|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
22-474 |
0e+00 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 686.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 22 GSSRGGPPPGKKFG----------NPGDRLRKKRWDLDELPKFEKNFYSEHLEVQRMSQYDVEEYRRKKEIT-VRGSGCP 90
Cdd:PTZ00110 47 GFRPGYGNYSGGYGgfgmnsygssTLGKRLQPIDWKSINLVPFEKNFYKEHPEVSALSSKEVDEIRKEKEITiIAGENVP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 91 KPVTNFHQAQFPQYVIDVLMQQNFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHINHQPYLERGDGPIC 170
Cdd:PTZ00110 127 KPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGDGPIV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 171 LVLAPTRELAQQVQQVAYDYGKSSRIKSTCVYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEA 250
Cdd:PTZ00110 207 LVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 251 DRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDY-VQINVGALELSANHNILQIVDVCMESEKDNKL 329
Cdd:PTZ00110 287 DRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEEpVHVNVGSLDLTACHNIKQEVFVVEEHEKRGKL 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 330 IQLMEEIMAEKeNKTIIFVETKKRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLSEFRSGKAPILIATDVASRGLDVED 409
Cdd:PTZ00110 367 KMLLQRIMRDG-DKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKD 445
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896683539 410 VKFVINYDYPNSSEDYIHRIGRTARSTNKGTAYTFFTPGNLRQARELIRVLEEARQAINPKLLQL 474
Cdd:PTZ00110 446 VKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKL 510
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
33-303 |
0e+00 |
|
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: 575.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 33 KFGNPGDRLRKKRWDLDELPKFEKNFYSEHLEVQRMSQYDVEEYRRKKEITVRGSGCPKPVTNFHQAQFPQYVIDVLMQQ 112
Cdd:cd18050 1 KFGNPGERLRKKKWDLSELPKFEKNFYVEHPEVARMTQYDVEELRRKKEITIRGVGCPKPVFAFHQANFPQYVMDVLLDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 113 NFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQVQQVAYDYGK 192
Cdd:cd18050 81 NFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQVQQVADDYGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 193 SSRIKSTCVYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPD 272
Cdd:cd18050 161 SSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPD 240
|
250 260 270
....*....|....*....|....*....|.
gi 1896683539 273 RQTLMWSATWPKEVRQLAEDFLKDYVQINVG 303
Cdd:cd18050 241 RQTLMWSATWPKEVRQLAEDFLRDYVQINIG 271
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
72-304 |
5.04e-172 |
|
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: 484.51 E-value: 5.04e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 72 DVEEYRRKKEITVRGSGCPKPVTNFHQAQFPQYVIDVLMQQNFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLP 151
Cdd:cd18049 2 EVEQYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 152 AIVHINHQPYLERGDGPICLVLAPTRELAQQVQQVAYDYGKSSRIKSTCVYGGAPKGPQIRDLERGVEICIATPGRLIDF 231
Cdd:cd18049 82 AIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDF 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1896683539 232 LEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYVQINVGA 304
Cdd:cd18049 162 LEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGA 234
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
94-470 |
6.28e-163 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 468.86 E-value: 6.28e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 94 TNFHQAQFPQYVIDVLMQQNFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHINHqpylERGDGPICLVL 173
Cdd:COG0513 2 MSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDP----SRPRAPQALIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 174 APTRELAQQVQQVAYDYGKSSRIKSTCVYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRM 253
Cdd:COG0513 78 APTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 254 LDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYVQINVGALELSANhNILQIVDVCMESEKDNKLIQLM 333
Cdd:COG0513 158 LDMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAE-TIEQRYYLVDKRDKLELLRRLL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 334 EEimaEKENKTIIFVETKKRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLSEFRSGKAPILIATDVASRGLDVEDVKFV 413
Cdd:COG0513 237 RD---EDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHV 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1896683539 414 INYDYPNSSEDYIHRIGRTARSTNKGTAYTFFTPgnlRQARELIRVLEEARQAINPK 470
Cdd:COG0513 314 INYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTP---DERRLLRAIEKLIGQKIEEE 367
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
105-301 |
1.63e-153 |
|
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: 436.03 E-value: 1.63e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 105 VIDVLMQQNFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQVQ 184
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGDGPIVLVLAPTRELAQQIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 185 QVAYDYGKSSRIKSTCVYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRK 264
Cdd:cd17966 81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1896683539 265 IVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYVQIN 301
Cdd:cd17966 161 IVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
105-300 |
7.25e-107 |
|
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: 317.08 E-value: 7.25e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 105 VIDVLMQQNFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHINHQPyLERGDGPICLVLAPTRELAQQVQ 184
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEP-KKKGRGPQALVLAPTRELAMQIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 185 QVAYDYGKSSRIKSTCVYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRK 264
Cdd:cd00268 80 EVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 1896683539 265 IVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYVQI 300
Cdd:cd00268 160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
83-300 |
2.38e-102 |
|
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: 306.61 E-value: 2.38e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 83 TVRGSGCPKPVTNFHQAQFPQYVIDVLMQQNFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHINHQPYL 162
Cdd:cd17953 1 KVRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 163 ERGDGPICLVLAPTRELAQQVQQVAYDYGKSSRIKSTCVYGGAPKGPQIRDLERGVEICIATPGRLIDFLEA--GK-TNL 239
Cdd:cd17953 81 KPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTAnnGRvTNL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1896683539 240 RRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYVQI 300
Cdd:cd17953 161 RRVTYVVLDEADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
102-466 |
2.66e-99 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 307.50 E-value: 2.66e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 102 PQYVIDVLMQQNFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHINHQPYlergdGPICLVLAPTRELAQ 181
Cdd:PRK11776 12 PPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRF-----RVQALVLCPTRELAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 182 QVqqvaydyGKSSR--------IKSTCVYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRM 253
Cdd:PRK11776 87 QV-------AKEIRrlarfipnIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 254 LDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYVQInvgalELSANHNILQIVDVCMESEKDNKLIQLM 333
Cdd:PRK11776 160 LDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEV-----KVESTHDLPAIEQRFYEVSPDERLPALQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 334 EEIMAEKENKTIIFVETKKRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLSEFRSGKAPILIATDVASRGLDVEDVKFV 413
Cdd:PRK11776 235 RLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAV 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1896683539 414 INYDYPNSSEDYIHRIGRTARSTNKGTAYTFFTPgnlrqaRELIRV--LEEARQA 466
Cdd:PRK11776 315 INYELARDPEVHVHRIGRTGRAGSKGLALSLVAP------EEMQRAnaIEDYLGR 363
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
105-300 |
3.21e-95 |
|
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: 287.39 E-value: 3.21e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 105 VIDVLMQQNFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQVQ 184
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGEGPIAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 185 QVAYDYGKSSRIKSTCVYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRK 264
Cdd:cd17952 81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1896683539 265 IVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYVQI 300
Cdd:cd17952 161 IVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
94-441 |
6.66e-88 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 277.21 E-value: 6.66e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 94 TNFHQAQFPQYVIDVLMQQNFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHINHQPylERGDGPI-CLV 172
Cdd:PRK11192 1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFP--RRKSGPPrILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 173 LAPTRELAQQVQQVAYDYGKSSRIKSTCVYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADR 252
Cdd:PRK11192 79 LTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 253 MLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKE-VRQLAEDFLKDYVQINVGAlELSANHNILQIVDVCmeSEKDNKLIQ 331
Cdd:PRK11192 159 MLDMGFAQDIETIAAETRWRKQTLLFSATLEGDaVQDFAERLLNDPVEVEAEP-SRRERKKIHQWYYRA--DDLEHKTAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 332 LMEEIMAEKENKTIIFVETKKRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLSEFRSGKAPILIATDVASRGLDVEDVK 411
Cdd:PRK11192 236 LCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVS 315
|
330 340 350
....*....|....*....|....*....|
gi 1896683539 412 FVINYDYPNSSEDYIHRIGRTARSTNKGTA 441
Cdd:PRK11192 316 HVINFDMPRSADTYLHRIGRTGRAGRKGTA 345
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
111-467 |
7.01e-86 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 272.45 E-value: 7.01e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 111 QQNFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHINHQPYLERGDGPI-CLVLAPTRELAQQVQQVAYD 189
Cdd:PRK10590 18 EQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVrALILTPTRELAAQIGENVRD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 190 YGKSSRIKSTCVYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQI 269
Cdd:PRK10590 98 YSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFIHDIRRVLAKL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 270 RPDRQTLMWSATWPKEVRQLAEDFLKDYVQINVgALELSANHNILQIVDVCMESEKDNKLIQLmeeIMAEKENKTIIFVE 349
Cdd:PRK10590 178 PAKRQNLLFSATFSDDIKALAEKLLHNPLEIEV-ARRNTASEQVTQHVHFVDKKRKRELLSQM---IGKGNWQQVLVFTR 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 350 TKKRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLSEFRSGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYIHRI 429
Cdd:PRK10590 254 TKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPEDYVHRI 333
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1896683539 430 GRTARSTNKGTAYTFFTPGNLRQARELIRVL--EEARQAI 467
Cdd:PRK10590 334 GRTGRAAATGEALSLVCVDEHKLLRDIEKLLkkEIPRIAI 373
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
107-303 |
1.89e-85 |
|
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: 263.19 E-value: 1.89e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 107 DVLMQQ----NFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHINHQP-----YLERGDGPICLVLAPTR 177
Cdd:cd17967 9 ELLLENikraGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGppsvgRGRRKAYPSALILAPTR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 178 ELAQQVQQVAYDYGKSSRIKSTCVYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMG 257
Cdd:cd17967 89 ELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDEADRMLDMG 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1896683539 258 FEPQIRKIVDQ----IRPDRQTLMWSATWPKEVRQLAEDFLKDYVQINVG 303
Cdd:cd17967 169 FEPQIRKIVEHpdmpPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVG 218
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
67-472 |
1.16e-81 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 263.57 E-value: 1.16e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 67 RMSQYDVEEYRRKKEITVRGSGCPKPVTNFHQAQFPQYVIDVLMQQNFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTL 146
Cdd:PLN00206 94 GLSSSQAELLRRKLEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 147 SYLLPAIVH---INHQPYLERgDGPICLVLAPTRELAQQVQQVAYDYGKSSRIKSTCVYGGAPKGPQIRDLERGVEICIA 223
Cdd:PLN00206 174 SFLVPIISRcctIRSGHPSEQ-RNPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVG 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 224 TPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVdQIRPDRQTLMWSATWPKEVRQLAEDFLKDYVQINVG 303
Cdd:PLN00206 253 TPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIF-QALSQPQVLLFSATVSPEVEKFASSLAKDIILISIG 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 304 ALElSANHNILQIVdVCMES-EKDNKLIqlmeEIMAEKEN---KTIIFVETKKRCDDLTRRMRR-DGWPAMCIHGDKSQP 378
Cdd:PLN00206 332 NPN-RPNKAVKQLA-IWVETkQKKQKLF----DILKSKQHfkpPAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMK 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 379 ERDWVLSEFRSGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYIHRIGRTARSTNKGTAYTFFTPGNLRQARELIR 458
Cdd:PLN00206 406 ERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVA 485
|
410
....*....|....
gi 1896683539 459 VLEEARQAInPKLL 472
Cdd:PLN00206 486 LLKSSGAAI-PREL 498
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
105-300 |
2.29e-79 |
|
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: 246.61 E-value: 2.29e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 105 VIDVLMQQNFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHINHQPYL-ERGDGPICLVLAPTRELAQQV 183
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPrEQRNGPGVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 184 QQVAYDYgKSSRIKSTCVYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIR 263
Cdd:cd17958 81 EAECSKY-SYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 1896683539 264 KIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYVQI 300
Cdd:cd17958 160 KILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
86-303 |
1.09e-77 |
|
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: 244.18 E-value: 1.09e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 86 GSGCPKPVTNFHQAQFPQYVIDVLMQQNFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHINHQ---PYL 162
Cdd:cd18051 13 GENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQgpgESL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 163 ERGDG--------PICLVLAPTRELAQQVQQVAYDYGKSSRIKSTCVYGGAPKGPQIRDLERGVEICIATPGRLIDFLEA 234
Cdd:cd18051 93 PSESGyygrrkqyPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLER 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1896683539 235 GKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQI----RPDRQTLMWSATWPKEVRQLAEDFLKDYVQINVG 303
Cdd:cd18051 173 GKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDtmppTGERQTLMFSATFPKEIQMLARDFLDNYIFLAVG 245
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
102-444 |
3.83e-77 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 248.73 E-value: 3.83e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 102 PQyVIDVLMQQNFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHI--NHQPYLERGDGPICLVLAPTREL 179
Cdd:PRK04837 17 PQ-VVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLlsHPAPEDRKVNQPRALIMAPTREL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 180 AQQVQQVAYDYGKSSRIKSTCVYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFE 259
Cdd:PRK04837 96 AVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMFDLGFI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 260 PQIRKIVDQIRP--DRQTLMWSATWPKEVRQLAEDFLKD--YVQInvgALELSANHNILQIVDVCMESEKDNKLIQLMEE 335
Cdd:PRK04837 176 KDIRWLFRRMPPanQRLNMLFSATLSYRVRELAFEHMNNpeYVEV---EPEQKTGHRIKEELFYPSNEEKMRLLQTLIEE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 336 imaEKENKTIIFVETKKRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLSEFRSGKAPILIATDVASRGLDVEDVKFVIN 415
Cdd:PRK04837 253 ---EWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFN 329
|
330 340
....*....|....*....|....*....
gi 1896683539 416 YDYPNSSEDYIHRIGRTARSTNKGTAYTF 444
Cdd:PRK04837 330 YDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
105-461 |
2.89e-75 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 249.77 E-value: 2.89e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 105 VIDVLMQQNFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHINhqPYLErgdGPICLVLAPTRELAQQVQ 184
Cdd:PRK11634 17 ILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLD--PELK---APQILVLAPTRELAVQVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 185 QVAYDYGKSSR-IKSTCVYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIR 263
Cdd:PRK11634 92 EAMTDFSKHMRgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFIEDVE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 264 KIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYVQINVGAlELSANHNILQIVDVCMESEKDNKLIQLMEeimAEKENK 343
Cdd:PRK11634 172 TIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQS-SVTTRPDISQSYWTVWGMRKNEALVRFLE---AEDFDA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 344 TIIFVETKKRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLSEFRSGKAPILIATDVASRGLDVEDVKFVINYDYPNSSE 423
Cdd:PRK11634 248 AIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSE 327
|
330 340 350
....*....|....*....|....*....|....*...
gi 1896683539 424 DYIHRIGRTARSTNKGTAYTFFTpgnlRQARELIRVLE 461
Cdd:PRK11634 328 SYVHRIGRTGRAGRAGRALLFVE----NRERRLLRNIE 361
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
84-303 |
3.53e-75 |
|
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: 238.33 E-value: 3.53e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 84 VRGSGCPKPVTNFHQAQFPQYVIDVLMQQNFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHINHQ---- 159
Cdd:cd18052 33 VTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEglta 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 160 PYLERGDGPICLVLAPTRELAQQVQQVAYDYGKSSRIKSTCVYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNL 239
Cdd:cd18052 113 SSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISL 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1896683539 240 RRCTYLVLDEADRMLDMGFEPQIRKIVDQI----RPDRQTLMWSATWPKEVRQLAEDFLK-DYVQINVG 303
Cdd:cd18052 193 SKLKYLILDEADRMLDMGFGPEIRKLVSEPgmpsKEDRQTLMFSATFPEEIQRLAAEFLKeDYLFLTVG 261
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
91-444 |
1.73e-74 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 246.40 E-value: 1.73e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 91 KPVTNFHQAQFPQY--VIDVLMQQNFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHINHQPYL--ERGD 166
Cdd:PRK04537 4 KPLTDLTFSSFDLHpaLLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALadRKPE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 167 GPICLVLAPTRELAQQVQQVAYDYGKSSRIKSTCVYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKT-NLRRCTYL 245
Cdd:PRK04537 84 DPRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVvSLHACEIC 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 246 VLDEADRMLDMGFEPQIRKIVDQI--RPDRQTLMWSATWPKEVRQLAEDFLKDYVQINVGALELSANHnILQIVDVCMES 323
Cdd:PRK04537 164 VLDEADRMFDLGFIKDIRFLLRRMpeRGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAAR-VRQRIYFPADE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 324 EKdnklIQLMEEIMAEKEN-KTIIFVETKKRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLSEFRSGKAPILIATDVAS 402
Cdd:PRK04537 243 EK----QTLLLGLLSRSEGaRTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAA 318
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1896683539 403 RGLDVEDVKFVINYDYPNSSEDYIHRIGRTARSTNKGTAYTF 444
Cdd:PRK04537 319 RGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISF 360
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
114-458 |
5.10e-74 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 240.11 E-value: 5.10e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 114 FKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHINHqpylergDGPIC--LVLAPTRELAQQVQQVAYDYG 191
Cdd:PTZ00424 48 FEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDY-------DLNACqaLILAPTRELAQQIQKVVLALG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 192 KSSRIKSTCVYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRP 271
Cdd:PTZ00424 121 DYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFKGQIYDVFKKLPP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 272 DRQTLMWSATWPKEVRQLAEDFLKDYVQINVGALELSAnHNILQI-VDVCMESEKDNKLIQLMEEIMAekeNKTIIFVET 350
Cdd:PTZ00424 201 DVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTL-EGIRQFyVAVEKEEWKFDTLCDLYETLTI---TQAIIYCNT 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 351 KKRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLSEFRSGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYIHRIG 430
Cdd:PTZ00424 277 RRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIG 356
|
330 340
....*....|....*....|....*...
gi 1896683539 431 RTARSTNKGTAYTFFTPGNLRQARELIR 458
Cdd:PTZ00424 357 RSGRFGRKGVAINFVTPDDIEQLKEIER 384
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
94-444 |
6.06e-73 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 239.43 E-value: 6.06e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 94 TNFHQAQFPQYVIDVLMQQNFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHINHQPYLE---RGDgPIC 170
Cdd:PRK01297 87 TRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKeryMGE-PRA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 171 LVLAPTRELAQQVQQVAYDYGKSSRIKSTCVYGGAPKGPQIRDLE-RGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDE 249
Cdd:PRK01297 166 LIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 250 ADRMLDMGFEPQIRKIVDQIRP--DRQTLMWSATWPKEVRQLAEDFLKDYVQINVGAlELSANHNILQIVDVCMESEKDN 327
Cdd:PRK01297 246 ADRMLDMGFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEP-ENVASDTVEQHVYAVAGSDKYK 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 328 KLIQLMEEimaEKENKTIIFVETKKRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLSEFRSGKAPILIATDVASRGLDV 407
Cdd:PRK01297 325 LLYNLVTQ---NPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHI 401
|
330 340 350
....*....|....*....|....*....|....*..
gi 1896683539 408 EDVKFVINYDYPNSSEDYIHRIGRTARSTNKGTAYTF 444
Cdd:PRK01297 402 DGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISF 438
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
105-300 |
1.20e-70 |
|
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: 224.89 E-value: 1.20e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 105 VIDVLMQQNFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHINHQP---YLERGDGPICLVLAPTRELAQ 181
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPpldEETKDDGPYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 182 QVQQVAYDYGKSSRIKSTCVYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQ 261
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1896683539 262 IRKIVDQI-----RPD---------------RQTLMWSATWPKEVRQLAEDFLKDYVQI 300
Cdd:cd17945 161 VTKILDAMpvsnkKPDteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
118-289 |
1.49e-63 |
|
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: 204.40 E-value: 1.49e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 118 TAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHINhqpylERGDGPICLVLAPTRELAQQVQQVAYDYGKSSRIK 197
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALD-----KLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 198 STCVYGGAPKGPQIRDLeRGVEICIATPGRLIDFLEAGKTnLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLM 277
Cdd:pfam00270 76 VASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILL 153
|
170
....*....|..
gi 1896683539 278 WSATWPKEVRQL 289
Cdd:pfam00270 154 LSATLPRNLEDL 165
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
105-301 |
2.88e-63 |
|
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: 205.27 E-value: 2.88e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 105 VIDVLMQQNFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHINHQ----PYLeRGDGPICLVLAPTRELA 180
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQekklPFI-KGEGPYGLIVCPSRELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 181 QQVQQVAYDY------GKSSRIKSTCVYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRML 254
Cdd:cd17951 80 RQTHEVIEYYckalqeGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1896683539 255 DMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYVQIN 301
Cdd:cd17951 160 DMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTVN 206
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
313-445 |
1.17e-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: 193.11 E-value: 1.17e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 313 ILQIVDVCMESEKDNKLIQLmeEIMAEKENKTIIFVETKKRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLSEFRSGKA 392
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLL--LLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKV 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1896683539 393 PILIATDVASRGLDVEDVKFVINYDYPNSSEDYIHRIGRTARSTNKGTAYTFF 445
Cdd:cd18787 79 RVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
105-300 |
9.09e-57 |
|
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: 188.29 E-value: 9.09e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 105 VIDVLMQQ----NFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVH-INHQPYLergdgpICLVLAPTREL 179
Cdd:cd17954 7 VCEELCEAceklGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQAlLENPQRF------FALVLAPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 180 AQQVQQVAYDYGKSSRIKSTCVYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKT-NLRRCTYLVLDEADRMLDMGF 258
Cdd:cd17954 81 AQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKGfSLKSLKFLVMDEADRLLNMDF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1896683539 259 EPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYVQI 300
Cdd:cd17954 161 EPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
113-316 |
1.55e-56 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 187.70 E-value: 1.55e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 113 NFKEPTAIQAQGFPLALSG-RDMVGIAQTGSGKTLSYLLPAIVHinhqpyLERGDGPICLVLAPTRELAQQVQQVAYDYG 191
Cdd:smart00487 5 GFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEA------LKRGKGGRVLVLVPTRELAEQWAEELKKLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 192 KSSRIKSTCVYGGAPKGPQIRDLERGV-EICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIR 270
Cdd:smart00487 79 PSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1896683539 271 PDRQTLMWSATWPKEVRQLAEDFLKDYVQINVGAlelSANHNILQI 316
Cdd:smart00487 159 KNVQLLLLSATPPEEIENLLELFLNDPVFIDVGF---TPLEPIEQF 201
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
105-300 |
8.70e-55 |
|
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: 183.17 E-value: 8.70e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 105 VIDVLMQQ-NFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHI-NHQPYLERGDGPICLVLAPTRELAQQ 182
Cdd:cd17949 1 LVSHLKSKmGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLlSLEPRVDRSDGTLALVLVPTRELALQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 183 VQQVAYDYGKSSR-IKSTCVYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKT-NLRRCTYLVLDEADRMLDMGFEP 260
Cdd:cd17949 81 IYEVLEKLLKPFHwIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQSfDVSNLRWLVLDEADRLLDMGFEK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1896683539 261 QIRKIVDQIR-------------PDRQTLMWSATWPKEVRQLAEDFLKDYVQI 300
Cdd:cd17949 161 DITKILELLDdkrskaggekskpSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
105-301 |
3.45e-53 |
|
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: 178.93 E-value: 3.45e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 105 VIDVLMQQNFKEPTAIQAQGFPLALS-GRDMVGIAQTGSGKTLSYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQ- 182
Cdd:cd17964 5 LLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGVSALIISPTRELALQi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 183 ---VQQVAYdygKSSRIKSTCVYGGAPKGPQIRDLER-GVEICIATPGRLIDFLE--AGKTNLRRCTYLVLDEADRMLDM 256
Cdd:cd17964 85 aaeAKKLLQ---GLRKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRLLDM 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1896683539 257 GFEPQIRKIVDQIRP----DRQTLMWSATWPKEVRQLAEDFL-KDYVQIN 301
Cdd:cd17964 162 GFRPDLEQILRHLPEknadPRQTLLFSATVPDEVQQIARLTLkKDYKFID 211
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
109-300 |
5.11e-52 |
|
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ribosomal subunits protein 1 homolog, and probable ATP-dependent RNA helicase DDX27) is involved in the processing of 5.8S and 28S ribosomal RNAs. More specifically, the encoded protein localizes to the nucleolus, where it interacts with the PeBoW complex to ensure proper 3' end formation of 47S rRNA. DDX27 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350705 [Multi-domain] Cd Length: 196 Bit Score: 175.52 E-value: 5.11e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 109 LMQQNFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHINHQPYLERGDGpiCLVLAPTRELAQQVQQVAY 188
Cdd:cd17947 5 LSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAATR--VLVLVPTRELAMQCFSVLQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 189 DYGKSSRIKSTCVYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKT-NLRRCTYLVLDEADRMLDMGFEPQIRKIVD 267
Cdd:cd17947 83 QLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSfDLDSIEILVLDEADRMLEEGFADELKEILR 162
|
170 180 190
....*....|....*....|....*....|...
gi 1896683539 268 QIRPDRQTLMWSATWPKEVRQLAEDFLKDYVQI 300
Cdd:cd17947 163 LCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
109-303 |
1.13e-51 |
|
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: 174.70 E-value: 1.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 109 LMQQNFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHINHQpylERGDGPICLVLAPTRELAQQVQQVAY 188
Cdd:cd17957 5 LEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKP---RKKKGLRALILAPTRELASQIYRELL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 189 DYGKSSRIKSTCVYGG-APKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVD 267
Cdd:cd17957 82 KLSKGTGLRIVLLSKSlEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEILA 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 1896683539 268 QIR-PDRQTLMWSATWPKEVRQLAEDFLKDYVQINVG 303
Cdd:cd17957 162 ACTnPNLQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
102-296 |
2.02e-50 |
|
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: 171.64 E-value: 2.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 102 PQYVIDVLMQQNFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHINHQPYlergdGPICLVLAPTRELAQ 181
Cdd:cd17955 7 SSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPY-----GIFALVLTPTRELAY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 182 QVQQVAYDYGKSSRIKSTCVYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAG---KTNLRRCTYLVLDEADRMLDMGF 258
Cdd:cd17955 82 QIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSddtTKVLSRVKFLVLDEADRLLTGSF 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 1896683539 259 EPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKD 296
Cdd:cd17955 162 EDDLATILSALPPKRQTLLFSATLTDALKALKELFGNK 199
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
109-302 |
2.96e-50 |
|
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: 170.93 E-value: 2.96e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 109 LMQQNFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHINHQPYlERGDGPICLVLAPTRELAQQVQQVAY 188
Cdd:cd17941 5 LKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERW-TPEDGLGALIISPTRELAMQIFEVLR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 189 DYGKSSRIKSTCVYGGapKGPQIrDLER--GVEICIATPGRLIDFLEA----GKTNLRrctYLVLDEADRMLDMGFEPQI 262
Cdd:cd17941 84 KVGKYHSFSAGLIIGG--KDVKE-EKERinRMNILVCTPGRLLQHMDEtpgfDTSNLQ---MLVLDEADRILDMGFKETL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1896683539 263 RKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYVQINV 302
Cdd:cd17941 158 DAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
105-301 |
5.12e-50 |
|
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: 170.56 E-value: 5.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 105 VIDVLMQQNFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHI-NHQPYLergdGPICLVLAPTRELAQQV 183
Cdd:cd17959 12 LLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLkAHSPTV----GARALILSPTRELALQT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 184 QQVAYDYGKSSRIKSTCVYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIR 263
Cdd:cd17959 88 LKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMGFAEQLH 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 1896683539 264 KIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYVQIN 301
Cdd:cd17959 168 EILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
109-290 |
2.46e-48 |
|
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: 165.61 E-value: 2.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 109 LMQQNFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHINHQPYLERgDGPICLVLAPTRELAQQVQQVAY 188
Cdd:cd17942 5 IEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPR-NGTGVIIISPTRELALQIYGVAK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 189 DYGKSSRIKSTCVYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGK----TNLRrctYLVLDEADRMLDMGFEPQIRK 264
Cdd:cd17942 84 ELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKgflyKNLQ---CLIIDEADRILEIGFEEEMRQ 160
|
170 180
....*....|....*....|....*.
gi 1896683539 265 IVDQIRPDRQTLMWSATWPKEVRQLA 290
Cdd:cd17942 161 IIKLLPKRRQTMLFSATQTRKVEDLA 186
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
117-300 |
1.57e-47 |
|
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: 163.49 E-value: 1.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 117 PTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHInhqpyLERGDGPICLVLAPTRELAQQVQQVAYDYGKSS-R 195
Cdd:cd17962 13 PTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRC-----LTEHRNPSALILTPTRELAVQIEDQAKELMKGLpP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 196 IKSTCVYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQT 275
Cdd:cd17962 88 MKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILENISHDHQT 167
|
170 180
....*....|....*....|....*
gi 1896683539 276 LMWSATWPKEVRQLAEDFLKDYVQI 300
Cdd:cd17962 168 ILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
105-281 |
2.29e-47 |
|
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: 164.33 E-value: 2.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 105 VIDVLMQQNFKEPTAIQAQGFPLALS-GRDMVGIAQTGSGKTLSYLLPAIVHI----NHQPYLERGDGPICLVLAPTREL 179
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLlsqkSSNGVGGKQKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 180 AQQVQQVAYDYGKSSRIKSTCVYGG--APKgpQIRDLERGVEICIATPGRLIDFLEAGKT---NLRRCTYLVLDEADRML 254
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGlaVQK--QERLLKKRPEIVVATPGRLWELIQEGNEhlaNLKSLRFLVLDEADRML 158
|
170 180 190
....*....|....*....|....*....|....*
gi 1896683539 255 DMG-FEpQIRKIVDQI-------RPDRQTLMWSAT 281
Cdd:cd17946 159 EKGhFA-ELEKILELLnkdragkKRKRQTFVFSAT 192
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
105-301 |
1.38e-45 |
|
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: 158.51 E-value: 1.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 105 VIDVLMQQNFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQVQ 184
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKKGQVGALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 185 QVAYDYGK--SSRIKSTCVYGGAPKGPQIRDLER-GVEICIATPGRLIDFLE--AGKTNLRRCTYLVLDEADRMLDMGFE 259
Cdd:cd17960 81 EVLQSFLEhhLPKLKCQLLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLSrkADKVKVKSLEVLVLDEADRLLDLGFE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1896683539 260 PQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYVQIN 301
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRVV 202
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
107-301 |
3.42e-45 |
|
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: 157.46 E-value: 3.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 107 DVLM---QQNFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHINHQPYLERGdgpicLVLAPTRELAQQV 183
Cdd:cd17940 9 ELLMgifEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQA-----LILVPTRELALQT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 184 QQVAYDYGKSSRIKSTCVYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIR 263
Cdd:cd17940 84 SQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQPIIE 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 1896683539 264 KIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYVQIN 301
Cdd:cd17940 164 KILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEIN 201
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
120-301 |
1.92e-39 |
|
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: 142.29 E-value: 1.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 120 IQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAI--VHINHQPyLERGDGPICLVLAPTRELAQQVQQVAYDYGKssRIK 197
Cdd:cd17944 16 IQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIekLQEDQQP-RKRGRAPKVLVLAPTRELANQVTKDFKDITR--KLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 198 STCVYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVD-QIRPDR--- 273
Cdd:cd17944 93 VACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSvSYKKDSedn 172
|
170 180 190
....*....|....*....|....*....|
gi 1896683539 274 -QTLMWSATWPKEVRQLAEDFLKD-YVQIN 301
Cdd:cd17944 173 pQTLLFSATCPDWVYNVAKKYMKSqYEQVD 202
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
111-296 |
2.95e-38 |
|
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: 139.26 E-value: 2.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 111 QQNFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHI-NHQPYLERGDGPICLVLAPTRELAQQVQQVAYD 189
Cdd:cd17961 11 KLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlKAKAESGEEQGTRALILVPTRELAQQVSKVLEQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 190 --YGKSSRIKSTCVYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKT-NLRRCTYLVLDEADRMLDMGFEPQIRKIV 266
Cdd:cd17961 91 ltAYCRKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLlLLSTLKYLVIDEADLVLSYGYEEDLKSLL 170
|
170 180 190
....*....|....*....|....*....|
gi 1896683539 267 DQIRPDRQTLMWSATWPKEVRQLAEDFLKD 296
Cdd:cd17961 171 SYLPKNYQTFLMSATLSEDVEALKKLVLHN 200
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
114-300 |
3.02e-38 |
|
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: 139.00 E-value: 3.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 114 FKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIvhinhQPYLERGDGPICLVLAPTRELAQQVQQVAYDYGKS 193
Cdd:cd17939 17 FEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGAL-----QRIDTTVRETQALVLAPTRELAQQIQKVVKALGDY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 194 SRIKSTCVYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDR 273
Cdd:cd17939 92 MGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQIYDIFQFLPPET 171
|
170 180
....*....|....*....|....*..
gi 1896683539 274 QTLMWSATWPKEVRQLAEDFLKDYVQI 300
Cdd:cd17939 172 QVVLFSATMPHEVLEVTKKFMRDPVRI 198
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
113-300 |
3.20e-38 |
|
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: 138.48 E-value: 3.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 113 NFKEPTAIQAQGFPLALSG--RDMVGIAQTGSGKTLSYLLPAivhinhqpyLERGDG----PICLVLAPTRELAQQVQQV 186
Cdd:cd17963 13 GFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAM---------LSRVDPtlksPQALCLAPTRELARQIGEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 187 AYDYGKSSRIKSTCvyggAPKGPQIRDLERGVE-ICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDM-GFEPQIRK 264
Cdd:cd17963 84 VEKMGKFTGVKVAL----AVPGNDVPRGKKITAqIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGHGDQSIR 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 1896683539 265 IVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYVQI 300
Cdd:cd17963 160 IKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
327-434 |
1.05e-35 |
|
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: 128.87 E-value: 1.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 327 NKLIQLMEEIMAEKENKTIIFVETKKRCDdLTRRMRRDGWPAMCIHGDKSQPERDWVLSEFRSGKAPILIATDVASRGLD 406
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100
....*....|....*....|....*...
gi 1896683539 407 VEDVKFVINYDYPNSSEDYIHRIGRTAR 434
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGR 107
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
114-300 |
7.12e-35 |
|
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: 129.87 E-value: 7.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 114 FKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHINHQPylergDGPICLVLAPTRELAQQVQQVAYDYGKS 193
Cdd:cd18046 19 FEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSL-----KATQALVLAPTRELAQQIQKVVMALGDY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 194 SRIKSTCVYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDR 273
Cdd:cd18046 94 MGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKDQIYDIFQKLPPDT 173
|
170 180
....*....|....*....|....*..
gi 1896683539 274 QTLMWSATWPKEVRQLAEDFLKDYVQI 300
Cdd:cd18046 174 QVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
117-291 |
1.02e-34 |
|
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: 129.36 E-value: 1.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 117 PTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPaIVHInhqpylergdgPICLVLAPTRELAQQVQQVAYDYGK---S 193
Cdd:cd17938 22 PTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLP-VLQI-----------VVALILEPSRELAEQTYNCIENFKKyldN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 194 SRIKSTCVYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQI---- 269
Cdd:cd17938 90 PKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQGNLETINRIYNRIpkit 169
|
170 180
....*....|....*....|....*
gi 1896683539 270 -RPDR-QTLMWSATWPK-EVRQLAE 291
Cdd:cd17938 170 sDGKRlQVIVCSATLHSfEVKKLAD 194
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
105-300 |
1.19e-34 |
|
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: 128.92 E-value: 1.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 105 VIDVLMQQNFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHINhqpyLERGdGPICLVLAPTRELAQQVQ 184
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLD----LERR-HPQVLILAPTREIAVQIH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 185 QVAYDYGKSSRIKSTCVY-GGAPKGPQIRDLeRGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIR 263
Cdd:cd17943 76 DVFKKIGKKLEGLKCEVFiGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVN 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 1896683539 264 KIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYVQI 300
Cdd:cd17943 155 WIFSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLV 191
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
105-292 |
1.45e-34 |
|
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: 129.79 E-value: 1.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 105 VIDVLMQQNFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHINHQPYLERG--DGPICLVLAPTRELAQQ 182
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGpfNAPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 183 VQQVAYDYGKSSRIKSTCVYGGAPKGpQIRDLERG-VEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQ 261
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITGGRTKR-QIRNPHFEeVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1896683539 262 IRKIV-------------DQIRPDRQTLMWSATWPKEVRQLAED 292
Cdd:cd17948 160 LSHFLrrfplasrrsentDGLDPGTQLVLVSATMPSGVGEVLSK 203
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
113-300 |
4.10e-31 |
|
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: 119.49 E-value: 4.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 113 NFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHINhqPYLERgdgPICLVLAPTRELAQQVQQVAYDYGK 192
Cdd:cd18045 18 GFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLD--IQVRE---TQALILSPTRELAVQIQKVLLALGD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 193 SSRIKSTCVYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPD 272
Cdd:cd18045 93 YMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKEQIYDVYRYLPPA 172
|
170 180
....*....|....*....|....*...
gi 1896683539 273 RQTLMWSATWPKEVRQLAEDFLKDYVQI 300
Cdd:cd18045 173 TQVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
114-302 |
1.26e-30 |
|
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: 118.22 E-value: 1.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 114 FKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHINHQPylergdGPI-CLVLAPTRELAQQVQQVAYDYGK 192
Cdd:cd17950 22 FEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVD------GQVsVLVICHTRELAFQISNEYERFSK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 193 S-SRIKSTCVYGGAPKGPQIRDLERGV-EICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRML-DMGFEPQIRKIVDQI 269
Cdd:cd17950 96 YmPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLeQLDMRRDVQEIFRAT 175
|
170 180 190
....*....|....*....|....*....|...
gi 1896683539 270 RPDRQTLMWSATWPKEVRQLAEDFLKDYVQINV 302
Cdd:cd17950 176 PHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
355-434 |
7.80e-28 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 106.14 E-value: 7.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 355 DDLTRRMRRDGWPAMCIHGDKSQPERDWVLSEFRSGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYIHRIGRTAR 434
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
117-259 |
4.55e-23 |
|
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: 97.70 E-value: 4.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 117 PTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPaIVhinhQPYLERGDGPI-CLVLAPTRELAQQVQQV--AYDYGKS 193
Cdd:cd17956 22 PWLLPSSKSTPPYRPGDLCVSAPTGSGKTLAYVLP-IV----QALSKRVVPRLrALIVVPTKELVQQVYKVfeSLCKGTG 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1896683539 194 SRIKSTCvyGG---APKGPQIRDLERG-----VEICIATPGRLIDFLEAGKT----NLRrctYLVLDEADRMLDMGFE 259
Cdd:cd17956 97 LKVVSLS--GQksfKKEQKLLLVDTSGrylsrVDILVATPGRLVDHLNSTPGftlkHLR---FLVIDEADRLLNQSFQ 169
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
138-300 |
5.72e-23 |
|
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: 97.83 E-value: 5.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 138 AQTGSGKTLSYLLPAIVHINHQPYLERGDG------------PICLVLAPTRELAQQVQQVAydygksSRIKSTCVYGGA 205
Cdd:cd17965 68 AETGSGKTLAYLAPLLDYLKRQEQEPFEEAeeeyesakdtgrPRSVILVPTHELVEQVYSVL------KKLSHTVKLGIK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 206 P----KGPQIRDLER----GVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLM 277
Cdd:cd17965 142 TfssgFGPSYQRLQLafkgRIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLIL 221
|
170 180
....*....|....*....|...
gi 1896683539 278 WSATWPKEVRQLAEDFLKDYVQI 300
Cdd:cd17965 222 CSATIPKEFDKTLRKLFPDVVRI 244
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
131-442 |
1.04e-19 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 92.40 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 131 GRDMVGIAQTGSGKTlsYLLPAIVHinhqpylERGDGPICLVLAPTRELAQQVQQvaydygkssRIKStcVYGGAPKGPQ 210
Cdd:COG1061 100 GGRGLVVAPTGTGKT--VLALALAA-------ELLRGKRVLVLVPRRELLEQWAE---------ELRR--FLGDPLAGGG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 211 IRDLERgvEICIATPGRLIDFLEAGKTNlRRCTYLVLDEADRmldmGFEPQIRKIVDQIRPDRQTLMwSAT-------WP 283
Cdd:COG1061 160 KKDSDA--PITVATYQSLARRAHLDELG-DRFGLVIIDEAHH----AGAPSYRRILEAFPAAYRLGL-TATpfrsdgrEI 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 284 KEVR------------QLAEDFLK--DYVQINVGALELSANHNIL-QIVDVCMESEKDNKLiQLMEEIMAE--KENKTII 346
Cdd:COG1061 232 LLFLfdgivyeyslkeAIEDGYLAppEYYGIRVDLTDERAEYDALsERLREALAADAERKD-KILRELLREhpDDRKTLV 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 347 FVETKKRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLSEFRSGKAPILIATDVASRGLDVEDVKFVInYDYPNSSE-DY 425
Cdd:COG1061 311 FCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI-LLRPTGSPrEF 389
|
330
....*....|....*...
gi 1896683539 426 IHRIGRTAR-STNKGTAY 442
Cdd:COG1061 390 IQRLGRGLRpAPGKEDAL 407
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
119-473 |
4.56e-18 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 86.73 E-value: 4.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 119 AIQAqgfplALSGRDMVGIAQTGSGKTLSYLLPAIVhinhqpylerGDGPiCLVLAPTRELAQ-QVQQVaydygKSSRIK 197
Cdd:COG0514 25 IIEA-----VLAGRDALVVMPTGGGKSLCYQLPALL----------LPGL-TLVVSPLIALMKdQVDAL-----RAAGIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 198 STCVYGGAPKGPQ---IRDLERG-VEICIATPGRL-----IDFLEAGKTNLrrctyLVLDEA--------DrmldmgFEP 260
Cdd:COG0514 84 AAFLNSSLSAEERrevLRALRAGeLKLLYVAPERLlnprfLELLRRLKISL-----FAIDEAhcisqwghD------FRP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 261 ---QIRKIVDQIrPDRQTLMWSATWPKEVR-----QLAedfLKDyVQINVGalelSAN-HNI-LQIVDVcmesEKDNKLI 330
Cdd:COG0514 153 dyrRLGELRERL-PNVPVLALTATATPRVRadiaeQLG---LED-PRVFVG----SFDrPNLrLEVVPK----PPDDKLA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 331 QLMEEIMAEKENKTIIFVETKKRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLSEFRSGKAPILIATdVA-SRGLDVED 409
Cdd:COG0514 220 QLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPD 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1896683539 410 VKFVINYDYPNSSEDYIHRIGRTARSTNKGTAYTFFTPGNLRQARELI--RVLEEARQAINPKLLQ 473
Cdd:COG0514 299 VRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIeqSPPDEERKRVERAKLD 364
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
93-308 |
4.47e-17 |
|
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: 80.45 E-value: 4.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 93 VTNFHQAQFPQYVIDVLMQQNFKEPTAIQAQGFPLALSG--RDMVGIAQTGSGKTLSYLLPAIVHINHQPYLergdgPIC 170
Cdd:cd18048 17 VKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLY-----PQC 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 171 LVLAPTRELAQQVQQVAYDYGK-SSRIKSTCVYGG--APKGPQIRdlergVEICIATPGRLIDF-LEAGKTNLRRCTYLV 246
Cdd:cd18048 92 LCLSPTFELALQTGKVVEEMGKfCVGIQVIYAIRGnrPGKGTDIE-----AQIVIGTPGTVLDWcFKLRLIDVTNISVFV 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1896683539 247 LDEADRMLDM-GFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYVQINVGALELS 308
Cdd:cd18048 167 LDEADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
301-438 |
7.74e-16 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 80.54 E-value: 7.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 301 NVGALELSANHNILQIVDVCMESEKDN-KLIQLMEEI----MAEKENKTIIFVETKKRCDDLTRRMRRDGWPAM------ 369
Cdd:COG1111 308 SKASKRLVSDPRFRKAMRLAEEADIEHpKLSKLREILkeqlGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGrfvgqa 387
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1896683539 370 CIHGDK--SQPERDWVLSEFRSGKAPILIATDVASRGLDVEDVKFVINYDyPNSSE-DYIHRIGRTARSTNK 438
Cdd:COG1111 388 SKEGDKglTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYE-PVPSEiRSIQRKGRTGRKREG 458
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
96-296 |
7.89e-14 |
|
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: 70.52 E-value: 7.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 96 FHQAQFPQYVIDVLMQQNFKEPTAIQAQGFPLALSG--RDMVGIAQTGSGKTLSYLLPAIVHINHQPYLERgdgpiCLVL 173
Cdd:cd18047 3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQ-----CLCL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 174 APTRELAQQVQQVAYDYGKSSRiKSTCVYggAPKGPQirdLERGV----EICIATPGRLIDF-LEAGKTNLRRCTYLVLD 248
Cdd:cd18047 78 SPTYELALQTGKVIEQMGKFYP-ELKLAY--AVRGNK---LERGQkiseQIVIGTPGTVLDWcSKLKFIDPKKIKVFVLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1896683539 249 EADRML-DMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKD 296
Cdd:cd18047 152 EADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPD 200
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
128-462 |
1.19e-13 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 73.59 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 128 ALSGRDMVGIAQTGSGKTLSYLLPAIVHinhqpylergDGpICLVLAPTRELAQ-QVQQ-----VAYDYGKS--SRIKST 199
Cdd:PRK11057 37 VLSGRDCLVVMPTGGGKSLCYQIPALVL----------DG-LTLVVSPLISLMKdQVDQllangVAAACLNStqTREQQL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 200 CVYGGAPKGpQIRDLergveicIATPGRLI--DFLEA-GKTNLrrcTYLVLDEADRMLDMG--FEPQIRKIvDQIR---P 271
Cdd:PRK11057 106 EVMAGCRTG-QIKLL-------YIAPERLMmdNFLEHlAHWNP---ALLAVDEAHCISQWGhdFRPEYAAL-GQLRqrfP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 272 DRQTLMWSATWPKEVRQlaedflkDYVQInvgaLELSANHNILQIVDV----CMESEKDNKLIQLMEEIMAEKENKTIIF 347
Cdd:PRK11057 174 TLPFMALTATADDTTRQ-------DIVRL----LGLNDPLIQISSFDRpnirYTLVEKFKPLDQLMRYVQEQRGKSGIIY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 348 VETKKRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLSEFRSGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYIH 427
Cdd:PRK11057 243 CNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQ 322
|
330 340 350
....*....|....*....|....*....|....*
gi 1896683539 428 RIGRTARSTNKGTAYTFFTPGNLRQAReliRVLEE 462
Cdd:PRK11057 323 ETGRAGRDGLPAEAMLFYDPADMAWLR---RCLEE 354
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
318-434 |
3.16e-13 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350181 [Multi-domain] Cd Length: 134 Bit Score: 66.85 E-value: 3.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 318 DVCMESEKDNKLIQLMEEIMAEKENKTIIFVETKKRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLSEFRSGKAPILIA 397
Cdd:cd18794 7 SVRPKDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVA 86
|
90 100 110
....*....|....*....|....*....|....*..
gi 1896683539 398 TDVASRGLDVEDVKFVINYDYPNSSEDYIHRIGRTAR 434
Cdd:cd18794 87 TVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGR 123
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
322-432 |
5.72e-13 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 71.41 E-value: 5.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 322 ESEKDNKLIQLMEEIMAEKEnKTIIFVETKKRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLSEFRSGKAP--ILIATD 399
Cdd:COG0553 531 RSAKLEALLELLEELLAEGE-KVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEApvFLISLK 609
|
90 100 110
....*....|....*....|....*....|....*....
gi 1896683539 400 VASRGLDVEDVKFVINYDYP------NSSEDYIHRIGRT 432
Cdd:COG0553 610 AGGEGLNLTAADHVIHYDLWwnpaveEQAIDRAHRIGQT 648
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
138-281 |
8.13e-12 |
|
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: 63.19 E-value: 8.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 138 AQTGSGKTLSYLLPAIVHINHQpylergdGPICLVLAPTRELAQQVQQVAYDYGKSSrIKSTCVYGGAPKGPQIRDLERG 217
Cdd:cd00046 8 APTGSGKTLAALLAALLLLLKK-------GKKVLVLVPTKALALQTAERLRELFGPG-IRVAVLVGGSSAEEREKNKLGD 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1896683539 218 VEICIATPGRLIDFLEA-GKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQ--IRPDRQTLMWSAT 281
Cdd:cd00046 80 ADIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRkaGLKNAQVILLSAT 146
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
328-437 |
1.79e-11 |
|
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: 61.84 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 328 KLIQLMEEIMAEKEN----KTIIFVETKK-------------------RCDDLTRRMRRDGWPAMcIHGDKSQPErdwVL 384
Cdd:cd18802 8 KLQKLIEILREYFPKtpdfRGIIFVERRAtavvlsrllkehpstlafiRCGFLIGRGNSSQRKRS-LMTQRKQKE---TL 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1896683539 385 SEFRSGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYIHRIGRtARSTN 437
Cdd:cd18802 84 DKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARAPN 135
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
326-430 |
5.84e-10 |
|
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: 57.49 E-value: 5.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 326 DNKLIQLMEEIMAEKEN--KTIIFVETKKRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLSEFRSGKAP--ILIATDVA 401
Cdd:cd18793 10 SGKLEALLELLEELREPgeKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAG 89
|
90 100 110
....*....|....*....|....*....|....*
gi 1896683539 402 SRGLDVEDVKFVINYDYP-NSS-----EDYIHRIG 430
Cdd:cd18793 90 GVGLNLTAANRVILYDPWwNPAveeqaIDRAHRIG 124
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
343-446 |
8.03e-10 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 55.40 E-value: 8.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 343 KTIIFVETKKRCDDLTRRMRrdgwpamcihgdksqperdwvlsefrsgkapILIATDVASRGLDVEDVKFVINYDYPNSS 422
Cdd:cd18785 5 KIIVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDPPSSA 53
|
90 100
....*....|....*....|....
gi 1896683539 423 EDYIHRIGRTARSTNKGTAYTFFT 446
Cdd:cd18785 54 ASYIQRVGRAGRGGKDEGEVILFV 77
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
102-250 |
6.89e-09 |
|
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: 58.31 E-value: 6.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 102 PQYVIDVLMQQNFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHInhqpylERGDGPICLVLAPTRELAQ 181
Cdd:COG1205 42 PPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEAL------LEDPGATALYLYPTKALAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 182 -QVQQV-AYDYGKSSRIKSTCVYGGAPkgPQIRD--LERGvEICIATPgrliDFLEAG--------KTNLRRCTYLVLDE 249
Cdd:COG1205 116 dQLRRLrELAEALGLGVRVATYDGDTP--PEERRwiREHP-DIVLTNP----DMLHYGllphhtrwARFFRNLRYVVIDE 188
|
.
gi 1896683539 250 A 250
Cdd:COG1205 189 A 189
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
306-436 |
1.14e-08 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 57.96 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 306 ELSANHNILQIVDVCMESEKD----NKLIQLMEEIMAEKEN-KTIIFVETKKRCDDLTRRMRRDGWPAM------CIHGD 374
Cdd:PRK13766 325 RLVEDPRFRKAVRKAKELDIEhpklEKLREIVKEQLGKNPDsRIIVFTQYRDTAEKIVDLLEKEGIKAVrfvgqaSKDGD 404
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896683539 375 K--SQPERDWVLSEFRSGKAPILIATDVASRGLDVEDVKFVINYDyPNSSE-DYIHRIGRTARST 436
Cdd:PRK13766 405 KgmSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYE-PVPSEiRSIQRKGRTGRQE 468
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
329-437 |
1.60e-08 |
|
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: 53.81 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 329 LIQLMEEImaEKENKTIIFVETKKRCDDLTRRMRR----DGWP--AMCIHGDKSQPERDWVLSEFRSGKAPILIATDVAS 402
Cdd:cd18796 28 YAEVIFLL--ERHKSTLVFTNTRSQAERLAQRLRElcpdRVPPdfIALHHGSLSRELREEVEAALKRGDLKVVVATSSLE 105
|
90 100 110
....*....|....*....|....*....|....*
gi 1896683539 403 RGLDVEDVKFVINYDYPNSSEDYIHRIGRTARSTN 437
Cdd:cd18796 106 LGIDIGDVDLVIQIGSPKSVARLLQRLGRSGHRPG 140
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
325-437 |
2.52e-08 |
|
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: 53.40 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 325 KDNKLIQLMEEI--MAEKENKTIIFVETKKRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLSEFRSGKAPILIATDVAS 402
Cdd:cd18790 9 TEGQVDDLLGEIrkRVARGERVLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLR 88
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1896683539 403 RGLDVEDVKFVINYD-----YPNSSEDYIHRIGRTARSTN 437
Cdd:cd18790 89 EGLDLPEVSLVAILDadkegFLRSETSLIQTIGRAARNVN 128
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
121-250 |
8.80e-08 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 52.20 E-value: 8.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 121 QAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHINHQPylergdGPICLVLAPTRELAQ-QVQQV-AYDYGKSSRIKS 198
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDP------GSRALYLYPTKALAQdQLRSLrELLEQLGLGIRV 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1896683539 199 TCVYGGAPKGPQIRDLERGVEICIATP-----------GRLIDFLEagktNLRrctYLVLDEA 250
Cdd:cd17923 79 ATYDGDTPREERRAIIRNPPRILLTNPdmlhyallphhDRWARFLR----NLR---YVVLDEA 134
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
137-414 |
1.92e-07 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 53.55 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 137 IAQTGSGKTLSYLLPAIVHINHQPyLERgdgpICLVLaPTRELAQQVQQVAYDYGKS------SRIKSTCVYGGAPKGPQ 210
Cdd:COG1203 153 TAPTGGGKTEAALLFALRLAAKHG-GRR----IIYAL-PFTSIINQTYDRLRDLFGEdvllhhSLADLDLLEEEEEYESE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 211 IRDLERGVE-----ICIATPGRLIDFLEAGKT--NLRRCTY----LVLDEADrMLDMGFEPQIRKIVDQIRPDRQT--LM 277
Cdd:COG1203 227 ARWLKLLKElwdapVVVTTIDQLFESLFSNRKgqERRLHNLansvIILDEVQ-AYPPYMLALLLRLLEWLKNLGGSviLM 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 278 wSATWPKEVRQLAEDFLkDYVQINVGALELSANHNILQIVDVCMESEKDNKLIQLMEEImAEKENKTIIFVETKKRCDDL 357
Cdd:COG1203 306 -TATLPPLLREELLEAY-ELIPDEPEELPEYFRAFVRKRVELKEGPLSDEELAELILEA-LHKGKSVLVIVNTVKDAQEL 382
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1896683539 358 TRRMRRDGW--PAMCIHG-----DKSQPERDwVLSEFRSGKAPILIATDVASRGLDVeDVKFVI 414
Cdd:COG1203 383 YEALKEKLPdeEVYLLHSrfcpaDRSEIEKE-IKERLERGKPCILVSTQVVEAGVDI-DFDVVI 444
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
99-185 |
3.48e-07 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 53.18 E-value: 3.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 99 AQFPQYVIDvLMQQNFKEPTAIQAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVH-INHQPYLERGDGPICLVLAPTR 177
Cdd:COG1201 8 SLLHPAVRA-WFAARFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTLAAFLPALDElARRPRPGELPDGLRVLYISPLK 86
|
....*...
gi 1896683539 178 ELAQQVQQ 185
Cdd:COG1201 87 ALANDIER 94
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
325-434 |
5.18e-07 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350188 [Multi-domain] Cd Length: 143 Bit Score: 49.28 E-value: 5.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 325 KDNKLIQLMEEIM----AEKENKTIIFVETKKRCDDLTRRMRRDGW---PAMCI-HGDK------SQPERDWVLSEFRSG 390
Cdd:cd18801 10 KLEKLEEIVKEHFkkkqEGSDTRVIIFSEFRDSAEEIVNFLSKIRPgirATRFIgQASGksskgmSQKEQKEVIEQFRKG 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1896683539 391 KAPILIATDVASRGLDVEDVKFVINYDyPNSSE-DYIHRIGRTAR 434
Cdd:cd18801 90 GYNVLVATSIGEEGLDIGEVDLIICYD-ASPSPiRMIQRMGRTGR 133
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
129-457 |
8.27e-07 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 51.82 E-value: 8.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 129 LSGRDMVGIAQTGSGKTLSYLLPAIVHinhqpylergdGPICLVLAPTRELAQ-QVQQVAydygkSSRIKSTCVYGGAPK 207
Cdd:PLN03137 473 MSGYDVFVLMPTGGGKSLTYQLPALIC-----------PGITLVISPLVSLIQdQIMNLL-----QANIPAASLSAGMEW 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 208 GPQIRDL-ERGVEIC-----IATPGR------LIDFLEA--GKTNLRRctyLVLDEADRMLDMG--FEPQIRK--IVDQI 269
Cdd:PLN03137 537 AEQLEILqELSSEYSkykllYVTPEKvaksdsLLRHLENlnSRGLLAR---FVIDEAHCVSQWGhdFRPDYQGlgILKQK 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 270 RPDRQTLMWSATWPKEVRqlaEDFLKDYVQINVGALELSANHNILQIVDVcmesEKDNKLIQLMEEIMaeKENK----TI 345
Cdd:PLN03137 614 FPNIPVLALTATATASVK---EDVVQALGLVNCVVFRQSFNRPNLWYSVV----PKTKKCLEDIDKFI--KENHfdecGI 684
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 346 IFVETKKRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLSEFRSGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDY 425
Cdd:PLN03137 685 IYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGY 764
|
330 340 350
....*....|....*....|....*....|..
gi 1896683539 426 IHRIGRTARSTNKGTAYTFFTPGNLRQARELI 457
Cdd:PLN03137 765 HQECGRAGRDGQRSSCVLYYSYSDYIRVKHMI 796
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
105-398 |
1.36e-06 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 51.05 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 105 VIDVLMQQNFKEPTAIQAQGFPLAL-SGRDMVGIAQTGSGKTLSYLLPAIVHINHqpylergdGPICLVLAPTRELAQQV 183
Cdd:COG1204 11 VIEFLKERGIEELYPPQAEALEAGLlEGKNLVVSAPTASGKTLIAELAILKALLN--------GGKALYIVPLRALASEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 184 -QQVAYDYGKSSrIKSTCVYGGAPKGPqiRDLERgVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEA------DRmldm 256
Cdd:COG1204 83 yREFKRDFEELG-IKVGVSTGDYDSDD--EWLGR-YDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAhliddeSR---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 257 GfePQIRKIVDQIR---PDRQTLMWSATW--PKEVRQL--AEDFLKDY--VQINVGALElsanHNILQIVDVcmESEKDN 327
Cdd:COG1204 155 G--PTLEVLLARLRrlnPEAQIVALSATIgnAEEIAEWldAELVKSDWrpVPLNEGVLY----DGVLRFDDG--SRRSKD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 328 KLIQLMEEIMAEKEnKTIIFVETKKRCDDLTRRM-----RRDGWPAM-------------------------CI------ 371
Cdd:COG1204 227 PTLALALDLLEEGG-QVLVFVSSRRDAESLAKKLadelkRRLTPEEReeleelaeellevseethtnekladCLekgvaf 305
|
330 340
....*....|....*....|....*...
gi 1896683539 372 -HGDKSQPERDWVLSEFRSGKAPILIAT 398
Cdd:COG1204 306 hHAGLPSELRRLVEDAFREGLIKVLVAT 333
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
245-434 |
2.24e-06 |
|
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: 49.74 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 245 LVLDEADRMLD--MGFepqIRKIVDQIRPDRQTLM-WSATWPKEVRQLAEDFlkDYVqINVGALELSANHNILQIvdvcM 321
Cdd:cd09639 127 LIFDEVHFYDEytLAL---ILAVLEVLKDNDVPILlMSATLPKFLKEYAEKI--GYV-EENEPLDLKPNERAPFI----K 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 322 ESEKDNKLIQLMEEIMAE--KENKTIIFVETKKRCDDLTRRMRRDG--WPAMCIHG-----DKSQPERDwVLSEFRSGKA 392
Cdd:cd09639 197 IESDKVGEISSLERLLEFikKGGSVAIIVNTVDRAQEFYQQLKEKGpeEEIMLIHSrftekDRAKKEAE-LLLEFKKSEK 275
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1896683539 393 PILIATDVASRGLDVeDVKFVINYDYPNSSedYIHRIGRTAR 434
Cdd:cd09639 276 FVIVATQVIEASLDI-SVDVMITELAPIDS--LIQRLGRLHR 314
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
119-288 |
7.00e-06 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 46.76 E-value: 7.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 119 AIQAqgfplALSGRDMVGIAQTGSGKTLSYLLPAIVhinhqpylergDGPICLVLAPTRELAQ-QVQQVaydygKSSRIK 197
Cdd:cd17920 20 AINA-----VLAGRDVLVVMPTGGGKSLCYQLPALL-----------LDGVTLVVSPLISLMQdQVDRL-----QQLGIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 198 STCVYGGAPKGPQIRDLER----GVEICIATPGRLI--DFLE--AGKTNLRRCTYLVLDEADRMLDMG--FEPQIRKIVD 267
Cdd:cd17920 79 AAALNSTLSPEEKREVLLRikngQYKLLYVTPERLLspDFLEllQRLPERKRLALIVVDEAHCVSQWGhdFRPDYLRLGR 158
|
170 180
....*....|....*....|...
gi 1896683539 268 QIR--PDRQTLMWSATWPKEVRQ 288
Cdd:cd17920 159 LRRalPGVPILALTATATPEVRE 181
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
339-445 |
7.99e-06 |
|
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350176 [Multi-domain] Cd Length: 153 Bit Score: 45.70 E-value: 7.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 339 EKENKTIIFVETKkrcDDLTRRMRRDGWPAmcIHGDKSQPERDWVLSEFRSGKAPILIATDVASRGLDVEDVKFVINYDY 418
Cdd:cd18789 47 EQGDKIIVFTDNV---EALYRYAKRLLKPF--ITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPEANVAIQISG 121
|
90 100
....*....|....*....|....*...
gi 1896683539 419 PNSSE-DYIHRIGRTARSTNKGTAYTFF 445
Cdd:cd18789 122 HGGSRrQEAQRLGRILRPKKGGGKNAFF 149
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
107-288 |
1.09e-05 |
|
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.
Pssm-ID: 350776 [Multi-domain] Cd Length: 201 Bit Score: 46.48 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 107 DVLMQQNFKEPT--AIQAqgfplALSGRDMVGIAQTGSGKTLSYLLPAIVhinhqpYLERGDGpICLVLAPTRELAQ-QV 183
Cdd:cd18018 6 RVFGHPSFRPGQeeAIAR-----LLSGRSTLVVLPTGAGKSLCYQLPALL------LRRRGPG-LTLVVSPLIALMKdQV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 184 QQVAydygksSRIKSTCVYGGAPKGPQIRDLER----GVEICIATPGRLI--DFLEAGKTnLRRCTYLVLDEADRMLDMG 257
Cdd:cd18018 74 DALP------RAIKAAALNSSLTREERRRILEKlragEVKILYVSPERLVneSFRELLRQ-TPPISLLVVDEAHCISEWS 146
|
170 180 190
....*....|....*....|....*....|....*.
gi 1896683539 258 --FEP---QIRKIVDQIRPDRQTLMWSATWPKEVRQ 288
Cdd:cd18018 147 hnFRPdylRLCRVLRELLGAPPVLALTATATKRVVE 182
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
120-250 |
1.88e-04 |
|
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: 42.25 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 120 IQAQGF-PLALSGRDMVGIAQTGSGKTLSYLLpAIVHinhqpYLERGDGpICLVLAPTRELaqqVQQVAYDYGKSSRI-- 196
Cdd:cd17921 5 IQREALrALYLSGDSVLVSAPTSSGKTLIAEL-AILR-----ALATSGG-KAVYIAPTRAL---VNQKEADLRERFGPlg 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1896683539 197 KSTCVYGGAPKGPQIRDLERgvEICIATPGRLIDFLEAGKT-NLRRCTYLVLDEA 250
Cdd:cd17921 75 KNVGLLTGDPSVNKLLLAEA--DILVATPEKLDLLLRNGGErLIQDVRLVVVDEA 127
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
128-252 |
1.69e-03 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef 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: 350793 [Multi-domain] Cd Length: 181 Bit Score: 39.42 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 128 ALSGRDMVgIAQTGSGKTLSYLLPAIVHinhqpyLERGDGPIcLVLAPTRELaqqVQQVAYDYGKSSRIKSTCVYGGAPK 207
Cdd:cd18035 14 ALNGNTLI-VLPTGLGKTIIAILVAADR------LTKKGGKV-LILAPSRPL---VEQHAENLKRVLNIPDKITSLTGEV 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1896683539 208 GPQIR-DLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADR 252
Cdd:cd18035 83 KPEERaERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
343-434 |
1.91e-03 |
|
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: 38.78 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 343 KTIIFVETKKRCDDLTR----RMRRDGWPAMCIHGDKS---QPERDWVLSEFRSGKAPILIATDVASRGLDVEDVKFVIN 415
Cdd:cd18797 37 KTIVFCRSRKLAELLLRylkaRLVEEGPLASKVASYRAgylAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVL 116
|
90
....*....|....*....
gi 1896683539 416 YDYPNSSEDYIHRIGRTAR 434
Cdd:cd18797 117 AGYPGSLASLWQQAGRAGR 135
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
129-299 |
2.61e-03 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type 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: 350786 [Multi-domain] Cd Length: 177 Bit Score: 38.85 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 129 LSGRDMVGIAQTGSGKTLSYLLPAIVHInhqpyLERGDGpicLVLAPTRELA-QQVQQVAYDYGKSSRIK-STCVYGGAP 206
Cdd:cd18028 15 LKGENLLISIPTASGKTLIAEMAMVNTL-----LEGGKA---LYLVPLRALAsEKYEEFKKLEEIGLKVGiSTGDYDEDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 207 KGPQIRDlergveICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIR---PDRQTLMWSATWP 283
Cdd:cd18028 87 EWLGDYD------IIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPTLESIVARLRrlnPNTQIIGLSATIG 160
|
170
....*....|....*.
gi 1896683539 284 KeVRQLAEDFLKDYVQ 299
Cdd:cd18028 161 N-PDELAEWLNAELVE 175
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
128-250 |
2.89e-03 |
|
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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: 350773 [Multi-domain] Cd Length: 209 Bit Score: 39.27 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 128 ALSGRDMVGIAQTGSGKTLSYLLPAIVhinhqpylerGDGpICLVLAPTRELAQ-QVQQVA-------YDYGKSSRIKST 199
Cdd:cd18015 30 TMAGRDVFLVMPTGGGKSLCYQLPALC----------SDG-FTLVVSPLISLMEdQLMALKklgisatMLNASSSKEHVK 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1896683539 200 CVYGgapkgpQIRDLERGVEICIATP------GRLIDFLEAGKtNLRRCTYLVLDEA 250
Cdd:cd18015 99 WVHA------ALTDKNSELKLLYVTPekiaksKRFMSKLEKAY-NAGRLARIAIDEV 148
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
121-295 |
3.55e-03 |
|
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom syndrome protein homolog or BLM) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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. Mutations in RecQ2 cause Bloom syndrome.
Pssm-ID: 350774 [Multi-domain] Cd Length: 208 Bit Score: 39.04 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 121 QAQGFPLALSGRDMVGIAQTGSGKTLSYLLPAIVHINhqpylergdgpICLVLAPTREL-AQQVQQVaydygKSSRIKST 199
Cdd:cd18016 22 QLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPG-----------VTVVISPLRSLiVDQVQKL-----TSLDIPAT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 200 CVYG--GAPKGPQI-RDLERG---VEICIATP------GRLIDFLEagktNLRRCTYL---VLDEADRMLDMG--FEPQI 262
Cdd:cd18016 86 YLTGdkTDAEATKIyLQLSKKdpiIKLLYVTPekisasNRLISTLE----NLYERKLLarfVIDEAHCVSQWGhdFRPDY 161
|
170 180 190
....*....|....*....|....*....|....*
gi 1896683539 263 RKI--VDQIRPDRQTLMWSATWPKEVRQLAEDFLK 295
Cdd:cd18016 162 KRLnmLRQKFPSVPMMALTATATPRVQKDILNQLK 196
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
317-398 |
3.86e-03 |
|
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: 37.92 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 317 VDVCMESEKDNKLIQLMEEIMAEKenKTIIFVETKKRCDDLTRRMRrdgwpamCI---HGDKSQPERDWVLSEFRSGKAP 393
Cdd:cd18795 21 VDVMNKFDSDIIVLLKIETVSEGK--PVLVFCSSRKECEKTAKDLA-------GIafhHAGLTREDRELVEELFREGLIK 91
|
....*
gi 1896683539 394 ILIAT 398
Cdd:cd18795 92 VLVAT 96
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
140-250 |
4.76e-03 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 38.40 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896683539 140 TGSGKTL-SYLLpaIVHINHQPYLERGDGPICLVLAPTRELAQqvQQVAYdYGKSSRIKSTCVYGGAPKGPQIRD----L 214
Cdd:cd18034 25 TGSGKTLiAVML--IKEMGELNRKEKNPKKRAVFLVPTVPLVA--QQAEA-IRSHTDLKVGEYSGEMGVDKWTKErwkeE 99
|
90 100 110
....*....|....*....|....*....|....*.
gi 1896683539 215 ERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEA 250
Cdd:cd18034 100 LEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
343-414 |
4.82e-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: 37.15 E-value: 4.82e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896683539 343 KTIIFVETKKRCDDLTRRMRRDGWPAMCIHGDKSQPERDWV---LSEFRSGKAPILIATDVASRGLDVEDVKFVI 414
Cdd:cd18799 8 KTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDEaliLLFFGELKPPILVTVDLLTTGVDIPEVDNVV 82
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
371-407 |
5.73e-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: 37.71 E-value: 5.73e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1896683539 371 IHGDKSQPERDWVLSEFRSGKAPILIATDVASRGLDV 407
Cdd:cd18811 67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDV 103
|
|
| |
