|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
135-559 |
1.72e-158 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 467.70 E-value: 1.72e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 135 SFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKElepgDGPIAVIVC 214
Cdd:COG0513 3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP----RAPQALILA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 215 PTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMF 294
Cdd:COG0513 79 PTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRML 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 295 DMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVvqgDIGEANEDVTQIVEILH--SGPSKWNwLTRR 372
Cdd:COG0513 159 DMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRI---EVAPENATAETIEQRYYlvDKRDKLE-LLRR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 373 LVEFTSSGSVLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVI 452
Cdd:COG0513 235 LLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 453 NYDVARDIDTHTHRIGRTGRAGEKGVAYTLLTPKDSNfagdLVRNLEGA-NQHVSKELLDLAMQNAWFRKSRFKGGKGKK 531
Cdd:COG0513 315 NYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERR----LLRAIEKLiGQKIEEEELPGFEPVEEKRLERLKPKIKEK 390
|
410 420
....*....|....*....|....*...
gi 133777033 532 LNIGGGGLGYRERPGlGSENSDRGNNNN 559
Cdd:COG0513 391 LKGKKAGRGGRPGPK-GERKARRGKRRR 417
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
74-533 |
2.80e-148 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 446.14 E-value: 2.80e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 74 SKKIIDPLPPIDHSEIDYPPFEKNFYNEHEEITNLTPQQLIDLR--HKLNLrVSGAAPPRPGSSFAHFGFDEQLMHQIRK 151
Cdd:PTZ00110 69 SSTLGKRLQPIDWKSINLVPFEKNFYKEHPEVSALSSKEVDEIRkeKEITI-IAGENVPKPVVSFEYTSFPDYILKSLKN 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 152 SEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIHAECKRFG 231
Cdd:PTZ00110 148 AGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGDGPIVLVLAPTRELAEQIREQCNKFG 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 232 KAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASHVRP 311
Cdd:PTZ00110 228 ASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRP 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 312 DRQTLLFSATFRKKIEKLARDILID-PIRVVQGDIG-EANEDVTQIVEIL--HSGPSKWNWLTRRLveFTSSGSVLLFVT 387
Cdd:PTZ00110 308 DRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDlTACHNIKQEVFVVeeHEKRGKLKMLLQRI--MRDGDKILIFVE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 388 KKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRI 467
Cdd:PTZ00110 386 TKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRI 465
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 133777033 468 GRTGRAGEKGVAYTLLTPKDSNFAGDLVRNLEGANQHVSKELLDLAMQNAWFRKSRFKGGKGKKLN 533
Cdd:PTZ00110 466 GRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSNERSNGTERRRWGGYGRFSN 531
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
145-341 |
1.98e-141 |
|
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: 414.89 E-value: 1.98e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 145 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIH 224
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGEGPIAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 225 AECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRS 304
Cdd:cd17952 81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 133777033 305 IASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVV 341
Cdd:cd17952 161 IVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRVV 197
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
154-494 |
1.70e-105 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 332.15 E-value: 1.70e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 154 YTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHImDQKELepgdGPIAVIVCPTRELCQQIHAECKRFGKA 233
Cdd:PRK11776 24 YTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL-DVKRF----RVQALVLCPTRELADQVAKEIRRLARF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 234 -YNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASHVRPD 312
Cdd:PRK11776 99 iPNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMGFQDAIDAIIRQAPAR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 313 RQTLLFSATFRKKIEKLARDILIDPIRVvqgdIGEANEDVTQI----VEILHSGpsKWNWLTRRLVEFTSSgSVLLFVTK 388
Cdd:PRK11776 179 RQTLLFSATYPEGIAAISQRFQRDPVEV----KVESTHDLPAIeqrfYEVSPDE--RLPALQRLLLHHQPE-SCVVFCNT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 389 KANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRIG 468
Cdd:PRK11776 252 KKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRIG 331
|
330 340
....*....|....*....|....*.
gi 133777033 469 RTGRAGEKGVAYTLLTPKDSNFAGDL 494
Cdd:PRK11776 332 RTGRAGSKGLALSLVAPEEMQRANAI 357
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
123-340 |
3.51e-102 |
|
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) is a component of the 17S U2 snRNP complex. It plays an important role in pre-mRNA splicing and has a role in antiviral innate immunity. DDX46 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350711 [Multi-domain] Cd Length: 222 Bit Score: 314.70 E-value: 3.51e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 123 RVSGAAPPRPGSSFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKEL 202
Cdd:cd17953 1 KVRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 203 EPGDGPIAVIVCPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHV---KKKATNL 279
Cdd:cd17953 81 KPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtanNGRVTNL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 133777033 280 QRVSYLVFDEADRMFDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 340
Cdd:cd17953 161 RRVTYVVLDEADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
145-341 |
1.67e-96 |
|
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: 298.90 E-value: 1.67e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 145 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIH 224
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGDGPIVLVLAPTRELAQQIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 225 AECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRS 304
Cdd:cd17966 81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 133777033 305 IASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVV 341
Cdd:cd17966 161 IVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
145-340 |
2.70e-96 |
|
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: 298.20 E-value: 2.70e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 145 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKElEPGDGPIAVIVCPTRELCQQIH 224
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPK-KKGRGPQALVLAPTRELAMQIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 225 AECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRS 304
Cdd:cd00268 80 EVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 133777033 305 IASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 340
Cdd:cd00268 160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
136-482 |
2.26e-92 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 296.85 E-value: 2.26e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 136 FAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDgPIAVIVCP 215
Cdd:PRK11192 3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRKSGP-PRILILTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 216 TRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFD 295
Cdd:PRK11192 82 TRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 296 MGFEYQVRSIASHVRPDRQTLLFSATFR-KKIEKLARDILIDPIRVvqgdigEAN------EDVTQIVEILHSGPSKWNW 368
Cdd:PRK11192 162 MGFAQDIETIAAETRWRKQTLLFSATLEgDAVQDFAERLLNDPVEV------EAEpsrrerKKIHQWYYRADDLEHKTAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 369 LTRRLVEFTSSGSVLlFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSI 448
Cdd:PRK11192 236 LCHLLKQPEVTRSIV-FVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDV 314
|
330 340 350
....*....|....*....|....*....|....
gi 133777033 449 KTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTL 482
Cdd:PRK11192 315 SHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
85-343 |
7.11e-89 |
|
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: 281.90 E-value: 7.11e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 85 DHSEIdyPPFEKNFYNEHEEITNLTPQQLIDLRHKLNLRVSGAAPPRPGSSFAHFGFDEQLMHQIRKSEYTQPTPIQCQG 164
Cdd:cd18050 15 DLSEL--PKFEKNFYVEHPEVARMTQYDVEELRRKKEITIRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 165 VPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIHAECKRFGKAYNLRSVAVYGG 244
Cdd:cd18050 93 FPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 245 GSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASHVRPDRQTLLFSATFRK 324
Cdd:cd18050 173 APKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPK 252
|
250
....*....|....*....
gi 133777033 325 KIEKLARDILIDPIRVVQG 343
Cdd:cd18050 253 EVRQLAEDFLRDYVQINIG 271
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
135-559 |
2.47e-80 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 265.52 E-value: 2.47e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 135 SFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPI-AVIV 213
Cdd:PRK10590 2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVrALIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 214 CPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRM 293
Cdd:PRK10590 82 TPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 294 FDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIGEANEDVTQIV---------EILHSGPS 364
Cdd:PRK10590 162 LDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVhfvdkkrkrELLSQMIG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 365 KWNWltrrlveftssGSVLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLD 444
Cdd:PRK10590 242 KGNW-----------QQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 445 IPSIKTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTLLTPKDSNFAGDLVRNLEganqhvsKELLDLAM---------- 514
Cdd:PRK10590 311 IEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLK-------KEIPRIAIpgyepdpsik 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 133777033 515 ----QNAwfRKSRFKGGKGKKLNIGGGGLGYRERPGLGSENSDRGNNNN 559
Cdd:PRK10590 384 aepiQNG--RQQRGGGGRGQGGGRGQQQGQPRRGEGGAKSASAKPAEKP 430
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
135-346 |
2.30e-79 |
|
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: 254.72 E-value: 2.30e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 135 SFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDG-----PI 209
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGrrkayPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 210 AVIVCPTRELCQQIHAECKRFgkAYN--LRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVF 287
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKF--SYRsgVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 133777033 288 DEADRMFDMGFEYQVRSIASH----VRPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIG 346
Cdd:cd17967 159 DEADRMLDMGFEPQIRKIVEHpdmpPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVGRVG 221
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
71-511 |
8.02e-79 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 263.57 E-value: 8.02e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 71 IAPSKKIIDPLPPIDHSEIDyppfeKNFYNEHEEITN-LTPQQLIDLRHKLNLRVSGAAPPRPGSSFAHFGFDEQLMHQI 149
Cdd:PLN00206 62 VAKSRVAVGAPKPKRLPATD-----ECFYVRDPGSTSgLSSSQAELLRRKLEIHVKGEAVPPPILSFSSCGLPPKLLLNL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 150 RKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGD--GPIAVIVCPTRELCQQIHAEC 227
Cdd:PLN00206 137 ETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTIRSGHPSEqrNPLAMVLTPTRELCVQVEDQA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 228 KRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIAS 307
Cdd:PLN00206 217 KVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQ 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 308 HVrPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIGEANEDVTQIVEILHSGPSKwnwltRRLVEFTSSGS-----V 382
Cdd:PLN00206 297 AL-SQPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKK-----QKLFDILKSKQhfkppA 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 383 LLFVTKKANAEELASNL-KQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDID 461
Cdd:PLN00206 371 VVFVSSRLGADLLANAItVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIK 450
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 133777033 462 THTHRIGRTGRAGEKGVAYTLLTPKDSNFAGDLVRNLEGANQHVSKELLD 511
Cdd:PLN00206 451 EYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKSSGAAIPRELAN 500
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
111-340 |
5.66e-77 |
|
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: 248.77 E-value: 5.66e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 111 QQLIDLRHKLNLRVSGAAPPRPGSSFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIW 190
Cdd:cd18049 1 QEVEQYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 191 PMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLID 270
Cdd:cd18049 81 PAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLID 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 271 HVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 340
Cdd:cd18049 161 FLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHI 230
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
130-488 |
7.25e-76 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 254.07 E-value: 7.25e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 130 PRPGSS-FAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAF---IWPMLIHIMDQKELEPG 205
Cdd:PRK01297 82 PQEGKTrFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFlisIINQLLQTPPPKERYMG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 206 DgPIAVIVCPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEG-AEIVVCTPGRLIDHVKKKATNLQRVSY 284
Cdd:PRK01297 162 E-PRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQRGEVHLDMVEV 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 285 LVFDEADRMFDMGFEYQVRSIASHVRP--DRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIGEANEDVTQIVEILhSG 362
Cdd:PRK01297 241 MVLDEADRMLDMGFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAV-AG 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 363 PSKWNwLTRRLVEFTSSGSVLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARG 442
Cdd:PRK01297 320 SDKYK-LLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRG 398
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 133777033 443 LDIPSIKTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTLLTPKDS 488
Cdd:PRK01297 399 IHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDA 444
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
78-346 |
5.23e-74 |
|
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: 242.18 E-value: 5.23e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 78 IDPLPPIDHSEIdYPPFEK--NFyNEHEEItnltpqqLIDlrhklnlrVSGAAPPRPGSSFAHFGFDEQLMHQIRKSEYT 155
Cdd:cd18052 2 IPPPPPEDEDEI-FATIQTgiNF-DKYDEI-------PVE--------VTGRNPPPAILTFEEANLCETLLKNIRKAGYE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 156 QPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIM-------DQKELEPgdgPIAVIVCPTRELCQQIHAECK 228
Cdd:cd18052 65 KPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMkegltasSFSEVQE---PQALIVAPTRELANQIFLEAR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 229 RFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASH 308
Cdd:cd18052 142 KFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSE 221
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 133777033 309 V----RPDRQTLLFSATFRKKIEKLARDIL-IDPIRVVQGDIG 346
Cdd:cd18052 222 PgmpsKEDRQTLMFSATFPEEIQRLAAEFLkEDYLFLTVGRVG 264
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
136-482 |
4.25e-73 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 245.27 E-value: 4.25e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 136 FAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPG--DGPIAVIV 213
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDRkvNQPRALIM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 214 CPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRM 293
Cdd:PRK04837 90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 294 FDMGFEYQVRSIASHVRP--DRQTLLFSATFRKKIEKLARDILIDPIRVVqgdIGEANEDVTQIVEILH--SGPSKWNwL 369
Cdd:PRK04837 170 FDLGFIKDIRWLFRRMPPanQRLNMLFSATLSYRVRELAFEHMNNPEYVE---VEPEQKTGHRIKEELFypSNEEKMR-L 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 370 TRRLVEFTSSGSVLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIK 449
Cdd:PRK04837 246 LQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVT 325
|
330 340 350
....*....|....*....|....*....|...
gi 133777033 450 TVINYDVARDIDTHTHRIGRTGRAGEKGVAYTL 482
Cdd:PRK04837 326 HVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
134-499 |
2.03e-72 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 249.38 E-value: 2.03e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 134 SSFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHImdQKELEpgdGPIAVIV 213
Cdd:PRK11634 6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNL--DPELK---APQILVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 214 CPTRELCQQIHAECKRFGK-AYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADR 292
Cdd:PRK11634 81 APTRELAVQVAEAMTDFSKhMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 293 MFDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV-VQGDIgEANEDVTQIVEILHsGPSKWNWLTR 371
Cdd:PRK11634 161 MLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVrIQSSV-TTRPDISQSYWTVW-GMRKNEALVR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 372 RLvEFTSSGSVLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTV 451
Cdd:PRK11634 239 FL-EAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLV 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 133777033 452 INYDVARDIDTHTHRIGRTGRAGEKGVAYTLLTPKDSNfagdLVRNLE 499
Cdd:PRK11634 318 VNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERR----LLRNIE 361
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
145-340 |
3.77e-72 |
|
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: 235.29 E-value: 3.77e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 145 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMD---QKELEPGDGPIAVIVCPTRELCQ 221
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRlppLDEETKDDGPYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 222 QIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQ 301
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 133777033 302 VRSIASHV-----RPD---------------RQTLLFSATFRKKIEKLARDILIDPIRV 340
Cdd:cd17945 161 VTKILDAMpvsnkKPDteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
135-479 |
2.72e-70 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 242.16 E-value: 2.72e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 135 SFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKEL---EPGDgPIAV 211
Cdd:PRK04537 10 TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALadrKPED-PRAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 212 IVCPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKK-KATNLQRVSYLVFDEA 290
Cdd:PRK04537 89 ILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQhKVVSLHACEICVLDEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 291 DRMFDMGFEYQVRSIASHV--RPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIGEANEDVTQivEILHSGPSKWNW 368
Cdd:PRK04537 169 DRMFDLGFIKDIRFLLRRMpeRGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQ--RIYFPADEEKQT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 369 LTRRLVEFTSSGSVLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSI 448
Cdd:PRK04537 247 LLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGV 326
|
330 340 350
....*....|....*....|....*....|.
gi 133777033 449 KTVINYDVARDIDTHTHRIGRTGRAGEKGVA 479
Cdd:PRK04537 327 KYVYNYDLPFDAEDYVHRIGRTARLGEEGDA 357
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
156-340 |
7.37e-69 |
|
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: 226.07 E-value: 7.37e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 156 QPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKE---LEPGDGPIAVIVCPTRELCQQIHAECKRFGK 232
Cdd:cd17951 12 KPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEKklpFIKGEGPYGLIVCPSRELARQTHEVIEYYCK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 233 AYN------LRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIA 306
Cdd:cd17951 92 ALQeggypqLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMIDMGFEEDIRTIF 171
|
170 180 190
....*....|....*....|....*....|....
gi 133777033 307 SHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 340
Cdd:cd17951 172 SYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
145-341 |
1.50e-68 |
|
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: 225.04 E-value: 1.50e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 145 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKEL-EPGDGPIAVIVCPTRELCQQI 223
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPrEQRNGPGVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 224 HAECKRFgKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVR 303
Cdd:cd17958 81 EAECSKY-SYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 133777033 304 SIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVV 341
Cdd:cd17958 160 KILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIVY 197
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
145-343 |
5.10e-65 |
|
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: 215.53 E-value: 5.10e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 145 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKElepGDGPIAVIVCPTRELCQQIH 224
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRK---KKGLRALILAPTRELASQIY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 225 AECKRFGKAYNLRSVAVygGGSMWEQAKALQE---GAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQ 301
Cdd:cd17957 78 RELLKLSKGTGLRIVLL--SKSLEAKAKDGPKsitKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQ 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 133777033 302 VRSI-ASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVVQG 343
Cdd:cd17957 156 TDEIlAACTNPNLQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
135-340 |
2.09e-64 |
|
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: 214.10 E-value: 2.09e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 135 SFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKElepgdGPIAVIVC 214
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQ-----RFFALVLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 215 PTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKK-KATNLQRVSYLVFDEADRM 293
Cdd:cd17954 76 PTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENtKGFSLKSLKFLVMDEADRL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 133777033 294 FDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 340
Cdd:cd17954 156 LNMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
134-340 |
3.61e-63 |
|
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: 210.62 E-value: 3.61e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 134 SSFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHImdqKELEPGDGPIAVIV 213
Cdd:cd17959 1 GGFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKL---KAHSPTVGARALIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 214 CPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRM 293
Cdd:cd17959 78 SPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 133777033 294 FDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 340
Cdd:cd17959 158 FEMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
158-329 |
1.19e-62 |
|
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: 1.19e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 158 TPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKelepgDGPIAVIVCPTRELCQQIHAECKRFGKAYNLR 237
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLD-----NGPQALVLAPTRELAEQIYEELKKLGKGLGLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 238 SVAVYGGGSMWEQAKALQeGAEIVVCTPGRLIDHVKKKaTNLQRVSYLVFDEADRMFDMGFEYQVRSIASHVRPDRQTLL 317
Cdd:pfam00270 76 VASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQER-KLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILL 153
|
170
....*....|..
gi 133777033 318 FSATFRKKIEKL 329
Cdd:pfam00270 154 LSATLPRNLEDL 165
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
124-346 |
2.26e-58 |
|
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: 199.11 E-value: 2.26e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 124 VSGAAPPRPGSSFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQ---K 200
Cdd:cd18051 11 ATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQgpgE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 201 ELEPGDG--------PIAVIVCPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHV 272
Cdd:cd18051 91 SLPSESGyygrrkqyPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDML 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 133777033 273 KKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASH-VRP---DRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIG 346
Cdd:cd18051 171 ERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQdTMPptgERQTLMFSATFPKEIQMLARDFLDNYIFLAVGRVG 248
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
135-487 |
3.43e-58 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 203.90 E-value: 3.43e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 135 SFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLiHIMDQKELEPGdgpiAVIVC 214
Cdd:PTZ00424 29 SFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAAL-QLIDYDLNACQ----ALILA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 215 PTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMF 294
Cdd:PTZ00424 104 PTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEML 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 295 DMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIGEANEDVTQIVEILHSGPSKWNWLTRrLV 374
Cdd:PTZ00424 184 SRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCD-LY 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 375 EFTSSGSVLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINY 454
Cdd:PTZ00424 263 ETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINY 342
|
330 340 350
....*....|....*....|....*....|...
gi 133777033 455 DVARDIDTHTHRIGRTGRAGEKGVAYTLLTPKD 487
Cdd:PTZ00424 343 DLPASPENYIHRIGRSGRFGRKGVAINFVTPDD 375
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
149-355 |
6.43e-58 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 196.17 E-value: 6.43e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 149 IRKSEYTQPTPIQCQGVPVALSG-RDMIGIAKTGSGKTAAFIWPMLIHIMdqkelePGDGPIAVIVCPTRELCQQIHAEC 227
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALK------RGKGGRVLVLVPTRELAEQWAEEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 228 KRFGKAYNLRSVAVYGGGSMWEQAKALQEG-AEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIA 306
Cdd:smart00487 75 KKLGPSLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 133777033 307 SHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDigEANEDVTQI 355
Cdd:smart00487 155 KLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
136-337 |
5.40e-56 |
|
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: 190.90 E-value: 5.40e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 136 FAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLihimdQKELEPGDGPIAVIVCP 215
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPIL-----QRLSEDPYGIFALVLTP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 216 TRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVK---KKATNLQRVSYLVFDEADR 292
Cdd:cd17955 76 TRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEADR 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 133777033 293 MFDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDP 337
Cdd:cd17955 156 LLTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
145-340 |
2.04e-53 |
|
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: 183.61 E-value: 2.04e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 145 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPmlihIMDQKELEPGDGPI--AVIVCPTRELCQQ 222
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLP----ILERLLYRPKKKAAtrVLVLVPTRELAMQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 223 IHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKAT-NLQRVSYLVFDEADRMFDMGFEYQ 301
Cdd:cd17947 77 CFSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSfDLDSIEILVLDEADRMLEEGFADE 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 133777033 302 VRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 340
Cdd:cd17947 157 LKEILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
352-483 |
1.18e-52 |
|
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: 179.24 E-value: 1.18e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 352 VTQIVEILHSGpSKWNWLTRRLVEFTSSGSVLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIP 431
Cdd:cd18787 1 IKQLYVVVEEE-EKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 133777033 432 VLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTLL 483
Cdd:cd18787 80 VLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
145-340 |
2.02e-52 |
|
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: 180.82 E-value: 2.02e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 145 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKelepgDGPIAVIVCPTRELCQQIH 224
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEH-----RNPSALILTPTRELAVQIE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 225 AECKRFGKAY-NLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVR 303
Cdd:cd17962 76 DQAKELMKGLpPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVL 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 133777033 304 SIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 340
Cdd:cd17962 156 DILENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
149-340 |
1.40e-49 |
|
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: 173.24 E-value: 1.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 149 IRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKeLEPGDGPIAVIVCPTRELCQQIHAECK 228
Cdd:cd17941 5 LKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRER-WTPEDGLGALIISPTRELAMQIFEVLR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 229 RFGKAYNLRSVAVYGGGSMWEQAKALQEgAEIVVCTPGRLIDHVKKK----ATNLQrvsYLVFDEADRMFDMGFEYQVRS 304
Cdd:cd17941 84 KVGKYHSFSAGLIIGGKDVKEEKERINR-MNILVCTPGRLLQHMDETpgfdTSNLQ---MLVLDEADRILDMGFKETLDA 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 133777033 305 IASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 340
Cdd:cd17941 160 IVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYI 195
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
141-334 |
1.14e-48 |
|
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350722 [Multi-domain] Cd Length: 211 Bit Score: 171.23 E-value: 1.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 141 FDEQLMHQIRKSEYTQPTPIQCQGVPVALS-GRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTREL 219
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGVSALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 220 CQQIHAECKR---FGKAYNLRSvaVYGGGSMWEQAKALQ-EGAEIVVCTPGRLIDHVK--KKATNLQRVSYLVFDEADRM 293
Cdd:cd17964 81 ALQIAAEAKKllqGLRKLRVQS--AVGGTSRRAELNRLRrGRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 133777033 294 FDMGFEYQVRSIASHVRP----DRQTLLFSATFRKKIEKLARDIL 334
Cdd:cd17964 159 LDMGFRPDLEQILRHLPEknadPRQTLLFSATVPDEVQQIARLTL 203
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
151-341 |
6.21e-48 |
|
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: 168.92 E-value: 6.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 151 KSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIM-DQKELEPGDGPIAVIVCPTRELCQQIHAECKR 229
Cdd:cd17949 8 KMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLsLEPRVDRSDGTLALVLVPTRELALQIYEVLEK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 230 FGK-AYNLRSVAVYGGgsmwEQAKA----LQEGAEIVVCTPGRLIDHVKK-KATNLQRVSYLVFDEADRMFDMGFEYQVR 303
Cdd:cd17949 88 LLKpFHWIVPGYLIGG----EKRKSekarLRKGVNILIATPGRLLDHLKNtQSFDVSNLRWLVLDEADRLLDMGFEKDIT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 133777033 304 SIASHVR-------------PDRQTLLFSATFRKKIEKLARDILIDPIRVV 341
Cdd:cd17949 164 KILELLDdkrskaggekskpSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
149-341 |
1.26e-46 |
|
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: 1.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 149 IRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIHAECK 228
Cdd:cd17960 5 VAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKKGQVGALIISPTRELATQIYEVLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 229 RFGKAY--NLRSVAVYGGGSMWEQ-AKALQEGAEIVVCTPGRLIDHVKKKAT--NLQRVSYLVFDEADRMFDMGFEYQVR 303
Cdd:cd17960 85 SFLEHHlpKLKCQLLIGGTNVEEDvKKFKRNGPNILVGTPGRLEELLSRKADkvKVKSLEVLVLDEADRLLDLGFEADLN 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 133777033 304 SIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVV 341
Cdd:cd17960 165 RILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRVV 202
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
142-338 |
1.63e-46 |
|
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: 164.68 E-value: 1.63e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 142 DEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGD-GPIAVIVCPTRELC 220
Cdd:cd17961 2 DPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGEEqGTRALILVPTRELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 221 QQIHAE-------CKRFgkaynLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKAT-NLQRVSYLVFDEADR 292
Cdd:cd17961 82 QQVSKVleqltayCRKD-----VRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLlLLSTLKYLVIDEADL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 133777033 293 MFDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPI 338
Cdd:cd17961 157 VLSYGYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
136-340 |
1.92e-45 |
|
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or p54) participates in mRNA regulation mediated by miRNA-mediated silencing. It also plays a role in global and transcript-specific messenger RNA (mRNA) storage, translational repression, and decay. It is a member of the DEAD-box helicase family, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350698 [Multi-domain] Cd Length: 201 Bit Score: 161.70 E-value: 1.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 136 FAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHImDQKElepgDGPIAVIVCP 215
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKI-DPKK----DVIQALILVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 216 TRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFD 295
Cdd:cd17940 76 TRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 133777033 296 MGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 340
Cdd:cd17940 156 QDFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
145-322 |
2.35e-45 |
|
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: 162.79 E-value: 2.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 145 LMHQIRKSEYTQPTPIQCQGVPVALS-GRDMIGIAKTGSGKTAAFIWPMLIHIMDQKE----LEPGDGPIAVIVCPTREL 219
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLLSQKSsngvGGKQKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 220 CQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKK---ATNLQRVSYLVFDEADRMFDM 296
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGnehLANLKSLRFLVLDEADRMLEK 160
|
170 180 190
....*....|....*....|....*....|....
gi 133777033 297 G-FEyQVRSIASHV-------RPDRQTLLFSATF 322
Cdd:cd17946 161 GhFA-ELEKILELLnkdragkKRKRQTFVFSATL 193
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
146-331 |
6.19e-44 |
|
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: 157.14 E-value: 6.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 146 MHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPmLIHIMDQKELEPGDGPIAVIVCPTRELCQQIHA 225
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIP-AIELLYKLKFKPRNGTGVIIISPTRELALQIYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 226 ECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKA----TNLQrvsYLVFDEADRMFDMGFEYQ 301
Cdd:cd17942 81 VAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKgflyKNLQ---CLIIDEADRILEIGFEEE 157
|
170 180 190
....*....|....*....|....*....|
gi 133777033 302 VRSIASHVRPDRQTLLFSATFRKKIEKLAR 331
Cdd:cd17942 158 MRQIIKLLPKRRQTMLFSATQTRKVEDLAR 187
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
142-338 |
7.52e-38 |
|
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called DEAD box RNA helicase DEAD5) and DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH)) are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350721 [Multi-domain] Cd Length: 196 Bit Score: 140.02 E-value: 7.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 142 DEQLMHQIRKSEYTQPTPIQCQGVPVALSG--RDMIGIAKTGSGKTAAFIWPMLIHImDQKELEPGdgpiAVIVCPTREL 219
Cdd:cd17963 2 KPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRV-DPTLKSPQ----ALCLAPTREL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 220 CQQIHAECKRFGK------AYNLRSVAVYGGGSMWEQakalqegaeIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRM 293
Cdd:cd17963 77 ARQIGEVVEKMGKftgvkvALAVPGNDVPRGKKITAQ---------IVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVM 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 133777033 294 FDM-GFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPI 338
Cdd:cd17963 148 LDTqGHGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNAN 193
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
133-340 |
1.16e-37 |
|
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: 139.79 E-value: 1.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 133 GSSFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLihimdqKELEPGDGPIAVI 212
Cdd:cd17950 1 SSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTL------QQLEPVDGQVSVL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 213 V-CPTRELCQQIHAECKRFGKaY--NLRSVAVYGGGSMWEQAKALQ-EGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFD 288
Cdd:cd17950 75 ViCHTRELAFQISNEYERFSK-YmpNVKTAVFFGGVPIKKDIEVLKnKCPHIVVGTPGRILALVREKKLKLSHVKHFVLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 133777033 289 EADRMF-DMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 340
Cdd:cd17950 154 ECDKMLeQLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEI 206
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
140-340 |
3.64e-37 |
|
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: 138.23 E-value: 3.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 140 GFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHI-MDQKELEpgdgpiAVIVCPTRE 218
Cdd:cd17939 3 GLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIdTTVRETQ------ALVLAPTRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 219 LCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGF 298
Cdd:cd17939 77 LAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 133777033 299 EYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 340
Cdd:cd17939 157 KDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
145-344 |
1.96e-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: 128.64 E-value: 1.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 145 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPG--DGPIAVIVCPTRELCQQ 222
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGpfNAPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 223 IHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQV 302
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 133777033 303 RSIASH-----VRPDR--------QTLLFSATFRKKIEKLARDIL-IDPIRVVQGD 344
Cdd:cd17948 161 SHFLRRfplasRRSENtdgldpgtQLVLVSATMPSGVGEVLSKVIdVDSIETVTSD 216
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
136-340 |
2.94e-33 |
|
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: 127.05 E-value: 2.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 136 FAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMdqkelepgdgpiAVIVCP 215
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIVV------------ALILEP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 216 TRELCQQIHAECKRFgKAY----NLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEAD 291
Cdd:cd17938 69 SRELAEQTYNCIENF-KKYldnpKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEAD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 133777033 292 RMFDMGFEYQVRSIASH-----VRPDR-QTLLFSATFRK-KIEKLARDILIDPIRV 340
Cdd:cd17938 148 RLLSQGNLETINRIYNRipkitSDGKRlQVIVCSATLHSfEVKKLADKIMHFPTWV 203
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
136-341 |
3.61e-33 |
|
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: 126.79 E-value: 3.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 136 FAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIwpmlIHIMDQKELEPgDGPIAVIVCP 215
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFS----ISILQQIDTSL-KATQALVLAP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 216 TRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFD 295
Cdd:cd18046 76 TRELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 133777033 296 MGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVV 341
Cdd:cd18046 156 RGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRIL 201
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
364-474 |
1.22e-31 |
|
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: 118.85 E-value: 1.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 364 SKWNWLtRRLVEFTSSGSVLLFV--TKKANAEELasnLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAAR 441
Cdd:pfam00271 1 EKLEAL-LELLKKERGGKVLIFSqtKKTLEAELL---LEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAER 76
|
90 100 110
....*....|....*....|....*....|...
gi 133777033 442 GLDIPSIKTVINYDVARDIDTHTHRIGRTGRAG 474
Cdd:pfam00271 77 GLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
145-331 |
2.17e-31 |
|
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: 121.22 E-value: 2.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 145 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLiHIMDqkeLEPGdGPIAVIVCPTRELCQQIH 224
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIAL-ESLD---LERR-HPQVLILAPTREIAVQIH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 225 AECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRS 304
Cdd:cd17943 76 DVFKKIGKKLEGLKCEVFIGGTPVKEDKKKLKGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNW 155
|
170 180
....*....|....*....|....*...
gi 133777033 305 IASHVRPDRQTLLFSATFRKK-IEKLAR 331
Cdd:cd17943 156 IFSSLPKNKQVIAFSATYPKNlDNLLAR 183
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
145-331 |
6.98e-31 |
|
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: 121.20 E-value: 6.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 145 LMHQIRKSEYTQPTPIQCQGVPVALSG---------RDMIGIAKTGSGKTAAFIWPMLihimdQKeLEPGDGPI--AVIV 213
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIV-----QA-LSKRVVPRlrALIV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 214 CPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEG--------AEIVVCTPGRLIDHVKKKAT-NLQRVSY 284
Cdd:cd17956 75 VPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRLVDHLNSTPGfTLKHLRF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 133777033 285 LVFDEADRMFDMGFEY---QV-RSIASHVRPDR----------------QTLLFSATFRKKIEKLAR 331
Cdd:cd17956 155 LVIDEADRLLNQSFQDwleTVmKALGRPTAPDLgsfgdanllersvrplQKLLFSATLTRDPEKLSS 221
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
136-341 |
7.00e-31 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor 4A-III (EIF4AIII, also known as DDX48) is part of the exon junction complex (EJC) that plays a major role in posttranscriptional regulation of mRNA. EJC consists of four proteins (eIF4AIII, Barentsz [Btz], Mago, and Y14), mRNA, and ATP. DDX48 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350803 [Multi-domain] Cd Length: 201 Bit Score: 120.26 E-value: 7.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 136 FAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLiHIMDQKELEPGdgpiAVIVCP 215
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVL-QCLDIQVRETQ----ALILSP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 216 TRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFD 295
Cdd:cd18045 76 TRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 133777033 296 MGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVV 341
Cdd:cd18045 156 KGFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRIL 201
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
159-321 |
1.49e-30 |
|
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: 119.18 E-value: 1.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 159 PIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIM-DQKELEPGDGPIAVIVCPTRELCQQIHAECKRFGKayNLR 237
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQeDQQPRKRGRAPKVLVLAPTRELANQVTKDFKDITR--KLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 238 SVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIAS-----HVRPD 312
Cdd:cd17944 93 VACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSvsykkDSEDN 172
|
....*....
gi 133777033 313 RQTLLFSAT 321
Cdd:cd17944 173 PQTLLFSAT 181
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
393-474 |
9.44e-29 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 109.99 E-value: 9.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 393 EELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRIGRTGR 472
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 133777033 473 AG 474
Cdd:smart00490 81 AG 82
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
171-469 |
5.83e-26 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 113.20 E-value: 5.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 171 GRDMIGIAKTGSGKTAafiwpMLIHIMDQKelepGDGPIAVIVCPTRELCQQIHAECKRFgkaynLRSVAVYGGgsmweq 250
Cdd:COG1061 100 GGRGLVVAPTGTGKTV-----LALALAAEL----LRGKRVLVLVPRRELLEQWAEELRRF-----LGDPLAGGG------ 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 251 akALQEGAEIVVCTPGRLIDHVKKKATNlQRVSYLVFDEADRMFDMGFeyqvRSIASHVRPDRqTLLFSAT--------- 321
Cdd:COG1061 160 --KKDSDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHHAGAPSY----RRILEAFPAAY-RLGLTATpfrsdgrei 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 322 ---------FRKKIEKLARDILIDPIRVV---------QGDIGEANEDVTQivEILHSGPSKWNWLTRRLVEFTSSGSVL 383
Cdd:COG1061 232 llflfdgivYEYSLKEAIEDGYLAPPEYYgirvdltdeRAEYDALSERLRE--ALAADAERKDKILRELLREHPDDRKTL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 384 LFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVInydVARDIDTH 463
Cdd:COG1061 310 VFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI---LLRPTGSP 386
|
....*....
gi 133777033 464 TH---RIGR 469
Cdd:COG1061 387 REfiqRLGR 395
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
152-341 |
4.47e-21 |
|
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: 93.21 E-value: 4.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 152 SEYTQPTPIQCQGVPvALSGRDMIGI-----------------AKTGSGKTAAFIWPMLIHIMDQKELEPGDG------- 207
Cdd:cd17965 26 DEEIKPSPIQTLAIK-KLLKTLMRKVtkqtsneepklevfllaAETGSGKTLAYLAPLLDYLKRQEQEPFEEAeeeyesa 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 208 -----PIAVIVCPTRELCQQIHAECKRFGKA--YNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQ 280
Cdd:cd17965 105 kdtgrPRSVILVPTHELVEQVYSVLKKLSHTvkLGIKTFSSGFGPSYQRLQLAFKGRIDILVTTPGKLASLAKSRPKILS 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 133777033 281 RVSYLVFDEADRMFDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVV 341
Cdd:cd17965 185 RVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLRKLFPDVVRIA 245
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
121-337 |
1.76e-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: 85.46 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 121 NLRVSGAAPPRP---GSSFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSG--RDMIGIAKTGSGKTAAFIWPMLIH 195
Cdd:cd18048 2 RVEVLQRDPTSPlfsVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 196 ImDQKELEPGdgpiAVIVCPTRELCQQIHAECKRFGKAYNLRSV--AVYGGgsmwEQAKALQEGAEIVVCTPGRLIDHV- 272
Cdd:cd18048 82 V-DALKLYPQ----CLCLSPTFELALQTGKVVEEMGKFCVGIQViyAIRGN----RPGKGTDIEAQIVIGTPGTVLDWCf 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 133777033 273 KKKATNLQRVSYLVFDEADRMFDM-GFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDP 337
Cdd:cd18048 153 KLRLIDVTNISVFVLDEADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDP 218
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
135-337 |
1.86e-17 |
|
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: 81.69 E-value: 1.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 135 SFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSG--RDMIGIAKTGSGKTAAFIWPMLIHImdqkelEPG-DGPIAV 211
Cdd:cd18047 2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV------EPAnKYPQCL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 212 IVCPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEgaEIVVCTPGRLIDH-VKKKATNLQRVSYLVFDEA 290
Cdd:cd18047 76 CLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISE--QIVIGTPGTVLDWcSKLKFIDPKKIKVFVLDEA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 133777033 291 DRMF-DMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDP 337
Cdd:cd18047 154 DVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
169-480 |
1.23e-16 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 83.79 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 169 LSGRDMIGIAKTGSGKTA-AFIWpMLIHIMDqkelepgdGPIAVIVCPTRELCQQIHAECKRFGKAYNLRSVAVYGGgsm 247
Cdd:COG1204 36 LEGKNLVVSAPTASGKTLiAELA-ILKALLN--------GGKALYIVPLRALASEKYREFKRDFEELGIKVGVSTGD--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 248 WEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEA------DRmfdmGFEYQVrsIASHVR---PDRQTLLF 318
Cdd:COG1204 104 YDSDDEWLGRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAhliddeSR----GPTLEV--LLARLRrlnPEAQIVAL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 319 SATFrKKIEKLAR----DILIDPIRVVQGDIGEANEDVTQIVEILHSGPSKWNWLTRRLVEftSSGSVLLFVTKKANAEE 394
Cdd:COG1204 178 SATI-GNAEEIAEwldaELVKSDWRPVPLNEGVLYDGVLRFDDGSRRSKDPTLALALDLLE--EGGQVLVFVSSRRDAES 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 395 LASNLKQE------GHNLGLL-------------------------------HGDMDQSERNKVISDFKKKDIPVLVATD 437
Cdd:COG1204 255 LAKKLADElkrrltPEEREELeelaeellevseethtnekladclekgvafhHAGLPSELRRLVEDAFREGLIKVLVATP 334
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 133777033 438 VAARGLDIPSiKTVINYDVAR----DIDTHTHR--IGRTGRAG--EKGVAY 480
Cdd:COG1204 335 TLAAGVNLPA-RRVIIRDTKRggmvPIPVLEFKqmAGRAGRPGydPYGEAI 384
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
357-488 |
1.21e-13 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 74.77 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 357 EILHSGPSKwnwlTRRLVEFT----SSGSVLLFVTKKANAEELASNLKQEGHNLGLLHGD--------MDQSERNKVISD 424
Cdd:COG1111 331 DIEHPKLSK----LREILKEQlgtnPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQaskegdkgLTQKEQIEILER 406
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 133777033 425 FKKKDIPVLVATDVAARGLDIPSIKTVINYD-VA---RDIdthtHRIGRTGRAGEKGVaYTLLTpKDS 488
Cdd:COG1111 407 FRAGEFNVLVATSVAEEGLDIPEVDLVIFYEpVPseiRSI----QRKGRTGRKREGRV-VVLIA-KGT 468
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
365-487 |
1.12e-11 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 67.86 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 365 KWNWLTRRLVEFTSsGSVLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATdVA-ARGL 443
Cdd:COG0514 217 KLAQLLDFLKEHPG-GSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGI 294
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 133777033 444 DIPSIKTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTLLTPKD 487
Cdd:COG0514 295 DKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPED 338
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
178-476 |
1.49e-11 |
|
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: 66.68 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 178 AKTGSGKT-AAFIWpmLIHIMDQKELEPGdgpiaVIVCPTRELCQQIHAECKR-FGKAYNLRSVAVYGGGSMWEQAKALQ 255
Cdd:cd09639 6 APTGYGKTeAALLW--ALHSLKSQKADRV-----IIALPTRATINAMYRRAKEaFGETGLYHSSILSSRIKEMGDSEEFE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 256 E-------------GAEIVVCTP-------GRLIDHVKKKATNLQRvSYLVFDEADRMFD---MGFEYQVRSIAshvRPD 312
Cdd:cd09639 79 HlfplyihsndtlfLDPITVCTIdqvlksvFGEFGHYEFTLASIAN-SLLIFDEVHFYDEytlALILAVLEVLK---DND 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 313 RQTLLFSATFRKKIEKLARDILIDpirvvqgdigEANE-------DVTQIVEILHSGPSKWNWLTRRLVEFTSSGSVLLF 385
Cdd:cd09639 155 VPILLMSATLPKFLKEYAEKIGYV----------EENEpldlkpnERAPFIKIESDKVGEISSLERLLEFIKKGGSVAII 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 386 VTKKANAEELASNLKQEGH--NLGLLHGDMDQSERNK----VISDFKKKDIPVLVATDVAARGLDIPSikTVINYDVArD 459
Cdd:cd09639 225 VNTVDRAQEFYQQLKEKGPeeEIMLIHSRFTEKDRAKkeaeLLLEFKKSEKFVIVATQVIEASLDISV--DVMITELA-P 301
|
330
....*....|....*..
gi 133777033 460 IDTHTHRIGRTGRAGEK 476
Cdd:cd09639 302 IDSLIQRLGRLHRYGEK 318
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
173-470 |
1.99e-11 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 67.56 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 173 DMigiaktGSGKTA---AFIwpmlihimdQKELEPGDGPIAVIVCPTReLCQQIHAECKRFgkAYNLRSVAVYGGGSMWE 249
Cdd:COG0553 268 DM------GLGKTIqalALL---------LELKERGLARPVLIVAPTS-LVGNWQRELAKF--APGLRVLVLDGTRERAK 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 250 QAKALQEgAEIVVCTpgrlIDHVKKKATNLQRV--SYLVFDEADRMFDMG-FEYQ-VRSIASHVR--------------- 310
Cdd:COG0553 330 GANPFED-ADLVITS----YGLLRRDIELLAAVdwDLVILDEAQHIKNPAtKRAKaVRALKARHRlaltgtpvenrleel 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 311 ------------PDRQTllFSATFRKKIEK--------LAR------------DILID-PIRVVQ--------------- 342
Cdd:COG0553 405 wslldflnpgllGSLKA--FRERFARPIEKgdeealerLRRllrpfllrrtkeDVLKDlPEKTEEtlyveltpeqralye 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 343 -------GDIGEANEDVTQIV----------------------EILHSGPSKWNWLTRRLVEFTSSG-SVLLFVTKKANA 392
Cdd:COG0553 483 avleylrRELEGAEGIRRRGLilaaltrlrqicshpallleegAELSGRSAKLEALLELLEELLAEGeKVLVFSQFTDTL 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 393 EELASNLKQEGHNLGLLHGDMDQSERNKVISDFK-KKDIPV-LVATDVAARGLDIPSIKTVINYD-----------VARd 459
Cdd:COG0553 563 DLLEERLEERGIEYAYLHGGTSAEERDELVDRFQeGPEAPVfLISLKAGGEGLNLTAADHVIHYDlwwnpaveeqaIDR- 641
|
410
....*....|.
gi 133777033 460 idthTHRIGRT 470
Cdd:COG0553 642 ----AHRIGQT 648
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
178-321 |
3.50e-11 |
|
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: 61.65 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 178 AKTGSGKT-AAFIWpmLIHIMDQKelepgdGPIAVIVCPTRELCQQIHAECKRFGKaYNLRSVAVYGGGSMWEQAKALQE 256
Cdd:cd00046 8 APTGSGKTlAALLA--ALLLLLKK------GKKVLVLVPTKALALQTAERLRELFG-PGIRVAVLVGGSSAEEREKNKLG 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 133777033 257 GAEIVVCTPGRLIDHVK-KKATNLQRVSYLVFDEADRM-FDMGFEYQVR-SIASHVRPDRQTLLFSAT 321
Cdd:cd00046 79 DADIIIATPDMLLNLLLrEDRLFLKDLKLIIVDEAHALlIDSRGALILDlAVRKAGLKNAQVILLSAT 146
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
180-489 |
7.49e-11 |
|
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: 65.49 E-value: 7.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 180 TGSGKT-AAFIWpMLIHimdqkeLEPGDGPIAVIVCPTRELCQQIHaecKRFGKAYNLrSVAVYGGGSMWEQAKALQEG- 257
Cdd:COG1203 156 TGGGKTeAALLF-ALRL------AAKHGGRRIIYALPFTSIINQTY---DRLRDLFGE-DVLLHHSLADLDLLEEEEEYe 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 258 --------------AEIVVCTPGRLIDHV-------KKKATNLQRvSYLVFDEADrMFDMgfEYQ---VRSIASHVRPDR 313
Cdd:COG1203 225 searwlkllkelwdAPVVVTTIDQLFESLfsnrkgqERRLHNLAN-SVIILDEVQ-AYPP--YMLallLRLLEWLKNLGG 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 314 QTLLFSATFRKKIeklaRDILIDPIRVVQGDIGEANEDVTQIVE---ILHSGPSKWNWLTRRLVE-FTSSGSVLLFVTKK 389
Cdd:COG1203 301 SVILMTATLPPLL----REELLEAYELIPDEPEELPEYFRAFVRkrvELKEGPLSDEELAELILEaLHKGKSVLVIVNTV 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 390 ANAEELASNLKQEGHNLG--LLHGDMDQSERNKVISD----FKKKDIPVLVATDVAARGLDipsiktvINYDVA-RD--- 459
Cdd:COG1203 377 KDAQELYEALKEKLPDEEvyLLHSRFCPADRSEIEKEikerLERGKPCILVSTQVVEAGVD-------IDFDVViRDlap 449
|
330 340 350
....*....|....*....|....*....|...
gi 133777033 460 IDTHTHRIGRT---GRAGEKGVAYtLLTPKDSN 489
Cdd:COG1203 450 LDSLIQRAGRCnrhGRKEEEGNVY-VFDPEDEG 481
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
178-476 |
7.60e-11 |
|
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.
Pssm-ID: 273707 [Multi-domain] Cd Length: 359 Bit Score: 64.78 E-value: 7.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 178 AKTGSGKT-AAFIWpmLIHIMDQKELEPGdgpiaVIVCPTRELCQQIHaecKRFGKAYNLRSVAVYGGGSMWEQAKALQE 256
Cdd:TIGR01587 6 APTGYGKTeAALLW--ALHSIKSQKADRV-----IIALPTRATINAMY---RRAKELFGSELVGLHHSSSFSRIKEMGDS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 257 GA------------------EIVVCTP-------GRLIDHVKKKATNLQRvSYLVFDEADRMFD---MGFEYQVRSIAsh 308
Cdd:TIGR01587 76 EEfehlfplyihsndklfldPITVCTIdqvlksvFGEFGHYEFTLASIAN-SLLIFDEVHFYDEytlALILAVLEVLK-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 309 vRPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIGEANEDVTQIVEILHSGPSKWNWLTRRLVEFTSSGSVLLFVTK 388
Cdd:TIGR01587 153 -DNDVPILLMSATLPKFLKEYAEKIGYVEFNEPLDLKEERRFENHRFILIESDKVGEISSLERLLEFIKKGGSIAIIVNT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 389 KANAEELASNLKQEGHNLG--LLHGDMDQSERNK----VISDFKKKDIP-VLVATDVAARGLDIPSikTVINYDVArDID 461
Cdd:TIGR01587 232 VDRAQEFYQQLKEKAPEEEiiLYHSRFTEKDRAKkeaeLLREMKKSNEKfVIVATQVIEASLDISA--DVMITELA-PID 308
|
330
....*....|....*
gi 133777033 462 THTHRIGRTGRAGEK 476
Cdd:TIGR01587 309 SLIQRLGRLHRYGRK 323
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
180-290 |
1.57e-10 |
|
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: 61.13 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 180 TGSGKTaaFIWPMLIHIM-DQKELEPGDGPIAVIVCPTRELCQQihaECKRFGKAYNLRSVAVYG--GGSMWEQAKALQE 256
Cdd:cd18034 25 TGSGKT--LIAVMLIKEMgELNRKEKNPKKRAVFLVPTVPLVAQ---QAEAIRSHTDLKVGEYSGemGVDKWTKERWKEE 99
|
90 100 110
....*....|....*....|....*....|....*.
gi 133777033 257 --GAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEA 290
Cdd:cd18034 100 leKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
356-468 |
5.69e-10 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 57.87 E-value: 5.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 356 VEILHSGpsKWNWLTRRLVEFTSSGS-VLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKK-KDIPV- 432
Cdd:cd18793 5 IEEVVSG--KLEALLELLEELREPGEkVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEdPDIRVf 82
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 133777033 433 LVATDVAARGLDIPSIKTVINYDV----ARD---IDtHTHRIG 468
Cdd:cd18793 83 LLSTKAGGVGLNLTAANRVILYDPwwnpAVEeqaID-RAHRIG 124
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
158-290 |
6.25e-10 |
|
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: 59.20 E-value: 6.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 158 TPIQCQGV-PVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQkelepgdGPIAVIVCPTRELCQQIHAECKRFGKAYNL 236
Cdd:cd17921 3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRALATS-------GGKAVYIAPTRALVNQKEADLRERFGPLGK 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 133777033 237 RSVAVYGGGSMweqAKALQEGAEIVVCTP----GRLIDHvkkKATNLQRVSYLVFDEA 290
Cdd:cd17921 76 NVGLLTGDPSV---NKLLLAEADILVATPekldLLLRNG---GERLIQDVRLVVVDEA 127
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
129-483 |
8.01e-10 |
|
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: 62.55 E-value: 8.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 129 PPRPGSsFAHF--GFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDqkelepGD 206
Cdd:COG1205 28 PAREAR-YAPWpdWLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLE------DP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 207 GPIAVIVCPTRELCQQIHAECKRFGKAYNLR-SVAVYGGGSMWEQAKALQEGAEIVVCTP-----GrLIDHVKKKATNLQ 280
Cdd:COG1205 101 GATALYLYPTKALARDQLRRLRELAEALGLGvRVATYDGDTPPEERRWIREHPDIVLTNPdmlhyG-LLPHHTRWARFFR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 281 RVSYLVFDEA---------------DRMfdmgfeyqvRSIASHVRPDRQTLLFSATfrkkI---EKLARDILIDPIRVVQ 342
Cdd:COG1205 180 NLRYVVIDEAhtyrgvfgshvanvlRRL---------RRICRHYGSDPQFILASAT----IgnpAEHAERLTGRPVTVVD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 343 GDiGEAnedvTQIVEILHSGPSKWNWLTRR---------LVEFTSSG-SVLLFVTKKANAEELASNLKQEGHNLGLL--- 409
Cdd:COG1205 247 ED-GSP----RGERTFVLWNPPLVDDGIRRsalaeaarlLADLVREGlRTLVFTRSRRGAELLARYARRALREPDLAdrv 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 133777033 410 ---HGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTLL 483
Cdd:COG1205 322 aayRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVLVA 398
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
389-514 |
1.17e-09 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 61.65 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 389 KANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRIG 468
Cdd:PRK11057 246 RAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETG 325
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 133777033 469 RTGRAGEKGVAYTLLTPKDSNFagdLVRNLE----GANQHVSKELLDlAM 514
Cdd:PRK11057 326 RAGRDGLPAEAMLFYDPADMAW---LRRCLEekpaGQQQDIERHKLN-AM 371
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
369-472 |
1.53e-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: 57.27 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 369 LTRRLVEFTSSGSVLLFVTKKANAEELASNLKQ------EGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARG 442
Cdd:cd18796 28 YAEVIFLLERHKSTLVFTNTRSQAERLAQRLRElcpdrvPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELG 107
|
90 100 110
....*....|....*....|....*....|
gi 133777033 443 LDIPSIKTVINYDVARDIDTHTHRIGRTGR 472
Cdd:cd18796 108 IDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
413-483 |
1.72e-09 |
|
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: 56.98 E-value: 1.72e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 133777033 413 MDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYD-VARDIDThTHRIGRTGRaGEKGVAYTLL 483
Cdd:cd18801 74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDaSPSPIRM-IQRMGRTGR-KRQGRVVVLL 143
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
391-485 |
3.82e-09 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350179 [Multi-domain] Cd Length: 160 Bit Score: 56.51 E-value: 3.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 391 NAEELASNLKQE--GHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRI- 467
Cdd:cd18792 46 SIEALAEELKELvpEARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFGLSQLHQLr 125
|
90
....*....|....*...
gi 133777033 468 GRTGRAGEKGVAYtLLTP 485
Cdd:cd18792 126 GRVGRGKHQSYCY-LLYP 142
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
375-499 |
6.87e-09 |
|
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350197 [Multi-domain] Cd Length: 151 Bit Score: 55.43 E-value: 6.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 375 EFTSSGSVLLFVTKKANAEELASNLKQ--EGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVI 452
Cdd:cd18810 21 ELLRGGQVFYVHNRIESIEKLATQLRQlvPEARIAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTII 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 133777033 453 --NYDVARDIDTHTHRiGRTGRAGEKGVAYtLLTPKDSNFAGDLVRNLE 499
Cdd:cd18810 101 ieRADKFGLAQLYQLR-GRVGRSKERAYAY-FLYPDQKKLTEDALKRLE 147
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
432-484 |
1.52e-08 |
|
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: 52.32 E-value: 1.52e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 133777033 432 VLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTLLT 484
Cdd:cd18785 25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILFV 77
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
388-500 |
1.69e-08 |
|
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: 54.27 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 388 KKANA--EELASNLKQEgHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTH 465
Cdd:cd18811 45 KAAVAmyEYLKERFRPE-LNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLH 123
|
90 100 110
....*....|....*....|....*....|....*.
gi 133777033 466 RI-GRTGRAGEKGVAYTLLTPKDSNFAGDLVRNLEG 500
Cdd:cd18811 124 QLrGRVGRGDHQSYCLLVYKDPLTETAKQRLRVMTE 159
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
371-475 |
2.46e-08 |
|
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: 53.37 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 371 RRLVEFTSSGSVLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKT 450
Cdd:cd18794 22 KRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRF 101
|
90 100
....*....|....*....|....*
gi 133777033 451 VINYDVARDIDTHTHRIGRTGRAGE 475
Cdd:cd18794 102 VIHYSLPKSMESYYQESGRAGRDGL 126
|
|
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
390-452 |
4.41e-08 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 56.60 E-value: 4.41e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 133777033 390 ANAEELASNLKQE--GHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATdvaargldipsikTVI 452
Cdd:COG1200 488 QAAEETYEELREAfpGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVAT-------------TVI 539
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
383-484 |
4.44e-08 |
|
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: 52.59 E-value: 4.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 383 LLFVTKKANAEELASNLKQEGHNLGLLHGD---------------MDQSERNKVISDFKKKDIPVLVATDVAARGLDIPS 447
Cdd:cd18802 29 IIFVERRATAVVLSRLLKEHPSTLAFIRCGfligrgnssqrkrslMTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPA 108
|
90 100 110
....*....|....*....|....*....|....*..
gi 133777033 448 IKTVINYDVARDIdthTHRIGRTGRAGEKGVAYTLLT 484
Cdd:cd18802 109 CNLVIRFDLPKTL---RSYIQSRGRARAPNSKYILMV 142
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
413-484 |
6.79e-08 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 56.42 E-value: 6.79e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 133777033 413 MDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYD-VARDIDThTHRIGRTGRaGEKGVAYTLLT 484
Cdd:PRK13766 407 MSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEpVPSEIRS-IQRKGRTGR-QEEGRVVVLIA 477
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
151-495 |
1.29e-07 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 55.49 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 151 KSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKT-AAFIWPmLIHIMDQKELEPGDGPIAVI-VCPTRELCQQIHaeck 228
Cdd:COG1201 19 AARFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAFLPA-LDELARRPRPGELPDGLRVLyISPLKALANDIE---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 229 RfgkayNLR-----------------SVAV-YGGGSMWEQAKALQEGAEIVVCTPGRLidHV----KKKATNLQRVSYLV 286
Cdd:COG1201 94 R-----NLRapleeigeaaglplpeiRVGVrTGDTPASERQRQRRRPPHILITTPESL--ALlltsPDARELLRGVRTVI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 287 FDEadrmfdmgfeyqVRSIAS---------------HVRPDR-QTLLFSATFRkKIEKLAR----DILIDPIRVVQGDIG 346
Cdd:COG1201 167 VDE------------IHALAGskrgvhlalslerlrALAPRPlQRIGLSATVG-PLEEVARflvgYEDPRPVTIVDAGAG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 347 -----EANEDVTQIVEILHSGPSKWNWLTRRLVEF-TSSGSVLLFVTKKANAEELASNLKQ----EGHNLGLLHGDMDQS 416
Cdd:COG1201 234 kkpdlEVLVPVEDLIERFPWAGHLWPHLYPRVLDLiEAHRTTLVFTNTRSQAERLFQRLNElnpeDALPIAAHHGSLSRE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 417 ERNKVISDFKKKDIPVLVAT---DVaarGLDIPSIKTVINYD----VARDIdthtHRIGRTG-RAGEKGVAYtlLTPKDs 488
Cdd:COG1201 314 QRLEVEEALKAGELRAVVATsslEL---GIDIGDVDLVIQVGspksVARLL----QRIGRAGhRVGEVSKGR--LVPTH- 383
|
....*..
gi 133777033 489 nfAGDLV 495
Cdd:COG1201 384 --RDELV 388
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
381-452 |
2.37e-07 |
|
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: 49.87 E-value: 2.37e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 133777033 381 SVLLFVTKKANAEELASNLKQEGHNLGLLHGD--MDQSERNKVISDFK-KKDIPVLVATDVAARGLDIPSIKTVI 452
Cdd:cd18799 8 KTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDysDRERGDEALILLFFgELKPPILVTVDLLTTGVDIPEVDNVV 82
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
375-482 |
1.19e-06 |
|
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: 49.09 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 375 EFTSSGSVLLFVTKKANAEELASNLKqeghNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSiKTVI-- 452
Cdd:cd18795 39 TVSEGKPVLVFCSSRKECEKTAKDLA----GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPA-RTVIik 113
|
90 100 110
....*....|....*....|....*....|....*....
gi 133777033 453 -----NYDVARDIDTHTHR--IGRTGRAG--EKGVAYTL 482
Cdd:cd18795 114 gtqryDGKGYRELSPLEYLqmIGRAGRPGfdTRGEAIIM 152
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
391-446 |
1.56e-06 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 51.69 E-value: 1.56e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 133777033 391 NAEELASNLKQE--GHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIP 446
Cdd:PRK10917 491 SAEETYEELQEAfpELRVGLLHGRMKPAEKDAVMAAFKAGEIDILVATTVIEVGVDVP 548
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
180-322 |
1.85e-06 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part 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: 350684 [Multi-domain] Cd Length: 146 Bit Score: 48.07 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 180 TGSGKT---AAFIWpmliHIMDQKELepgdgpiavIVCPTRELCQQIHAECKRFGKAynlRSVAVYGGGSmweqaKALQE 256
Cdd:cd17926 27 TGSGKTltaLALIA----YLKELRTL---------IVVPTDALLDQWKERFEDFLGD---SSIGLIGGGK-----KKDFD 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 133777033 257 GAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFeyqvRSIASHVRPDRQtLLFSATF 322
Cdd:cd17926 86 DANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHHLPAKTF----SEILKELNAKYR-LGLTATP 146
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
157-289 |
2.29e-06 |
|
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: 49.01 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 157 PTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHImdQKELEPGDGPIAVIVCPTRELC-QQIHAECKRFGKAYN 235
Cdd:cd18036 3 LRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHL--EKRRSAGEKGRVVVLVNKVPLVeQQLEKFFKYFRKGYK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 133777033 236 LrsVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATN----LQRVSYLVFDE 289
Cdd:cd18036 81 V--TGLSGDSSHKVSFGQIVKASDVIICTPQILINNLLSGREEervyLSDFSLLIFDE 136
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
383-476 |
3.84e-06 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 50.66 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 383 LLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDT 462
Cdd:PLN03137 684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEG 763
|
90
....*....|....
gi 133777033 463 HTHRIGRTGRAGEK 476
Cdd:PLN03137 764 YHQECGRAGRDGQR 777
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
171-289 |
4.03e-06 |
|
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: 47.58 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 171 GRDMIGIAKTGSGKT-AAFIWPmLIHIMDQKElepgdGPIAVI-VCPTRELCQQIHAECKRFGKAYNL-RSVAV-YGGGS 246
Cdd:cd17922 1 GRNVLIAAPTGSGKTeAAFLPA-LSSLADEPE-----KGVQVLyISPLKALINDQERRLEEPLDEIDLeIPVAVrHGDTS 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 133777033 247 MWEQAKALQEGAEIVVCTP---GRLIDHvKKKATNLQRVSYLVFDE 289
Cdd:cd17922 75 QSEKAKQLKNPPGILITTPeslELLLVN-KKLRELFAGLRYVVVDE 119
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
382-455 |
7.61e-06 |
|
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350177 [Multi-domain] Cd Length: 171 Bit Score: 46.85 E-value: 7.61e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 133777033 382 VLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYD 455
Cdd:cd18790 30 VLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILD 103
|
|
| PRK10689 |
PRK10689 |
transcription-repair coupling factor; Provisional |
410-499 |
1.30e-05 |
|
transcription-repair coupling factor; Provisional
Pssm-ID: 182649 [Multi-domain] Cd Length: 1147 Bit Score: 48.97 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 410 HGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVI-----NYDVARdidTHTHRiGRTGRAGEKGVAYtLLT 484
Cdd:PRK10689 842 HGQMRERELERVMNDFHHQRFNVLVCTTIIETGIDIPTANTIIieradHFGLAQ---LHQLR-GRVGRSHHQAYAW-LLT 916
|
90
....*....|....*
gi 133777033 485 PKDSNFAGDLVRNLE 499
Cdd:PRK10689 917 PHPKAMTTDAQKRLE 931
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
156-292 |
1.62e-05 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex 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. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part 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: 350685 [Multi-domain] Cd Length: 201 Bit Score: 46.66 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 156 QPTPIQCQGVPVALSGRDMIGIAKTGSGKTaaFIwPMLI--HIMDQKELEPGdGPIAVIVcPTRELC-QQIHAECKRFGK 232
Cdd:cd17927 2 KPRNYQLELAQPALKGKNTIICLPTGSGKT--FV-AVLIceHHLKKFPAGRK-GKVVFLA-NKVPLVeQQKEVFRKHFER 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 133777033 233 AYnLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKK-KATNLQRVSYLVFDEADR 292
Cdd:cd17927 77 PG-YKVTGLSGDTSENVSVEQIVESSDVIIVTPQILVNDLKSgTIVSLSDFSLLVFDECHN 136
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
160-265 |
5.83e-05 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 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: 350781 [Multi-domain] Cd Length: 206 Bit Score: 45.04 E-value: 5.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 160 IQCQGVPVAL-SGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDgPIAVIVCPTRELCQQIHAECK-RFGKaYNLR 237
Cdd:cd18023 5 IQSEVFPDLLySDKNFVVSAPTGSGKTVLFELAILRLLKERNPLPWGN-RKVVYIAPIKALCSEKYDDWKeKFGP-LGLS 82
|
90 100
....*....|....*....|....*...
gi 133777033 238 SVAVYGGGSMWEQAKAlqEGAEIVVCTP 265
Cdd:cd18023 83 CAELTGDTEMDDTFEI--QDADIILTTP 108
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
383-489 |
6.16e-05 |
|
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase 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: 350185 [Multi-domain] Cd Length: 174 Bit Score: 44.22 E-value: 6.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 383 LLFVTK---KANAEELASNLKQEGHNLGLLHgdmdqSERNKVISDFKKKDIPVLVAT----DVAARGLDIP-SIKTVINY 454
Cdd:cd18798 28 LIFVSIdygKEYAEELKEFLERHGIKAELAL-----SSTEKNLEKFEEGEIDVLIGVasyyGVLVRGIDLPeRIKYAIFY 102
|
90 100 110
....*....|....*....|....*....|....*....
gi 133777033 455 DVArdIDTHTHRIGRTGR--AGE--KGVAYTLLTPKDSN 489
Cdd:cd18798 103 GVP--VTTYIQASGRTSRlyAGGltKGLSVVLVDDPELF 139
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
378-482 |
9.31e-05 |
|
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family members 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: 350178 [Multi-domain] Cd Length: 171 Bit Score: 43.68 E-value: 9.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 378 SSGSVLLFVTKKANAEELASNLKQEGHNLGL-------LHGDMDQSERNKVI---SDFKKKdipVLVATDVAARGLDIPS 447
Cdd:cd18791 42 EPGDILVFLPGQEEIERLCELLREELLSPDLgkllvlpLHSSLPPEEQQRVFeppPPGVRK---VVLATNIAETSITIPG 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 133777033 448 IKTVI--------NYDVARDIDT-HTHRIG------RTGRAG--EKGVAYTL 482
Cdd:cd18791 119 VVYVIdsglvkekVYDPRTGLSSlVTVWISkasaeqRAGRAGrtRPGKCYRL 170
|
|
| VirD4 |
COG3505 |
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ... |
177-232 |
1.58e-04 |
|
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: 44.98 E-value: 1.58e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 133777033 177 IAKTGSGKTAAFIWPMLIHimdqkeLEPGDGpiAVIVCPTRELCQQIHAECKRFGK 232
Cdd:COG3505 5 IGPTGSGKTVGLVIPNLTQ------LARGES--VVVTDPKGDLAELTAGFRRRAGY 52
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
167-292 |
2.06e-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: 42.89 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 167 VALSGRDMIgIAKTGSGKTAAFIWPMLihimdqKELEPGDGPIaVIVCPTRELCQQiHAEckRFGKAYNL--RSVAVYGG 244
Cdd:cd18035 13 VALNGNTLI-VLPTGLGKTIIAILVAA------DRLTKKGGKV-LILAPSRPLVEQ-HAE--NLKRVLNIpdKITSLTGE 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 133777033 245 GSMWEQAKALQEGaEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADR 292
Cdd:cd18035 82 VKPEERAERWDAS-KIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
|
|
| dermokine |
cd21118 |
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ... |
525-770 |
2.51e-04 |
|
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.
Pssm-ID: 411053 [Multi-domain] Cd Length: 495 Bit Score: 44.61 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 525 KGGKGKKLNIGGGGLGYRERPGLGSEnsdRGNNNNV-MSNyeayKPSTGAMGdrltamkaafqsqykshfvaaSLSNQKA 603
Cdd:cd21118 168 QGGNGGPLNYGTNSQGAVAQPGYGTV---RGNNQNSgCTN----PPPSGSHE---------------------SFSNSGG 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 604 GTSSAGASGWTSAGSLNSVPTNSAQQGHNSPDNPMTSSTKNIPGFNNSGNISSAPVTYPSIGAQGVNNTASGNNSREGIG 683
Cdd:cd21118 220 SSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSGGSNGGSSGNSGSGSGGSSSGGSNGWGGSSSSGGSGG 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 684 GGNGKRERYTENRGGSRHSHGDGGNRhgdggrhgdgyrYPESGSRHTDGHRHGEtrhggsagrhGESRGANDGRNGESRK 763
Cdd:cd21118 300 SGGGNKPECNNPGNDVRMAGGGGSQG------------SKESSGSHGSNGGNGQ----------AEAVGGLNTLNSDAST 357
|
....*..
gi 133777033 764 EGFNREN 770
Cdd:cd21118 358 LPFNFDT 364
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
290-474 |
2.81e-04 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 44.49 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 290 ADRMFDMGFEYQ------VRSIASHVRPDRQTLLFSATFRKKIEK---LARDILIDPIRVVQGDIGEANEDvTQIVEILH 360
Cdd:PRK01172 141 ADEIHIIGDEDRgptletVLSSARYVNPDARILALSATVSNANELaqwLNASLIKSNFRPVPLKLGILYRK-RLILDGYE 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 361 SGPSKWNWLTRRLVEftSSGSVLLFVTKKANAEELASNLKQE-------------------------GHNLGLLHGDMDQ 415
Cdd:PRK01172 220 RSQVDINSLIKETVN--DGGQVLVFVSSRKNAEDYAEMLIQHfpefndfkvssennnvyddslnemlPHGVAFHHAGLSN 297
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 133777033 416 SERNKVISDFKKKDIPVLVATDVAARGLDIPSiKTVINYDVARDIDTHT---------HRIGRTGRAG 474
Cdd:PRK01172 298 EQRRFIEEMFRNRYIKVIVATPTLAAGVNLPA-RLVIVRDITRYGNGGIrylsnmeikQMIGRAGRPG 364
|
|
| secA |
PRK12898 |
preprotein translocase subunit SecA; Reviewed |
364-523 |
2.95e-04 |
|
preprotein translocase subunit SecA; Reviewed
Pssm-ID: 237253 [Multi-domain] Cd Length: 656 Bit Score: 44.23 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 364 SKWNWLTRRLVEFTSSGSVLLFVTKK-ANAEELASNLKQEGHNLGLLHGDMDQSErNKVISDFKKKDiPVLVATDVAARG 442
Cdd:PRK12898 457 AKWAAVAARVRELHAQGRPVLVGTRSvAASERLSALLREAGLPHQVLNAKQDAEE-AAIVARAGQRG-RITVATNMAGRG 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 443 LDIPsiktvINYDVARD-----IDTHTHR--------IGRTGRAGEKGVAYTLLTPKD---SNFAGDLVRNLEGANQHVS 506
Cdd:PRK12898 535 TDIK-----LEPGVAARgglhvILTERHDsaridrqlAGRCGRQGDPGSYEAILSLEDdllQSFLGSRGLAIRRMELLGP 609
|
170
....*....|....*..
gi 133777033 507 KELLDLAMQNAWFRKSR 523
Cdd:PRK12898 610 RGGRALGALLLRRAQRR 626
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
382-477 |
7.60e-04 |
|
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: 40.70 E-value: 7.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 382 VLLFVTKKANAEELASNLkqeghNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIktvinyDVARDID 461
Cdd:cd18789 52 IIVFTDNVEALYRYAKRL-----LKPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPEA------NVAIQIS 120
|
90 100
....*....|....*....|...
gi 133777033 462 TH-------THRIGRTGRAGEKG 477
Cdd:cd18789 121 GHggsrrqeAQRLGRILRPKKGG 143
|
|
| DEXQc_arch_SWI2_SNF2 |
cd18012 |
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ... |
173-290 |
1.14e-03 |
|
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging to SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprises a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. Archaeal SWI2 and SNF2 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: 350770 [Multi-domain] Cd Length: 218 Bit Score: 41.01 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 173 DMigiaktGSGKTAAfiwpMLIHIMDQKElEPGDGPiAVIVCPTrELCQQIHAECKRFgkAYNLRSVAVYGGGSMWEQAK 252
Cdd:cd18012 31 DM------GLGKTLQ----TLALLLSRKE-EGRKGP-SLVVAPT-SLIYNWEEEAAKF--APELKVLVIHGTKRKREKLR 95
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 133777033 253 ALqEGAEIVVCTPG---RLIDHVKKkatnlQRVSYLVFDEA 290
Cdd:cd18012 96 AL-EDYDLVITSYGllrRDIELLKE-----VKFHYLVLDEA 130
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
180-322 |
1.22e-03 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 40.35 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 180 TGSGKTAafiwpMLIHIMDQKeLEPGDGPIAVIVCPTRELCQQIHAECKRFGKAYNLRSvAVYGGGSMweqaKALQEGAE 259
Cdd:pfam04851 32 TGSGKTL-----TAAKLIARL-FKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYVEIG-EIISGDKK----DESVDDNK 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 133777033 260 IVVCTP---GRLIDHVKKKATNLQRVsYLVFDEADRMFDMGFeyqvRSIASHVRPdrQTLL-FSATF 322
Cdd:pfam04851 101 IVVTTIqslYKALELASLELLPDFFD-VIIIDEAHRSGASSY----RNILEYFKP--AFLLgLTATP 160
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
168-290 |
1.98e-03 |
|
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: 39.88 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 168 ALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKelepgdGPIAVIVCPTRELCQQIHAECKRFGKAYNLR-SVAVYGG-G 245
Cdd:cd17923 12 ARAGRSVVVTTGTASGKSLCYQLPILEALLRDP------GSRALYLYPTKALAQDQLRSLRELLEQLGLGiRVATYDGdT 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 133777033 246 SMWEQAKALQEGAEIVVCTPGRL----IDHVKKKATNLQRVSYLVFDEA 290
Cdd:cd17923 86 PREERRAIIRNPPRILLTNPDMLhyalLPHHDRWARFLRNLRYVVLDEA 134
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
159-290 |
5.39e-03 |
|
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: 39.16 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 159 PIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIhimdQKELEPGdgpIAVIVCPTRELCQ-QIHAeCKRFGKAYNLR 237
Cdd:cd18018 15 PGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALL----LRRRGPG---LTLVVSPLIALMKdQVDA-LPRAIKAAALN 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 133777033 238 SVAvyGGGSMWEQAKALQEG-AEIVVCTPGRLID-HVKKKATNLQRVSYLVFDEA 290
Cdd:cd18018 87 SSL--TREERRRILEKLRAGeVKILYVSPERLVNeSFRELLRQTPPISLLVVDEA 139
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
154-290 |
7.10e-03 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 38.67 E-value: 7.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133777033 154 YTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIhimdqkelepgDGPIAVIVCPTRELCQ-QIHaECKRFGK 232
Cdd:cd17920 10 YDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALL-----------LDGVTLVVSPLISLMQdQVD-RLQQLGI 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 133777033 233 aynlRSVAVYGGGSMWEQAKALQEGAE----IVVCTPGRLI-DHVKK---KATNLQRVSYLVFDEA 290
Cdd:cd17920 78 ----RAAALNSTLSPEEKREVLLRIKNgqykLLYVTPERLLsPDFLEllqRLPERKRLALIVVDEA 139
|
|
| |
