|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
16-402 |
0e+00 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 629.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 16 GQDEFFTSYDDVHESFDAMGLQENLLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVLQQLDFSL 95
Cdd:PTZ00424 15 STGTIESNYDEIVDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 96 IQCQALVLAPTRELAQQIEKVMRALGDYLGVKVHACVGGTSVREDQRILQAGVHVVVGTPGRVFDMLKRQSLRADNIKMF 175
Cdd:PTZ00424 95 NACQALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 176 VLDEADEMLSRGFKDQIYDIFQLLPPKIQVGVFSATMPPEALEITRKFMSKPVRILVKRDELTLEGIKQFYVNVEKEEWK 255
Cdd:PTZ00424 175 ILDEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 256 LETLCDLYETLAITQSVIFVNTRRKVDWLTDKMRSRDHTVSATHGDMDQNTRDIIMREFRSGSSRVLITTDLLARGIDVQ 335
Cdd:PTZ00424 255 FDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQ 334
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145332383 336 QVSLVINFDLPTQPENYLHRIGRSGRFGRKGVAINFVTRDDERMLFDIQKFYNVVVEELPSNVADLL 402
Cdd:PTZ00424 335 QVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPMEVADYL 401
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
30-395 |
1.70e-158 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 452.68 E-value: 1.70e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 30 SFDAMGLQENLLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVLQQLDFSLI-QCQALVLAPTRE 108
Cdd:COG0513 3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPrAPQALILAPTRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 109 LAQQIEKVMRALGDYLGVKVHACVGGTSVREDQRILQAGVHVVVGTPGRVFDMLKRQSLRADNIKMFVLDEADEMLSRGF 188
Cdd:COG0513 83 LALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 189 KDQIYDIFQLLPPKIQVGVFSATMPPEALEITRKFMSKPVRILVKRDELTLEGIKQFYVNVEKEEwKLETLCDLYETLAI 268
Cdd:COG0513 163 IEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRD-KLELLRRLLRDEDP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 269 TQSVIFVNTRRKVDWLTDKMRSRDHTVSATHGDMDQNTRDIIMREFRSGSSRVLITTDLLARGIDVQQVSLVINFDLPTQ 348
Cdd:COG0513 242 ERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPED 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 145332383 349 PENYLHRIGRSGRFGRKGVAINFVTRDDERMLFDIQKFYNVVVEELP 395
Cdd:COG0513 322 PEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEE 368
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
33-231 |
8.74e-137 |
|
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: 388.99 E-value: 8.74e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 33 AMGLQENLLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVLQQLDFSLIQCQALVLAPTRELAQQ 112
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 113 IEKVMRALGDYLGVKVHACVGGTSVREDQRILQAGVHVVVGTPGRVFDMLKRQSLRADNIKMFVLDEADEMLSRGFKDQI 192
Cdd:cd17939 81 IQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQI 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 145332383 193 YDIFQLLPPKIQVGVFSATMPPEALEITRKFMSKPVRIL 231
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 ... |
31-231 |
5.83e-126 |
|
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: 361.76 E-value: 5.83e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 31 FDAMGLQENLLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVLQQLDFSLIQCQALVLAPTRELA 110
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 111 QQIEKVMRALGDYLGVKVHACVGGTSVREDQRILQAGVHVVVGTPGRVFDMLKRQSLRADNIKMFVLDEADEMLSRGFKD 190
Cdd:cd18046 81 QQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 145332383 191 QIYDIFQLLPPKIQVGVFSATMPPEALEITRKFMSKPVRIL 231
Cdd:cd18046 161 QIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRIL 201
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
31-231 |
5.88e-106 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor 4A-III (EIF4AIII, also known as DDX48) is part of the exon junction complex (EJC) that plays a major role in posttranscriptional regulation of mRNA. EJC consists of four proteins (eIF4AIII, Barentsz [Btz], Mago, and Y14), mRNA, and ATP. DDX48 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350803 [Multi-domain] Cd Length: 201 Bit Score: 310.94 E-value: 5.88e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 31 FDAMGLQENLLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVLQQLDFSLIQCQALVLAPTRELA 110
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 111 QQIEKVMRALGDYLGVKVHACVGGTSVREDQRILQAGVHVVVGTPGRVFDMLKRQSLRADNIKMFVLDEADEMLSRGFKD 190
Cdd:cd18045 81 VQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 145332383 191 QIYDIFQLLPPKIQVGVFSATMPPEALEITRKFMSKPVRIL 231
Cdd:cd18045 161 QIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRIL 201
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
30-396 |
7.87e-99 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 301.72 E-value: 7.87e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 30 SFDAMGLQENLLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVLQQLDFSLIQCQALVLAPTREL 109
Cdd:PRK11776 5 AFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTREL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 110 AQQIEKVMRALGDYL-GVKVHACVGGTSVREDQRILQAGVHVVVGTPGRVFDMLKRQSLRADNIKMFVLDEADEMLSRGF 188
Cdd:PRK11776 85 ADQVAKEIRRLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMGF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 189 KDQIYDIFQLLPPKIQVGVFSATMPPEALEITRKFMSKPVRILV--KRDELTLEgiKQFYvNVEKEEwKLETLCDLYETL 266
Cdd:PRK11776 165 QDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVesTHDLPAIE--QRFY-EVSPDE-RLPALQRLLLHH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 267 AITQSVIFVNTRRKVDWLTDKMRSRDHTVSATHGDMDQNTRDIIMREFRSGSSRVLITTDLLARGIDVQQVSLVINFDLP 346
Cdd:PRK11776 241 QPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 145332383 347 TQPENYLHRIGRSGRFGRKGVAINFVTRDDERMLFDIQKFYN--VVVEELPS 396
Cdd:PRK11776 321 RDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGrkLNWEPLPS 372
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
26-402 |
5.71e-83 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 265.94 E-value: 5.71e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 26 DVHESFDAMGLQENLLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVLQQLDFSLIQCQALVLAP 105
Cdd:PRK11634 3 EFETTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 106 TRELAQQIEKVMRALGDYL-GVKVHACVGGTSVREDQRILQAGVHVVVGTPGRVFDMLKRQSLRADNIKMFVLDEADEML 184
Cdd:PRK11634 83 TRELAVQVAEAMTDFSKHMrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEML 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 185 SRGFKDQIYDIFQLLPPKIQVGVFSATMPPEALEITRKFMSKPVRILVKRDELTLEGIKQFYVNVEKEEwKLETLCDLYE 264
Cdd:PRK11634 163 RMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMR-KNEALVRFLE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 265 TLAITQSVIFVNTRRKVDWLTDKMRSRDHTVSATHGDMDQNTRDIIMREFRSGSSRVLITTDLLARGIDVQQVSLVINFD 344
Cdd:PRK11634 242 AEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYD 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 145332383 345 LPTQPENYLHRIGRSGRFGRKGVAINFVTRDDERMLFDIQKFYNVVVEELPSNVADLL 402
Cdd:PRK11634 322 IPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAELL 379
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
40-230 |
9.23e-82 |
|
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: 248.90 E-value: 9.23e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 40 LLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVLQQLDFSLIQC----QALVLAPTRELAQQIEK 115
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKgrgpQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 116 VMRALGDYLGVKVHACVGGTSVREDQRILQAGVHVVVGTPGRVFDMLKRQSLRADNIKMFVLDEADEMLSRGFKDQIYDI 195
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 145332383 196 FQLLPPKIQVGVFSATMPPEALEITRKFMSKPVRI 230
Cdd:cd00268 161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
29-399 |
2.07e-76 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 243.31 E-value: 2.07e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 29 ESFDamgLQENLLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVLQQL-DF---SLIQCQALVLA 104
Cdd:PRK11192 4 SELE---LDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLlDFprrKSGPPRILILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 105 PTRELAQQIEKVMRALGDYLGVKVHACVGGTSVREDQRILQAGVHVVVGTPGRVFDMLKRQSLRADNIKMFVLDEADEML 184
Cdd:PRK11192 81 PTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 185 SRGFKDQIYDIFQLLPPKIQVGVFSATMPPEALE-ITRKFMSKPVRILVK--RDELtlEGIKQFYVNVEKEEWKLETLCD 261
Cdd:PRK11192 161 DMGFAQDIETIAAETRWRKQTLLFSATLEGDAVQdFAERLLNDPVEVEAEpsRRER--KKIHQWYYRADDLEHKTALLCH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 262 LYETLAITQSVIFVNTRRKVDWLTDKMRSRDHTVSATHGDMDQNTRDIIMREFRSGSSRVLITTDLLARGIDVQQVSLVI 341
Cdd:PRK11192 239 LLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVI 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145332383 342 NFDLPTQPENYLHRIGRSGRFGRKGVAINFVTRDDERMLFDIQKFYNV-----VVEEL-PSNVA 399
Cdd:PRK11192 319 NFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEplkarVIDELrPKTKA 382
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
30-385 |
5.33e-75 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 240.48 E-value: 5.33e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 30 SFDAMGLQENLLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVLQQLDFSLIQCQ------ALVL 103
Cdd:PRK10590 2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKgrrpvrALIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 104 APTRELAQQIEKVMRALGDYLGVKVHACVGGTSVREDQRILQAGVHVVVGTPGRVFDMLKRQSLRADNIKMFVLDEADEM 183
Cdd:PRK10590 82 TPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 184 LSRGFKDQIYDIFQLLPPKIQVGVFSATMPPEALEITRKFMSKPVRILVKRDELTLEGIKQFYVNVEKEEwKLETLCDLY 263
Cdd:PRK10590 162 LDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKR-KRELLSQMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 264 ETLAITQSVIFVNTRRKVDWLTDKMRSRDHTVSATHGDMDQNTRDIIMREFRSGSSRVLITTDLLARGIDVQQVSLVINF 343
Cdd:PRK10590 241 GKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNY 320
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 145332383 344 DLPTQPENYLHRIGRSGRFGRKGVAINFVTRDDERMLFDIQK 385
Cdd:PRK10590 321 ELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEK 362
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
31-385 |
4.55e-69 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 225.56 E-value: 4.55e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 31 FDAMGLQENLLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVLQQLDFSLIQCQ-------ALVL 103
Cdd:PRK01297 89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKErymgeprALII 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 104 APTRELAQQIEKVMRALGDYLGVKVHACVGGTSVREDQRILQAG-VHVVVGTPGRVFDMLKRQSLRADNIKMFVLDEADE 182
Cdd:PRK01297 169 APTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEADR 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 183 MLSRGFKDQIYDIFQLLPPKI--QVGVFSATMPPEALEITRKFMSKPVRILVKRDELTLEGIKQ-FYVNVEKEEWKLetL 259
Cdd:PRK01297 249 MLDMGFIPQVRQIIRQTPRKEerQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQhVYAVAGSDKYKL--L 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 260 CDLYETLAITQSVIFVNTRRKVDWLTDKMRSRDHTVSATHGDMDQNTRDIIMREFRSGSSRVLITTDLLARGIDVQQVSL 339
Cdd:PRK01297 327 YNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISH 406
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 145332383 340 VINFDLPTQPENYLHRIGRSGRFGRKGVAINFVTRDDERMLFDIQK 385
Cdd:PRK01297 407 VINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEE 452
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
29-385 |
2.66e-68 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 225.42 E-value: 2.66e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 29 ESFDAMGLQENLLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFcsgVLQQldFSLIQCQA-------- 100
Cdd:PTZ00110 130 VSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAF---LLPA--IVHINAQPllrygdgp 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 101 --LVLAPTRELAQQIEKVMRALGDYLGVKVHACVGGTSVREDQRILQAGVHVVVGTPGRVFDMLKRQSLRADNIKMFVLD 178
Cdd:PTZ00110 205 ivLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLD 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 179 EADEMLSRGFKDQIYDIFQLLPPKIQVGVFSATMPPEALEITRKFMS-KPVRILVKRDELTL-EGIKQfYVNVEKEEWKL 256
Cdd:PTZ00110 285 EADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKeEPVHVNVGSLDLTAcHNIKQ-EVFVVEEHEKR 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 257 ETLCDLYETLAITQS--VIFVNTRRKVDWLTDKMRSRDHTVSATHGDMDQNTRDIIMREFRSGSSRVLITTDLLARGIDV 334
Cdd:PTZ00110 364 GKLKMLLQRIMRDGDkiLIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDV 443
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 145332383 335 QQVSLVINFDLPTQPENYLHRIGRSGRFGRKGVAINFVTRDDERMLFDIQK 385
Cdd:PTZ00110 444 KDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVK 494
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
36-230 |
4.86e-65 |
|
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: 205.89 E-value: 4.86e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 36 LQENLLRGIYAYGFEKPSAIQQRGIvPFC-----KGLdvIQQAQSGTGKTATFCSGVLQQLDFSLIQCQALVLAPTRELA 110
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETAL-PLIlsdppENL--IAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 111 QQIEKVMRALGDYLGVKVHACVGGTSVREDQRILQagvHVVVGTPGRVFDMLKRQSLRADNIKMFVLDEADEML-SRGFK 189
Cdd:cd17963 78 RQIGEVVEKMGKFTGVKVALAVPGNDVPRGKKITA---QIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLdTQGHG 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 145332383 190 DQIYDIFQLLPPKIQVGVFSATMPPEALEITRKFMSKPVRI 230
Cdd:cd17963 155 DQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
31-230 |
6.72e-65 |
|
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: 205.99 E-value: 6.72e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 31 FDAMGLQENLLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVLQQLDFSLIQCQALVLAPTRELA 110
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 111 QQIEKVMRALGDYLGVKVHACVGGTSVREDQRILQAGVHVVVGTPGRVFDMLKRQSLRADNIKMFVLDEADEMLSRGFKD 190
Cdd:cd17940 81 LQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 145332383 191 QIYDIFQLLPPKIQVGVFSATMPPEALEITRKFMSKPVRI 230
Cdd:cd17940 161 IIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
30-381 |
2.50e-62 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 208.87 E-value: 2.50e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 30 SFDAMGLQENLLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATF-------CSGVLQQLDFSLIQCQALV 102
Cdd:PLN00206 122 SFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFlvpiisrCCTIRSGHPSEQRNPLAMV 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 103 LAPTRELAQQIEKVMRALGDYLGVKVHACVGGTSVREDQRILQAGVHVVVGTPGRVFDMLKRQSLRADNIKMFVLDEADE 182
Cdd:PLN00206 202 LTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDC 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 183 MLSRGFKDQIYDIFQLLpPKIQVGVFSATMPPEALEITRKFMSKPVRILVKRDELTLEGIKQFYVNVEKEEWKLEtlcdL 262
Cdd:PLN00206 282 MLERGFRDQVMQIFQAL-SQPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQK----L 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 263 YETLAITQ-----SVIFVNTRRKVDWLTDKMRSRDHTVSAT-HGDMDQNTRDIIMREFRSGSSRVLITTDLLARGIDVQQ 336
Cdd:PLN00206 357 FDILKSKQhfkppAVVFVSSRLGADLLANAITVVTGLKALSiHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLR 436
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 145332383 337 VSLVINFDLPTQPENYLHRIGRSGRFGRKGVAINFVTrDDERMLF 381
Cdd:PLN00206 437 VRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVN-EEDRNLF 480
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
30-386 |
1.16e-61 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 208.65 E-value: 1.16e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 30 SFDAMGLQENLLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVLQQL-------DFSLIQCQALV 102
Cdd:PRK04537 10 TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlsrpalaDRKPEDPRALI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 103 LAPTRELAQQIEKVMRALGDYLGVKVHACVGGTSVREDQRILQAGVHVVVGTPGRVFDMLKRQ---SLRADNIkmFVLDE 179
Cdd:PRK04537 90 LAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHkvvSLHACEI--CVLDE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 180 ADEMLSRGFKDQIYDIFQLLPPKI--QVGVFSATMPPEALEITRKFMSKPVRILVKRDELTLEGIKQ-FYVNVEKEewKL 256
Cdd:PRK04537 168 ADRMFDLGFIKDIRFLLRRMPERGtrQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQrIYFPADEE--KQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 257 ETLCDLYETLAITQSVIFVNTRRKVDWLTDKMRSRDHTVSATHGDMDQNTRDIIMREFRSGSSRVLITTDLLARGIDVQQ 336
Cdd:PRK04537 246 TLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDG 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 145332383 337 VSLVINFDLPTQPENYLHRIGRSGRFGRKGVAINFVTRDDERMLFDIQKF 386
Cdd:PRK04537 326 VKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAY 375
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
31-371 |
8.73e-61 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 202.51 E-value: 8.73e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 31 FDAMGLQENLLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVLQQL-------DFSLIQCQALVL 103
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLlshpapeDRKVNQPRALIM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 104 APTRELAQQIEKVMRALGDYLGVKVHACVGGTSVREDQRILQAGVHVVVGTPGRVFDMLKRQSLRADNIKMFVLDEADEM 183
Cdd:PRK04837 90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 184 LSRGFKDQIYDIFQLLPPKIQ--VGVFSATMPPEALEITRKFMSKPVRILVKRDELTLEGIKQ--FYVNVEKeewKLETL 259
Cdd:PRK04837 170 FDLGFIKDIRWLFRRMPPANQrlNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEelFYPSNEE---KMRLL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 260 CDLYETLAITQSVIFVNTRRKVDWLTDKMRSRDHTVSATHGDMDQNTRDIIMREFRSGSSRVLITTDLLARGIDVQQVSL 339
Cdd:PRK04837 247 QTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTH 326
|
330 340 350
....*....|....*....|....*....|..
gi 145332383 340 VINFDLPTQPENYLHRIGRSGRFGRKGVAINF 371
Cdd:PRK04837 327 VFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
242-372 |
1.11e-59 |
|
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: 190.03 E-value: 1.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 242 IKQFYVNVEKEEWKLETLCDLYETLAITQSVIFVNTRRKVDWLTDKMRSRDHTVSATHGDMDQNTRDIIMREFRSGSSRV 321
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 145332383 322 LITTDLLARGIDVQQVSLVINFDLPTQPENYLHRIGRSGRFGRKGVAINFV 372
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
53-219 |
5.73e-56 |
|
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: 181.67 E-value: 5.73e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 53 SAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVLQQLDFSLIQCQALVLAPTRELAQQIEKVMRALGDYLGVKVHACV 132
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 133 GGTSVREDQRILqAGVHVVVGTPGRVFDMLKRQSlRADNIKMFVLDEADEMLSRGFKDQIYDIFQLLPPKIQVGVFSATM 212
Cdd:pfam00270 81 GGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATL 158
|
....*..
gi 145332383 213 PPEALEI 219
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 ... |
30-232 |
1.83e-55 |
|
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: 181.77 E-value: 1.83e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 30 SFDAMGLQENLLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVLQQLDFSLIQCQALVLAPTREL 109
Cdd:cd17950 3 GFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTREL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 110 AQQIEKVMRALGDYL-GVKVHACVGGTSVREDQRILQAGV-HVVVGTPGRVFDMLKRQSLRADNIKMFVLDEADEML-SR 186
Cdd:cd17950 83 AFQISNEYERFSKYMpNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLeQL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 145332383 187 GFKDQIYDIFQLLPPKIQVGVFSATMPPEALEITRKFMSKPVRILV 232
Cdd:cd17950 163 DMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
40-230 |
2.52e-54 |
|
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: 178.23 E-value: 2.52e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 40 LLRGIYAYGFEKPSAIQQRGI-VPFCkGLDVIQQAQSGTGKTATFCSGVLQQLDFSLIQCQALVLAPTRELAQQIEKVMR 118
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIpLGLA-GHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 119 ALGDYL-GVKVHACVGGTSVREDqRILQAGVHVVVGTPGRVFDMLKRQSLRADNIKMFVLDEADEMLSRGFKDQIYDIFQ 197
Cdd:cd17943 80 KIGKKLeGLKCEVFIGGTPVKED-KKKLKGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFS 158
|
170 180 190
....*....|....*....|....*....|...
gi 145332383 198 LLPPKIQVGVFSATMPPEALEITRKFMSKPVRI 230
Cdd:cd17943 159 SLPKNKQVIAFSATYPKNLDNLLARYMRKPVLV 191
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
44-245 |
1.97e-51 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 171.14 E-value: 1.97e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 44 IYAYGFEKPSAIQQRGIVPFCKGL-DVIQQAQSGTGKTATFCSGVLQQLDfSLIQCQALVLAPTRELAQQIEKVMRALGD 122
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEALK-RGKGGRVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 123 YLGVKVHACVGGTSVREDQRILQAGV-HVVVGTPGRVFDMLKRQSLRADNIKMFVLDEADEMLSRGFKDQIYDIFQLLPP 201
Cdd:smart00487 80 SLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 145332383 202 KIQVGVFSATMPPEALEITRKFMSKPVRILVKRdeLTLEGIKQF 245
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 ... |
36-226 |
1.90e-48 |
|
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: 163.52 E-value: 1.90e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 36 LQENLLRGIYAYGFEKPSAIQQRGIVP-FCKGLDVIQQAQSGTGKTATFCSGVLQQLDFSLIQCQ-----ALVLAPTREL 109
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPiLSTGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRrsgvsALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 110 AQQIEKVMRALGDYL-GVKVHACVGGTSVRED-QRILQAGVHVVVGTPGRVFDMLKRQSLRAD--NIKMFVLDEADEMLS 185
Cdd:cd17964 81 ALQIAAEAKKLLQGLrKLRVQSAVGGTSRRAElNRLRRGRPDILVATPGRLIDHLENPGVAKAftDLDYLVLDEADRLLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 145332383 186 RGFKDQIYDIFQLLPPKIQVG----VFSATMPPEALEITRKFMSK 226
Cdd:cd17964 161 MGFRPDLEQILRHLPEKNADPrqtlLFSATVPDEVQQIARLTLKK 205
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
31-228 |
2.99e-48 |
|
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: 162.78 E-value: 2.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 31 FDAMGLQENLLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVLQQLDFSLIQCQALVLAPTRELA 110
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 111 QQIEKVMRALGDYLGVKVHACVGGTSVREDQRILQAGVHVVVGTPGRVFDMLKRQSLRA---DNIKMFVLDEADEMLSRG 187
Cdd:cd17955 81 YQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDTTkvlSRVKFLVLDEADRLLTGS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 145332383 188 FKDQIYDIFQLLPPKIQVGVFSATMPPEALEITRKFMSKPV 228
Cdd:cd17955 161 FEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPF 201
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
40-230 |
4.74e-48 |
|
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ribosomal subunits protein 1 homolog, and probable ATP-dependent RNA helicase DDX27) is involved in the processing of 5.8S and 28S ribosomal RNAs. More specifically, the encoded protein localizes to the nucleolus, where it interacts with the PeBoW complex to ensure proper 3' end formation of 47S rRNA. DDX27 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350705 [Multi-domain] Cd Length: 196 Bit Score: 162.04 E-value: 4.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 40 LLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVLQQLDFSLIQ---CQALVLAPTRELAQQIEKV 116
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKkaaTRVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 117 MRALGDYLGVKVHACVGGTSVREDQRILQAGVHVVVGTPGRVFDMLKR-QSLRADNIKMFVLDEADEMLSRGFKDQIYDI 195
Cdd:cd17947 81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNsPSFDLDSIEILVLDEADRMLEEGFADELKEI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 145332383 196 FQLLPPKIQVGVFSATMPPEALEITRKFMSKPVRI 230
Cdd:cd17947 161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
30-230 |
2.60e-46 |
|
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: 157.86 E-value: 2.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 30 SFDAMGLQENLLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVLQQLdfsLIQCQ---ALVLAPT 106
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQAL---LENPQrffALVLAPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 107 RELAQQIEKVMRALGDYLGVKVHACVGGTSVREDQRILQAGVHVVVGTPGRVFDMLKRQ---SLRadNIKMFVLDEADEM 183
Cdd:cd17954 78 RELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTkgfSLK--SLKFLVMDEADRL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 145332383 184 LSRGFKDQIYDIFQLLPPKIQVGVFSATMPPEALEITRKFMSKPVRI 230
Cdd:cd17954 156 LNMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
30-224 |
7.89e-45 |
|
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes Drosophila melanogaster Vasa, which is essential for development. DEAD box protein 3 (DDX3) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DDX3 and DDX4 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350725 [Multi-domain] Cd Length: 221 Bit Score: 154.57 E-value: 7.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 30 SFDAMGLQENLLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVLQQL----------DFSLIQCQ 99
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLledgppsvgrGRRKAYPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 100 ALVLAPTRELAQQIEKVMRALGDYLGVKVHACVGGTSVREDQRILQAGVHVVVGTPGRVFDMLKRQSLRADNIKMFVLDE 179
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 145332383 180 ADEMLSRGFKDQIYDIFQL--LPPKI--QVGVFSATMPPEALEITRKFM 224
Cdd:cd17967 161 ADRMLDMGFEPQIRKIVEHpdMPPKGerQTLMFSATFPREIQRLAADFL 209
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
30-230 |
7.91e-44 |
|
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350717 [Multi-domain] Cd Length: 205 Bit Score: 151.30 E-value: 7.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 30 SFDAMGLQENLLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVLQQLDFSLIQ--CQALVLAPTR 107
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTvgARALILSPTR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 108 ELAQQIEKVMRALGDYLGVKVHACVGGTSVREDQRILQAGVHVVVGTPGRVFDMLKRQSLRADNIKMFVLDEADEMLSRG 187
Cdd:cd17959 82 ELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 145332383 188 FKDQIYDIFQLLPPKIQVGVFSATMPPEALEITRKFMSKPVRI 230
Cdd:cd17959 162 FAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
40-230 |
1.92e-41 |
|
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and PRP28 homolog) is involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation. Diseases associated with DDX23 include distal hereditary motor neuropathy, type II. DDX23 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350703 [Multi-domain] Cd Length: 220 Bit Score: 145.54 E-value: 1.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 40 LLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVLQQLDFSLIQC--------QALVLAPTRELAQ 111
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDeetkddgpYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 112 QIEKVMRALGDYLGVKVHACVGGTSVREDQRILQAGVHVVVGTPGRVFDMLKRQSLRADNIKMFVLDEADEMLSRGFKDQ 191
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 145332383 192 IYDIFQLLPPKI--------------------QVGVFSATMPPEALEITRKFMSKPVRI 230
Cdd:cd17945 161 VTKILDAMPVSNkkpdteeaeklaasgkhryrQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
35-230 |
3.75e-41 |
|
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: 144.83 E-value: 3.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 35 GLQENLLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVLQQldfslIQCQ----------ALVLA 104
Cdd:cd17953 18 GLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRH-----IKDQrpvkpgegpiGLIMA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 105 PTRELAQQIEKVMRALGDYLGVKVHACVGGTSVREDQRILQAGVHVVVGTPGRVFDMLKRQSLRADNIK---MFVLDEAD 181
Cdd:cd17953 93 PTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNGRVTNLRrvtYVVLDEAD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 145332383 182 EMLSRGFKDQIYDIFQLLPPKIQVGVFSATMPPEALEITRKFMSKPVRI 230
Cdd:cd17953 173 RMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
29-224 |
1.04e-40 |
|
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DEAD-box helicases are a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350810 [Multi-domain] Cd Length: 264 Bit Score: 145.11 E-value: 1.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 29 ESFDAMGLQENLLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVLQQL--------DFSLIQC-Q 99
Cdd:cd18052 43 LTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMmkegltasSFSEVQEpQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 100 ALVLAPTRELAQQIEKVMRALGDYLGVKVHACVGGTSVREDQRILQAGVHVVVGTPGRVFDMLKRQSLRADNIKMFVLDE 179
Cdd:cd18052 123 ALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 145332383 180 ADEMLSRGFKDQIYDIFQLL--PPKI--QVGVFSATMPPEALEITRKFM 224
Cdd:cd18052 203 ADRMLDMGFGPEIRKLVSEPgmPSKEdrQTLMFSATFPEEIQRLAAEFL 251
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
40-230 |
1.64e-40 |
|
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: 142.30 E-value: 1.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 40 LLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVLQQLDFSLIQCQALVLAPTRELAQQIEKVMRA 119
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 120 LGD-YLGVKVHACVGGTSVREDQRILQAGVHVVVGTPGRVFDMLKRQSLRADNIKMFVLDEADEMLSRGFKDQIYDIFQL 198
Cdd:cd17962 81 LMKgLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILEN 160
|
170 180 190
....*....|....*....|....*....|..
gi 145332383 199 LPPKIQVGVFSATMPPEALEITRKFMSKPVRI 230
Cdd:cd17962 161 ISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
40-230 |
6.11e-40 |
|
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: 141.01 E-value: 6.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 40 LLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVLQQL-DFSLIQCQ----ALVLAPTRELAQQIE 114
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHImDQRELEKGegpiAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 115 KVMRALGDYLGVKVHACVGGTSVREDQRILQAGVHVVVGTPGRVFDMLKRQSLRADNIKMFVLDEADEMLSRGFKDQIYD 194
Cdd:cd17952 81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 145332383 195 IFQLLPPKIQVGVFSATMPPEALEITRKFMSKPVRI 230
Cdd:cd17952 161 IVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
40-230 |
6.96e-40 |
|
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350718 [Multi-domain] Cd Length: 202 Bit Score: 140.79 E-value: 6.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 40 LLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVLQQL-----DFSLIQCQALVLAPTRELAQQIE 114
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrkaNLKKGQVGALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 115 KVMRALGDYLGVKVHA--CVGGTSVRED-QRILQAGVHVVVGTPGRVFDMLKRQSLRAD--NIKMFVLDEADEMLSRGFK 189
Cdd:cd17960 81 EVLQSFLEHHLPKLKCqlLIGGTNVEEDvKKFKRNGPNILVGTPGRLEELLSRKADKVKvkSLEVLVLDEADRLLDLGFE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 145332383 190 DQIYDIFQLLPPKIQVGVFSATMPPEALEITRKFMSKPVRI 230
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
31-228 |
1.58e-39 |
|
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: 140.15 E-value: 1.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 31 FDAMGLQENLLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVLQQLdfsliqcQALVLAPTRELA 110
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV-------VALILEPSRELA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 111 QQIEKVMRALGDYL---GVKVHACVGGTSVREDQRILQAGVHVVVGTPGRVFDMLKRQSLRADNIKMFVLDEADEMLSRG 187
Cdd:cd17938 74 EQTYNCIENFKKYLdnpKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 145332383 188 FKDQIYDIFQLLPP------KIQVGVFSATM-PPEALEITRKFMSKPV 228
Cdd:cd17938 154 NLETINRIYNRIPKitsdgkRLQVIVCSATLhSFEVKKLADKIMHFPT 201
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
40-212 |
2.95e-38 |
|
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: 137.76 E-value: 2.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 40 LLRGIYAYGFEKPSAIQQRGI-VPFCKGLDVIQQAQSGTGKTATF----CSGVLQQLDFSLIQ-----CQALVLAPTREL 109
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALpAAIRDGKDVIGAAETGSGKTLAFgipiLERLLSQKSSNGVGgkqkpLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 110 AQQIEKVMRALGDYLGVKVHACVGGTSVREDQRILQAGVHVVVGTPGRVFDML-KRQSL--RADNIKMFVLDEADEMLSR 186
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIqEGNEHlaNLKSLRFLVLDEADRMLEK 160
|
170 180 190
....*....|....*....|....*....|...
gi 145332383 187 GFKDQIYDIFQLLP-------PKIQVGVFSATM 212
Cdd:cd17946 161 GHFAELEKILELLNkdragkkRKRQTFVFSATL 193
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
36-228 |
2.42e-37 |
|
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: 134.25 E-value: 2.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 36 LQENLLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVLQQ-LDFSLIQC-----QALVLAPTREL 109
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKiLKAKAESGeeqgtRALILVPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 110 AQQIEKVMRALGDYLG--VKVHACVGGTSVREDQRILQAGVHVVVGTPGRVFDMLKRQSLRA-DNIKMFVLDEADEMLSR 186
Cdd:cd17961 81 AQQVSKVLEQLTAYCRkdVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLlSTLKYLVIDEADLVLSY 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 145332383 187 GFKDQIYDIFQLLPPKIQVGVFSATMPPEALEITRKFMSKPV 228
Cdd:cd17961 161 GYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
40-232 |
1.54e-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: 131.94 E-value: 1.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 40 LLRGIYAYGFEKPSAIQqRGIVPF-CKGLDVIQQAQSGTGKTATFCSGVLQQLDFSLIQC--QALVLAPTRELAQQIEKV 116
Cdd:cd17957 1 LLNNLEESGYREPTPIQ-MQAIPIlLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKKglRALILAPTRELASQIYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 117 MRALGDYLGVKVHACVGGTSVR-EDQRILQAGVHVVVGTPGRVFDMLKRQSLRADNIKMFVLDEADEMLSRGFKDQIYDI 195
Cdd:cd17957 80 LLKLSKGTGLRIVLLSKSLEAKaKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEI 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 145332383 196 FQLLP-PKIQVGVFSATMPPEALEITRKFMSKPVRILV 232
Cdd:cd17957 160 LAACTnPNLQRSLFSATIPSEVEELARSVMKDPIRIIV 197
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
40-230 |
1.71e-36 |
|
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: 131.72 E-value: 1.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 40 LLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFC---------SGVLQQLDFSLiqcqALVLAPTRELA 110
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLlpaivhinaQPPLERGDGPI----VLVLAPTRELA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 111 QQIEKVMRALGDYLGVKVHACVGGTSVREDQRILQAGVHVVVGTPGRVFDMLKRQSLRADNIKMFVLDEADEMLSRGFKD 190
Cdd:cd17966 77 QQIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 145332383 191 QIYDIFQLLPPKIQVGVFSATMPPEALEITRKFMSKPVRI 230
Cdd:cd17966 157 QIRKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
29-238 |
2.06e-36 |
|
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: 132.84 E-value: 2.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 29 ESFDAMGLQENLLRGIYAYGFEKPSAIQQRGIvPFCKG---LDVIQQAQSGTGKTATFCSGVLQQLDFSLIQCQALVLAP 105
Cdd:cd18048 18 KSFEELHLKEELLRGIYAMGFNRPSKIQENAL-PMMLAdppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLSP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 106 TRELAQQIEKVMRALGDY-LGVKVHACVGGTSVREDQRILQagvHVVVGTPGRVFD-MLKRQSLRADNIKMFVLDEADEM 183
Cdd:cd18048 97 TFELALQTGKVVEEMGKFcVGIQVIYAIRGNRPGKGTDIEA---QIVIGTPGTVLDwCFKLRLIDVTNISVFVLDEADVM 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 145332383 184 LS-RGFKDQIYDIFQLLPPKIQVGVFSATMPPEALEITRKFMSKPVRILVKRDELT 238
Cdd:cd18048 174 INvQGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
40-230 |
2.26e-35 |
|
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: 129.00 E-value: 2.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 40 LLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVL-----QQLDFSLIQCQ---ALVLAPTRELAQ 111
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLImfaleQEKKLPFIKGEgpyGLIVCPSRELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 112 QIEKVMRAL------GDYLGVKVHACVGGTSVREDQRILQAGVHVVVGTPGRVFDMLKRQSLRADNIKMFVLDEADEMLS 185
Cdd:cd17951 81 QTHEVIEYYckalqeGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 145332383 186 RGFKDQIYDIFQLLPPKIQVGVFSATMPPEALEITRKFMSKPVRI 230
Cdd:cd17951 161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
21-234 |
3.06e-34 |
|
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD box, X isoform, or DDX14) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. This protein has multiple conserved domains and is thought to play roles in both the nucleus and cytoplasm. Nuclear roles include transcriptional regulation, mRNP assembly, pre-mRNA splicing, and mRNA export. In the cytoplasm, this protein is thought to be involved in translation, cellular signaling, and viral replication. Misregulation of this gene has been implicated in tumorigenesis. Diseases associated with DDX3 include mental retardation, X-linked 102 and agenesis of the corpus callosum, with facial anomalies and robin sequence. DDX3 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350809 [Multi-domain] Cd Length: 249 Bit Score: 127.46 E-value: 3.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 21 FTSYDDVH------------ESFDAMGLQENLLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVL 88
Cdd:cd18051 1 FDKYEDIPveatgencpphiETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 89 QQL-----DFSLIQCQ-----------ALVLAPTRELAQQIEKVMRALGdYLGvKVHACV--GGTSVREDQRILQAGVHV 150
Cdd:cd18051 81 SQIyeqgpGESLPSESgyygrrkqyplALVLAPTRELASQIYDEARKFA-YRS-RVRPCVvyGGADIGQQMRDLERGCHL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 151 VVGTPGRVFDMLKRQSLRADNIKMFVLDEADEMLSRGFKDQIYDIFQ--LLPPK--IQVGVFSATMPPEALEITRKFMSK 226
Cdd:cd18051 159 LVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEqdTMPPTgeRQTLMFSATFPKEIQMLARDFLDN 238
|
....*...
gi 145332383 227 PVRILVKR 234
Cdd:cd18051 239 YIFLAVGR 246
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
254-363 |
1.73e-33 |
|
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: 120.78 E-value: 1.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 254 WKLETLCDLYETLAITQSVIFVNTRRKVDwlTDKMRSR-DHTVSATHGDMDQNTRDIIMREFRSGSSRVLITTDLLARGI 332
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLE--AELLLEKeGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
|
90 100 110
....*....|....*....|....*....|.
gi 145332383 333 DVQQVSLVINFDLPTQPENYLHRIGRSGRFG 363
Cdd:pfam00271 79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
41-211 |
3.48e-33 |
|
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein and is activated by Myc protein. DDX18 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350700 [Multi-domain] Cd Length: 198 Bit Score: 123.24 E-value: 3.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 41 LRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFC---SGVLQQLDFSLIQCQA-LVLAPTRELAQQIEKV 116
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLipaIELLYKLKFKPRNGTGvIIISPTRELALQIYGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 117 MRALGDYLGVKVHACVGGTSVREDQRILQAGVHVVVGTPGRVFDMLKRQS-LRADNIKMFVLDEADEMLSRGFKDQIYDI 195
Cdd:cd17942 82 AKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKgFLYKNLQCLIIDEADRILEIGFEEEMRQI 161
|
170
....*....|....*.
gi 145332383 196 FQLLPPKIQVGVFSAT 211
Cdd:cd17942 162 IKLLPKRRQTMLFSAT 177
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
41-232 |
2.55e-32 |
|
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: 120.86 E-value: 2.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 41 LRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVLQQLDF----SLIQCQALVLAPTRELAQQIEKV 116
Cdd:cd17941 2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRerwtPEDGLGALIISPTRELAMQIFEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 117 MRALGDYLGVKVHACVGGTSVREDQ-RIlqAGVHVVVGTPGRVFD-MLKRQSLRADNIKMFVLDEADEMLSRGFKDQIYD 194
Cdd:cd17941 82 LRKVGKYHSFSAGLIIGGKDVKEEKeRI--NRMNILVCTPGRLLQhMDETPGFDTSNLQMLVLDEADRILDMGFKETLDA 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 145332383 195 IFQLLPPKIQVGVFSATMPPEALEITRKFMSKPVRILV 232
Cdd:cd17941 160 IVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
40-230 |
3.06e-32 |
|
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: 120.65 E-value: 3.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 40 LLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVLQQLDFSLIQCQ------ALVLAPTRELAQQI 113
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPREqrngpgVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 114 EKVMRALgDYLGVKVhACVGGTSVREDQ-RILQAGVHVVVGTPGRVFDMLKRQSLRADNIKMFVLDEADEMLSRGFKDQI 192
Cdd:cd17958 81 EAECSKY-SYKGLKS-VCVYGGGNRNEQiEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQI 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 145332383 193 YDIFQLLPPKIQVGVFSATMPPEALEITRKFMSKPVRI 230
Cdd:cd17958 159 RKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
48-230 |
2.98e-31 |
|
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: 118.46 E-value: 2.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 48 GFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVLQQL--DFSLIQ----CQALVLAPTRELAQQIEKVMRALG 121
Cdd:cd17949 10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLlsLEPRVDrsdgTLALVLVPTRELALQIYEVLEKLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 122 DylgvKVHACV-----GGTSVR-EDQRiLQAGVHVVVGTPGRVFDMLKR-QSLRADNIKMFVLDEADEMLSRGFKDQIYD 194
Cdd:cd17949 90 K----PFHWIVpgyliGGEKRKsEKAR-LRKGVNILIATPGRLLDHLKNtQSFDVSNLRWLVLDEADRLLDMGFEKDITK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 145332383 195 IFQLL-------------PPKIQVGVFSATMPPEALEITRKFMSKPVRI 230
Cdd:cd17949 165 ILELLddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
29-227 |
9.65e-29 |
|
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: 111.35 E-value: 9.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 29 ESFDAMGLQENLLRGIYAYGFEKPSAIQQRGIvPFCKG---LDVIQQAQSGTGKTATFCSGVLQQLDFSLIQCQALVLAP 105
Cdd:cd18047 1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENAL-PLMLAeppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 106 TRELAQQIEKVMRALGD-YLGVKVHACVGGTSVREDQRILQagvHVVVGTPGRVFD-MLKRQSLRADNIKMFVLDEADEM 183
Cdd:cd18047 80 TYELALQTGKVIEQMGKfYPELKLAYAVRGNKLERGQKISE---QIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEADVM 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 145332383 184 L-SRGFKDQIYDIFQLLPPKIQVGVFSATMPPEALEITRKFMSKP 227
Cdd:cd18047 157 IaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
31-230 |
7.29e-28 |
|
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, G17P1, or HUMP68) is involved in pathways that include the alteration of RNA structures, plays a role as a coregulator of transcription, a regulator of splicing, and in the processing of small noncoding RNAs. It synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. Dysregulation of this gene may play a role in cancer development. DDX5 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350807 [Multi-domain] Cd Length: 234 Bit Score: 109.71 E-value: 7.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 31 FDAMGLQENLLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFC---------SGVLQQLDFSLIqcqaL 101
Cdd:cd18049 26 FYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLlpaivhinhQPFLERGDGPIC----L 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 102 VLAPTRELAQQIEKVMRALGDYLGVKVHACVGGTSVREDQRILQAGVHVVVGTPGRVFDMLKRQSLRADNIKMFVLDEAD 181
Cdd:cd18049 102 VLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEAD 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 145332383 182 EMLSRGFKDQIYDIFQLLPPKIQVGVFSATMPPEALEITRKFMSKPVRI 230
Cdd:cd18049 182 RMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHI 230
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
282-363 |
4.52e-27 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 102.68 E-value: 4.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 282 DWLTDKMRSRDHTVSATHGDMDQNTRDIIMREFRSGSSRVLITTDLLARGIDVQQVSLVINFDLPTQPENYLHRIGRSGR 361
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 145332383 362 FG 363
Cdd:smart00490 81 AG 82
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
55-226 |
6.53e-26 |
|
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: 103.77 E-value: 6.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 55 IQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVLQQLDFSLIQC------QALVLAPTRELAQQIEKVMRALGDYLGVkv 128
Cdd:cd17944 16 IQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRkrgrapKVLVLAPTRELANQVTKDFKDITRKLSV-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 129 hACV-GGTSVREDQRILQAGVHVVVGTPGRVFDMLKRQSLRADNIKMFVLDEADEMLSRGFKDQIYDIFQLLPPK----- 202
Cdd:cd17944 94 -ACFyGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSVSYKKdsedn 172
|
170 180
....*....|....*....|....
gi 145332383 203 IQVGVFSATMPPEALEITRKFMSK 226
Cdd:cd17944 173 PQTLLFSATCPDWVYNVAKKYMKS 196
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
36-219 |
1.16e-25 |
|
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350706 [Multi-domain] Cd Length: 231 Bit Score: 103.60 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 36 LQENLLRgiyaYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVLQQLDFSLIQCQ-------ALVLAPTRE 108
Cdd:cd17948 1 LVEILQR----QGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEgpfnaprGLVITPSRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 109 LAQQIEKVMRALGDYLGVKVHACVGGTSVREDQRILQAGVHVVVGTPGRVFDMLKRQSLRADNIKMFVLDEADEMLSRGF 188
Cdd:cd17948 77 LAEQIGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 145332383 189 KDQIYDI---FQL----------LPPKIQVGVFSATMPPEALEI 219
Cdd:cd17948 157 NEKLSHFlrrFPLasrrsentdgLDPGTQLVLVSATMPSGVGEV 200
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
49-230 |
3.27e-25 |
|
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: 103.55 E-value: 3.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 49 FEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVLQQLDFSLIQCQA-----LVLAPTRELAQQIEKVMRALGDY 123
Cdd:cd18050 82 FKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGdgpicLVLAPTRELAQQVQQVADDYGKS 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 124 LGVKVHACVGGTSVREDQRILQAGVHVVVGTPGRVFDMLKRQSLRADNIKMFVLDEADEMLSRGFKDQIYDIFQLLPPKI 203
Cdd:cd18050 162 SRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDR 241
|
170 180
....*....|....*....|....*..
gi 145332383 204 QVGVFSATMPPEALEITRKFMSKPVRI 230
Cdd:cd18050 242 QTLMWSATWPKEVRQLAEDFLRDYVQI 268
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
68-211 |
4.20e-20 |
|
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: 85.92 E-value: 4.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 68 DVIQQAQSGTGKTATFCSGVLQQLDfsLIQCQALVLAPTRELAQQIEKVMRALGDyLGVKVHACVGGTSVREDQRILQAG 147
Cdd:cd00046 3 NVLITAPTGSGKTLAALLAALLLLL--KKGKKVLVLVPTKALALQTAERLRELFG-PGIRVAVLVGGSSAEEREKNKLGD 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145332383 148 VHVVVGTPGRVFDMLKRQ-SLRADNIKMFVLDEADEMLSRGFKDQIYD--IFQLLPPKIQVGVFSAT 211
Cdd:cd00046 80 ADIIIATPDMLLNLLLREdRLFLKDLKLIIVDEAHALLIDSRGALILDlaVRKAGLKNAQVILLSAT 146
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
52-233 |
6.63e-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: 79.21 E-value: 6.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 52 PSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVLQQL-DFSLIQCQALVLAPTRELAQQIEKVMRALGDYLGVKVHA 130
Cdd:cd17956 22 PWLLPSSKSTPPYRPGDLCVSAPTGSGKTLAYVLPIVQALsKRVVPRLRALIVVPTKELVQQVYKVFESLCKGTGLKVVS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 131 CVGGTSVREDQRILQAGVH--------VVVGTPGRVFDMLKRQ---SLraDNIKMFVLDEADEMLSRGFKDqiydifqlL 199
Cdd:cd17956 102 LSGQKSFKKEQKLLLVDTSgrylsrvdILVATPGRLVDHLNSTpgfTL--KHLRFLVIDEADRLLNQSFQD--------W 171
|
170 180 190
....*....|....*....|....*....|....
gi 145332383 200 PPKIQVGVFSATMPPEALEITRKFMSKPVRILVK 233
Cdd:cd17956 172 LETVMKALGRPTAPDLGSFGDANLLERSVRPLQK 205
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
76-379 |
2.15e-14 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 74.68 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 76 GTGKTATFcSGVLQQLdfsLIQCQALVLAPTRELAQQ-IEKVMRALGDYLGvkvhacvgGTSVREDQRilqagvHVVVGT 154
Cdd:COG1061 110 GTGKTVLA-LALAAEL---LRGKRVLVLVPRRELLEQwAEELRRFLGDPLA--------GGGKKDSDA------PITVAT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 155 PGRVFDMLKRQSLRaDNIKMFVLDEADEMLSRGFKDqiydIFQLLPPKIQVGvFSATmpPE---------------ALEI 219
Cdd:COG1061 172 YQSLARRAHLDELG-DRFGLVIIDEAHHAGAPSYRR----ILEAFPAAYRLG-LTAT--PFrsdgreillflfdgiVYEY 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 220 T-----RKFMSKPVRILVKRDELTLEG-----IKQFYVN--VEKEEWKLETLCDLYETLA-ITQSVIFVNTRRKVDWLTD 286
Cdd:COG1061 244 SlkeaiEDGYLAPPEYYGIRVDLTDERaeydaLSERLREalAADAERKDKILRELLREHPdDRKTLVFCSSVDHAEALAE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 287 KMRSRDHTVSATHGDMDQNTRDIIMREFRSGSSRVLITTDLLARGIDVQQVSLVINFDlPTQ-PENYLHRIGR---SGRF 362
Cdd:COG1061 324 LLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLR-PTGsPREFIQRLGRglrPAPG 402
|
330
....*....|....*..
gi 145332383 363 GRKGVAINFVTRDDERM 379
Cdd:COG1061 403 KEDALVYDFVGNDVPVL 419
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
73-230 |
1.16e-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: 70.10 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 73 AQSGTGKTATFCSGVLQQL------DF-----------SLIQCQALVLAPTRELAQQIEKVMRALGDY--LGVKVHACVG 133
Cdd:cd17965 68 AETGSGKTLAYLAPLLDYLkrqeqePFeeaeeeyesakDTGRPRSVILVPTHELVEQVYSVLKKLSHTvkLGIKTFSSGF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 134 GTSVREDQRILQAGVHVVVGTPGrvfdmlKRQSLRADNIKMF------VLDEADEMLSRGFKDQIYDIFQLLPPKIQVGV 207
Cdd:cd17965 148 GPSYQRLQLAFKGRIDILVTTPG------KLASLAKSRPKILsrvthlVVDEADTLFDRSFLQDTTSIIKRAPKLKHLIL 221
|
170 180
....*....|....*....|...
gi 145332383 208 FSATMPPEALEITRKFMSKPVRI 230
Cdd:cd17965 222 CSATIPKEFDKTLRKLFPDVVRI 244
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
35-376 |
5.18e-13 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 70.63 E-value: 5.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 35 GLQENLLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGVLQqldfSLIQ---CQALVLAPTRELAQ 111
Cdd:COG1205 40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLE----ALLEdpgATALYLYPTKALAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 112 -QIEKvMRALGDYLGVKVHACV--GGTSVREDQRILQAGvHVVVGTPgrvfDMLKRQSLRAD--------NIKMFVLDEA 180
Cdd:COG1205 116 dQLRR-LRELAEALGLGVRVATydGDTPPEERRWIREHP-DIVLTNP----DMLHYGLLPHHtrwarffrNLRYVVIDEA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 181 demlsrgfkdQIYDifqllppkiqvGVF---------------------------SATM--PPEALEitrKFMSKPVRiL 231
Cdd:COG1205 190 ----------HTYR-----------GVFgshvanvlrrlrricrhygsdpqfilaSATIgnPAEHAE---RLTGRPVT-V 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 232 VKRD--------------ELTLEGIKQFYVnvekeewkLETlCDLYETLAI--TQSVIFVNTRRKV----DWLTDKMRSR 291
Cdd:COG1205 245 VDEDgsprgertfvlwnpPLVDDGIRRSAL--------AEA-ARLLADLVRegLRTLVFTRSRRGAellaRYARRALREP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 292 DHT--VSATHGDMDQNTRDIIMREFRSGSSRVLITTDLLARGIDVQQVSLVINFDLPTQPENYLHRIGRSGRFGRKGVAI 369
Cdd:COG1205 316 DLAdrVAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV 395
|
....*..
gi 145332383 370 nFVTRDD 376
Cdd:COG1205 396 -LVAGDD 401
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
157-380 |
1.57e-12 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 68.63 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 157 RVFDMLKRQslradNIKMFVLDEA--------D---EMLsrgfkdQIYDIFQLLPpKIQVGVFSATMPPEA-LEITRKF- 223
Cdd:COG0514 122 RFLELLRRL-----KISLFAIDEAhcisqwghDfrpDYR------RLGELRERLP-NVPVLALTATATPRVrADIAEQLg 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 224 MSKPVRIL--VKRDELTLEgIKQFYVNvEKEEWKLETLCDLYETLAItqsvIFVNTRRKVDWLTDKMRSRDHTVSATHGD 301
Cdd:COG0514 190 LEDPRVFVgsFDRPNLRLE-VVPKPPD-DKLAQLLDFLKEHPGGSGI----VYCLSRKKVEELAEWLREAGIRAAAYHAG 263
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145332383 302 MDQNTRDIIMREFRSGSSRVLITTDLLARGIDVQQVSLVINFDLPTQPENYLHRIGRSGRFGRKGVAINFVTRDDERML 380
Cdd:COG0514 264 LDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQ 342
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
262-361 |
7.01e-11 |
|
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: 59.97 E-value: 7.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 262 LYETLAITQSVIFVNTRRKVDWLTDKMRSR------DHTVSATHGDMDQNTRDIIMREFRSGSSRVLITTDLLARGIDVQ 335
Cdd:cd18796 32 IFLLERHKSTLVFTNTRSQAERLAQRLRELcpdrvpPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIG 111
|
90 100
....*....|....*....|....*.
gi 145332383 336 QVSLVINFDLPTQPENYLHRIGRSGR 361
Cdd:cd18796 112 DVDLVIQIGSPKSVARLLQRLGRSGH 137
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
246-358 |
2.21e-10 |
|
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: 58.37 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 246 YVNVEKEEWKLETLCDLYETLAITQSVIFVNTR---------------RKVDWLTDKMRSRDHTVSATHGDMDQNTRDII 310
Cdd:cd18802 3 IVVIPKLQKLIEILREYFPKTPDFRGIIFVERRatavvlsrllkehpsTLAFIRCGFLIGRGNSSQRKRSLMTQRKQKET 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 145332383 311 MREFRSGSSRVLITTDLLARGIDVQQVSLVINFDLPTQPENYLHRIGR 358
Cdd:cd18802 83 LDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR 130
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
272-371 |
2.22e-10 |
|
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: 57.99 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 272 VIFVNTRRKVDWLTDKMRSRDHTVSATHGDMDQNTRDIIMREFRSGSSRVLITTDLLARGIDVQQVSLVINFDLPTQPEN 351
Cdd:cd18794 34 IIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMES 113
|
90 100
....*....|....*....|
gi 145332383 352 YLHRIGRSGRFGRKGVAINF 371
Cdd:cd18794 114 YYQESGRAGRDGLPSECILF 133
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
130-371 |
8.57e-10 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 60.50 E-value: 8.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 130 ACVGGTSVREDQRILQAGVH-----VVVGTPGRVF--DMLKRqsLRADNIKMFVLDEADEMLSRG--FKDQIYDIFQLLP 200
Cdd:PRK11057 93 ACLNSTQTREQQLEVMAGCRtgqikLLYIAPERLMmdNFLEH--LAHWNPALLAVDEAHCISQWGhdFRPEYAALGQLRQ 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 201 --PKIQVGVFSATmppeALEITRKFMskpVRILVKRDELTLegIKQF------YVNVEKEEwKLETLCDLYETLAITQSV 272
Cdd:PRK11057 171 rfPTLPFMALTAT----ADDTTRQDI---VRLLGLNDPLIQ--ISSFdrpnirYTLVEKFK-PLDQLMRYVQEQRGKSGI 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 273 IFVNTRRKVDWLTDKMRSRDHTVSATHGDMDQNTRDIIMREFRSGSSRVLITTDLLARGIDVQQVSLVINFDLPTQPENY 352
Cdd:PRK11057 241 IYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESY 320
|
250
....*....|....*....
gi 145332383 353 LHRIGRSGRFGRKGVAINF 371
Cdd:PRK11057 321 YQETGRAGRDGLPAEAMLF 339
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
255-363 |
6.80e-09 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 54.02 E-value: 6.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 255 KLETLCDLYETLAITQ--SVIFVNTRRKVDWLTDKMRSRDHTVSATHGDMDQNTRDIIMREFRSGSS--RVLITTDLLAR 330
Cdd:cd18793 12 KLEALLELLEELREPGekVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDirVFLLSTKAGGV 91
|
90 100 110
....*....|....*....|....*....|...
gi 145332383 331 GIDVQQVSLVINFDLPTQPENYLHRIGRSGRFG 363
Cdd:cd18793 92 GLNLTAANRVILYDPWWNPAVEEQAIDRAHRIG 124
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
272-380 |
8.10e-08 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 54.46 E-value: 8.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 272 VIFVNTRRKVDWLTDKMRSRDHTVSATHGDMDQNTRDIIMREFRSGSS--RVLITTDLLARGIDVQQVSLVINFDLPTQP 349
Cdd:COG0553 553 LVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEapVFLISLKAGGEGLNLTAADHVIHYDLWWNP 632
|
90 100 110
....*....|....*....|....*....|....*
gi 145332383 350 ENYLHRIGRSGRFG-RKGV-AINFVTRD--DERML 380
Cdd:COG0553 633 AVEEQAIDRAHRIGqTRDVqVYKLVAEGtiEEKIL 667
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
321-372 |
1.51e-07 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 48.47 E-value: 1.51e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 145332383 321 VLITTDLLARGIDVQQVSLVINFDLPTQPENYLHRIGRSGRFG-RKGVAINFV 372
Cdd:cd18785 25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGkDEGEVILFV 77
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
100-400 |
2.61e-07 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 52.59 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 100 ALVLAPTRELAQQI-EKVMRALGDyLGVKVHACVGGTsVREDQRILQAgvHVVVGTPGRvFDMLKRQSLR-ADNIKMFVL 177
Cdd:COG1204 69 ALYIVPLRALASEKyREFKRDFEE-LGIKVGVSTGDY-DSDDEWLGRY--DILVATPEK-LDSLLRNGPSwLRDVDLVVV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 178 DEA----DEmlSRGFK-DQIYDIFQLLPPKIQVgVF-SATMP-PEalEITRKFMSKPVRIL---VKRDELTLEGIKQFYV 247
Cdd:COG1204 144 DEAhlidDE--SRGPTlEVLLARLRRLNPEAQI-VAlSATIGnAE--EIAEWLDAELVKSDwrpVPLNEGVLYDGVLRFD 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 248 NVEKEEwkLETLCDL-YETLAI-TQSVIFVNTRRKV------------DWLTDKMRSR------------DHT------- 294
Cdd:COG1204 219 DGSRRS--KDPTLALaLDLLEEgGQVLVFVSSRRDAeslakkladelkRRLTPEEREEleelaeellevsEEThtnekla 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 295 ------VSATHGDMDQNTRDIIMREFRSGSSRVLITTDLLARGI----------DVQQVSLVinfDLPtqPENYLHRIGR 358
Cdd:COG1204 297 dclekgVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVnlparrviirDTKRGGMV---PIP--VLEFKQMAGR 371
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 145332383 359 SGRFGR--KGVAInFVTRDDERMLFDIQKFYNVVVEELPSNVAD 400
Cdd:COG1204 372 AGRPGYdpYGEAI-LVAKSSDEADELFERYILGEPEPIRSKLAN 414
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
66-180 |
1.74e-06 |
|
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: 47.96 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 66 GLDVIQQAQSGTGKTATFCSGVLQQLdFSLIQCQALVLAPTRELAQQIEKVMRALGDYL--GVKVHACVGGTSVREDQRI 143
Cdd:cd17923 15 GRSVVVTTGTASGKSLCYQLPILEAL-LRDPGSRALYLYPTKALAQDQLRSLRELLEQLglGIRVATYDGDTPREERRAI 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 145332383 144 LQAGVHVVVGTPgrvfDMLKRQSLRAD--------NIKMFVLDEA 180
Cdd:cd17923 94 IRNPPRILLTNP----DMLHYALLPHHdrwarflrNLRYVVLDEA 134
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
302-366 |
2.10e-05 |
|
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: 43.88 E-value: 2.10e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145332383 302 MDQNTRDIIMREFRSGSSRVLITTDLLARGIDVQQVSLVINFDLPTQPENYLHRIGRSGRfGRKG 366
Cdd:cd18801 74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR-KRQG 137
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
272-377 |
3.64e-05 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 45.88 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 272 VIFVNTRRKVDWLTDKMRSRDHTV------SATHGD--MDQNTRDIIMREFRSGSSRVLITTDLLARGIDVQQVSLVINF 343
Cdd:COG1111 357 IVFTQYRDTAEMIVEFLSEPGIKAgrfvgqASKEGDkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFY 436
|
90 100 110
....*....|....*....|....*....|....*.
gi 145332383 344 DLPTQPENYLHRIGRSGRFGRKGVAInFVTRD--DE 377
Cdd:COG1111 437 EPVPSEIRSIQRKGRTGRKREGRVVV-LIAKGtrDE 471
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
290-360 |
5.70e-05 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 45.69 E-value: 5.70e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145332383 290 SRDHtvsatHGDMDQNTRDIIMREFRSGSSRVLITTDLLARGIDVQQVSLVINFDLPTQPENYLHRIGRSG 360
Cdd:PRK09751 304 ARSH-----HGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
73-180 |
7.52e-05 |
|
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: 43.02 E-value: 7.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 73 AQSGTGKT--ATFCsgVLQqldfSLIQCQ--ALVLAPTRELAQQIEKVMRALGDYLGVKVHACVGGTSVReDQRILQAgv 148
Cdd:cd17921 24 APTSSGKTliAELA--ILR----ALATSGgkAVYIAPTRALVNQKEADLRERFGPLGKNVGLLTGDPSVN-KLLLAEA-- 94
|
90 100 110
....*....|....*....|....*....|....
gi 145332383 149 HVVVGTPGRvFDML--KRQSLRADNIKMFVLDEA 180
Cdd:cd17921 95 DILVATPEK-LDLLlrNGGERLIQDVRLVVVDEA 127
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
272-365 |
1.02e-04 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 44.50 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 272 VIFVNTRRKVDWLTDKMRSRDHTVSATHGDMDQNTRDIIMREFRSGSSRVLITTDLLARGIDVQQVSLVINFDLPTQPEN 351
Cdd:PLN03137 684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEG 763
|
90
....*....|....
gi 145332383 352 YLHRIGRSGRFGRK 365
Cdd:PLN03137 764 YHQECGRAGRDGQR 777
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
270-369 |
1.71e-04 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 41.47 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 270 QSVIFVNTRRKVDWLTDKMRSRD-------HTVSATHGDMDQNTRDIIMREFRSGSSRVLITTDLLARGIDVQQVSLVIN 342
Cdd:cd18797 37 KTIVFCRSRKLAELLLRYLKARLveegplaSKVASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVL 116
|
90 100
....*....|....*....|....*..
gi 145332383 343 FDLPTQPENYLHRIGRSGRFGRKGVAI 369
Cdd:cd18797 117 AGYPGSLASLWQQAGRAGRRGKDSLVI 143
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
299-385 |
2.77e-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: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 299 HGDMDQNTRDIIMREFRSGSSRVLITTDLLARGIDVQQVSLVINFDLPTQPENYLHRI-GRSGRFGRKGVAInFVTRDDE 377
Cdd:cd18810 58 HGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIERADKFGLAQLYQLrGRVGRSKERAYAY-FLYPDQK 136
|
....*...
gi 145332383 378 RMLFDIQK 385
Cdd:cd18810 137 KLTEDALK 144
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
273-376 |
2.82e-04 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 43.17 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 273 IFVNTRRKVDWLTDKMRSR----DHTVSATHGDMDQNTRDIIMREFRSGSSRVLITT---DLlarGIDVQQVSLVINFDL 345
Cdd:COG1201 277 VFTNTRSQAERLFQRLNELnpedALPIAAHHGSLSREQRLEVEEALKAGELRAVVATsslEL---GIDIGDVDLVIQVGS 353
|
90 100 110
....*....|....*....|....*....|...
gi 145332383 346 PTQPENYLHRIGRSG-RFGRKGVAINFVT-RDD 376
Cdd:COG1201 354 PKSVARLLQRIGRAGhRVGEVSKGRLVPThRDE 386
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
299-379 |
4.70e-04 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350179 [Multi-domain] Cd Length: 160 Bit Score: 40.33 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 299 HGDMDQNTRDIIMREFRSGSSRVLITTDLLARGIDVQQVSLVINFDlptqPENY----LHRI-GRSGRFGRKGVAInFVT 373
Cdd:cd18792 67 HGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIED----ADRFglsqLHQLrGRVGRGKHQSYCY-LLY 141
|
....*.
gi 145332383 374 RDDERM 379
Cdd:cd18792 142 PDPKKL 147
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
270-369 |
6.16e-04 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350182 [Multi-domain] Cd Length: 154 Bit Score: 39.84 E-value: 6.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 270 QSVIFVNTRRKVDWLTDKMRSrdhtVSATHGDMDQNTRDIIMREFRSGSSRVLITTDLLARGI----------DVQQVSL 339
Cdd:cd18795 45 PVLVFCSSRKECEKTAKDLAG----IAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVnlpartviikGTQRYDG 120
|
90 100 110
....*....|....*....|....*....|..
gi 145332383 340 VINFDLPtqPENYLHRIGRSGR--FGRKGVAI 369
Cdd:cd18795 121 KGYRELS--PLEYLQMIGRAGRpgFDTRGEAI 150
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
68-218 |
7.15e-04 |
|
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpB belongs to 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: 438711 [Multi-domain] Cd Length: 174 Bit Score: 40.01 E-value: 7.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 68 DVIQQAQSGTGKTATFCSGVLQQLDFSliQCQALVLAPTRELAQQIEKVM-RALGDYLGVKVhacvgGTSVREDQRILQA 146
Cdd:cd17990 19 QVVLEAPPGAGKTTRVPLALLAELWIA--GGKIIVLEPRRVAARAAARRLaTLLGEAPGETV-----GYRVRGESRVGRR 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145332383 147 gVHVVVGTPGRVFDMLKR-QSLraDNIKMFVLDEADEM-----LSRGFkdqIYDIFQLLPPKIQVGVFSATMPPEALE 218
Cdd:cd17990 92 -TRVEVVTEGVLLRRLQRdPEL--SGVGAVILDEFHERsldadLALAL---LLEVQQLLRDDLRLLAMSATLDGDGLA 163
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
76-180 |
9.24e-04 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 40.33 E-value: 9.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 76 GTGKTatFCSGVL------QQLDFSLIQCQALVLAPTRELAQQIEKVMRalgDYLGVKVHACVGGTSV--REDQRILQ-- 145
Cdd:cd18034 26 GSGKT--LIAVMLikemgeLNRKEKNPKKRAVFLVPTVPLVAQQAEAIR---SHTDLKVGEYSGEMGVdkWTKERWKEel 100
|
90 100 110
....*....|....*....|....*....|....*
gi 145332383 146 AGVHVVVGTPGRVFDMLKRQSLRADNIKMFVLDEA 180
Cdd:cd18034 101 EKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
277-344 |
1.22e-03 |
|
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: 39.54 E-value: 1.22e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145332383 277 TRRKVDWLTDKMRSRDHTVSATHGDMDQNTRDIIMREFRSGSSRVLITTDLLARGIDVQQVSLVINFD 344
Cdd:cd18790 36 TKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILD 103
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
207-394 |
1.41e-03 |
|
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
Pssm-ID: 187770 [Multi-domain] Cd Length: 353 Bit Score: 40.49 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 207 VFSATMPpealEITRKFMSKpVRILVKRDELTLEGIKQFYVNVEKEEWK-----LETLCDLYetLAITQSVIFVNTRRKV 281
Cdd:cd09639 159 LMSATLP----KFLKEYAEK-IGYVEENEPLDLKPNERAPFIKIESDKVgeissLERLLEFI--KKGGSVAIIVNTVDRA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 282 DWLTDKMRSRDHTVSAT--HGDMDQNTR----DIIMREFRSGSSRVLITTdllargiDVQQVSLVINFDL----PTQPEN 351
Cdd:cd09639 232 QEFYQQLKEKGPEEEIMliHSRFTEKDRakkeAELLLEFKKSEKFVIVAT-------QVIEASLDISVDVmiteLAPIDS 304
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 145332383 352 YLHRIGRSGRFGRKGVAINFVTRD-DERmlfDIQKFYNVVVEEL 394
Cdd:cd09639 305 LIQRLGRLHRYGEKNGEEVYIITDaPDG---KGQKPYPYDLVER 345
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
299-361 |
1.54e-03 |
|
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: 38.86 E-value: 1.54e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145332383 299 HGDMDQNTRDIIMREFRSGSSRVLITTDLLARGIDVQQVSLVINFDlptqPENY----LHRI-GRSGR 361
Cdd:cd18811 68 HGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIED----AERFglsqLHQLrGRVGR 131
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
67-154 |
2.38e-03 |
|
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: 38.55 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 67 LDVIQQAQSGTGKTATFCSGVLQQLDFSLiqcQALVLAPTRELAQQIEKVMRALgdYLGVKVHACVGGTSvredQRILQa 146
Cdd:cd17918 37 MDRLLSGDVGSGKTLVALGAALLAYKNGK---QVAILVPTEILAHQHYEEARKF--LPFINVELVTGGTK----AQILS- 106
|
....*...
gi 145332383 147 GVHVVVGT 154
Cdd:cd17918 107 GISLLVGT 114
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
262-376 |
2.98e-03 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 39.87 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 262 LYETLA--I---TQSVIFVNTR----RKVDWLTDKMRSR--DHTVSATHGDMDQNTRDIIMREFRSGSSRVLITTDLLAR 330
Cdd:PRK13767 273 LYETLHelIkehRTTLIFTNTRsgaeRVLYNLRKRFPEEydEDNIGAHHSSLSREVRLEVEEKLKRGELKVVVSSTSLEL 352
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 145332383 331 GIDVQQVSLVINFDLPTQPENYLHRIGRSG-RFGR--KGVAInFVTRDD 376
Cdd:PRK13767 353 GIDIGYIDLVVLLGSPKSVSRLLQRIGRAGhRLGEvsKGRII-VVDRDD 400
|
|
| PRK05580 |
PRK05580 |
primosome assembly protein PriA; Validated |
290-369 |
4.31e-03 |
|
primosome assembly protein PriA; Validated
Pssm-ID: 235514 [Multi-domain] Cd Length: 679 Bit Score: 39.37 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 290 SRDHTvsATHGDMDQntrdiIMREFRSGSSRVLITTDLLARGIDVQQVSLV--INFDLptqpenYLHR------------ 355
Cdd:PRK05580 459 DRDTT--RRKGALEQ-----LLAQFARGEADILIGTQMLAKGHDFPNVTLVgvLDADL------GLFSpdfrasertfql 525
|
90
....*....|....*...
gi 145332383 356 ----IGRSGRFGRKGVAI 369
Cdd:PRK05580 526 ltqvAGRAGRAEKPGEVL 543
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
273-358 |
9.37e-03 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350186 [Multi-domain] Cd Length: 116 Bit Score: 36.00 E-value: 9.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 273 IFVNTRRKVDWLTDKMRSRD-HTVSATHGDMDQNTRD--IIMREFRSGSSRVLITTDLLARGIDVQQVSLVInFDLPTQP 349
Cdd:cd18799 11 IFCVSIEHAEFMAEAFNEAGiDAVALNSDYSDRERGDeaLILLFFGELKPPILVTVDLLTTGVDIPEVDNVV-FLRPTES 89
|
90
....*....|
gi 145332383 350 EN-YLHRIGR 358
Cdd:cd18799 90 RTlFLQMLGR 99
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
51-179 |
9.71e-03 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350794 [Multi-domain] Cd Length: 204 Bit Score: 37.07 E-value: 9.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332383 51 KPSAIQQRGIVPFCKGLDVIQQAQSGTGKT--ATF-CSGVLQQLDFSLIQCQALVLAPTRELA-QQIEKVMRALGDylGV 126
Cdd:cd18036 2 ELRNYQLELVLPALRGKNTIICAPTGSGKTrvAVYiCRHHLEKRRSAGEKGRVVVLVNKVPLVeQQLEKFFKYFRK--GY 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 145332383 127 KVHACVGGTSVREDQRILQAGVHVVVGTPGRVFDML----KRQSLRADNIKMFVLDE 179
Cdd:cd18036 80 KVTGLSGDSSHKVSFGQIVKASDVIICTPQILINNLlsgrEEERVYLSDFSLLIFDE 136
|
|
| |
