39e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 23 FEDLGLKEEILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTVNSNVRE----TQVLLLSPT 98
Cdd:PRK11192 3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRksgpPRILILTPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 99 RELAEQSQKVCLALGDYCNIEVHCCIGGKKVSDDIKALESGVQIVSGTPGRVNHMITDRHLNTRNIKQLILDEADEMLNR 178
Cdd:PRK11192 83 RELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLDM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 179 GFKEQVysvyrylpPTI--------QVVLVSATLPHD-VIEITNKFMNNPFKVLVK--RDELtlEGIKQFFISVEKEQWK 247
Cdd:PRK11192 163 GFAQDI--------ETIaaetrwrkQTLLFSATLEGDaVQDFAERLLNDPVEVEAEpsRRER--KKIHQWYYRADDLEHK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 248 FDTLCDLYESLIITQAVIFCNTKEKVDWLAKKMKDGNFEVCKMHGEMSQKERNDIMQRFRKGESRVLISTDLWGRGLDVQ 327
Cdd:PRK11192 233 TALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDID 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 71033289 328 QVSLVVNYDLPNSRESYIHRIGRSGRYGRKGVAINFVKDDDIRILRDIEQY 378
Cdd:PRK11192 313 DVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERY 363
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
32-222 |
1.46e-79 |
|
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: 243.12 E-value: 1.46e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 32 ILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTVNSN----VRETQVLLLSPTRELAEQSQK 107
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEpkkkGRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 108 VCLALGDYCNIEVHCCIGGKKVSDDIKALESGVQIVSGTPGRVNHMITDRHLNTRNIKQLILDEADEMLNRGFKEQVYSV 187
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 71033289 188 YRYLPPTIQVVLVSATLPHDVIEITNKFMNNPFKV 222
Cdd:cd00268 161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
22-386 |
2.58e-75 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 240.87 E-value: 2.58e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 22 SFEDLGLKEEILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTVNSNV------RETQVLLL 95
Cdd:PRK10590 2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQphakgrRPVRALIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 96 SPTRELAEQSQKVCLALGDYCNIEVHCCIGGKKVSDDIKALESGVQIVSGTPGRVNHMITDRHLNTRNIKQLILDEADEM 175
Cdd:PRK10590 82 TPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 176 LNRGFKEQVYSVYRYLPPTIQVVLVSATLPHDVIEITNKFMNNPFKVLVKRDELTLEGIKQFFISVEKEQwKFDTLCDLY 255
Cdd:PRK10590 162 LDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKR-KRELLSQMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 256 ESLIITQAVIFCNTKEKVDWLAKKM-KDGnFEVCKMHGEMSQKERNDIMQRFRKGESRVLISTDLWGRGLDVQQVSLVVN 334
Cdd:PRK10590 241 GKGNWQQVLVFTRTKHGANHLAEQLnKDG-IRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVN 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 71033289 335 YDLPNSRESYIHRIGRSGRYGRKGVAINFVKDDDIRILRDIEQYYSTQIDEM 386
Cdd:PRK10590 320 YELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRI 371
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
23-383 |
1.28e-69 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 225.24 E-value: 1.28e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 23 FEDLGLKEEILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFcLGA-----LQTVNSNVRET---QVLL 94
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAF-LTAtfhylLSHPAPEDRKVnqpRALI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 95 LSPTRELAEQSQKVCLALGDYCNIEVHCCIGGKKVSDDIKALESGVQIVSGTPGRVNHMITDRHLNTRNIKQLILDEADE 174
Cdd:PRK04837 89 MAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 175 MLNRGFKEQVYSVYRYLPPTIQ--VVLVSATLPHDVIEITNKFMNNPFKVLVKRDELTLEGIKQ--FFISVEKeqwKFDT 250
Cdd:PRK04837 169 MFDLGFIKDIRWLFRRMPPANQrlNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEelFYPSNEE---KMRL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 251 LCDLYESLIITQAVIFCNTK---EKV-DWLAKkmkDGNfEVCKMHGEMSQKERNDIMQRFRKGESRVLISTDLWGRGLDV 326
Cdd:PRK04837 246 LQTLIEEEWPDRAIIFANTKhrcEEIwGHLAA---DGH-RVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHI 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 71033289 327 QQVSLVVNYDLPNSRESYIHRIGRSGRYGRKGVAINFVKDDDIRILRDIEQYYSTQI 383
Cdd:PRK04837 322 PAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIGHSI 378
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
23-387 |
2.30e-68 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 223.25 E-value: 2.30e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 23 FEDLGLKEEILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGA----LQTVNSNVR---ETQVLLL 95
Cdd:PRK01297 89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIinqlLQTPPPKERymgEPRALII 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 96 SPTRELAEQSQKVCLALGDYCNIEVHCCIGGKKVSDDIKALESG-VQIVSGTPGRVNHMITDRHLNTRNIKQLILDEADE 174
Cdd:PRK01297 169 APTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEADR 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 175 MLNRGFKEQVYSVYRYLPPTI--QVVLVSATLPHDVIEITNKFMNNPFKVLVKRDELTLEGIKQFFISVEKEQwKFDTLC 252
Cdd:PRK01297 249 MLDMGFIPQVRQIIRQTPRKEerQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSD-KYKLLY 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 253 DLYESLIITQAVIFCNTKEKVDWLAKKMKDGNFEVCKMHGEMSQKERNDIMQRFRKGESRVLISTDLWGRGLDVQQVSLV 332
Cdd:PRK01297 328 NLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHV 407
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 71033289 333 VNYDLPNSRESYIHRIGRSGRYGRKGVAINFVKDDDIRILRDIEQYYSTQID-EMP 387
Cdd:PRK01297 408 INFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKIScEMP 463
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
20-375 |
4.13e-68 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 224.65 E-value: 4.13e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 20 VESFEDLGLKEEILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTVNSNVRETQ-----VLL 94
Cdd:PTZ00110 129 VVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYgdgpiVLV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 95 LSPTRELAEQSQKVCLALGDYCNIEVHCCIGGKKVSDDIKALESGVQIVSGTPGRVNHMITDRHLNTRNIKQLILDEADE 174
Cdd:PTZ00110 209 LAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADR 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 175 MLNRGFKEQVYSVYRYLPPTIQVVLVSATLPHDVIEITNKFMNN-PFKVLVKRDELTL-EGIKQFFISVEkEQWKFDTLC 252
Cdd:PTZ00110 289 MLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDLTAcHNIKQEVFVVE-EHEKRGKLK 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 253 DLYESLII--TQAVIFCNTKEKVDWLAKKMK-DGNFEVCkMHGEMSQKERNDIMQRFRKGESRVLISTDLWGRGLDVQQV 329
Cdd:PTZ00110 368 MLLQRIMRdgDKILIFVETKKGADFLTKELRlDGWPALC-IHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDV 446
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 71033289 330 SLVVNYDLPNSRESYIHRIGRSGRYGRKGVAINFVKDDDIRILRDI 375
Cdd:PTZ00110 447 KYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDL 492
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
23-222 |
5.88e-63 |
|
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: 200.60 E-value: 5.88e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 23 FEDLGLKEEILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTVNSNVRETQVLLLSPTRELA 102
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 103 EQSQKVCLALGDYCNIEVHCCIGGKKVSDDIKALESGVQIVSGTPGRVNHMITDRHLNTRNIKQLILDEADEMLNRGFKE 182
Cdd:cd17940 81 LQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 71033289 183 QVYSVYRYLPPTIQVVLVSATLPHDVIEITNKFMNNPFKV 222
Cdd:cd17940 161 IIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
234-364 |
3.80e-62 |
|
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350174 [Multi-domain] Cd Length: 131 Bit Score: 195.80 E-value: 3.80e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 234 IKQFFISVEKEQWKFDTLCDLYESLIITQAVIFCNTKEKVDWLAKKMKDGNFEVCKMHGEMSQKERNDIMQRFRKGESRV 313
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 71033289 314 LISTDLWGRGLDVQQVSLVVNYDLPNSRESYIHRIGRSGRYGRKGVAINFV 364
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
28-222 |
4.00e-62 |
|
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: 198.18 E-value: 4.00e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 28 LKEEILKGIFAYGFDKPSAVQQRAIKPILEG--RDVIIQSQSGTGKTCVFCLGALQTVNSNVRETQVLLLSPTRELAEQS 105
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 106 QKVCLALGDYCNIEVHCCIGGKKVSDDIKALEsgvQIVSGTPGRVNHMITDRHLNTRNIKQLILDEADEMLN-RGFKEQV 184
Cdd:cd17963 81 GEVVEKMGKFTGVKVALAVPGNDVPRGKKITA---QIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDtQGHGDQS 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 71033289 185 YSVYRYLPPTIQVVLVSATLPHDVIEITNKFMNNPFKV 222
Cdd:cd17963 158 IRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
16-394 |
8.83e-62 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 208.65 E-value: 8.83e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 16 DYPLVE-SFEDLGLKEEILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQT-------VNSNV 87
Cdd:PRK04537 3 DKPLTDlTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRllsrpalADRKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 88 RETQVLLLSPTRELAEQSQKVCLALGDYCNIEVHCCIGGKKVSDDIKALESGVQIVSGTPGR-VNHMITDRHLNTRNIKQ 166
Cdd:PRK04537 83 EDPRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRlIDYVKQHKVVSLHACEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 167 LILDEADEMLNRGFKEQVYSVYRYLPP--TIQVVLVSATLPHDVIEITNKFMNNPFKVLVKRDELTLEGIKQFfISVEKE 244
Cdd:PRK04537 163 CVLDEADRMFDLGFIKDIRFLLRRMPErgTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQR-IYFPAD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 245 QWKFDTLCDLYESLIITQAVIFCNTKEKVDWLAKKMKDGNFEVCKMHGEMSQKERNDIMQRFRKGESRVLISTDLWGRGL 324
Cdd:PRK04537 242 EEKQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGL 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 325 DVQQVSLVVNYDLPNSRESYIHRIGRSGRYGRKGVAINFVKDDDIRILRDIEQYYSTQIDEMPMNiSELL 394
Cdd:PRK04537 322 HIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKIPVEPVT-AELL 390
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
18-377 |
7.79e-60 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 201.94 E-value: 7.79e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 18 PLVESFEDLGLKEEILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVF-------CLGALQTVNSNVRET 90
Cdd:PLN00206 118 PPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFlvpiisrCCTIRSGHPSEQRNP 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 91 QVLLLSPTRELAEQSQKVCLALGDYCNIEVHCCIGGKKVSDDIKALESGVQIVSGTPGRVNHMITDRHLNTRNIKQLILD 170
Cdd:PLN00206 198 LAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLD 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 171 EADEMLNRGFKEQVYSVYRYLPpTIQVVLVSATLPHDVIEITNKFMNNPFKVLVKRDELTLEGIKQFFISVEKEQWK--- 247
Cdd:PLN00206 278 EVDCMLERGFRDQVMQIFQALS-QPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKqkl 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 248 FDTLcdLYESLIITQAVIFCNTKEKVDWLAKKM-KDGNFEVCKMHGEMSQKERNDIMQRFRKGESRVLISTDLWGRGLDV 326
Cdd:PLN00206 357 FDIL--KSKQHFKPPAVVFVSSRLGADLLANAItVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDL 434
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 71033289 327 QQVSLVVNYDLPNSRESYIHRIGRSGRYGRKGVAINFVKDDDIRILRDIEQ 377
Cdd:PLN00206 435 LRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVA 485
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
32-222 |
2.59e-59 |
|
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, Component Of Gems 3, Gemin-3, and SMN-Interacting Protein) interacts directly with SMN (survival of motor neurons), the spinal muscular atrophy gene product, and may play a catalytic role in the function of the SMN complex on ribonucleoproteins. Diseases associated with DDX20 include spinal muscular atrophy and muscular atrophy. DDX20 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350701 [Multi-domain] Cd Length: 192 Bit Score: 190.94 E-value: 2.59e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 32 ILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTVNSNVRETQVLLLSPTRELAEQSQKVCLA 111
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 112 LGDYC-NIEVHCCIGGKKVSDDIKALeSGVQIVSGTPGRVNHMITDRHLNTRNIKQLILDEADEMLNRGFKEQVYSVYRY 190
Cdd:cd17943 81 IGKKLeGLKCEVFIGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSS 159
|
170 180 190
....*....|....*....|....*....|..
gi 71033289 191 LPPTIQVVLVSATLPHDVIEITNKFMNNPFKV 222
Cdd:cd17943 160 LPKNKQVIAFSATYPKNLDNLLARYMRKPVLV 191
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
45-211 |
2.04e-55 |
|
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: 179.75 E-value: 2.04e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 45 SAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTVNSNVRETQVLLLSPTRELAEQSQKVCLALGDYCNIEVHCCI 124
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 125 GGKKVSDDIKALEsGVQIVSGTPGRVNHMITDRHLnTRNIKQLILDEADEMLNRGFKEQVYSVYRYLPPTIQVVLVSATL 204
Cdd:pfam00270 81 GGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATL 158
|
....*..
gi 71033289 205 PHDVIEI 211
Cdd:pfam00270 159 PRNLEDL 165
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
22-224 |
1.22e-50 |
|
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: 169.06 E-value: 1.22e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 22 SFEDLGLKEEILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTVNSNVRETQVLLLSPTREL 101
Cdd:cd17950 3 GFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTREL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 102 AEQSQKVCLALGDYC-NIEVHCCIGGKKVSDDIKALESGV-QIVSGTPGRVNHMITDRHLNTRNIKQLILDEADEMLNR- 178
Cdd:cd17950 83 AFQISNEYERFSKYMpNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLEQl 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 71033289 179 GFKEQVYSVYRYLPPTIQVVLVSATLPHDVIEITNKFMNNPFKVLV 224
Cdd:cd17950 163 DMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
36-237 |
3.36e-50 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 167.67 E-value: 3.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 36 IFAYGFDKPSAVQQRAIKPILEG-RDVIIQSQSGTGKTCVFCLGALQTVNSNvRETQVLLLSPTRELAEQSQKVCLALGD 114
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRG-KGGRVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 115 YCNIEVHCCIGGKKVSDDIKALESGV-QIVSGTPGRVNHMITDRHLNTRNIKQLILDEADEMLNRGFKEQVYSVYRYLPP 193
Cdd:smart00487 80 SLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 71033289 194 TIQVVLVSATLPHDVIEITNKFMNNPFKVLVKRdeLTLEGIKQF 237
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
28-223 |
2.07e-46 |
|
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: 158.13 E-value: 2.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 28 LKEEILKGIFAYGFDKPSAVQQRAIKPILE-GRDVIIQSQSGTGKTCVFCLGALQTV-----NSNVRETQVLLLSPTREL 101
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLlntkpAGRRSGVSALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 102 AEQSQKVCLALGDYC-NIEVHCCIGGKKVSDDIKALES-GVQIVSGTPGRVNHMITDRHL--NTRNIKQLILDEADEMLN 177
Cdd:cd17964 81 ALQIAAEAKKLLQGLrKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLENPGVakAFTDLDYLVLDEADRLLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 71033289 178 RGFKEQVYSVYRYLPP----TIQVVLVSATLPHDVIEITNKFMNNPFKVL 223
Cdd:cd17964 161 MGFRPDLEQILRHLPEknadPRQTLLFSATVPDEVQQIARLTLKKDYKFI 210
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
22-225 |
1.51e-45 |
|
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: 155.54 E-value: 1.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 22 SFEDLGLKEEILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTVNSnvRETQV----LLLSP 97
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKA--HSPTVgaraLILSP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 98 TRELAEQSQKVCLALGDYCNIEVHCCIGGKKVSDDIKALESGVQIVSGTPGRVNHMITDRHLNTRNIKQLILDEADEMLN 177
Cdd:cd17959 80 TRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 71033289 178 RGFKEQVYSVYRYLPPTIQVVLVSATLPHDVIEITNKFMNNPfkVLVK 225
Cdd:cd17959 160 MGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEP--VLIR 205
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
18-230 |
5.67e-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: 152.48 E-value: 5.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 18 PL--VESFEDLGLKEEILKGIFAYGFDKPSAVQQRAIKPILEG--RDVIIQSQSGTGKTCVFCLGALQTVNSNVRETQVL 93
Cdd:cd18048 13 PLfsVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 94 LLSPTRELAEQSQKVCLALGDYCN-IEVHCCIGGKKVSddiKALESGVQIVSGTPGRV-NHMITDRHLNTRNIKQLILDE 171
Cdd:cd18048 93 CLSPTFELALQTGKVVEEMGKFCVgIQVIYAIRGNRPG---KGTDIEAQIVIGTPGTVlDWCFKLRLIDVTNISVFVLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 172 ADEMLN-RGFKEQVYSVYRYLPPTIQVVLVSATLPHDVIEITNKFMNNPFKVLVKRDELT 230
Cdd:cd18048 170 ADVMINvQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
28-220 |
2.64e-43 |
|
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: 149.66 E-value: 2.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 28 LKEEILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTV------NSNVRETQVLLLSPTREL 101
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlkakaeSGEEQGTRALILVPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 102 AEQSQKVCLALGDYCNIEVHCC-IGGKKVSDDIKALESGV-QIVSGTPGR-VNHMITDRHLNTRNIKQLILDEADEMLNR 178
Cdd:cd17961 81 AQQVSKVLEQLTAYCRKDVRVVnLSASSSDSVQRALLAEKpDIVVSTPARlLSHLESGSLLLLSTLKYLVIDEADLVLSY 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 71033289 179 GFKEQVYSVYRYLPPTIQVVLVSATLPHDVIEITNKFMNNPF 220
Cdd:cd17961 161 GYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
32-222 |
5.89e-43 |
|
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: 148.56 E-value: 5.89e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 32 ILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTV---NSNVRETQVLLLSPTRELAEQSQKV 108
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLlyrPKKKAATRVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 109 CLALGDYCNIEVHCCIGGKKVSDDIKALESGVQIVSGTPGR-VNHMITDRHLNTRNIKQLILDEADEMLNRGFKEQVYSV 187
Cdd:cd17947 81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRlIDHLRNSPSFDLDSIEILVLDEADRMLEEGFADELKEI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 71033289 188 YRYLPPTIQVVLVSATLPHDVIEITNKFMNNPFKV 222
Cdd:cd17947 161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
23-220 |
5.32e-41 |
|
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: 143.90 E-value: 5.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 23 FEDLGLKEEILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTVNSNVRETQVLLLSPTRELA 102
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 103 EQSQKVCLALGDYCNIEVHCCIGGKKVSDDIKALESGVQIVSGTPGRVNHMIT---DRHLNTRNIKQLILDEADEMLNRG 179
Cdd:cd17955 81 YQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEADRLLTGS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 71033289 180 FKEQVYSVYRYLPPTIQVVLVSATLPHDVIEITNKFMNNPF 220
Cdd:cd17955 161 FEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPF 201
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
32-222 |
6.87e-40 |
|
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350724 [Multi-domain] Cd Length: 197 Bit Score: 140.58 E-value: 6.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 32 ILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTVNSNVRETQ-----VLLLSPTRELAEQSQ 106
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERgdgpiVLVLAPTRELAQQIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 107 KVCLALGDYCNIEVHCCIGGKKVSDDIKALESGVQIVSGTPGRVNHMITDRHLNTRNIKQLILDEADEMLNRGFKEQVYS 186
Cdd:cd17966 81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 71033289 187 VYRYLPPTIQVVLVSATLPHDVIEITNKFMNNPFKV 222
Cdd:cd17966 161 IVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
32-222 |
1.30e-39 |
|
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: 139.91 E-value: 1.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 32 ILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTVNSNV--RETQ----VLLLSPTRELAEQS 105
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPipREQRngpgVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 106 QKVCLALgDYCNIEVHCCIGGKKVSDDIKALESGVQIVSGTPGRVNHMITDRHLNTRNIKQLILDEADEMLNRGFKEQVY 185
Cdd:cd17958 81 EAECSKY-SYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 71033289 186 SVYRYLPPTIQVVLVSATLPHDVIEITNKFMNNPFKV 222
Cdd:cd17958 160 KILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
22-222 |
5.35e-39 |
|
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: 138.60 E-value: 5.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 22 SFEDLGLKEEILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTVNSNVRETQVLLLSPTREL 101
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 102 AEQSQKVCLALGDYCNIEVHCCIGGKKVSDDIKALESGVQIVSGTPGR-VNHMITDRHLNTRNIKQLILDEADEMLNRGF 180
Cdd:cd17954 81 AQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRlVDHLENTKGFSLKSLKFLVMDEADRLLNMDF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 71033289 181 KEQVYSVYRYLPPTIQVVLVSATLPHDVIEITNKFMNNPFKV 222
Cdd:cd17954 161 EPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
23-219 |
1.34e-38 |
|
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350696 [Multi-domain] Cd Length: 204 Bit Score: 137.45 E-value: 1.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 23 FEDLGLKEEILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTVnsnvretQVLLLSPTRELA 102
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV-------VALILEPSRELA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 103 EQSQKVCLALGDYCN---IEVHCCIGGKKVSDDIKALESGVQIVSGTPGRVNHMITDRHLNTRNIKQLILDEADEMLNRG 179
Cdd:cd17938 74 EQTYNCIENFKKYLDnpkLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 71033289 180 FKEQVYSVYRYLPP------TIQVVLVSATLpH--DVIEITNKFMNNP 219
Cdd:cd17938 154 NLETINRIYNRIPKitsdgkRLQVIVCSATL-HsfEVKKLADKIMHFP 200
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
246-355 |
5.42e-38 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 132.72 E-value: 5.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 246 WKFDTLCDLYESLIITQAVIFCNTKEKVDwLAKKMKDGNFEVCKMHGEMSQKERNDIMQRFRKGESRVLISTDLWGRGLD 325
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 71033289 326 VQQVSLVVNYDLPNSRESYIHRIGRSGRYG 355
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
20-222 |
1.35e-37 |
|
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: 135.20 E-value: 1.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 20 VESFEDLGLKEEILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTVNSN--VRETQ---VLL 94
Cdd:cd17953 11 IQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQrpVKPGEgpiGLI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 95 LSPTRELAEQSQKVCLALGDYCNIEVHCCIGGKKVSDDIKALESGVQIVSGTPGRVNHMIT---DRHLNTRNIKQLILDE 171
Cdd:cd17953 91 MAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTannGRVTNLRRVTYVVLDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 71033289 172 ADEMLNRGFKEQVYSVYRYLPPTIQVVLVSATLPHDVIEITNKFMNNPFKV 222
Cdd:cd17953 171 ADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
22-218 |
1.53e-36 |
|
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: 132.61 E-value: 1.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 22 SFEDLGLKEEILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCL----------GALQTVNSNVRETQ 91
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLpiisklledgPPSVGRGRRKAYPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 92 VLLLSPTRELAEQ----SQKVCLALGdycnIEVHCCIGGKKVSDDIKALESGVQIVSGTPGRVNHMITDRHLNTRNIKQL 167
Cdd:cd17967 81 ALILAPTRELAIQiyeeARKFSYRSG----VRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 71033289 168 ILDEADEMLNRGFKEQVYSVYRY--LPPTI--QVVLVSATLPHDVIEITNKFMNN 218
Cdd:cd17967 157 VLDEADRMLDMGFEPQIRKIVEHpdMPPKGerQTLMFSATFPREIQRLAADFLKN 211
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
32-224 |
4.25e-36 |
|
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: 130.79 E-value: 4.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 32 ILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTVNSNVRET--QVLLLSPTRELAEQSQKVC 109
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKKglRALILAPTRELASQIYREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 110 LALGDycNIEVHCCI---GGKKVSDDIKALESGVQIVSGTPGRVNHMITDRHLNTRNIKQLILDEADEMLNRGFKEQVYS 186
Cdd:cd17957 81 LKLSK--GTGLRIVLlskSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDE 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 71033289 187 VYRYLP-PTIQVVLVSATLPHDVIEITNKFMNNPFKVLV 224
Cdd:cd17957 159 ILAACTnPNLQRSLFSATIPSEVEELARSVMKDPIRIIV 197
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
32-222 |
4.55e-36 |
|
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: 130.77 E-value: 4.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 32 ILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTVNS---NVRETQV--LLLSPTRELAEQSQ 106
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKrkaNLKKGQVgaLIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 107 KVCLALGDYCNIEVHC--CIGGKKVS-DDIKALESGVQIVSGTPGRVNHMITDRH--LNTRNIKQLILDEADEMLNRGFK 181
Cdd:cd17960 81 EVLQSFLEHHLPKLKCqlLIGGTNVEeDVKKFKRNGPNILVGTPGRLEELLSRKAdkVKVKSLEVLVLDEADRLLDLGFE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 71033289 182 EQVYSVYRYLPPTIQVVLVSATLPHDVIEITNKFMNNPFKV 222
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
32-219 |
7.75e-36 |
|
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: 130.10 E-value: 7.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 32 ILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTVNSNvRETQ-----VLLLSPTRELAEQSQ 106
Cdd:cd17941 1 TLKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRE-RWTPedglgALIISPTRELAMQIF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 107 KVCLALGDYCNIEVHCCIGGKKVSDDIKALeSGVQIVSGTPGRV-NHMITDRHLNTRNIKQLILDEADEMLNRGFKEQVY 185
Cdd:cd17941 80 EVLRKVGKYHSFSAGLIIGGKDVKEEKERI-NRMNILVCTPGRLlQHMDETPGFDTSNLQMLVLDEADRILDMGFKETLD 158
|
170 180 190
....*....|....*....|....*....|....
gi 71033289 186 SVYRYLPPTIQVVLVSATLPHDVIEITNKFMNNP 219
Cdd:cd17941 159 AIVENLPKSRQTLLFSATQTKSVKDLARLSLKNP 192
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
18-217 |
9.76e-36 |
|
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: 131.63 E-value: 9.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 18 PLVESFEDLGLKEEILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTV---------NSNVR 88
Cdd:cd18052 40 PAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMmkegltassFSEVQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 89 ETQVLLLSPTRELAEQSQKVCLALGDYCNIEVHCCIGGKKVSDDIKALESGVQIVSGTPGRVNHMITDRHLNTRNIKQLI 168
Cdd:cd18052 120 EPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLI 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 71033289 169 LDEADEMLNRGFKEQVYSVYRYL--PPTI--QVVLVSATLPHDVIEITNKFMN 217
Cdd:cd18052 200 LDEADRMLDMGFGPEIRKLVSEPgmPSKEdrQTLMFSATFPEEIQRLAAEFLK 252
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
32-203 |
1.37e-35 |
|
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: 129.40 E-value: 1.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 32 ILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTVNS----NVRETQVLLLSPTRELAEQSQK 107
Cdd:cd17942 1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKlkfkPRNGTGVIIISPTRELALQIYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 108 VCLALGDYCNIEVHCCIGGKKVSDDIKALESGVQIVSGTPGR-VNHMITDRHLNTRNIKQLILDEADEMLNRGFKEQVYS 186
Cdd:cd17942 81 VAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRlLDHLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQ 160
|
170
....*....|....*..
gi 71033289 187 VYRYLPPTIQVVLVSAT 203
Cdd:cd17942 161 IIKLLPKRRQTMLFSAT 177
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
32-222 |
1.07e-34 |
|
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: 126.76 E-value: 1.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 32 ILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTVnSNVRETQ------VLLLSPTRELAEQS 105
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHI-MDQRELEkgegpiAVIVAPTRELAQQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 106 QKVCLALGDYCNIEVHCCIGGKKVSDDIKALESGVQIVSGTPGRVNHMITDRHLNTRNIKQLILDEADEMLNRGFKEQVY 185
Cdd:cd17952 80 YLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 71033289 186 SVYRYLPPTIQVVLVSATLPHDVIEITNKFMNNPFKV 222
Cdd:cd17952 160 SIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
40-222 |
1.95e-34 |
|
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: 126.12 E-value: 1.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 40 GFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTVNSNVRETQVLLLSPTRELAEQSQKVCLALGD-YCNI 118
Cdd:cd17962 9 GYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKELMKgLPPM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 119 EVHCCIGGKKVSDDIKALESGVQIVSGTPGRVNHMITDRHLNTRNIKQLILDEADEMLNRGFKEQVYSVYRYLPPTIQVV 198
Cdd:cd17962 89 KTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILENISHDHQTI 168
|
170 180
....*....|....*....|....
gi 71033289 199 LVSATLPHDVIEITNKFMNNPFKV 222
Cdd:cd17962 169 LVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
32-219 |
2.28e-33 |
|
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: 123.97 E-value: 2.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 32 ILKGIFAYGFDKPSAVQQRAIkPI-LEGRDVIIQSQSGTGKTCVFCLGALQTVNSNVRET--------QVLLLSPTRELA 102
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAI-PIgLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDeetkddgpYALILAPTRELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 103 EQSQKVCLALGDYCNIEVHCCIGGKKVSDDIKALESGVQIVSGTPGRVNHMITDRHLNTRNIKQLILDEADEMLNRGFKE 182
Cdd:cd17945 80 QQIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 71033289 183 QVYSVYRYLPPTI--------------------QVVLVSATLPHDVIEITNKFMNNP 219
Cdd:cd17945 160 QVTKILDAMPVSNkkpdteeaeklaasgkhryrQTMMFTATMPPAVEKIAKGYLRRP 216
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
40-219 |
1.19e-32 |
|
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: 121.92 E-value: 1.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 40 GFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTVNSNV----RE--TQVLLLSPTRELAEQSQKVCLALG 113
Cdd:cd17949 10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEprvdRSdgTLALVLVPTRELALQIYEVLEKLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 114 DYC-NIEVHCCIGG-KKVSDdiKA-LESGVQIVSGTPGR-VNHMITDRHLNTRNIKQLILDEADEMLNRGFKEQVYSVYR 189
Cdd:cd17949 90 KPFhWIVPGYLIGGeKRKSE--KArLRKGVNILIATPGRlLDHLKNTQSFDVSNLRWLVLDEADRLLDMGFEKDITKILE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 71033289 190 YL-------------PPTIQVVLVSATLPHDVIEITNKFMNNP 219
Cdd:cd17949 168 LLddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDP 210
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
32-205 |
1.01e-31 |
|
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: 119.37 E-value: 1.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 32 ILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGA-LQTVNSNVR------ETQV-LLLSPTRELAE 103
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLiMFALEQEKKlpfikgEGPYgLIVCPSRELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 104 QSQKVC------LALGDYCNIEVHCCIGGKKVSDDIKALESGVQIVSGTPGRVNHMITDRHLNTRNIKQLILDEADEMLN 177
Cdd:cd17951 81 QTHEVIeyyckaLQEGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
|
170 180
....*....|....*....|....*...
gi 71033289 178 RGFKEQVYSVYRYLPPTIQVVLVSATLP 205
Cdd:cd17951 161 MGFEEDIRTIFSYFKGQRQTLLFSATMP 188
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
21-219 |
1.48e-31 |
|
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: 119.05 E-value: 1.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 21 ESFEDLGLKEEILKGIFAYGFDKPSAVQQRAIKPILEG--RDVIIQSQSGTGKTCVFCLGALQTVNSNVRETQVLLLSPT 98
Cdd:cd18047 1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 99 RELAEQSQKVCLALGD-YCNIEVHCCIGGKKVSDDIKALEsgvQIVSGTPGRV-NHMITDRHLNTRNIKQLILDEADEML 176
Cdd:cd18047 81 YELALQTGKVIEQMGKfYPELKLAYAVRGNKLERGQKISE---QIVIGTPGTVlDWCSKLKFIDPKKIKVFVLDEADVMI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 71033289 177 -NRGFKEQVYSVYRYLPPTIQVVLVSATLPHDVIEITNKFMNNP 219
Cdd:cd18047 158 aTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
274-355 |
4.55e-31 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 113.46 E-value: 4.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 274 DWLAKKMKDGNFEVCKMHGEMSQKERNDIMQRFRKGESRVLISTDLWGRGLDVQQVSLVVNYDLPNSRESYIHRIGRSGR 353
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 71033289 354 YG 355
Cdd:smart00490 81 AG 82
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
18-218 |
1.64e-29 |
|
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, G17P1, or HUMP68) is involved in pathways that include the alteration of RNA structures, plays a role as a coregulator of transcription, a regulator of splicing, and in the processing of small noncoding RNAs. It synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. Dysregulation of this gene may play a role in cancer development. DDX5 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350807 [Multi-domain] Cd Length: 234 Bit Score: 114.34 E-value: 1.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 18 PLVEsFEDLGLKEEILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTVNSNVRETQ-----V 92
Cdd:cd18049 22 PVLN-FYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERgdgpiC 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 93 LLLSPTRELAEQSQKVCLALGDYCNIEVHCCIGGKKVSDDIKALESGVQIVSGTPGRVNHMITDRHLNTRNIKQLILDEA 172
Cdd:cd18049 101 LVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 71033289 173 DEMLNRGFKEQVYSVYRYLPPTIQVVLVSATLPHDVIEITNKFMNN 218
Cdd:cd18049 181 DRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKD 226
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
20-218 |
1.83e-29 |
|
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: 115.11 E-value: 1.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 20 VESFEDLGLKEEILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTVNSNVRETQ-----VLL 94
Cdd:cd18050 61 VFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERgdgpiCLV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 95 LSPTRELAEQSQKVCLALGDYCNIEVHCCIGGKKVSDDIKALESGVQIVSGTPGRVNHMITDRHLNTRNIKQLILDEADE 174
Cdd:cd18050 141 LAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADR 220
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 71033289 175 MLNRGFKEQVYSVYRYLPPTIQVVLVSATLPHDVIEITNKFMNN 218
Cdd:cd18050 221 MLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRD 264
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
20-218 |
6.24e-29 |
|
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: 112.83 E-value: 6.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 20 VESFEDLGLKEEILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGAL--------------QTVNS 85
Cdd:cd18051 20 IETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILsqiyeqgpgeslpsESGYY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 86 NVRETQ--VLLLSPTRELA----EQSQKVClalgdYCNiEVHCCI--GGKKVSDDIKALESGVQIVSGTPGRVNHMITDR 157
Cdd:cd18051 100 GRRKQYplALVLAPTRELAsqiyDEARKFA-----YRS-RVRPCVvyGGADIGQQMRDLERGCHLLVATPGRLVDMLERG 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71033289 158 HLNTRNIKQLILDEADEMLNRGFKEQVYSVYRY--LPPT--IQVVLVSATLPHDVIEITNKFMNN 218
Cdd:cd18051 174 KIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPTgeRQTLMFSATFPKEIQMLARDFLDN 238
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
47-220 |
8.04e-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: 111.48 E-value: 8.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 47 VQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTVNSNV------RETQVLLLSPTRELAEQSQKvclalgDYCNI-- 118
Cdd:cd17944 16 IQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQqprkrgRAPKVLVLAPTRELANQVTK------DFKDItr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 119 --EVHCCIGGKKVSDDIKALESGVQIVSGTPGRVNHMITDRHLNTRNIKQLILDEADEMLNRGFKEQVYSV----YRYLP 192
Cdd:cd17944 90 klSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEIlsvsYKKDS 169
|
170 180
....*....|....*....|....*....
gi 71033289 193 P-TIQVVLVSATLPHDVIEITNKFMNNPF 220
Cdd:cd17944 170 EdNPQTLLFSATCPDWVYNVAKKYMKSQY 198
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
31-217 |
9.46e-27 |
|
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: 106.68 E-value: 9.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 31 EILKGifaYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTV--NSNVRETQ-----VLLLSPTRELAE 103
Cdd:cd17948 3 EILQR---QGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLlrYKLLAEGPfnaprGLVITPSRELAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 104 QSQKVCLALGDYCNIEVHCCIGGKKVSDDIKALESGVQIVSGTPGRVNHMITDRHLNTRNIKQLILDEADEMLNRGFKEQ 183
Cdd:cd17948 80 QIGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 71033289 184 VYSVYRYLP-------------PTIQVVLVSATLPHDVIEITNKFMN 217
Cdd:cd17948 160 LSHFLRRFPlasrrsentdgldPGTQLVLVSATMPSGVGEVLSKVID 206
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
32-182 |
1.45e-21 |
|
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: 92.30 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 32 ILKGIFAYGFDKPSAVQQRAIKP-ILEGRDVIIQSQSGTGKTCVF-------CLGALQTVNSNVRET--QVLLLSPTREL 101
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAaIRDGKDVIGAAETGSGKTLAFgipilerLLSQKSSNGVGGKQKplRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 102 AEQSQKVCLALGDYCNIEVHCCIGGKKVSDDIKALESGVQIVSGTPGRVNHMIT--DRHLNT-RNIKQLILDEADEMLNR 178
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQegNEHLANlKSLRFLVLDEADRMLEK 160
|
....*
gi 71033289 179 G-FKE 182
Cdd:cd17946 161 GhFAE 165
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
44-208 |
1.41e-17 |
|
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: 81.14 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 44 PSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTVNSN-VRETQVLLLSPTRELAEQSQKVCLALGDYCNIEVHC 122
Cdd:cd17956 22 PWLLPSSKSTPPYRPGDLCVSAPTGSGKTLAYVLPIVQALSKRvVPRLRALIVVPTKELVQQVYKVFESLCKGTGLKVVS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 123 CIGGKKVSDDIKAL--------ESGVQIVSGTPGR-VNHMITDRHLNTRNIKQLILDEADEMLNRGFKEQVYSVYRYL-- 191
Cdd:cd17956 102 LSGQKSFKKEQKLLlvdtsgryLSRVDILVATPGRlVDHLNSTPGFTLKHLRFLVIDEADRLLNQSFQDWLETVMKALgr 181
|
170 180 190
....*....|....*....|....*....|....*
gi 71033289 192 ------------------PPTIQVVLVSATLPHDV 208
Cdd:cd17956 182 ptapdlgsfgdanllersVRPLQKLLFSATLTRDP 216
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
58-203 |
6.58e-16 |
|
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: 74.36 E-value: 6.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 58 GRDVIIQSQSGTGKTCVFCLGALQtvNSNVRETQVLLLSPTRELAEQSQKVCLALGDYcNIEVHCCIGGKKVSDDIKALE 137
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALL--LLLKKGKKVLVLVPTKALALQTAERLRELFGP-GIRVAVLVGGSSAEEREKNKL 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71033289 138 SGVQIVSGTPGRVNHMIT-DRHLNTRNIKQLILDEADEMLNRGFKEQV--YSVYRYLPPTIQVVLVSAT 203
Cdd:cd00046 78 GDADIIIATPDMLLNLLLrEDRLFLKDLKLIIVDEAHALLIDSRGALIldLAVRKAGLKNAQVILLSAT 146
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
48-375 |
2.85e-15 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 77.37 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 48 QQRAIKPIL-----EGRDVIIQSQSGTGKTcVFCLGALQTVNSNVRetqVLLLSPTRELAEQSQKVCLALgdycnievhc 122
Cdd:COG1061 85 QQEALEALLaalerGGGRGLVVAPTGTGKT-VLALALAAELLRGKR---VLVLVPRRELLEQWAEELRRF---------- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 123 cIGGKKVSDDIKALESGVQIVsgTPGRVNHMITDRHLNtRNIKQLILDEADEMLNRGFKEqvysVYRYLPPTIqVVLVSA 202
Cdd:COG1061 151 -LGDPLAGGGKKDSDAPITVA--TYQSLARRAHLDELG-DRFGLVIIDEAHHAGAPSYRR----ILEAFPAAY-RLGLTA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 203 TlPH--DVIEITNKFMNN-----------------PFKVLVKRDELTLEGIKQFFIS-------VEKEQWKFDTLCDLYE 256
Cdd:COG1061 222 T-PFrsDGREILLFLFDGivyeyslkeaiedgylaPPEYYGIRVDLTDERAEYDALSerlrealAADAERKDKILRELLR 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 257 SLI-ITQAVIFCNTKEKVDWLAKKMKDGNFEVCKMHGEMSQKERNDIMQRFRKGESRVLISTDLWGRGLDVQQVSLVVNY 335
Cdd:COG1061 301 EHPdDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILL 380
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 71033289 336 DLPNSRESYIHRIGRsG--RYGRKGVA--INFVkDDDIRILRDI 375
Cdd:COG1061 381 RPTGSPREFIQRLGR-GlrPAPGKEDAlvYDFV-GNDVPVLEEL 422
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
18-379 |
4.10e-15 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 77.18 E-value: 4.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 18 PLVESFEDlGLKEEILKGIFAYGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTVNSNVRETqVLLLSP 97
Cdd:COG1205 32 ARYAPWPD-WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPGAT-ALYLYP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 98 TRELA-EQSQKVcLALGDYCNIEVHCCI--GGKKVSDDIKALESGvQIVSGTPGRVNHMITDRH------LntRNIKQLI 168
Cdd:COG1205 110 TKALArDQLRRL-RELAEALGLGVRVATydGDTPPEERRWIREHP-DIVLTNPDMLHYGLLPHHtrwarfF--RNLRYVV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 169 LDEADEMlnRG-FKEQVYSVYR-------YLPPTIQVVLVSATL--PHdviEITNKFMNNPFkVLVKRD----------- 227
Cdd:COG1205 186 IDEAHTY--RGvFGSHVANVLRrlrricrHYGSDPQFILASATIgnPA---EHAERLTGRPV-TVVDEDgsprgertfvl 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 228 ---ELTLEGIKQffiSVEKEqwkfdtLCDLYESLII--TQAVIFCNTKEKVDWLAKKMKDGNFE------VCKMHGEMSQ 296
Cdd:COG1205 260 wnpPLVDDGIRR---SALAE------AARLLADLVRegLRTLVFTRSRRGAELLARYARRALREpdladrVAAYRAGYLP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 297 KERNDIMQRFRKGESRVLIST---DLwgrGLDVQQVSLVVNYDLPNSRESYIHRIGRSGRYGRKGVAInFVKDDDIrilr 373
Cdd:COG1205 331 EERREIERGLRSGELLGVVSTnalEL---GIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV-LVAGDDP---- 402
|
....*.
gi 71033289 374 dIEQYY 379
Cdd:COG1205 403 -LDQYY 407
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
247-349 |
5.66e-15 |
|
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: 71.35 E-value: 5.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 247 KFDTLCDLYESLIITQ--AVIFCNTKEKVDWLAKKMKDGNFEVCKMHGEMSQKERNDIMQRFRKGES--RVLISTDLWGR 322
Cdd:cd18793 12 KLEALLELLEELREPGekVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDirVFLLSTKAGGV 91
|
90 100 110
....*....|....*....|....*....|...
gi 71033289 323 GLDVQQVSLVVNYDLP------NSRESYIHRIG 349
Cdd:cd18793 92 GLNLTAANRVILYDPWwnpaveEQAIDRAHRIG 124
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
264-373 |
3.27e-14 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 74.02 E-value: 3.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 264 VIFCNTKEKVDWLAKKMKDGNFEVCKMHGEMSQKERNDIMQRFRKGESRVLISTDLWGRGLDVQQVSLVVNYDLPNSRES 343
Cdd:COG0514 234 IVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEA 313
|
90 100 110
....*....|....*....|....*....|
gi 71033289 344 YIHRIGRSGRYGRKGVAINFVKDDDIRILR 373
Cdd:COG0514 314 YYQEIGRAGRDGLPAEALLLYGPEDVAIQR 343
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
247-361 |
7.51e-14 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 73.23 E-value: 7.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 247 KFDTLCDLYESLIIT----QAVIFCNTKEKVDWLAKKMKDGNFEVCKMHGE--------MSQKERNDIMQRFRKGESRVL 314
Cdd:COG1111 336 KLSKLREILKEQLGTnpdsRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQaskegdkgLTQKEQIEILERFRAGEFNVL 415
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 71033289 315 ISTDLWGRGLDVQQVSLVVNYDL-PNS-ResYIHRIGRSGRYGRKGVAI 361
Cdd:COG1111 416 VATSVAEEGLDIPEVDLVIFYEPvPSEiR--SIQRKGRTGRKREGRVVV 462
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
263-363 |
1.36e-13 |
|
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: 67.23 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 263 AVIFCNTKEKVDWLAKKMKDGNFEVCKMHGEMSQKERNDIMQRFRKGESRVLISTDLWGRGLDVQQVSLVVNYDLPNSRE 342
Cdd:cd18794 33 GIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSME 112
|
90 100
....*....|....*....|.
gi 71033289 343 SYIHRIGRSGRYGRKGVAINF 363
Cdd:cd18794 113 SYYQESGRAGRDGLPSECILF 133
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
28-205 |
2.10e-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: 69.33 E-value: 2.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 28 LKEEILKGIFAYGFD-KPSAVQQRAIKPILE---------------GRDV-IIQSQSGTGKTCVFCLGAL---------- 80
Cdd:cd17965 14 IIKEILKGSNKTDEEiKPSPIQTLAIKKLLKtlmrkvtkqtsneepKLEVfLLAAETGSGKTLAYLAPLLdylkrqeqep 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 81 -----QTVNSNVRETQV--LLLSPTRELAEQSQKVCLALGDYC--NIEVHCCIGGKKVSDDIKALESGVQIVSGTPGRVN 151
Cdd:cd17965 94 feeaeEEYESAKDTGRPrsVILVPTHELVEQVYSVLKKLSHTVklGIKTFSSGFGPSYQRLQLAFKGRIDILVTTPGKLA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 71033289 152 HMITDRHLNTRNIKQLILDEADEMLNRGFKEQVYSVYRYLPPTIQVVLVSATLP 205
Cdd:cd17965 174 SLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIP 227
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
238-350 |
1.59e-12 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350189 [Multi-domain] Cd Length: 142 Bit Score: 64.53 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 238 FISVEKEQWKFDTLCDLYESLIITQAVIFCNTKEKVDWLAKKMKD---------------GNFEVCKMHGEMSQKERNDI 302
Cdd:cd18802 3 IVVIPKLQKLIEILREYFPKTPDFRGIIFVERRATAVVLSRLLKEhpstlafircgfligRGNSSQRKRSLMTQRKQKET 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 71033289 303 MQRFRKGESRVLISTDLWGRGLDVQQVSLVVNYDLPNSRESYIHRIGR 350
Cdd:cd18802 83 LDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR 130
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
28-373 |
3.80e-12 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 67.82 E-value: 3.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 28 LKEEILKGIFAYGFDKPSavQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALqtvnsnVRETQVLLLSPTRELAEQSQK 107
Cdd:PRK11057 12 LAKQVLQETFGYQQFRPG--QQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPAL------VLDGLTLVVSPLISLMKDQVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 108 VCLALGdycnIEVHC---CIGGKKVSDDIKALESG-VQIVSGTPGRVnhMITD--RHLNTRNIKQLILDEADEMLNRG-- 179
Cdd:PRK11057 84 QLLANG----VAAAClnsTQTREQQLEVMAGCRTGqIKLLYIAPERL--MMDNflEHLAHWNPALLAVDEAHCISQWGhd 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 180 FKEQvysvYRYLP------PTIQVVLVSATLP----HDVIEITNkfMNNPFKVLVKRDELTLEgikqfFISVEK----EQ 245
Cdd:PRK11057 158 FRPE----YAALGqlrqrfPTLPFMALTATADdttrQDIVRLLG--LNDPLIQISSFDRPNIR-----YTLVEKfkplDQ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 246 -WKFdtlcdlyeslIITQ----AVIFCNTKEKVDWLAKKMKDGNFEVCKMHGEMSQKERNDIMQRFRKGESRVLISTDLW 320
Cdd:PRK11057 227 lMRY----------VQEQrgksGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAF 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 71033289 321 GRGLDVQQVSLVVNYDLPNSRESYIHRIGRSGRYGRKGVAINFVKDDDIRILR 373
Cdd:PRK11057 297 GMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPADMAWLR 349
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
294-358 |
3.30e-11 |
|
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: 60.83 E-value: 3.30e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71033289 294 MSQKERNDIMQRFRKGESRVLISTDLWGRGLDVQQVSLVVNYDLPNSRESYIHRIGRSGRyGRKG 358
Cdd:cd18801 74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR-KRQG 137
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
247-349 |
4.72e-11 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 64.48 E-value: 4.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 247 KFDTLCDLYESLIITQ--AVIFCNTKEKVDWLAKKMKDGNFEVCKMHGEMSQKERNDIMQRFRKGES--RVLISTDLWGR 322
Cdd:COG0553 534 KLEALLELLEELLAEGekVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEapVFLISLKAGGE 613
|
90 100 110
....*....|....*....|....*....|...
gi 71033289 323 GLDVQQVSLVVNYDLP------NSRESYIHRIG 349
Cdd:COG0553 614 GLNLTAADHVIHYDLWwnpaveEQAIDRAHRIG 646
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
140-317 |
1.51e-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: 62.79 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 140 VQIVSGTPGRVNHMITdRHLNTRNiKQLILDEAdemlnrgfkeQVYSVYrYLPPTIQ-----------VVLVSATLPHDV 208
Cdd:COG1203 247 DQLFESLFSNRKGQER-RLHNLAN-SVIILDEV----------QAYPPY-MLALLLRllewlknlggsVILMTATLPPLL 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 209 IEitnkFMNNPFKVLVKRDELTLEGIKQFF---ISVEKEQWKFDTLCDLYESLIIT--QAVIFCNTKEKVDWLAKKMKD- 282
Cdd:COG1203 314 RE----ELLEAYELIPDEPEELPEYFRAFVrkrVELKEGPLSDEELAELILEALHKgkSVLVIVNTVKDAQELYEALKEk 389
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 71033289 283 -GNFEVCKMHGEMSQKER----NDIMQRFRKGESRVLIST 317
Cdd:COG1203 390 lPDEEVYLLHSRFCPADRseieKEIKERLERGKPCILVST 429
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
167-357 |
3.03e-10 |
|
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: 61.29 E-value: 3.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 167 LILDEAD--EMLNRGFKEQVYSVYRYLppTIQVVLVSATLPhDVIEITNKFMNNPFKvlvkRDELTLEGIKQFFISVEKE 244
Cdd:cd09639 127 LIFDEVHfyDEYTLALILAVLEVLKDN--DVPILLMSATLP-KFLKEYAEKIGYVEE----NEPLDLKPNERAPFIKIES 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 245 QWKFD--TLCDLYESLI-ITQAVIFCNTKEKVDWLAKKMKDGNFEVCKM--HGEMSQKER----NDIMQRFRKGESRVLI 315
Cdd:cd09639 200 DKVGEisSLERLLEFIKkGGSVAIIVNTVDRAQEFYQQLKEKGPEEEIMliHSRFTEKDRakkeAELLLEFKKSEKFVIV 279
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 71033289 316 STDLWGRGLDVQQVSLVVNYDLPNsreSYIHRIGRSGRYGRK 357
Cdd:cd09639 280 ATQVIEASLDISVDVMITELAPID---SLIQRLGRLHRYGEK 318
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
265-353 |
1.38e-09 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 56.12 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 265 IFCNTKEKVDWLAKKMKD--------GNFEVckMHGEMSQKERNDIMQRFRKGESRVLIST---DLwgrGLDVQQVSLVV 333
Cdd:cd18796 43 VFTNTRSQAERLAQRLRElcpdrvppDFIAL--HHGSLSRELREEVEAALKRGDLKVVVATsslEL---GIDIGDVDLVI 117
|
90 100
....*....|....*....|
gi 71033289 334 NYDLPNSRESYIHRIGRSGR 353
Cdd:cd18796 118 QIGSPKSVARLLQRLGRSGH 137
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
258-364 |
1.65e-09 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 53.86 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 258 LIITQAVIFCNTKEKVDWLAKKMKdgnfevckmhgemsqkerndimqrfrkgesrVLISTDLWGRGLDVQQVSLVVNYDL 337
Cdd:cd18785 1 VMVVKIIVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDP 49
|
90 100
....*....|....*....|....*...
gi 71033289 338 PNSRESYIHRIGRSGRYG-RKGVAINFV 364
Cdd:cd18785 50 PSSAASYIQRVGRAGRGGkDEGEVILFV 77
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
294-358 |
1.64e-08 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 56.42 E-value: 1.64e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71033289 294 MSQKERNDIMQRFRKGESRVLISTDLWGRGLDVQQVSLVVNYD-LPnsreSYIHRIGRSGRYGRKG 358
Cdd:PRK13766 407 MSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEpVP----SEIRSIQRKGRTGRQE 468
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
43-171 |
5.89e-08 |
|
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: 52.03 E-value: 5.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 43 KPSAVQQRAIKPIL------EGRDVIIQSQSGTGKTCVFCLGALQTVNsnvRETQVLLLSPTRELAEQSQKVCLALgdYC 116
Cdd:cd17918 15 SLTKDQAQAIKDIEkdlhspEPMDRLLSGDVGSGKTLVALGAALLAYK---NGKQVAILVPTEILAHQHYEEARKF--LP 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 71033289 117 NIEVHCCIGGKKVSDdikalESGVQIVSGTpgrvnHMITDRHLNTRNIKQLILDE 171
Cdd:cd17918 90 FINVELVTGGTKAQI-----LSGISLLVGT-----HALLHLDVKFKNLDLVIVDE 134
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
48-204 |
1.55e-07 |
|
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: 51.05 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 48 QQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTVNSNVReTQVLLLSPTRELAeQSQK-VCLALGDYC--NIEVHCCI 124
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDPG-SRALYLYPTKALA-QDQLrSLRELLEQLglGIRVATYD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 125 GGKKVSDDIKALESGVQIVSGTPGRVNHMITDRHLN----TRNIKQLILDEAdEMLNRGFKEQVYSVYRYL-------PP 193
Cdd:cd17923 83 GDTPREERRAIIRNPPRILLTNPDMLHYALLPHHDRwarfLRNLRYVVLDEA-HTYRGVFGSHVALLLRRLrrlcrryGA 161
|
170
....*....|.
gi 71033289 194 TIQVVLVSATL 204
Cdd:cd17923 162 DPQFILTSATI 172
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
47-319 |
1.73e-07 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 52.98 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 47 VQQRAI-KPILEGRDVIIQSQSGTGKTCVFCLGALQTVNSNVRetqVLLLSPTRELAEQ------------SQKVCLALG 113
Cdd:COG1204 26 PQAEALeAGLLEGKNLVVSAPTASGKTLIAELAILKALLNGGK---ALYIVPLRALASEkyrefkrdfeelGIKVGVSTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 114 DYcnievhcciggkkVSDDIKALESGVqIVSgTPGRVNHMITDRHLNTRNIKQLILDEA----DEmlNRGFK-EQVYSVY 188
Cdd:COG1204 103 DY-------------DSDDEWLGRYDI-LVA-TPEKLDSLLRNGPSWLRDVDLVVVDEAhlidDE--SRGPTlEVLLARL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 189 RYLPPTIQVVLVSATLPHdvIEITNKFMNNPfkvLVKRD----ELTLEGIKQFFISV-EKEQWKFDTLCDLYESLII--T 261
Cdd:COG1204 166 RRLNPEAQIVALSATIGN--AEEIAEWLDAE---LVKSDwrpvPLNEGVLYDGVLRFdDGSRRSKDPTLALALDLLEegG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 71033289 262 QAVIFCNTKEKVDWLAKKMKDgnfEVCKMHGEMSQKERNDIMQRFRKGESRVLISTDL 319
Cdd:COG1204 241 QVLVFVSSRRDAESLAKKLAD---ELKRRLTPEEREELEELAEELLEVSEETHTNEKL 295
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
278-353 |
2.33e-07 |
|
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: 50.04 E-value: 2.33e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71033289 278 KKMKDGNFEVCKMHGEMSQKERNDIMQRFRKGESRVLISTDLWGRGLDVQQVSLVVNYDLPNSRESYIHRI-GRSGR 353
Cdd:cd18811 55 KERFRPELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLHQLrGRVGR 131
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
264-388 |
1.93e-06 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 50.28 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 264 VIFCNTKEKVDWLAKKMKDGNFEVCKMHGEMSQKERNDIMQRFRKGESRVLISTDLWGRGLDVQQVSLVVNYDLPNSRES 343
Cdd:PLN03137 684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEG 763
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 71033289 344 YIHRIGRSGRYG-RKGVAINFVKDDDIRILRDIEQyysTQIDEMPM 388
Cdd:PLN03137 764 YHQECGRAGRDGqRSSCVLYYSYSDYIRVKHMISQ---GGVEQSPM 806
|
|
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
283-317 |
4.45e-06 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 48.89 E-value: 4.45e-06
10 20 30
....*....|....*....|....*....|....*
gi 71033289 283 GNFEVCKMHGEMSQKERNDIMQRFRKGESRVLIST 317
Cdd:COG1200 502 PGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVAT 536
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
259-350 |
4.73e-06 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350186 [Multi-domain] Cd Length: 116 Bit Score: 45.24 E-value: 4.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 259 IITQAVIFCNTKEKVDWLAKKMKDGNFEVCKMHGEMSQKERND---IMQRFRKGESRVLISTDLWGRGLDVQQVSLVVnY 335
Cdd:cd18799 5 VEIKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDealILLFFGELKPPILVTVDLLTTGVDIPEVDNVV-F 83
|
90
....*....|....*.
gi 71033289 336 DLP-NSRESYIHRIGR 350
Cdd:cd18799 84 LRPtESRTLFLQMLGR 99
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
269-353 |
5.09e-06 |
|
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350177 [Multi-domain] Cd Length: 171 Bit Score: 46.47 E-value: 5.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 269 TKEKVDWLAKKMKDGNFEVCKMHGEMSQKERNDIMQRFRKGESRVLISTDLWGRGLDVQQVSLVVNYD-----LPNSRES 343
Cdd:cd18790 36 TKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDadkegFLRSETS 115
|
90
....*....|
gi 71033289 344 YIHRIGRSGR 353
Cdd:cd18790 116 LIQTIGRAAR 125
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
271-367 |
5.39e-06 |
|
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: 46.11 E-value: 5.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 271 EKVDWLAKKMKD--GNFEVCKMHGEMSQKERNDIMQRFRKGESRVLISTDLWGRGLDVQQVSLVVNYDLPNSRESYIHRI 348
Cdd:cd18792 45 KSIEALAEELKElvPEARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFGLSQLHQL 124
|
90 100
....*....|....*....|
gi 71033289 349 -GRSGRYGRKGVAINFVKDD 367
Cdd:cd18792 125 rGRVGRGKHQSYCYLLYPDP 144
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
48-205 |
7.24e-06 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 46.10 E-value: 7.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 48 QQRAIKPI-LEGRDVIIQSQSGTGKTCVFCLGALQTVNSNvrETQVLLLSPTRELAEQ------------SQKVCLALGD 114
Cdd:cd17921 6 QREALRALyLSGDSVLVSAPTSSGKTLIAELAILRALATS--GGKAVYIAPTRALVNQkeadlrerfgplGKNVGLLTGD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 115 YcnievhcciggkkVSDDIKALESgvQIVSGTPGRVNHMITD-RHLNTRNIKQLILDEA----DEmlNRGFK-EQVYSVY 188
Cdd:cd17921 84 P-------------SVNKLLLAEA--DILVATPEKLDLLLRNgGERLIQDVRLVVVDEAhligDG--ERGVVlELLLSRL 146
|
170
....*....|....*..
gi 71033289 189 RYLPPTIQVVLVSATLP 205
Cdd:cd17921 147 LRINKNARFVGLSATLP 163
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
296-361 |
7.31e-06 |
|
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: 45.33 E-value: 7.31e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71033289 296 QKERNDIMQRFRKGESRVLISTDLWGRGLDVQQVSLVVNYDLPNSRESYIHRIGRSGRYGRKGVAI 361
Cdd:cd18797 78 AEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKDSLVI 143
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
283-317 |
1.44e-05 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 47.07 E-value: 1.44e-05
10 20 30
....*....|....*....|....*....|....*
gi 71033289 283 GNFEVCKMHGEMSQKERNDIMQRFRKGESRVLIST 317
Cdd:PRK10917 504 PELRVGLLHGRMKPAEKDAVMAAFKAGEIDILVAT 538
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
291-352 |
1.82e-05 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 47.23 E-value: 1.82e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71033289 291 HGEMSQKERNDIMQRFRKGESRVLISTDLWGRGLDVQQVSLVVNYDLPNSRESYIHRIGRSG 352
Cdd:PRK09751 308 HGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
48-364 |
4.63e-05 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 45.64 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 48 QQRAIKPILEGRDVIIQSQSGTGKTCVFCLGALQTVNSNVRETQVLllsPTRELAEQSQKVCLALGDYcNIEVHCCIGGk 127
Cdd:PRK01172 27 QRMAIEQLRKGENVIVSVPTAAGKTLIAYSAIYETFLAGLKSIYIV---PLRSLAMEKYEELSRLRSL-GMRVKISIGD- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 128 kvSDDIKALESGVQIVSGTPGRVNHMITDRHLNTRNIKQLILDE----ADEmlNRGFK-EQVYSVYRYLPPTIQVVLVSA 202
Cdd:PRK01172 102 --YDDPPDFIKRYDVVILTSEKADSLIHHDPYIINDVGLIVADEihiiGDE--DRGPTlETVLSSARYVNPDARILALSA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 203 TLPH--------DVIEITNKFMNNPFKV-LVKRDELTLEGikqffisvekeqwkfDTLCDLYESLIIT-------QAVIF 266
Cdd:PRK01172 178 TVSNanelaqwlNASLIKSNFRPVPLKLgILYRKRLILDG---------------YERSQVDINSLIKetvndggQVLVF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 267 CNTKEKVDWLAKKM-----KDGNFEVC------------KM--------HGEMSQKERNDIMQRFRKGESRVLISTDLWG 321
Cdd:PRK01172 243 VSSRKNAEDYAEMLiqhfpEFNDFKVSsennnvyddslnEMlphgvafhHAGLSNEQRRFIEEMFRNRYIKVIVATPTLA 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 71033289 322 RGLDVqQVSLVVNYDLPNSRESYI---------HRIGRSGR--YGRKGVAINFV 364
Cdd:PRK01172 323 AGVNL-PARLVIVRDITRYGNGGIrylsnmeikQMIGRAGRpgYDQYGIGYIYA 375
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
247-358 |
6.47e-05 |
|
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350176 [Multi-domain] Cd Length: 153 Bit Score: 42.62 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 247 KFDTLcdlyESLI-----ITQAVIFCNTKEKVDWLAKKMkdgNFEVckMHGEMSQKERNDIMQRFRKGESRVLISTDLWG 321
Cdd:cd18789 35 KLRAL----EELLkrheqGDKIIVFTDNVEALYRYAKRL---LKPF--ITGETPQSEREEILQNFREGEYNTLVVSKVGD 105
|
90 100 110
....*....|....*....|....*....|....*....
gi 71033289 322 RGLDVQQ--VSLVVNYdLPNSRESYIHRIGRSGRYGRKG 358
Cdd:cd18789 106 EGIDLPEanVAIQISG-HGGSRRQEAQRLGRILRPKKGG 143
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
265-366 |
1.11e-04 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 44.32 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 265 IFCNTK---EKvdW---LAKKMKDGNFEVCKMHGEMSQKERNDIMQRFRKGESRVLIST---DLwgrGLDVQQVSLVVNY 335
Cdd:COG1201 277 VFTNTRsqaER--LfqrLNELNPEDALPIAAHHGSLSREQRLEVEEALKAGELRAVVATsslEL---GIDIGDVDLVIQV 351
|
90 100 110
....*....|....*....|....*....|..
gi 71033289 336 DLPNSRESYIHRIGRSG-RYGRKGVAINFVKD 366
Cdd:COG1201 352 GSPKSVARLLQRIGRAGhRVGEVSKGRLVPTH 383
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
291-360 |
2.70e-04 |
|
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350197 [Multi-domain] Cd Length: 151 Bit Score: 40.79 E-value: 2.70e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71033289 291 HGEMSQKERNDIMQRFRKGESRVLISTDLWGRGLDVQQVSLVVNYDLPNSRESYIHRI-GRSGRYGRKGVA 360
Cdd:cd18810 58 HGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIERADKFGLAQLYQLrGRVGRSKERAYA 128
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
58-204 |
9.22e-04 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 39.49 E-value: 9.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 58 GRDVIIQSQSGTGKTCVFCLGALQTVNSNVRE-TQVLLLSPTRELA----EQSQKVCLALGDYCNIEV-HcciGGKKVSD 131
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKgVQVLYISPLKALIndqeRRLEEPLDEIDLEIPVAVrH---GDTSQSE 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71033289 132 DIKALESGVQIVSGTPGRVNHMITDRHLNT--RNIKQLILDEADEML--NRG--FKEQVYSVYRYLPPTIQVVLVSATL 204
Cdd:cd17922 78 KAKQLKNPPGILITTPESLELLLVNKKLRElfAGLRYVVVDEIHALLgsKRGvqLELLLERLRKLTGRPLRRIGLSATL 156
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
265-367 |
1.75e-03 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 40.64 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71033289 265 IFCNTK---EKVDWLAKKMKDGNFEVCKM---HGEMSQKERNDIMQRFRKGESRVLI-STDLwGRGLDVQQVSLVVNYDL 337
Cdd:PRK13767 289 IFTNTRsgaERVLYNLRKRFPEEYDEDNIgahHSSLSREVRLEVEEKLKRGELKVVVsSTSL-ELGIDIGYIDLVVLLGS 367
|
90 100 110
....*....|....*....|....*....|...
gi 71033289 338 PNSRESYIHRIGRSG-RYGR--KGVAINFVKDD 367
Cdd:PRK13767 368 PKSVSRLLQRIGRAGhRLGEvsKGRIIVVDRDD 400
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
30-80 |
1.99e-03 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 39.05 E-value: 1.99e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 71033289 30 EEILKGIFayGFDKPSAVQQRAIKPILEGRDVIIQSQSGTGKTCVFCLGAL 80
Cdd:cd17920 1 EQILKEVF--GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPAL 49
|
|
| SF2_C_priA |
cd18804 |
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ... |
295-361 |
5.21e-03 |
|
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: 37.99 E-value: 5.21e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71033289 295 SQKERNDIMQRFRKGESRVLISTDLWGRGLDVQQVSLVV--NYD----LPNSRES-----YIHRI-GRSGRYGRKGVAI 361
Cdd:cd18804 129 KKGALEKLLDQFERGEIDILIGTQMIAKGLDFPNVTLVGilNADsglnSPDFRASerafqLLTQVsGRAGRGDKPGKVI 207
|
|
| |
