|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
32-500 |
0e+00 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 690.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 32 GNPGERLRKKKWDLSELPKFEKNFYVEHPEVARLTPYEVDELRRKKEITVRGGDVCPKPVFAFHHANFPQYVMDVLMDQH 111
Cdd:PTZ00110 70 STLGKRLQPIDWKSINLVPFEKNFYKEHPEVSALSSKEVDEIRKEKEITIIAGENVPKPVVSFEYTSFPDYILKSLKNAG 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 112 FTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQVQQVADDYGKC 191
Cdd:PTZ00110 150 FTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGDGPIVLVLAPTRELAEQIREQCNKFGAS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 192 SRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDR 271
Cdd:PTZ00110 230 SKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDR 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 272 QTLMWSATWPKEVRQLAEDFLRDY-TQINVGNLELSANHNILQIVDVCMESEKDHKLIQLMEEIMAEKeNKTIIFVETKR 350
Cdd:PTZ00110 310 QTLMWSATWPKEVQSLARDLCKEEpVHVNVGSLDLTACHNIKQEVFVVEEHEKRGKLKMLLQRIMRDG-DKILIFVETKK 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 351 RCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLNEFRSGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYVHRIGRT 430
Cdd:PTZ00110 389 GADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRT 468
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 431 ARSTNKGTAYTFFTPGNLKQARELIKVLEEANQAINPKLMQLVDHRGGGGGGGGRSRYRttSSANNPNLM 500
Cdd:PTZ00110 469 GRAGAKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSNERSNGTERRRWGGYG--RFSNNVNNI 536
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
30-301 |
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: 591.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 30 KFGNPGERLRKKKWDLSELPKFEKNFYVEHPEVARLTPYEVDELRRKKEITVRGGdVCPKPVFAFHHANFPQYVMDVLMD 109
Cdd:cd18050 1 KFGNPGERLRKKKWDLSELPKFEKNFYVEHPEVARMTQYDVEELRRKKEITIRGV-GCPKPVFAFHQANFPQYVMDVLLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 110 QHFTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQVQQVADDYG 189
Cdd:cd18050 80 QNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQVQQVADDYG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 190 KCSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRP 269
Cdd:cd18050 160 KSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRP 239
|
250 260 270
....*....|....*....|....*....|..
gi 93587673 270 DRQTLMWSATWPKEVRQLAEDFLRDYTQINVG 301
Cdd:cd18050 240 DRQTLMWSATWPKEVRQLAEDFLRDYVQINIG 271
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
69-301 |
5.08e-167 |
|
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: 476.81 E-value: 5.08e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 69 EVDELRRKKEITVRGGDvCPKPVFAFHHANFPQYVMDVLMDQHFTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLL 148
Cdd:cd18049 2 EVEQYRRSKEITVRGHN-CPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 149 PAIVHINHQPYLERGDGPICLVLAPTRELAQQVQQVADDYGKCSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLID 228
Cdd:cd18049 81 PAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLID 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 93587673 229 FLESGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYTQINVG 301
Cdd:cd18049 161 FLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIG 233
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
94-468 |
1.68e-162 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 472.32 E-value: 1.68e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 94 FHHANFPQYVMDVLMDQHFTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHqpylERGDGPICLVLAP 173
Cdd:COG0513 4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDP----SRPRAPQALILAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 174 TRELAQQVQQVADDYGKCSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESGKTNLRRCTYLVLDEADRMLD 253
Cdd:COG0513 80 TRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 254 MGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYTQINVGNLELSANhNILQIVdvcMESEKDHKLIQLMEE 333
Cdd:COG0513 160 MGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAE-TIEQRY---YLVDKRDKLELLRRL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 334 IMAEKENKTIIFVETKRRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLNEFRSGKAPILIATDVASRGLDVEDVKFVIN 413
Cdd:COG0513 236 LRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVIN 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 93587673 414 YDYPNSSEDYVHRIGRTARSTNKGTAYTFFTPgnlKQARELIKVLEEANQAINPK 468
Cdd:COG0513 316 YDLPEDPEDYVHRIGRTGRAGAEGTAISLVTP---DERRLLRAIEKLIGQKIEEE 367
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
103-299 |
1.99e-154 |
|
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: 442.96 E-value: 1.99e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 103 VMDVLMDQHFTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQVQ 182
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGDGPIVLVLAPTRELAQQIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 183 QVADDYGKCSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESGKTNLRRCTYLVLDEADRMLDMGFEPQIRK 262
Cdd:cd17966 81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 93587673 263 IVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYTQIN 299
Cdd:cd17966 161 IVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
103-298 |
6.65e-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: 321.31 E-value: 6.65e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 103 VMDVLMDQHFTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPyLERGDGPICLVLAPTRELAQQVQ 182
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEP-KKKGRGPQALVLAPTRELAMQIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 183 QVADDYGKCSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESGKTNLRRCTYLVLDEADRMLDMGFEPQIRK 262
Cdd:cd00268 80 EVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 93587673 263 IVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYTQI 298
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) ... |
80-298 |
6.69e-99 |
|
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: 301.60 E-value: 6.69e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 80 TVRGGDvCPKPVFAFHHANFPQYVMDVLMDQHFTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPY 159
Cdd:cd17953 1 KVRGKD-CPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 160 LERGDGPICLVLAPTRELAQQVQQVADDYGKCSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFL--ESGK-TN 236
Cdd:cd17953 80 VKPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtaNNGRvTN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 93587673 237 LRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYTQI 298
Cdd:cd17953 160 LRRVTYVVLDEADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
112-445 |
1.09e-97 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 307.11 E-value: 1.09e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 112 FTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYlergdGPICLVLAPTRELAQQVqqvADDYGKC 191
Cdd:PRK11776 24 YTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRF-----RVQALVLCPTRELADQV---AKEIRRL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 192 SR----LKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQI 267
Cdd:PRK11776 96 ARfipnIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMGFQDAIDAIIRQA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 268 RPDRQTLMWSATWPKEVRQLAEDFLRDYTQInvgnlELSANHNILQIVDVCMESEKDHKLIQLMEEIMAEKENKTIIFVE 347
Cdd:PRK11776 176 PARRQTLLFSATYPEGIAAISQRFQRDPVEV-----KVESTHDLPAIEQRFYEVSPDERLPALQRLLLHHQPESCVVFCN 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 348 TKRRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLNEFRSGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYVHRI 427
Cdd:PRK11776 251 TKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRI 330
|
330
....*....|....*...
gi 93587673 428 GRTARSTNKGTAYTFFTP 445
Cdd:PRK11776 331 GRTGRAGSKGLALSLVAP 348
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
103-294 |
2.15e-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: 291.63 E-value: 2.15e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 103 VMDVLMDQHFTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQVQ 182
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGEGPIAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 183 QVADDYGKCSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESGKTNLRRCTYLVLDEADRMLDMGFEPQIRK 262
Cdd:cd17952 81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
|
170 180 190
....*....|....*....|....*....|..
gi 93587673 263 IVDQIRPDRQTLMWSATWPKEVRQLAEDFLRD 294
Cdd:cd17952 161 IVGHVRPDRQTLLFSATFKKKIEQLARDILSD 192
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
104-439 |
5.12e-86 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 276.05 E-value: 5.12e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 104 MDVLMDQHFTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPylERGDGPI-CLVLAPTRELAQQVQ 182
Cdd:PRK11192 13 LEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFP--RRKSGPPrILILTPTRELAMQVA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 183 QVADDYGKCSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESGKTNLRRCTYLVLDEADRMLDMGFEPQIRK 262
Cdd:PRK11192 91 DQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIET 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 263 IVDQIRPDRQTLMWSATWPKE-VRQLAEDFLRDYTQINVgNLELSANHNILQIVDVCmeSEKDHKLIQLMEEIMAEKENK 341
Cdd:PRK11192 171 IAAETRWRKQTLLFSATLEGDaVQDFAERLLNDPVEVEA-EPSRRERKKIHQWYYRA--DDLEHKTALLCHLLKQPEVTR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 342 TIIFVETKRRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLNEFRSGKAPILIATDVASRGLDVEDVKFVINYDYPNSSE 421
Cdd:PRK11192 248 SIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRSAD 327
|
330
....*....|....*...
gi 93587673 422 DYVHRIGRTARSTNKGTA 439
Cdd:PRK11192 328 TYLHRIGRTGRAGRKGTA 345
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
94-301 |
7.14e-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: 265.50 E-value: 7.14e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 94 FHHANFPQYVMDVLMDQHFTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQP-----YLERGDGPIC 168
Cdd:cd17967 2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGppsvgRGRRKAYPSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 169 LVLAPTRELAQQVQQVADDYGKCSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESGKTNLRRCTYLVLDEA 248
Cdd:cd17967 82 LILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDEA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 93587673 249 DRMLDMGFEPQIRKIVDQ----IRPDRQTLMWSATWPKEVRQLAEDFLRDYTQINVG 301
Cdd:cd17967 162 DRMLDMGFEPQIRKIVEHpdmpPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVG 218
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
109-459 |
9.25e-84 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 270.91 E-value: 9.25e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 109 DQHFTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGPI-CLVLAPTRELAQQVQQVADD 187
Cdd:PRK10590 18 EQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVrALILTPTRELAAQIGENVRD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 188 YGKCSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQI 267
Cdd:PRK10590 98 YSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFIHDIRRVLAKL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 268 RPDRQTLMWSATWPKEVRQLAEDFLRDYTQINVGNLElSANHNILQIVDVCMESEKDHKLIQLmeeIMAEKENKTIIFVE 347
Cdd:PRK10590 178 PAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRN-TASEQVTQHVHFVDKKRKRELLSQM---IGKGNWQQVLVFTR 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 348 TKRRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLNEFRSGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYVHRI 427
Cdd:PRK10590 254 TKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPEDYVHRI 333
|
330 340 350
....*....|....*....|....*....|..
gi 93587673 428 GRTARSTNKGTAYTFFTPGNLKQARELIKVLE 459
Cdd:PRK10590 334 GRTGRAAATGEALSLVCVDEHKLLRDIEKLLK 365
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
48-468 |
2.84e-81 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 266.27 E-value: 2.84e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 48 LPKFEKNFYVEHPEV-ARLTPYEVDELRRKKEITVRGGDVcPKPVFAFHHANFPQYVMDVLMDQHFTEPTPIQCQGFPLA 126
Cdd:PLN00206 77 LPATDECFYVRDPGStSGLSSSQAELLRRKLEIHVKGEAV-PPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 127 LSGRDMVGIAQTGSGKTLAYLLPAIVH---INHQPYLERgDGPICLVLAPTRELAQQVQQVADDYGKCSRLKSTCIYGGA 203
Cdd:PLN00206 156 LSGRSLLVSADTGSGKTASFLVPIISRcctIRSGHPSEQ-RNPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGD 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 204 PKGPQIRDLERGVEICIATPGRLIDFLESGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVdQIRPDRQTLMWSATWPKE 283
Cdd:PLN00206 235 AMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIF-QALSQPQVLLFSATVSPE 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 284 VRQLAEDFLRDYTQINVGNLElSANHNILQIVdVCMES-EKDHKLIqlmeEIMAEKEN---KTIIFVETKRRCDDLTRRM 359
Cdd:PLN00206 314 VEKFASSLAKDIILISIGNPN-RPNKAVKQLA-IWVETkQKKQKLF----DILKSKQHfkpPAVVFVSSRLGADLLANAI 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 360 RR-DGWPAMCIHGDKSQPERDWVLNEFRSGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYVHRIGRTARSTNKGT 438
Cdd:PLN00206 388 TVvTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGT 467
|
410 420 430
....*....|....*....|....*....|
gi 93587673 439 AYTFFTPGNLKQARELIKVLEEANQAInPK 468
Cdd:PLN00206 468 AIVFVNEEDRNLFPELVALLKSSGAAI-PR 496
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
103-298 |
5.47e-81 |
|
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: 254.31 E-value: 5.47e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 103 VMDVLMDQHFTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYL-ERGDGPICLVLAPTRELAQQV 181
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPrEQRNGPGVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 182 QqvaddyGKCSR-----LKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESGKTNLRRCTYLVLDEADRMLDMGF 256
Cdd:cd17958 81 E------AECSKysykgLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 93587673 257 EPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYTQI 298
Cdd:cd17958 155 EPQIRKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
92-442 |
1.92e-76 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 250.66 E-value: 1.92e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 92 FAFHhanfPQyVMDVLMDQHFTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHI--NHQPYLERGDGPICL 169
Cdd:PRK04837 13 FALH----PQ-VVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLlsHPAPEDRKVNQPRAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 170 VLAPTRELAQQVQQVADDYGKCSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESGKTNLRRCTYLVLDEAD 249
Cdd:PRK04837 88 IMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEAD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 250 RMLDMGFEPQIRKIVDQIRP--DRQTLMWSATWPKEVRQLAEDFLRDYTQINVGNLELSAnHNILQIVDVCMESEKDHKL 327
Cdd:PRK04837 168 RMFDLGFIKDIRWLFRRMPPanQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTG-HRIKEELFYPSNEEKMRLL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 328 IQLMEEimaEKENKTIIFVETKRRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLNEFRSGKAPILIATDVASRGLDVED 407
Cdd:PRK04837 247 QTLIEE---EWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPA 323
|
330 340 350
....*....|....*....|....*....|....*
gi 93587673 408 VKFVINYDYPNSSEDYVHRIGRTARSTNKGTAYTF 442
Cdd:PRK04837 324 VTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
84-301 |
2.65e-76 |
|
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: 2.65e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 84 GDVCPKPVFAFHHANFPQYVMDVLMDQHFTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQ---PYL 160
Cdd:cd18051 13 GENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQgpgESL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 161 ERGDG--------PICLVLAPTRELAQQVQQVADDYGKCSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLES 232
Cdd:cd18051 93 PSESGyygrrkqyPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLER 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 93587673 233 GKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQI----RPDRQTLMWSATWPKEVRQLAEDFLRDYTQINVG 301
Cdd:cd18051 173 GKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDtmppTGERQTLMFSATFPKEIQMLARDFLDNYIFLAVG 245
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
94-442 |
1.80e-75 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 249.44 E-value: 1.80e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 94 FHHANFPQYVMDVLMDQHFTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLE---RGDgPICLV 170
Cdd:PRK01297 89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKeryMGE-PRALI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 171 LAPTRELAQQVQQVADDYGKCSRLKSTCIYGGAPKGPQIRDLE-RGVEICIATPGRLIDFLESGKTNLRRCTYLVLDEAD 249
Cdd:PRK01297 168 IAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEAD 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 250 RMLDMGFEPQIRKIVDQIRP--DRQTLMWSATWPKEVRQLAEDFLRDYTQINVgNLELSANHNILQIVDVCMESEKdHKL 327
Cdd:PRK01297 248 RMLDMGFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVEI-EPENVASDTVEQHVYAVAGSDK-YKL 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 328 IQLMeeIMAEKENKTIIFVETKRRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLNEFRSGKAPILIATDVASRGLDVED 407
Cdd:PRK01297 326 LYNL--VTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDG 403
|
330 340 350
....*....|....*....|....*....|....*
gi 93587673 408 VKFVINYDYPNSSEDYVHRIGRTARSTNKGTAYTF 442
Cdd:PRK01297 404 ISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISF 438
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
103-442 |
3.00e-74 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 250.54 E-value: 3.00e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 103 VMDVLMDQHFTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINhqPYLErgdGPICLVLAPTRELAQQVQ 182
Cdd:PRK11634 17 ILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLD--PELK---APQILVLAPTRELAVQVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 183 QVADDYGKCSR-LKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESGKTNLRRCTYLVLDEADRMLDMGFEPQIR 261
Cdd:PRK11634 92 EAMTDFSKHMRgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFIEDVE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 262 KIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYTQINVGNlELSANHNILQIVDVCMESEKDHKLIQLMEeimAEKENK 341
Cdd:PRK11634 172 TIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQS-SVTTRPDISQSYWTVWGMRKNEALVRFLE---AEDFDA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 342 TIIFVETKRRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLNEFRSGKAPILIATDVASRGLDVEDVKFVINYDYPNSSE 421
Cdd:PRK11634 248 AIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSE 327
|
330 340
....*....|....*....|.
gi 93587673 422 DYVHRIGRTARSTNKGTAYTF 442
Cdd:PRK11634 328 SYVHRIGRTGRAGRAGRALLF 348
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
112-442 |
3.93e-74 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 248.71 E-value: 3.93e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 112 FTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYL--ERGDGPICLVLAPTRELAQQVQQVADDYG 189
Cdd:PRK04537 29 FTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALadRKPEDPRALILAPTRELAIQIHKDAVKFG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 190 KCSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESGKT-NLRRCTYLVLDEADRMLDMGFEPQIRKIVDQI- 267
Cdd:PRK04537 109 ADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVvSLHACEICVLDEADRMFDLGFIKDIRFLLRRMp 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 268 -RPDRQTLMWSATWPKEVRQLAEDFLRDYTQINVGNLELSANHnILQIVDVCMESEKdhklIQLMEEIMAEKEN-KTIIF 345
Cdd:PRK04537 189 eRGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAAR-VRQRIYFPADEEK----QTLLLGLLSRSEGaRTMVF 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 346 VETKRRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLNEFRSGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYVH 425
Cdd:PRK04537 264 VNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVYNYDLPFDAEDYVH 343
|
330
....*....|....*..
gi 93587673 426 RIGRTARSTNKGTAYTF 442
Cdd:PRK04537 344 RIGRTARLGEEGDAISF 360
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
84-303 |
1.29e-73 |
|
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: 237.56 E-value: 1.29e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 84 GDVCPKPVFAFHHANFPQYVMDVLMDQHFTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQ----PY 159
Cdd:cd18052 35 GRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEgltaSS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 160 LERGDGPICLVLAPTRELAQQVQQVADDYGKCSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESGKTNLRR 239
Cdd:cd18052 115 FSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSK 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 93587673 240 CTYLVLDEADRMLDMGFEPQIRKIVDQI----RPDRQTLMWSATWPKEVRQLAEDFLR-DYTQINVGNL 303
Cdd:cd18052 195 LKYLILDEADRMLDMGFGPEIRKLVSEPgmpsKEDRQTLMFSATFPEEIQRLAAEFLKeDYLFLTVGRV 263
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
112-454 |
3.84e-72 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 238.57 E-value: 3.84e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 112 FTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHqpylergDGPIC--LVLAPTRELAQQVQQVADDYG 189
Cdd:PTZ00424 48 FEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDY-------DLNACqaLILAPTRELAQQIQKVVLALG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 190 KCSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRP 269
Cdd:PTZ00424 121 DYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFKGQIYDVFKKLPP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 270 DRQTLMWSATWPKEVRQLAEDFLRDYTQINVGNLELSAnHNILQI-VDVCMESEKDHKLIQLMEEIMAekeNKTIIFVET 348
Cdd:PTZ00424 201 DVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTL-EGIRQFyVAVEKEEWKFDTLCDLYETLTI---TQAIIYCNT 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 349 KRRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLNEFRSGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYVHRIG 428
Cdd:PTZ00424 277 RRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIG 356
|
330 340
....*....|....*....|....*.
gi 93587673 429 RTARSTNKGTAYTFFTPGNLKQAREL 454
Cdd:PTZ00424 357 RSGRFGRKGVAINFVTPDDIEQLKEI 382
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
103-293 |
1.81e-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: 227.59 E-value: 1.81e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 103 VMDVLMDQHFTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQP---YLERGDGPICLVLAPTRELAQ 179
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPpldEETKDDGPYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 180 QVQQVADDYGKCSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESGKTNLRRCTYLVLDEADRMLDMGFEPQ 259
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 93587673 260 IRKIVDQI-----RPD---------------RQTLMWSATWPKEVRQLAEDFLR 293
Cdd:cd17945 161 VTKILDAMpvsnkKPDteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLR 214
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
116-287 |
1.08e-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: 207.87 E-value: 1.08e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 116 TPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINhqpylERGDGPICLVLAPTRELAQQVQQVADDYGKCSRLK 195
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALD-----KLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 196 STCIYGGAPKGPQIRDLeRGVEICIATPGRLIDFLESGKTnLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLM 275
Cdd:pfam00270 76 VASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILL 153
|
170
....*....|..
gi 93587673 276 WSATWPKEVRQL 287
Cdd:pfam00270 154 LSATLPRNLEDL 165
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
103-299 |
5.08e-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: 207.58 E-value: 5.08e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 103 VMDVLMDQHFTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQ----PYLeRGDGPICLVLAPTRELA 178
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQekklPFI-KGEGPYGLIVCPSRELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 179 QQVQQVADDY------GKCSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESGKTNLRRCTYLVLDEADRML 252
Cdd:cd17951 80 RQTHEVIEYYckalqeGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 93587673 253 DMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYTQIN 299
Cdd:cd17951 160 DMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTVN 206
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
311-443 |
4.67e-60 |
|
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: 196.96 E-value: 4.67e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 311 ILQIVDVCMESEKDHKLIQLmeEIMAEKENKTIIFVETKRRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLNEFRSGKA 390
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLL--LLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKV 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 93587673 391 PILIATDVASRGLDVEDVKFVINYDYPNSSEDYVHRIGRTARSTNKGTAYTFF 443
Cdd:cd18787 79 RVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
112-314 |
1.37e-56 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 190.40 E-value: 1.37e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 112 FTEPTPIQCQGFPLALSG-RDMVGIAQTGSGKTLAYLLPAIVHinhqpyLERGDGPICLVLAPTRELAQQVQQVADDYGK 190
Cdd:smart00487 6 FEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEA------LKRGKGGRVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 191 CSRLKSTCIYGGAPKGPQIRDLERGV-EICIATPGRLIDFLESGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRP 269
Cdd:smart00487 80 SLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 93587673 270 DRQTLMWSATWPKEVRQLAEDFLRDYTQINVGNlelSANHNILQI 314
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLNDPVFIDVGF---TPLEPIEQF 201
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
112-294 |
1.38e-55 |
|
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: 187.52 E-value: 1.38e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 112 FTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVH-INHQPYLergdgpICLVLAPTRELAQQVQQVADDYGK 190
Cdd:cd17954 20 WKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQAlLENPQRF------FALVLAPTRELAQQISEQFEALGS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 191 CSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESGKT-NLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRP 269
Cdd:cd17954 94 SIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKGfSLKSLKFLVMDEADRLLNMDFEPEIDKILKVIPR 173
|
170 180
....*....|....*....|....*
gi 93587673 270 DRQTLMWSATWPKEVRQLAEDFLRD 294
Cdd:cd17954 174 ERTTYLFSATMTTKVAKLQRASLKN 198
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
111-299 |
5.63e-54 |
|
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: 183.55 E-value: 5.63e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 111 HFTEPTPIQCQGFPLALS-GRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQVQQVADDYG 189
Cdd:cd17964 13 GFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGVSALIISPTRELALQIAAEAKKLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 190 KCSR-LKSTCIYGGAPKGPQIRDLER-GVEICIATPGRLIDFLE--SGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVD 265
Cdd:cd17964 93 QGLRkLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRLLDMGFRPDLEQILR 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 93587673 266 QIRP----DRQTLMWSATWPKEVRQLAEDFLR-DYTQIN 299
Cdd:cd17964 173 HLPEknadPRQTLLFSATVPDEVQQIARLTLKkDYKFID 211
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
112-298 |
7.90e-54 |
|
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: 7.90e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 112 FTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHI-NHQPYLERGDGPICLVLAPTRELAQQVQQVADDYGK 190
Cdd:cd17949 11 IEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLlSLEPRVDRSDGTLALVLVPTRELALQIYEVLEKLLK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 191 CSR-LKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESGKT-NLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIR 268
Cdd:cd17949 91 PFHwIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQSfDVSNLRWLVLDEADRLLDMGFEKDITKILELLD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 93587673 269 -------------PDRQTLMWSATWPKEVRQLAEDFLRDYTQI 298
Cdd:cd17949 171 dkrskaggekskpSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
103-301 |
3.17e-52 |
|
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: 178.55 E-value: 3.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 103 VMDVLMDQHFTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQpylERGDGPICLVLAPTRELAQQVQ 182
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKP---RKKKGLRALILAPTRELASQIY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 183 QVADDYGKCSRLKSTCIYGG-APKGPQIRDLERGVEICIATPGRLIDFLESGKTNLRRCTYLVLDEADRMLDMGFEPQIR 261
Cdd:cd17957 78 RELLKLSKGTGLRIVLLSKSlEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 93587673 262 KIVDQIR-PDRQTLMWSATWPKEVRQLAEDFLRDYTQINVG 301
Cdd:cd17957 158 EILAACTnPNLQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
107-288 |
1.67e-51 |
|
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: 176.29 E-value: 1.67e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 107 LMDQHFTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGpiCLVLAPTRELAQQVQQVAD 186
Cdd:cd17947 5 LSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAATR--VLVLVPTRELAMQCFSVLQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 187 DYGKCSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESGKT-NLRRCTYLVLDEADRMLDMGFEPQIRKIVD 265
Cdd:cd17947 83 QLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSfDLDSIEILVLDEADRMLEEGFADELKEILR 162
|
170 180
....*....|....*....|...
gi 93587673 266 QIRPDRQTLMWSATWPKEVRQLA 288
Cdd:cd17947 163 LCPRTRQTMLFSATMTDEVKDLA 185
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
94-299 |
1.12e-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: 174.42 E-value: 1.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 94 FHHANFPQYVMDVLMDQHFTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHI-NHQPYLergdGPICLVLA 172
Cdd:cd17959 3 FQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLkAHSPTV----GARALILS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 173 PTRELAQQVQQVADDYGKCSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESGKTNLRRCTYLVLDEADRML 252
Cdd:cd17959 79 PTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 93587673 253 DMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYTQIN 299
Cdd:cd17959 159 EMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
94-292 |
1.27e-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: 174.33 E-value: 1.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 94 FHHANFPQYVMDVLMDQHFTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYlergdGPICLVLAP 173
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPY-----GIFALVLTP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 174 TRELAQQV--QQVAddYGKCSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESG---KTNLRRCTYLVLDEA 248
Cdd:cd17955 76 TRELAYQIaeQFRA--LGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSddtTKVLSRVKFLVLDEA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 93587673 249 DRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFL 292
Cdd:cd17955 154 DRLLTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFG 197
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
107-300 |
1.62e-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: 174.02 E-value: 1.62e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 107 LMDQHFTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYlERGDGPICLVLAPTRELAQQVQQVAD 186
Cdd:cd17941 5 LKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERW-TPEDGLGALIISPTRELAMQIFEVLR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 187 DYGKCSRLKSTCIYGGapKGPQIrDLER--GVEICIATPGRLIDFLES----GKTNLRrctYLVLDEADRMLDMGFEPQI 260
Cdd:cd17941 84 KVGKYHSFSAGLIIGG--KDVKE-EKERinRMNILVCTPGRLLQHMDEtpgfDTSNLQ---MLVLDEADRILDMGFKETL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 93587673 261 RKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYTQINV 300
Cdd:cd17941 158 DAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
104-288 |
1.18e-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: 168.69 E-value: 1.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 104 MDVLMDQHFTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERgDGPICLVLAPTRELAQQVQQ 183
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPR-NGTGVIIISPTRELALQIYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 184 VADDYGKCSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESGK----TNLRrctYLVLDEADRMLDMGFEPQ 259
Cdd:cd17942 81 VAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKgflyKNLQ---CLIIDEADRILEIGFEEE 157
|
170 180
....*....|....*....|....*....
gi 93587673 260 IRKIVDQIRPDRQTLMWSATWPKEVRQLA 288
Cdd:cd17942 158 MRQIIKLLPKRRQTMLFSATQTRKVEDLA 186
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
115-298 |
3.05e-48 |
|
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: 167.73 E-value: 3.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 115 PTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHInhqpyLERGDGPICLVLAPTRELAQQVQQVADDYGK-CSR 193
Cdd:cd17962 13 PTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRC-----LTEHRNPSALILTPTRELAVQIEDQAKELMKgLPP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 194 LKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQT 273
Cdd:cd17962 88 MKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILENISHDHQT 167
|
170 180
....*....|....*....|....*
gi 93587673 274 LMWSATWPKEVRQLAEDFLRDYTQI 298
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 ... |
103-279 |
4.58e-48 |
|
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: 168.57 E-value: 4.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 103 VMDVLMDQHFTEPTPIQCQGFPLALS-GRDMVGIAQTGSGKTLAYLLPAIVHI----NHQPYLERGDGPICLVLAPTREL 177
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLlsqkSSNGVGGKQKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 178 AQQVQQVADDYGKCSRLKSTCIYGG--APKgpQIRDLERGVEICIATPGRLIDFLESGKT---NLRRCTYLVLDEADRML 252
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGlaVQK--QERLLKKRPEIVVATPGRLWELIQEGNEhlaNLKSLRFLVLDEADRML 158
|
170 180 190
....*....|....*....|....*....|....*
gi 93587673 253 DMG-FEpQIRKIVDQI-------RPDRQTLMWSAT 279
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, ... |
103-293 |
2.89e-47 |
|
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: 165.06 E-value: 2.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 103 VMDVLMDQHFTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQVQ 182
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKKGQVGALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 183 QVADDYGKCS--RLKSTCIYGGAPKGPQIRDLER-GVEICIATPGRLIDFLESGKT--NLRRCTYLVLDEADRMLDMGFE 257
Cdd:cd17960 81 EVLQSFLEHHlpKLKCQLLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLSRKADkvKVKSLEVLVLDEADRLLDLGFE 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 93587673 258 PQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLR 293
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLR 196
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
105-299 |
1.12e-44 |
|
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: 158.23 E-value: 1.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 105 DVLM---DQHFTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGdgpicLVLAPTRELAQQV 181
Cdd:cd17940 9 ELLMgifEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQA-----LILVPTRELALQT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 182 QQVADDYGKCSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESGKTNLRRCTYLVLDEADRMLDMGFEPQIR 261
Cdd:cd17940 84 SQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQPIIE 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 93587673 262 KIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYTQIN 299
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 ... |
117-299 |
2.30e-40 |
|
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: 146.53 E-value: 2.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 117 PIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAI--VHINHQPyLERGDGPICLVLAPTRELAQQVQQVADDYGKcsRL 194
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIekLQEDQQP-RKRGRAPKVLVLAPTRELANQVTKDFKDITR--KL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 195 KSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVD-QIRPDR-- 271
Cdd:cd17944 92 SVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSvSYKKDSed 171
|
170 180 190
....*....|....*....|....*....|.
gi 93587673 272 --QTLMWSATWPKEVRQLAEDFLRD-YTQIN 299
Cdd:cd17944 172 npQTLLFSATCPDWVYNVAKKYMKSqYEQVD 202
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
109-294 |
2.18e-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: 140.80 E-value: 2.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 109 DQHFTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHI-NHQPYLERGDGPICLVLAPTRELAQQVQQVADD 187
Cdd:cd17961 11 KLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlKAKAESGEEQGTRALILVPTRELAQQVSKVLEQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 188 Y-GKCSR-LKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESGKT-NLRRCTYLVLDEADRMLDMGFEPQIRKIV 264
Cdd:cd17961 91 LtAYCRKdVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLlLLSTLKYLVIDEADLVLSYGYEEDLKSLL 170
|
170 180 190
....*....|....*....|....*....|
gi 93587673 265 DQIRPDRQTLMWSATWPKEVRQLAEDFLRD 294
Cdd:cd17961 171 SYLPKNYQTFLMSATLSEDVEALKKLVLHN 200
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
112-298 |
1.14e-36 |
|
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: 135.91 E-value: 1.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 112 FTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIvhinhQPYLERGDGPICLVLAPTRELAQQVQQVADDYGKC 191
Cdd:cd17939 17 FEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGAL-----QRIDTTVRETQALVLAPTRELAQQIQKVVKALGDY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 192 SRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDR 271
Cdd:cd17939 92 MGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQIYDIFQFLPPET 171
|
170 180
....*....|....*....|....*..
gi 93587673 272 QTLMWSATWPKEVRQLAEDFLRDYTQI 298
Cdd:cd17939 172 QVVLFSATMPHEVLEVTKKFMRDPVRI 198
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
112-298 |
1.67e-36 |
|
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: 135.40 E-value: 1.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 112 FTEPTPIQCQGFPLALSG--RDMVGIAQTGSGKTLAYLLPAivhinhqpyLERGDG----PICLVLAPTRELAQQVQQVA 185
Cdd:cd17963 14 FNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAM---------LSRVDPtlksPQALCLAPTRELARQIGEVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 186 DDYGKCSRLKSTCiyggAPKGPQIRDLERGVE-ICIATPGRLIDFLESGKTNLRRCTYLVLDEADRMLDM-GFEPQIRKI 263
Cdd:cd17963 85 EKMGKFTGVKVAL----AVPGNDVPRGKKITAqIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGHGDQSIRI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 93587673 264 VDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYTQI 298
Cdd:cd17963 161 KRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
326-432 |
3.69e-36 |
|
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: 131.18 E-value: 3.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 326 KLIQLMEEIMAEKENKTIIFVETKRRCDdLTRRMRRDGWPAMCIHGDKSQPERDWVLNEFRSGKAPILIATDVASRGLDV 405
Cdd:pfam00271 2 KLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDL 80
|
90 100
....*....|....*....|....*..
gi 93587673 406 EDVKFVINYDYPNSSEDYVHRIGRTAR 432
Cdd:pfam00271 81 PDVDLVINYDLPWNPASYIQRIGRAGR 107
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
115-289 |
1.53e-35 |
|
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: 132.83 E-value: 1.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 115 PTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPaIVHInhqpylergdgPICLVLAPTRELAQQVQQVADDYGK---C 191
Cdd:cd17938 22 PTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLP-VLQI-----------VVALILEPSRELAEQTYNCIENFKKyldN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 192 SRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQI---- 267
Cdd:cd17938 90 PKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQGNLETINRIYNRIpkit 169
|
170 180
....*....|....*....|....*
gi 93587673 268 -RPDR-QTLMWSATWPK-EVRQLAE 289
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, ... |
103-298 |
1.96e-35 |
|
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: 132.39 E-value: 1.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 103 VMDVLMDQHFTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINhqpyLERGdGPICLVLAPTRELAQQVQ 182
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLD----LERR-HPQVLILAPTREIAVQIH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 183 QVADDYG-KCSRLKSTCIYGGAPKGPQIRDLeRGVEICIATPGRLIDFLESGKTNLRRCTYLVLDEADRMLDMGFEPQIR 261
Cdd:cd17943 76 DVFKKIGkKLEGLKCEVFIGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVN 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 93587673 262 KIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYTQI 298
Cdd:cd17943 155 WIFSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLV 191
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
103-290 |
2.90e-33 |
|
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: 127.48 E-value: 2.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 103 VMDVLMDQHFTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERG--DGPICLVLAPTRELAQQ 180
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGpfNAPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 181 VQQVADDYGKCSRLKSTCIYGGAPKGpQIRDLERG-VEICIATPGRLIDFLESGKTNLRRCTYLVLDEADRMLDMGFEPQ 259
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITGGRTKR-QIRNPHFEeVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 93587673 260 IRKIV-------------DQIRPDRQTLMWSATWPKEVRQLAED 290
Cdd:cd17948 160 LSHFLrrfplasrrsentDGLDPGTQLVLVSATMPSGVGEVLSK 203
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
112-298 |
2.95e-32 |
|
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: 123.71 E-value: 2.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 112 FTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPylergDGPICLVLAPTRELAQQVQQVADDYGKC 191
Cdd:cd18046 19 FEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSL-----KATQALVLAPTRELAQQIQKVVMALGDY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 192 SRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDR 271
Cdd:cd18046 94 MGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKDQIYDIFQKLPPDT 173
|
170 180
....*....|....*....|....*..
gi 93587673 272 QTLMWSATWPKEVRQLAEDFLRDYTQI 298
Cdd:cd18046 174 QVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
112-300 |
3.01e-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: 3.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 112 FTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPylergdGPI-CLVLAPTRELAQQVQQVADDYGK 190
Cdd:cd17950 22 FEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVD------GQVsVLVICHTRELAFQISNEYERFSK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 191 -CSRLKSTCIYGGAPKGPQIRDLERGV-EICIATPGRLIDFLESGKTNLRRCTYLVLDEADRML-DMGFEPQIRKIVDQI 267
Cdd:cd17950 96 yMPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLeQLDMRRDVQEIFRAT 175
|
170 180 190
....*....|....*....|....*....|...
gi 93587673 268 RPDRQTLMWSATWPKEVRQLAEDFLRDYTQINV 300
Cdd:cd17950 176 PHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
353-432 |
4.42e-28 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 107.68 E-value: 4.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 353 DDLTRRMRRDGWPAMCIHGDKSQPERDWVLNEFRSGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYVHRIGRTAR 432
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
112-298 |
4.70e-28 |
|
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: 111.79 E-value: 4.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 112 FTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINhqPYLERgdgPICLVLAPTRELAQQVQQVADDYGKC 191
Cdd:cd18045 19 FEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLD--IQVRE---TQALILSPTRELAVQIQKVLLALGDY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 192 SRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDR 271
Cdd:cd18045 94 MNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKEQIYDVYRYLPPAT 173
|
170 180
....*....|....*....|....*..
gi 93587673 272 QTLMWSATWPKEVRQLAEDFLRDYTQI 298
Cdd:cd18045 174 QVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
103-257 |
2.58e-24 |
|
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: 101.94 E-value: 2.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 103 VMDVLMDQHFTEPTPIQ---------CQGFPLALSGRDMVGIAQTGSGKTLAYLLPaIVhinhQPYLERGDGPI-CLVLA 172
Cdd:cd17956 1 LLKNLQNNGITSAFPVQaavipwllpSSKSTPPYRPGDLCVSAPTGSGKTLAYVLP-IV----QALSKRVVPRLrALIVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 173 PTRELAQQVQQVADDYGKCSRLKsTCIYGG----APKGPQIRDLERG-----VEICIATPGRLIDFLESGKT----NLRr 239
Cdd:cd17956 76 PTKELVQQVYKVFESLCKGTGLK-VVSLSGqksfKKEQKLLLVDTSGrylsrVDILVATPGRLVDHLNSTPGftlkHLR- 153
|
170
....*....|....*...
gi 93587673 240 ctYLVLDEADRMLDMGFE 257
Cdd:cd17956 154 --FLVIDEADRLLNQSFQ 169
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
114-283 |
5.10e-24 |
|
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: 101.68 E-value: 5.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 114 EPTPIQCQGFPlALSGRDMVGI-----------------AQTGSGKTLAYLLPAIVHINHQPYLERGDG----------- 165
Cdd:cd17965 30 KPSPIQTLAIK-KLLKTLMRKVtkqtsneepklevfllaAETGSGKTLAYLAPLLDYLKRQEQEPFEEAeeeyesakdtg 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 166 -PICLVLAPTRELAQQVQQVAddygkcSRLKSTCIYGGAP----KGPQIRDLER----GVEICIATPGRLIDFLESGKTN 236
Cdd:cd17965 109 rPRSVILVPTHELVEQVYSVL------KKLSHTVKLGIKTfssgFGPSYQRLQLafkgRIDILVTTPGKLASLAKSRPKI 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 93587673 237 LRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKE 283
Cdd:cd17965 183 LSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKE 229
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
129-440 |
6.09e-20 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 93.94 E-value: 6.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 129 GRDMVGIAQTGSGKTlaYLLPAIVHinhqpylERGDGPICLVLAPTRELAQQVQQvaddygKCSRLKSTCIYGGAPKgpq 208
Cdd:COG1061 100 GGRGLVVAPTGTGKT--VLALALAA-------ELLRGKRVLVLVPRRELLEQWAE------ELRRFLGDPLAGGGKK--- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 209 irdlERGVEICIATPGRLIDFLESGKTNlRRCTYLVLDEADRmldmGFEPQIRKIVDQIRPDRQTLMwSAT-------WP 281
Cdd:COG1061 162 ----DSDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHH----AGAPSYRRILEAFPAAYRLGL-TATpfrsdgrEI 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 282 KEVR------------QLAEDFLR--DYTQINVGNLELSANHNIL-QIVD---VCMESEKDHKLIQLMEEIMAEKenKTI 343
Cdd:COG1061 232 LLFLfdgivyeyslkeAIEDGYLAppEYYGIRVDLTDERAEYDALsERLRealAADAERKDKILRELLREHPDDR--KTL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 344 IFVETKRRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLNEFRSGKAPILIATDVASRGLDVEDVKFVInYDYPNSSE-D 422
Cdd:COG1061 310 VFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI-LLRPTGSPrE 388
|
330
....*....|....*....
gi 93587673 423 YVHRIGRTAR-STNKGTAY 440
Cdd:COG1061 389 FIQRLGRGLRpAPGKEDAL 407
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
112-306 |
2.29e-18 |
|
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: 84.69 E-value: 2.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 112 FTEPTPIQCQGFPLALSG--RDMVGIAQTGSGKTLAYLLPAIVHINHQPYLergdgPICLVLAPTRELAQQVQQVADDYG 189
Cdd:cd18048 38 FNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLY-----PQCLCLSPTFELALQTGKVVEEMG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 190 K-CSRLKSTCIYGG--APKGPQIRdlergVEICIATPGRLIDFLESGK-TNLRRCTYLVLDEADRMLDM-GFEPQIRKIV 264
Cdd:cd18048 113 KfCVGIQVIYAIRGnrPGKGTDIE-----AQIVIGTPGTVLDWCFKLRlIDVTNISVFVLDEADVMINVqGHSDHSVRVK 187
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 93587673 265 DQIRPDRQTLMWSATWPKEVRQLAEDFLRDYTQINVGNLELS 306
Cdd:cd18048 188 RSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELT 229
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
126-455 |
1.30e-17 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 85.96 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 126 ALSGRDMVGIAQTGSGKTLAYLLPAIVhinhqpylerGDGPiCLVLAPTRELAQ-QVQQvADDYGkcsrLKSTCIYGGAP 204
Cdd:COG0514 29 VLAGRDALVVMPTGGGKSLCYQLPALL----------LPGL-TLVVSPLIALMKdQVDA-LRAAG----IRAAFLNSSLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 205 KGPQ---IRDLERG-VEICIATPGRL-----IDFLESGKTNLrrctyLVLDEA--------DrmldmgFEP---QIRKIV 264
Cdd:COG0514 93 AEERrevLRALRAGeLKLLYVAPERLlnprfLELLRRLKISL-----FAIDEAhcisqwghD------FRPdyrRLGELR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 265 DQIrPDRQTLMWSATWPKEVR-----QLAedfLRDYTQINVG----NLELSanhnilqiVDVCMESEKDHKLIQLMEEIm 335
Cdd:COG0514 162 ERL-PNVPVLALTATATPRVRadiaeQLG---LEDPRVFVGSfdrpNLRLE--------VVPKPPDDKLAQLLDFLKEH- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 336 aeKENKTIIFVETKRRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLNEFRSGKAPILIATdVA-SRGLDVEDVKFVINY 414
Cdd:COG0514 229 --PGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHY 305
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 93587673 415 DYPNSSEDYVHRIGRTARSTNKGTAYTFFTPGNLKQARELI 455
Cdd:COG0514 306 DLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFI 346
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
304-436 |
1.79e-16 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 83.24 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 304 ELSANHNILQIVDVCMESEKDH-KLIQLMEEI----MAEKENKTIIFVETKRRCDDLTRRMRRDGWPAM------CIHGD 372
Cdd:COG1111 313 RLVSDPRFRKAMRLAEEADIEHpKLSKLREILkeqlGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGrfvgqaSKEGD 392
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 93587673 373 K--SQPERDWVLNEFRSGKAPILIATDVASRGLDVEDVKFVINYDyPNSSE-DYVHRIGRTARSTNK 436
Cdd:COG1111 393 KglTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYE-PVPSEiRSIQRKGRTGRKREG 458
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
100-294 |
5.03e-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: 71.29 E-value: 5.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 100 PQYVMDVlMDQHFTEPTPIQCQGFPLALSG--RDMVGIAQTGSGKTLAYLLPAIVHINhqPYLERGDgpiCLVLAPTREL 177
Cdd:cd18047 10 PQLLQGV-YAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVE--PANKYPQ---CLCLSPTYEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 178 AQQVQQVADDYGKcsrLKSTCIYGGAPKGPQirdLERGV----EICIATPGRLIDFLESGK-TNLRRCTYLVLDEADRML 252
Cdd:cd18047 84 ALQTGKVIEQMGK---FYPELKLAYAVRGNK---LERGQkiseQIVIGTPGTVLDWCSKLKfIDPKKIKVFVLDEADVMI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 93587673 253 -DMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRD 294
Cdd:cd18047 158 aTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPD 200
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
320-430 |
1.51e-13 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 73.72 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 320 ESEKDHKLIQLMEEIMAEKEnKTIIFVETKRRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLNEFRSGKAP--ILIATD 397
Cdd:COG0553 531 RSAKLEALLELLEELLAEGE-KVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEApvFLISLK 609
|
90 100 110
....*....|....*....|....*....|....*....
gi 93587673 398 VASRGLDVEDVKFVINYDYP------NSSEDYVHRIGRT 430
Cdd:COG0553 610 AGGEGLNLTAADHVIHYDLWwnpaveEQAIDRAHRIGQT 648
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
136-279 |
4.18e-13 |
|
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: 67.04 E-value: 4.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 136 AQTGSGKTLAYLLPAIVHINHQpylergdGPICLVLAPTRELAQQVQQVADDYGKCSrLKSTCIYGGAPKGPQIRDLERG 215
Cdd:cd00046 8 APTGSGKTLAALLAALLLLLKK-------GKKVLVLVPTKALALQTAERLRELFGPG-IRVAVLVGGSSAEEREKNKLGD 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 93587673 216 VEICIATPGRLIDFLES-GKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQ--IRPDRQTLMWSAT 279
Cdd:cd00046 80 ADIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRkaGLKNAQVILLSAT 146
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
316-432 |
1.03e-12 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350181 [Multi-domain] Cd Length: 134 Bit Score: 65.69 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 316 DVCMESEKDHKLIQLMEEIMAEKENKTIIFVETKRRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLNEFRSGKAPILIA 395
Cdd:cd18794 7 SVRPKDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVA 86
|
90 100 110
....*....|....*....|....*....|....*..
gi 93587673 396 TDVASRGLDVEDVKFVINYDYPNSSEDYVHRIGRTAR 432
Cdd:cd18794 87 TVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGR 123
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
321-435 |
4.82e-12 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350189 [Multi-domain] Cd Length: 142 Bit Score: 63.76 E-value: 4.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 321 SEKDHKLIQ-LMEEIMAEKENKTIIFVETKR-------------------RCDDLTRRMRRDGWPAMcIHGDKSQPErdw 380
Cdd:cd18802 6 IPKLQKLIEiLREYFPKTPDFRGIIFVERRAtavvlsrllkehpstlafiRCGFLIGRGNSSQRKRS-LMTQRKQKE--- 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 93587673 381 VLNEFRSGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYVHRIGRtARSTN 435
Cdd:cd18802 82 TLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARAPN 135
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
126-460 |
5.06e-12 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 68.97 E-value: 5.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 126 ALSGRDMVGIAQTGSGKTLAYLLPAIVHinhqpylergDGpICLVLAPTRELAQ-QVQQVADDYGKCSRLKST------- 197
Cdd:PRK11057 37 VLSGRDCLVVMPTGGGKSLCYQIPALVL----------DG-LTLVVSPLISLMKdQVDQLLANGVAAACLNSTqtreqql 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 198 CIYGGAPKGpQIRDLergveicIATPGRLI--DFLES-GKTNLrrcTYLVLDEADRMLDMG--FEPQIRKIvDQIR---P 269
Cdd:PRK11057 106 EVMAGCRTG-QIKLL-------YIAPERLMmdNFLEHlAHWNP---ALLAVDEAHCISQWGhdFRPEYAAL-GQLRqrfP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 270 DRQTLMWSATWPKEVRQlaeDFLR----DYTQINVGNLElsaNHNILQivdvcMESEKDHKLIQLMEEIMAEKENKTIIF 345
Cdd:PRK11057 174 TLPFMALTATADDTTRQ---DIVRllglNDPLIQISSFD---RPNIRY-----TLVEKFKPLDQLMRYVQEQRGKSGIIY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 346 VETKRRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLNEFRSGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYVH 425
Cdd:PRK11057 243 CNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQ 322
|
330 340 350
....*....|....*....|....*....|....*
gi 93587673 426 RIGRTARSTNKGTAYTFFTPGNLKQAReliKVLEE 460
Cdd:PRK11057 323 ETGRAGRDGLPAEAMLFYDPADMAWLR---RCLEE 354
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
311-428 |
1.99e-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: 59.03 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 311 ILQIVDVCMEsekdhKLIQLMEEIMAEKEnKTIIFVETKRRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLNEFRSGKA 390
Cdd:cd18793 5 IEEVVSGKLE-----ALLELLEELREPGE-KVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPD 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 93587673 391 P--ILIATDVASRGLDVEDVKFVINYDYP-NSS-----EDYVHRIG 428
Cdd:cd18793 79 IrvFLLSTKAGGVGLNLTAANRVILYDPWwNPAveeqaIDRAHRIG 124
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
341-444 |
9.33e-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: 9.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 341 KTIIFVETKRRCDDLTRRMRrdgwpamcihgdksqperdwvlnefrsgkapILIATDVASRGLDVEDVKFVINYDYPNSS 420
Cdd:cd18785 5 KIIVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDPPSSA 53
|
90 100
....*....|....*....|....
gi 93587673 421 EDYVHRIGRTARSTNKGTAYTFFT 444
Cdd:cd18785 54 ASYIQRVGRAGRGGKDEGEVILFV 77
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
304-434 |
2.73e-09 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 60.27 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 304 ELSANHNILQIVDVCMESEKDH----KLIQLMEEIMAEKEN-KTIIFVETKRRCDDLTRRMRRDGWPAM------CIHGD 372
Cdd:PRK13766 325 RLVEDPRFRKAVRKAKELDIEHpkleKLREIVKEQLGKNPDsRIIVFTQYRDTAEKIVDLLEKEGIKAVrfvgqaSKDGD 404
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 93587673 373 K--SQPERDWVLNEFRSGKAPILIATDVASRGLDVEDVKFVINYDyPNSSE-DYVHRIGRTARST 434
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 ... |
327-435 |
5.03e-09 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 55.35 E-value: 5.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 327 LIQLMEEImaEKENKTIIFVETKRRCDDLTRRMRR----DGWP--AMCIHGDKSQPERDWVLNEFRSGKAPILIATDVAS 400
Cdd:cd18796 28 YAEVIFLL--ERHKSTLVFTNTRSQAERLAQRLRElcpdRVPPdfIALHHGSLSRELREEVEAALKRGDLKVVVATSSLE 105
|
90 100 110
....*....|....*....|....*....|....*
gi 93587673 401 RGLDVEDVKFVINYDYPNSSEDYVHRIGRTARSTN 435
Cdd:cd18796 106 LGIDIGDVDLVIQIGSPKSVARLLQRLGRSGHRPG 140
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
64-248 |
5.30e-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: 59.46 E-value: 5.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 64 RLTPYEVDELRRKKEITVRGGDVCPKPvfafhhANFPQYVMDVLMDQHFTEPTPIQCQGFPLALSGRDMVGIAQTGSGKT 143
Cdd:COG1205 12 RASPRYGDQIVHVRTIPAREARYAPWP------DWLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 144 LAYLLPAIVHInhqpylERGDGPICLVLAPTRELAQ-QV---QQVADDYGkcSRLKSTCIYGGAPkgPQIRD--LERGvE 217
Cdd:COG1205 86 LAYLLPVLEAL------LEDPGATALYLYPTKALARdQLrrlRELAEALG--LGVRVATYDGDTP--PEERRwiREHP-D 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 93587673 218 ICIATPgrliDFLESG--------KTNLRRCTYLVLDEA 248
Cdd:COG1205 155 IVLTNP----DMLHYGllphhtrwARFFRNLRYVVIDEA 189
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
330-435 |
5.75e-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: 53.02 E-value: 5.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 330 LMEEI--MAEKENKTIIFVETKRRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLNEFRSGKAPILIATDVASRGLDVED 407
Cdd:cd18790 16 LLGEIrkRVARGERVLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPE 95
|
90 100 110
....*....|....*....|....*....|...
gi 93587673 408 VKFVINYD-----YPNSSEDYVHRIGRTARSTN 435
Cdd:cd18790 96 VSLVAILDadkegFLRSETSLIQTIGRAARNVN 128
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
112-429 |
1.99e-07 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 54.34 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 112 FTEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVH-INHQPYLERGDGPICLVLAPTRELAQQVQQvaddygk 190
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTLAAFLPALDElARRPRPGELPDGLRVLYISPLKALANDIER------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 191 csRLKSTC--IYGGAPKG-PQIR------D---------LERGVEICIATPGRLidFL----ESGKTNLRRCTYLVLDE- 247
Cdd:COG1201 95 --NLRAPLeeIGEAAGLPlPEIRvgvrtgDtpaserqrqRRRPPHILITTPESL--ALlltsPDARELLRGVRTVIVDEi 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 248 ---AD--R--MLDMGFEpqiRkiVDQIRPDR-QTLMWSATwpkeVRQLAE--DFL------RDYTQINVG---NLELSan 308
Cdd:COG1201 171 halAGskRgvHLALSLE---R--LRALAPRPlQRIGLSAT----VGPLEEvaRFLvgyedpRPVTIVDAGagkKPDLE-- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 309 hnILQIVDVCMESEK--DHKLIQLMEEIMAE-KENK-TIIFVETKRRCDDLTRRM--RRDGW--PAMCIHG--DKSQpeR 378
Cdd:COG1201 240 --VLVPVEDLIERFPwaGHLWPHLYPRVLDLiEAHRtTLVFTNTRSQAERLFQRLneLNPEDalPIAAHHGslSREQ--R 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 93587673 379 DWVLNEFRSGKAPILIATdvAS--RGLDVEDVKFVINYDYPNSSEDYVHRIGR 429
Cdd:COG1201 316 LEVEEALKAGELRAVVAT--SSleLGIDIGDVDLVIQVGSPKSVARLLQRIGR 366
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
322-432 |
3.50e-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: 50.05 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 322 EKDHKLIQLMEEIMAE--------KENKTIIFVETKRRCDDLTRRMRRDGW---PAMCI-HGDK------SQPERDWVLN 383
Cdd:cd18801 5 EKIHPKLEKLEEIVKEhfkkkqegSDTRVIIFSEFRDSAEEIVNFLSKIRPgirATRFIgQASGksskgmSQKEQKEVIE 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 93587673 384 EFRSGKAPILIATDVASRGLDVEDVKFVINYDyPNSSE-DYVHRIGRTAR 432
Cdd:cd18801 85 QFRKGGYNVLVATSIGEEGLDIGEVDLIICYD-ASPSPiRMIQRMGRTGR 133
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
135-412 |
7.20e-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: 52.39 E-value: 7.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 135 IAQTGSGKTLAYLLPAIVHINHQpyleRGDGpICLVLaPTRELAQQVQQVADDYGK------CSRLKSTCIYGGAPKGPQ 208
Cdd:COG1203 153 TAPTGGGKTEAALLFALRLAAKH----GGRR-IIYAL-PFTSIINQTYDRLRDLFGedvllhHSLADLDLLEEEEEYESE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 209 IRDLERGVE-----ICIATPGRLIDFLESGKT--NLRRCTY----LVLDEADrMLDMGFEPQIRKIVDQIRPDRQT--LM 275
Cdd:COG1203 227 ARWLKLLKElwdapVVVTTIDQLFESLFSNRKgqERRLHNLansvIILDEVQ-AYPPYMLALLLRLLEWLKNLGGSviLM 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 276 wSATWPKEVRQLAEDFLRDYTQiNVGNLELSANHNILQIVDVCMESEKDHKLIQLMEEImAEKENKTIIFVETKRRCDDL 355
Cdd:COG1203 306 -TATLPPLLREELLEAYELIPD-EPEELPEYFRAFVRKRVELKEGPLSDEELAELILEA-LHKGKSVLVIVNTVKDAQEL 382
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 93587673 356 TRRMRRDGW--PAMCIHG-----DKSQPERDwVLNEFRSGKAPILIATDVASRGLDVeDVKFVI 412
Cdd:COG1203 383 YEALKEKLPdeEVYLLHSrfcpaDRSEIEKE-IKERLERGKPCILVSTQVVEAGVDI-DFDVVI 444
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
125-248 |
7.61e-07 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 49.89 E-value: 7.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 125 LALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPylergdGPICLVLAPTRELAQ-QVQQVADDYGKC-SRLKSTCIYGG 202
Cdd:cd17923 11 AARAGRSVVVTTGTASGKSLCYQLPILEALLRDP------GSRALYLYPTKALAQdQLRSLRELLEQLgLGIRVATYDGD 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 93587673 203 APKGPQIRDLERGVEICIATP-----------GRLIDFLEsgktNLRrctYLVLDEA 248
Cdd:cd17923 85 TPREERRAIIRNPPRILLTNPdmlhyallphhDRWARFLR----NLR---YVVLDEA 134
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
126-286 |
2.36e-06 |
|
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: 48.79 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 126 ALSGRDMVGIAQTGSGKTLAYLLPAIVhinhqpYLERGDGpICLVLAPTRELAQ-QVQQVAddygkcSRLKSTCIYGGAP 204
Cdd:cd18018 24 LLSGRSTLVVLPTGAGKSLCYQLPALL------LRRRGPG-LTLVVSPLIALMKdQVDALP------RAIKAAALNSSLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 205 KGPQIRDLER----GVEICIATPGRLIDflESGKTNLRRCT---YLVLDEADRMLDMG--FEP---QIRKIVDQIRPDRQ 272
Cdd:cd18018 91 REERRRILEKlragEVKILYVSPERLVN--ESFRELLRQTPpisLLVVDEAHCISEWShnFRPdylRLCRVLRELLGAPP 168
|
170
....*....|....
gi 93587673 273 TLMWSATWPKEVRQ 286
Cdd:cd18018 169 VLALTATATKRVVE 182
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
127-455 |
7.96e-06 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 49.12 E-value: 7.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 127 LSGRDMVGIAQTGSGKTLAYLLPAIVHinhqpylergdGPICLVLAPTRELAQ-QVQQVADdygkcSRLKSTCIYGGAPK 205
Cdd:PLN03137 473 MSGYDVFVLMPTGGGKSLTYQLPALIC-----------PGITLVISPLVSLIQdQIMNLLQ-----ANIPAASLSAGMEW 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 206 GPQIRDL-ERGVEIC-----IATPGR------LIDFLES--GKTNLRRctyLVLDEADRMLDMG--FEPQIRK--IVDQI 267
Cdd:PLN03137 537 AEQLEILqELSSEYSkykllYVTPEKvaksdsLLRHLENlnSRGLLAR---FVIDEAHCVSQWGhdFRPDYQGlgILKQK 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 268 RPDRQTLMWSATWPKEVRqlaEDFLRDYTQINVGNLELSAN-----HNILQIVDVCMESEKdhKLIqlmeeimaeKENK- 341
Cdd:PLN03137 614 FPNIPVLALTATATASVK---EDVVQALGLVNCVVFRQSFNrpnlwYSVVPKTKKCLEDID--KFI---------KENHf 679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 342 ---TIIFVETKRRCDDLTRRMRRDGWPAMCIHGDKSQPERDWVLNEFRSGKAPILIATDVASRGLDVEDVKFVINYDYPN 418
Cdd:PLN03137 680 decGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPK 759
|
330 340 350
....*....|....*....|....*....|....*..
gi 93587673 419 SSEDYVHRIGRTARSTNKGTAYTFFTPGNLKQARELI 455
Cdd:PLN03137 760 SIEGYHQECGRAGRDGQRSSCVLYYSYSDYIRVKHMI 796
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
126-286 |
1.09e-05 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 46.76 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 126 ALSGRDMVGIAQTGSGKTLAYLLPAIVhinhqpylergDGPICLVLAPTRELAQ-QVQQvaddygkCSRL--KSTCIYGG 202
Cdd:cd17920 24 VLAGRDVLVVMPTGGGKSLCYQLPALL-----------LDGVTLVVSPLISLMQdQVDR-------LQQLgiRAAALNST 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 203 APKGPQIRDLER----GVEICIATPGRLI--DFLE--SGKTNLRRCTYLVLDEADRMLDMG--FEPQIRKIVDQIR--PD 270
Cdd:cd17920 86 LSPEEKREVLLRikngQYKLLYVTPERLLspDFLEllQRLPERKRLALIVVDEAHCVSQWGhdFRPDYLRLGRLRRalPG 165
|
170
....*....|....*.
gi 93587673 271 RQTLMWSATWPKEVRQ 286
Cdd:cd17920 166 VPILALTATATPEVRE 181
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
116-248 |
1.23e-05 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 46.10 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 116 TPIQCQGF-PLALSGRDMVGIAQTGSGKTLAYLLpAIVHinhqpYLERGDGpICLVLAPTRELaqqVQQVADDYGKC-SR 193
Cdd:cd17921 3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAEL-AILR-----ALATSGG-KAVYIAPTRAL---VNQKEADLRERfGP 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 93587673 194 LKSTCI-YGGAPKGPQIRDLERgvEICIATPGRLiDFL--ESGKTNLRRCTYLVLDEA 248
Cdd:cd17921 73 LGKNVGlLTGDPSVNKLLLAEA--DILVATPEKL-DLLlrNGGERLIQDVRLVVVDEA 127
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
337-443 |
1.54e-05 |
|
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350176 [Multi-domain] Cd Length: 153 Bit Score: 45.32 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 337 EKENKTIIFVETKrrcDDLTRRMRRDGWPAmcIHGDKSQPERDWVLNEFRSGKAPILIATDVASRGLDVED--VKFVINY 414
Cdd:cd18789 47 EQGDKIIVFTDNV---EALYRYAKRLLKPF--ITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPEanVAIQISG 121
|
90 100
....*....|....*....|....*....
gi 93587673 415 DYpNSSEDYVHRIGRTARSTNKGTAYTFF 443
Cdd:cd18789 122 HG-GSRRQEAQRLGRILRPKKGGGKNAFF 149
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
138-248 |
5.91e-05 |
|
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: 44.56 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 138 TGSGKTL-AYLLpaIVHINHQPYLERGDGPICLVLAPTRELA-QQVQQVAddygKCSRLKSTCIYGGAPKGPQIRD---- 211
Cdd:cd18034 25 TGSGKTLiAVML--IKEMGELNRKEKNPKKRAVFLVPTVPLVaQQAEAIR----SHTDLKVGEYSGEMGVDKWTKErwke 98
|
90 100 110
....*....|....*....|....*....|....*..
gi 93587673 212 LERGVEICIATPGRLIDFLESGKTNLRRCTYLVLDEA 248
Cdd:cd18034 99 ELEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
103-396 |
8.85e-05 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 45.66 E-value: 8.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 103 VMDVLMDQHFTEPTPIQCQGFPLAL-SGRDMVGIAQTGSGKTL-AYLlpAIVHinhqpYLERGdgPICLVLAPTRELAQQ 180
Cdd:COG1204 11 VIEFLKERGIEELYPPQAEALEAGLlEGKNLVVSAPTASGKTLiAEL--AILK-----ALLNG--GKALYIVPLRALASE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 181 V-QQVADDYGKcSRLKSTCIYGGAPKGPqiRDLERgVEICIATPGRLIDFLESGKTNLRRCTYLVLDEA------DRmld 253
Cdd:COG1204 82 KyREFKRDFEE-LGIKVGVSTGDYDSDD--EWLGR-YDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAhliddeSR--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 254 mGfePQIRKIVDQIR---PDRQTLMWSATWPKevrqlAEDFLR--DYTQIN-----VGNLELSANHNILQIVDVcmESEK 323
Cdd:COG1204 155 -G--PTLEVLLARLRrlnPEAQIVALSATIGN-----AEEIAEwlDAELVKsdwrpVPLNEGVLYDGVLRFDDG--SRRS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 324 DHKLIQLMEEIMAEKEnKTIIFVETKRRCDDLTRRM-----RRDGWPAM-------------------------CI---- 369
Cdd:COG1204 225 KDPTLALALDLLEEGG-QVLVFVSSRRDAESLAKKLadelkRRLTPEEReeleelaeellevseethtnekladCLekgv 303
|
330 340 350
....*....|....*....|....*....|
gi 93587673 370 ---HGDKSQPERDWVLNEFRSGKAPILIAT 396
Cdd:COG1204 304 afhHAGLPSELRRLVEDAFREGLIKVLVAT 333
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
243-432 |
9.73e-05 |
|
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: 45.11 E-value: 9.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 243 LVLDEADRMLD--MGFepqIRKIVDQIRPDRQTLM-WSATWPKEVRQLAEDFLRDytqINVGNLELSANHNILQIVdvcM 319
Cdd:cd09639 127 LIFDEVHFYDEytLAL---ILAVLEVLKDNDVPILlMSATLPKFLKEYAEKIGYV---EENEPLDLKPNERAPFIK---I 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 320 ESEKDHKlIQLMEEIMAE--KENKTIIFVETKRRCDDLTRRMRRDG--WPAMCIHG-----DKSQPERDwVLNEFRSGKA 390
Cdd:cd09639 198 ESDKVGE-ISSLERLLEFikKGGSVAIIVNTVDRAQEFYQQLKEKGpeEEIMLIHSrftekDRAKKEAE-LLLEFKKSEK 275
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 93587673 391 PILIATDVASRGLDVeDVKFVINYDYPNSSedYVHRIGRTAR 432
Cdd:cd09639 276 FVIVATQVIEASLDI-SVDVMITELAPIDS--LIQRLGRLHR 314
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
126-250 |
3.12e-04 |
|
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: 42.12 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 126 ALSGRDMVgIAQTGSGKTLAYLLPAIVHinhqpyLERGDGPIcLVLAPTRELAQQ----VQQVADDYGKCSRLKstciyg 201
Cdd:cd18035 14 ALNGNTLI-VLPTGLGKTIIAILVAADR------LTKKGGKV-LILAPSRPLVEQhaenLKRVLNIPDKITSLT------ 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 93587673 202 GAPKGPQIRDLERGVEICIATPGRLIDFLESGKTNLRRCTYLVLDEADR 250
Cdd:cd18035 80 GEVKPEERAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
315-396 |
1.79e-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: 39.46 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 315 VDVCMESEKDHKLIQLMEEIMAEKenKTIIFVETKRRCDDLTRRMRrdgwpamCI---HGDKSQPERDWVLNEFRSGKAP 391
Cdd:cd18795 21 VDVMNKFDSDIIVLLKIETVSEGK--PVLVFCSSRKECEKTAKDLA-------GIafhHAGLTREDRELVEELFREGLIK 91
|
....*
gi 93587673 392 ILIAT 396
Cdd:cd18795 92 VLVAT 96
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
114-247 |
2.45e-03 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350794 [Multi-domain] Cd Length: 204 Bit Score: 39.77 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 114 EPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPylERGDGPICLVLAPTRELAQQVQQVADDYgkCSR 193
Cdd:cd18036 2 ELRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKRR--SAGEKGRVVVLVNKVPLVEQQLEKFFKY--FRK 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 93587673 194 L-KSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLESGKTNLR----RCTYLVLDE 247
Cdd:cd18036 78 GyKVTGLSGDSSHKVSFGQIVKASDVIICTPQILINNLLSGREEERvylsDFSLLIFDE 136
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
341-412 |
2.80e-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: 37.92 E-value: 2.80e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 93587673 341 KTIIFVETKRRCDDLTRRMRRDGWPAMCIHGDKSQPERDWV---LNEFRSGKAPILIATDVASRGLDVEDVKFVI 412
Cdd:cd18799 8 KTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDEaliLLFFGELKPPILVTVDLLTTGVDIPEVDNVV 82
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
129-247 |
3.42e-03 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 38.72 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 129 GRDMVGIAQTGSGKTLAYLLPAIVHINHQPylerGDGPICLVLAPTRELAQQVQQVADDYGKCSRLKSTCI--YGGAPKG 206
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEP----EKGVQVLYISPLKALINDQERRLEEPLDEIDLEIPVAvrHGDTSQS 76
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 93587673 207 PQIRDLERGVEICIATPGRLIDFLESGKTN--LRRCTYLVLDE 247
Cdd:cd17922 77 EKAKQLKNPPGILITTPESLELLLVNKKLRelFAGLRYVVVDE 119
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
117-248 |
4.13e-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: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 117 PIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVhinhqpylerGDGpICLVLAPTRELAQ-QVQQVADDYGKCSRLK 195
Cdd:cd18015 21 PLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALC----------SDG-FTLVVSPLISLMEdQLMALKKLGISATMLN 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 93587673 196 STC-------IYGgapkgpQIRDLERGVEICIATP------GRLIDFLESGKtNLRRCTYLVLDEA 248
Cdd:cd18015 90 ASSskehvkwVHA------ALTDKNSELKLLYVTPekiaksKRFMSKLEKAY-NAGRLARIAIDEV 148
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
127-291 |
4.44e-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: 38.47 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 127 LSGRDMVGIAQTGSGKTLAYLLPAIVHInhqpyLERGDGpicLVLAPTRELA-QQVQQVADDYGKCSRLK-STCIYGGAP 204
Cdd:cd18028 15 LKGENLLISIPTASGKTLIAEMAMVNTL-----LEGGKA---LYLVPLRALAsEKYEEFKKLEEIGLKVGiSTGDYDEDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 205 KGPQIRDlergveICIATPGRLIDFLESGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIR---PDRQTLMWSATWP 281
Cdd:cd18028 87 EWLGDYD------IIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPTLESIVARLRrlnPNTQIIGLSATIG 160
|
170
....*....|
gi 93587673 282 KeVRQLAEDF 291
Cdd:cd18028 161 N-PDELAEWL 169
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
107-188 |
6.46e-03 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 38.17 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93587673 107 LMDQHFTEPTPIQ-----------CQGFPlalsgRDMVGIAQTGSGKTLAYLLPAIVhinhqpYLERGDGpiCLVLAPTR 175
Cdd:cd17918 8 LCKSLPFSLTKDQaqaikdiekdlHSPEP-----MDRLLSGDVGSGKTLVALGAALL------AYKNGKQ--VAILVPTE 74
|
90
....*....|...
gi 93587673 176 ELAQQVQQVADDY 188
Cdd:cd17918 75 ILAHQHYEEARKF 87
|
|
| VirD4 |
COG3505 |
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ... |
135-190 |
6.83e-03 |
|
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442728 [Multi-domain] Cd Length: 402 Bit Score: 39.20 E-value: 6.83e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 93587673 135 IAQTGSGKTLAYLLPAIVHinhqpyLERGDGpiCLVLAPTRELAQQVQQVADDYGK 190
Cdd:COG3505 5 IGPTGSGKTVGLVIPNLTQ------LARGES--VVVTDPKGDLAELTAGFRRRAGY 52
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
369-405 |
7.81e-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: 7.81e-03
10 20 30
....*....|....*....|....*....|....*..
gi 93587673 369 IHGDKSQPERDWVLNEFRSGKAPILIATDVASRGLDV 405
Cdd:cd18811 67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDV 103
|
|
| DinG |
COG1199 |
Rad3-related DNA helicase DinG [Replication, recombination and repair]; |
128-153 |
9.87e-03 |
|
Rad3-related DNA helicase DinG [Replication, recombination and repair];
Pssm-ID: 440812 [Multi-domain] Cd Length: 629 Bit Score: 39.14 E-value: 9.87e-03
10 20
....*....|....*....|....*.
gi 93587673 128 SGRDMVGIAQTGSGKTLAYLLPAIVH 153
Cdd:COG1199 32 EGRHLLIEAGTGTGKTLAYLVPALLA 57
|
|
| |
