|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
254-664 |
1.98e-157 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 468.86 E-value: 1.98e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 254 SFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKElepgDGPIAVIVC 333
Cdd:COG0513 3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP----RAPQALILA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 334 PTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMF 413
Cdd:COG0513 79 PTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRML 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 414 DMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVvqgDIGEANEDVTQIVEILH--SGPSKWNwLTRR 491
Cdd:COG0513 159 DMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRI---EVAPENATAETIEQRYYlvDKRDKLE-LLRR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 492 LVEFTSSGSVLLFVTKKANAEELANNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVI 571
Cdd:COG0513 235 LLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 572 NYDVARDIDTHTHRIGRTGRAGEKGVAYTLLTPKDSNfagdLVRNLEGA-NQHVSKELLDLAMQNAWFRKSRFKGGKGKK 650
Cdd:COG0513 315 NYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERR----LLRAIEKLiGQKIEEEELPGFEPVEEKRLERLKPKIKEK 390
|
410
....*....|....
gi 45446743 651 LNIGGGGLGYRERP 664
Cdd:COG0513 391 LKGKKAGRGGRPGP 404
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
198-652 |
6.45e-147 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 446.53 E-value: 6.45e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 198 DPLPPIDHSEIDYPPFEKNFYNEHEEITNLTPQQLIDLR--HKLNLrVSGAAPPRPGSSFAHFGFDEQLMHQIRKSEYTQ 275
Cdd:PTZ00110 74 KRLQPIDWKSINLVPFEKNFYKEHPEVSALSSKEVDEIRkeKEITI-IAGENVPKPVVSFEYTSFPDYILKSLKNAGFTE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 276 PTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIHAECKRFGKAYNL 355
Cdd:PTZ00110 153 PTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKI 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 356 RSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASHVRPDRQTL 435
Cdd:PTZ00110 233 RNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 436 LFSATFRKKIEKLARDILID-PIRVVQGDIG-EANEDVTQIVEIL--HSGPSKWNWLTRRLveFTSSGSVLLFVTKKANA 511
Cdd:PTZ00110 313 MWSATWPKEVQSLARDLCKEePVHVNVGSLDlTACHNIKQEVFVVeeHEKRGKLKMLLQRI--MRDGDKILIFVETKKGA 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 512 EELANNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRIGRTGR 591
Cdd:PTZ00110 391 DFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGR 470
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45446743 592 AGEKGVAYTLLTPKDSNFAGDLVRNLEGANQHVSKELLDLAMQNAWFRKSRFKGGKGKKLN 652
Cdd:PTZ00110 471 AGAKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSNERSNGTERRRWGGYGRFSN 531
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
264-460 |
5.62e-140 |
|
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: 5.62e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 264 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIH 343
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGEGPIAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 344 AECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRS 423
Cdd:cd17952 81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 45446743 424 IASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVV 460
Cdd:cd17952 161 IVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRVV 197
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
273-613 |
5.36e-105 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 334.08 E-value: 5.36e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 273 YTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHImDQKELepgdGPIAVIVCPTRELCQQIHAECKRFGKA 352
Cdd:PRK11776 24 YTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL-DVKRF----RVQALVLCPTRELADQVAKEIRRLARF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 353 -YNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASHVRPD 431
Cdd:PRK11776 99 iPNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMGFQDAIDAIIRQAPAR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 432 RQTLLFSATFRKKIEKLARDILIDPIRVvqgdIGEANEDVTQI----VEILHSGpsKWNWLTRRLVEFTSSgSVLLFVTK 507
Cdd:PRK11776 179 RQTLLFSATYPEGIAAISQRFQRDPVEV----KVESTHDLPAIeqrfYEVSPDE--RLPALQRLLLHHQPE-SCVVFCNT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 508 KANAEELANNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRIG 587
Cdd:PRK11776 252 KKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRIG 331
|
330 340
....*....|....*....|....*.
gi 45446743 588 RTGRAGEKGVAYTLLTPKDSNFAGDL 613
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) ... |
242-459 |
4.73e-101 |
|
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: 4.73e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 242 RVSGAAPPRPGSSFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKEL 321
Cdd:cd17953 1 KVRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 322 EPGDGPIAVIVCPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHV---KKKATNL 398
Cdd:cd17953 81 KPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtanNGRVTNL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45446743 399 QRVSYLVFDEADRMFDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 459
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 ... |
264-460 |
1.92e-95 |
|
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: 1.92e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 264 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIH 343
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGDGPIVLVLAPTRELAQQIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 344 AECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRS 423
Cdd:cd17966 81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 45446743 424 IASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVV 460
Cdd:cd17966 161 IVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
264-459 |
3.09e-95 |
|
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: 3.09e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 264 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKElEPGDGPIAVIVCPTRELCQQIH 343
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPK-KKGRGPQALVLAPTRELAMQIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 344 AECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRS 423
Cdd:cd00268 80 EVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 45446743 424 IASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 459
Cdd:cd00268 160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
255-601 |
1.81e-91 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 297.24 E-value: 1.81e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 255 FAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDgPIAVIVCP 334
Cdd:PRK11192 3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRKSGP-PRILILTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 335 TRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFD 414
Cdd:PRK11192 82 TRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 415 MGFEYQVRSIASHVRPDRQTLLFSATFR-KKIEKLARDILIDPIRVvqgdigEAN------EDVTQIVEILHSGPSKWNW 487
Cdd:PRK11192 162 MGFAQDIETIAAETRWRKQTLLFSATLEgDAVQDFAERLLNDPVEV------EAEpsrrerKKIHQWYYRADDLEHKTAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 488 LTRRLVEFTSSGSVLlFVTKKANAEELANNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSI 567
Cdd:PRK11192 236 LCHLLKQPEVTRSIV-FVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDV 314
|
330 340 350
....*....|....*....|....*....|....
gi 45446743 568 KTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTL 601
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 ... |
204-459 |
2.34e-87 |
|
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: 280.36 E-value: 2.34e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 204 DHSEIdyPPFEKNFYNEHEEITNLTPQQLIDLRHKLNLRVSGAAPPRPGSSFAHFGFDEQLMHQIRKSEYTQPTPIQCQG 283
Cdd:cd18050 15 DLSEL--PKFEKNFYVEHPEVARMTQYDVEELRRKKEITIRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 284 VPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIHAECKRFGKAYNLRSVAVYGG 363
Cdd:cd18050 93 FPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 364 GSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASHVRPDRQTLLFSATFRK 443
Cdd:cd18050 173 APKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPK 252
|
250
....*....|....*.
gi 45446743 444 KIEKLARDILIDPIRV 459
Cdd:cd18050 253 EVRQLAEDFLRDYVQI 268
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
254-688 |
2.70e-79 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 265.13 E-value: 2.70e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 254 SFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPI-AVIV 332
Cdd:PRK10590 2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVrALIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 333 CPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRM 412
Cdd:PRK10590 82 TPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 413 FDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIGEANEDVTQIV---------EILHSGPS 483
Cdd:PRK10590 162 LDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVhfvdkkrkrELLSQMIG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 484 KWNWltrrlveftssGSVLLFVTKKANAEELANNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLD 563
Cdd:PRK10590 242 KGNW-----------QQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 564 IPSIKTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTLLTPKDSNFAGDLVRNLEganqhvsKELLDLAM---------- 633
Cdd:PRK10590 311 IEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLK-------KEIPRIAIpgyepdpsik 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 45446743 634 ----QNAwfRKSRFKGGKGKKLNIGGGGLGYRERPGLGSENMDRGNNNVMSNYEAYKPS 688
Cdd:PRK10590 384 aepiQNG--RQQRGGGGRGQGGGRGQQQGQPRRGEGGAKSASAKPAEKPSRRLGDAKPA 440
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
190-630 |
1.34e-78 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 265.11 E-value: 1.34e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 190 IAPTKKIIDPLPPIDHSEIDyppfeKNFYNEHEEITN-LTPQQLIDLRHKLNLRVSGAAPPRPGSSFAHFGFDEQLMHQI 268
Cdd:PLN00206 62 VAKSRVAVGAPKPKRLPATD-----ECFYVRDPGSTSgLSSSQAELLRRKLEIHVKGEAVPPPILSFSSCGLPPKLLLNL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 269 RKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGD--GPIAVIVCPTRELCQQIHAEC 346
Cdd:PLN00206 137 ETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTIRSGHPSEqrNPLAMVLTPTRELCVQVEDQA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 347 KRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIAS 426
Cdd:PLN00206 217 KVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQ 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 427 HVrPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIGEANEDVTQIVEILHSGPSKwnwltRRLVEFTSSGS-----V 501
Cdd:PLN00206 297 AL-SQPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKK-----QKLFDILKSKQhfkppA 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 502 LLFVTKKANAEELANNL-KQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDID 580
Cdd:PLN00206 371 VVFVSSRLGADLLANAItVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIK 450
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 45446743 581 THTHRIGRTGRAGEKGVAYTLLTPKDSNFAGDLVRNLEGANQHVSKELLD 630
Cdd:PLN00206 451 EYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKSSGAAIPRELAN 500
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
254-465 |
1.55e-78 |
|
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: 1.55e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 254 SFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDG-----PI 328
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGrrkayPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 329 AVIVCPTRELCQQIHAECKRFgkAYN--LRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVF 406
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKF--SYRsgVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45446743 407 DEADRMFDMGFEYQVRSIASH----VRPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIG 465
Cdd:cd17967 159 DEADRMLDMGFEPQIRKIVEHpdmpPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVGRVG 221
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
230-459 |
3.49e-76 |
|
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: 3.49e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 230 QQLIDLRHKLNLRVSGAAPPRPGSSFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIW 309
Cdd:cd18049 1 QEVEQYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 310 PMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLID 389
Cdd:cd18049 81 PAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLID 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 390 HVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 459
Cdd:cd18049 161 FLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHI 230
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
249-607 |
1.95e-74 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 252.53 E-value: 1.95e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 249 PRPGSS-FAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAF---IWPMLIHIMDQKELEPG 324
Cdd:PRK01297 82 PQEGKTrFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFlisIINQLLQTPPPKERYMG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 325 DgPIAVIVCPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEG-AEIVVCTPGRLIDHVKKKATNLQRVSY 403
Cdd:PRK01297 162 E-PRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQRGEVHLDMVEV 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 404 LVFDEADRMFDMGFEYQVRSIASHVRP--DRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIGEANEDVTQIVEILhSG 481
Cdd:PRK01297 241 MVLDEADRMLDMGFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAV-AG 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 482 PSKWNwLTRRLVEFTSSGSVLLFVTKKANAEELANNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARG 561
Cdd:PRK01297 320 SDKYK-LLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRG 398
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 45446743 562 LDIPSIKTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTLLTPKDS 607
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 ... |
197-465 |
2.94e-73 |
|
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DEAD-box helicases are a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350810 [Multi-domain] Cd Length: 264 Bit Score: 242.18 E-value: 2.94e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 197 IDPLPPIDHSEIdYPPFEK--NFyNEHEEItnltpqqLIDlrhklnlrVSGAAPPRPGSSFAHFGFDEQLMHQIRKSEYT 274
Cdd:cd18052 2 IPPPPPEDEDEI-FATIQTgiNF-DKYDEI-------PVE--------VTGRNPPPAILTFEEANLCETLLKNIRKAGYE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 275 QPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIM-------DQKELEPgdgPIAVIVCPTRELCQQIHAECK 347
Cdd:cd18052 65 KPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMkegltasSFSEVQE---PQALIVAPTRELANQIFLEAR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 348 RFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASH 427
Cdd:cd18052 142 KFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSE 221
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 45446743 428 V----RPDRQTLLFSATFRKKIEKLARDIL-IDPIRVVQGDIG 465
Cdd:cd18052 222 PgmpsKEDRQTLMFSATFPEEIQRLAAEFLkEDYLFLTVGRVG 264
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
255-601 |
7.56e-72 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 243.73 E-value: 7.56e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 255 FAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPG--DGPIAVIV 332
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDRkvNQPRALIM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 333 CPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRM 412
Cdd:PRK04837 90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 413 FDMGFeyqVRSIASHVR--PD---RQTLLFSATFRKKIEKLARDILIDPIRVVqgdIGEANEDVTQIVEILH--SGPSKW 485
Cdd:PRK04837 170 FDLGF---IKDIRWLFRrmPPanqRLNMLFSATLSYRVRELAFEHMNNPEYVE---VEPEQKTGHRIKEELFypSNEEKM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 486 NwLTRRLVEFTSSGSVLLFVTKKANAEELANNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIP 565
Cdd:PRK04837 244 R-LLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIP 322
|
330 340 350
....*....|....*....|....*....|....*.
gi 45446743 566 SIKTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTL 601
Cdd:PRK04837 323 AVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
253-618 |
7.65e-72 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 249.77 E-value: 7.65e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 253 SSFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHImdQKELEpgdGPIAVIV 332
Cdd:PRK11634 6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNL--DPELK---APQILVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 333 CPTRELCQQIHAECKRFGK-AYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADR 411
Cdd:PRK11634 81 APTRELAVQVAEAMTDFSKhMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 412 MFDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV-VQGDIgEANEDVTQIVEILHsGPSKWNWLTR 490
Cdd:PRK11634 161 MLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVrIQSSV-TTRPDISQSYWTVW-GMRKNEALVR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 491 RLvEFTSSGSVLLFVTKKANAEELANNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTV 570
Cdd:PRK11634 239 FL-EAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLV 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 45446743 571 INYDVARDIDTHTHRIGRTGRAGEKGVAYTLLTPKDSNfagdLVRNLE 618
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 ... |
264-459 |
1.91e-71 |
|
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: 1.91e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 264 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMD---QKELEPGDGPIAVIVCPTRELCQ 340
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRlppLDEETKDDGPYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 341 QIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQ 420
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 45446743 421 VRSIASHV-----RPD---------------RQTLLFSATFRKKIEKLARDILIDPIRV 459
Cdd:cd17945 161 VTKILDAMpvsnkKPDteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
254-598 |
1.32e-69 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 242.16 E-value: 1.32e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 254 SFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKEL---EPGDgPIAV 330
Cdd:PRK04537 10 TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALadrKPED-PRAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 331 IVCPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKK-KATNLQRVSYLVFDEA 409
Cdd:PRK04537 89 ILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQhKVVSLHACEICVLDEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 410 DRMFDMGFEYQVRSIASHV--RPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIGEANEDVTQivEILHSGPSKWNW 487
Cdd:PRK04537 169 DRMFDLGFIKDIRFLLRRMpeRGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQ--RIYFPADEEKQT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 488 LTRRLVEFTSSGSVLLFVTKKANAEELANNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSI 567
Cdd:PRK04537 247 LLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGV 326
|
330 340 350
....*....|....*....|....*....|.
gi 45446743 568 KTVINYDVARDIDTHTHRIGRTGRAGEKGVA 598
Cdd:PRK04537 327 KYVYNYDLPFDAEDYVHRIGRTARLGEEGDA 357
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
275-459 |
3.23e-68 |
|
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: 3.23e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 275 QPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKE---LEPGDGPIAVIVCPTRELCQQIHAECKRFGK 351
Cdd:cd17951 12 KPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEKklpFIKGEGPYGLIVCPSRELARQTHEVIEYYCK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 352 AYN------LRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIA 425
Cdd:cd17951 92 ALQeggypqLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMIDMGFEEDIRTIF 171
|
170 180 190
....*....|....*....|....*....|....
gi 45446743 426 SHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 459
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 ... |
264-460 |
4.12e-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: 225.42 E-value: 4.12e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 264 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKEL-EPGDGPIAVIVCPTRELCQQI 342
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPrEQRNGPGVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 343 HAECKRFgKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVR 422
Cdd:cd17958 81 EAECSKY-SYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 45446743 423 SIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVV 460
Cdd:cd17958 160 KILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIVY 197
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
264-462 |
1.88e-64 |
|
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: 1.88e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 264 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKElepGDGPIAVIVCPTRELCQQIH 343
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRK---KKGLRALILAPTRELASQIY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 344 AECKRFGKAYNLRSVAVygGGSMWEQAKALQE---GAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQ 420
Cdd:cd17957 78 RELLKLSKGTGLRIVLL--SKSLEAKAKDGPKsitKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQ 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 45446743 421 VRSI-ASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVVQG 462
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 ... |
254-459 |
7.47e-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: 7.47e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 254 SFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKElepgdGPIAVIVC 333
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQ-----RFFALVLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 334 PTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKK-KATNLQRVSYLVFDEADRM 412
Cdd:cd17954 76 PTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENtKGFSLKSLKFLVMDEADRL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 45446743 413 FDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 459
Cdd:cd17954 156 LNMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
253-459 |
1.22e-62 |
|
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: 1.22e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 253 SSFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHImdqKELEPGDGPIAVIV 332
Cdd:cd17959 1 GGFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKL---KAHSPTVGARALIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 333 CPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRM 412
Cdd:cd17959 78 SPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 45446743 413 FDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 459
Cdd:cd17959 158 FEMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
277-448 |
3.84e-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: 3.84e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 277 TPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKelepgDGPIAVIVCPTRELCQQIHAECKRFGKAYNLR 356
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLD-----NGPQALVLAPTRELAEQIYEELKKLGKGLGLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 357 SVAVYGGGSMWEQAKALQeGAEIVVCTPGRLIDHVKKKaTNLQRVSYLVFDEADRMFDMGFEYQVRSIASHVRPDRQTLL 436
Cdd:pfam00270 76 VASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQER-KLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILL 153
|
170
....*....|..
gi 45446743 437 FSATFRKKIEKL 448
Cdd:pfam00270 154 LSATLPRNLEDL 165
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
243-465 |
6.30e-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: 6.30e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 243 VSGAAPPRPGSSFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQ---K 319
Cdd:cd18051 11 ATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQgpgE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 320 ELEPGDG--------PIAVIVCPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHV 391
Cdd:cd18051 91 SLPSESGyygrrkqyPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDML 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45446743 392 KKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASH-VRP---DRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIG 465
Cdd:cd18051 171 ERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQdTMPptgERQTLMFSATFPKEIQMLARDFLDNYIFLAVGRVG 248
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
254-606 |
1.07e-57 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 203.90 E-value: 1.07e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 254 SFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLiHIMDQKELEPGdgpiAVIVC 333
Cdd:PTZ00424 29 SFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAAL-QLIDYDLNACQ----ALILA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 334 PTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMF 413
Cdd:PTZ00424 104 PTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEML 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 414 DMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIGEANEDVTQIVEILHSGPSKWNWLTRrLV 493
Cdd:PTZ00424 184 SRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCD-LY 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 494 EFTSSGSVLLFVTKKANAEELANNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINY 573
Cdd:PTZ00424 263 ETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINY 342
|
330 340 350
....*....|....*....|....*....|...
gi 45446743 574 DVARDIDTHTHRIGRTGRAGEKGVAYTLLTPKD 606
Cdd:PTZ00424 343 DLPASPENYIHRIGRSGRFGRKGVAINFVTPDD 375
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
268-474 |
1.69e-57 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 196.17 E-value: 1.69e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 268 IRKSEYTQPTPIQCQGVPVALSG-RDMIGIAKTGSGKTAAFIWPMLIHIMdqkelePGDGPIAVIVCPTRELCQQIHAEC 346
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALK------RGKGGRVLVLVPTRELAEQWAEEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 347 KRFGKAYNLRSVAVYGGGSMWEQAKALQEG-AEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIA 425
Cdd:smart00487 75 KKLGPSLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 45446743 426 SHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDigEANEDVTQI 474
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 ... |
255-456 |
1.30e-55 |
|
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: 1.30e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 255 FAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLihimdQKELEPGDGPIAVIVCP 334
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPIL-----QRLSEDPYGIFALVLTP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 335 TRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVK---KKATNLQRVSYLVFDEADR 411
Cdd:cd17955 76 TRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEADR 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 45446743 412 MFDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDP 456
Cdd:cd17955 156 LLTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
264-459 |
4.32e-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: 4.32e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 264 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPmlihIMDQKELEPGDGPI--AVIVCPTRELCQQ 341
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLP----ILERLLYRPKKKAAtrVLVLVPTRELAMQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 342 IHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKAT-NLQRVSYLVFDEADRMFDMGFEYQ 420
Cdd:cd17947 77 CFSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSfDLDSIEILVLDEADRMLEEGFADE 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 45446743 421 VRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 459
Cdd:cd17947 157 LKEILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
471-602 |
1.15e-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: 180.01 E-value: 1.15e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 471 VTQIVEILHSGpSKWNWLTRRLVEFTSSGSVLLFVTKKANAEELANNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIP 550
Cdd:cd18787 1 IKQLYVVVEEE-EKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 45446743 551 VLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTLL 602
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 ... |
264-459 |
4.06e-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: 4.06e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 264 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKelepgDGPIAVIVCPTRELCQQIH 343
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEH-----RNPSALILTPTRELAVQIE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 344 AECKRFGKAY-NLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVR 422
Cdd:cd17962 76 DQAKELMKGLpPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVL 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 45446743 423 SIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 459
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 ... |
268-459 |
2.50e-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: 2.50e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 268 IRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKeLEPGDGPIAVIVCPTRELCQQIHAECK 347
Cdd:cd17941 5 LKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRER-WTPEDGLGALIISPTRELAMQIFEVLR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 348 RFGKAYNLRSVAVYGGGSMWEQAKALQEgAEIVVCTPGRLIDHVKKK----ATNLQrvsYLVFDEADRMFDMGFEYQVRS 423
Cdd:cd17941 84 KVGKYHSFSAGLIIGGKDVKEEKERINR-MNILVCTPGRLLQHMDETpgfdTSNLQ---MLVLDEADRILDMGFKETLDA 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 45446743 424 IASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 459
Cdd:cd17941 160 IVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYI 195
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
260-453 |
1.97e-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: 1.97e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 260 FDEQLMHQIRKSEYTQPTPIQCQGVPVALS-GRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTREL 338
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGVSALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 339 CQQIHAECKR---FGKAYNLRSvaVYGGGSMWEQAKALQ-EGAEIVVCTPGRLIDHVK--KKATNLQRVSYLVFDEADRM 412
Cdd:cd17964 81 ALQIAAEAKKllqGLRKLRVQS--AVGGTSRRAELNRLRrGRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 45446743 413 FDMGFEYQVRSIASHVRP----DRQTLLFSATFRKKIEKLARDIL 453
Cdd:cd17964 159 LDMGFRPDLEQILRHLPEknadPRQTLLFSATVPDEVQQIARLTL 203
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
270-460 |
1.05e-47 |
|
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: 1.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 270 KSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIM-DQKELEPGDGPIAVIVCPTRELCQQIHAECKR 348
Cdd:cd17949 8 KMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLsLEPRVDRSDGTLALVLVPTRELALQIYEVLEK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 349 FGK-AYNLRSVAVYGGgsmwEQAKA----LQEGAEIVVCTPGRLIDHVKK-KATNLQRVSYLVFDEADRMFDMGFEYQVR 422
Cdd:cd17949 88 LLKpFHWIVPGYLIGG----EKRKSekarLRKGVNILIATPGRLLDHLKNtQSFDVSNLRWLVLDEADRLLDMGFEKDIT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 45446743 423 SIASHVR-------------PDRQTLLFSATFRKKIEKLARDILIDPIRVV 460
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, ... |
268-460 |
2.01e-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: 2.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 268 IRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIHAECK 347
Cdd:cd17960 5 VAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKKGQVGALIISPTRELATQIYEVLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 348 RFGKAY--NLRSVAVYGGGSMWEQ-AKALQEGAEIVVCTPGRLIDHVKKKAT--NLQRVSYLVFDEADRMFDMGFEYQVR 422
Cdd:cd17960 85 SFLEHHlpKLKCQLLIGGTNVEEDvKKFKRNGPNILVGTPGRLEELLSRKADkvKVKSLEVLVLDEADRLLDLGFEADLN 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 45446743 423 SIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVV 460
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 ... |
261-457 |
2.58e-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: 2.58e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 261 DEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGD-GPIAVIVCPTRELC 339
Cdd:cd17961 2 DPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGEEqGTRALILVPTRELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 340 QQIHAE-------CKRFgkaynLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKAT-NLQRVSYLVFDEADR 411
Cdd:cd17961 82 QQVSKVleqltayCRKD-----VRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLlLLSTLKYLVIDEADL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 45446743 412 MFDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPI 457
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 ... |
255-459 |
2.92e-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: 2.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 255 FAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHImDQKElepgDGPIAVIVCP 334
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKI-DPKK----DVIQALILVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 335 TRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFD 414
Cdd:cd17940 76 TRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 45446743 415 MGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 459
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 ... |
264-441 |
3.63e-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: 3.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 264 LMHQIRKSEYTQPTPIQCQGVPVALS-GRDMIGIAKTGSGKTAAFIWPMLIHIMDQKE----LEPGDGPIAVIVCPTREL 338
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLLSQKSsngvGGKQKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 339 CQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKK---ATNLQRVSYLVFDEADRMFDM 415
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGnehLANLKSLRFLVLDEADRMLEK 160
|
170 180 190
....*....|....*....|....*....|....
gi 45446743 416 G-FEyQVRSIASHV-------RPDRQTLLFSATF 441
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 ... |
265-450 |
8.93e-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: 8.93e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 265 MHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPmLIHIMDQKELEPGDGPIAVIVCPTRELCQQIHA 344
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIP-AIELLYKLKFKPRNGTGVIIISPTRELALQIYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 345 ECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKA----TNLQrvsYLVFDEADRMFDMGFEYQ 420
Cdd:cd17942 81 VAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKgflyKNLQ---CLIIDEADRILEIGFEEE 157
|
170 180 190
....*....|....*....|....*....|
gi 45446743 421 VRSIASHVRPDRQTLLFSATFRKKIEKLAR 450
Cdd:cd17942 158 MRQIIKLLPKRRQTMLFSATQTRKVEDLAR 187
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
261-457 |
9.44e-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: 9.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 261 DEQLMHQIRKSEYTQPTPIQCQGVPVALSG--RDMIGIAKTGSGKTAAFIWPMLIHImDQKELEPGdgpiAVIVCPTREL 338
Cdd:cd17963 2 KPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRV-DPTLKSPQ----ALCLAPTREL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 339 CQQIHAECKRFGK------AYNLRSVAVYGGGSMWEQakalqegaeIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRM 412
Cdd:cd17963 77 ARQIGEVVEKMGKftgvkvALAVPGNDVPRGKKITAQ---------IVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVM 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 45446743 413 FDM-GFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPI 457
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 ... |
252-459 |
1.46e-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: 1.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 252 GSSFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLihimdqKELEPGDGPIAVI 331
Cdd:cd17950 1 SSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTL------QQLEPVDGQVSVL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 332 V-CPTRELCQQIHAECKRFGKaY--NLRSVAVYGGGSMWEQAKALQ-EGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFD 407
Cdd:cd17950 75 ViCHTRELAFQISNEYERFSK-YmpNVKTAVFFGGVPIKKDIEVLKnKCPHIVVGTPGRILALVREKKLKLSHVKHFVLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 45446743 408 EADRMF-DMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 459
Cdd:cd17950 154 ECDKMLeQLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEI 206
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
259-459 |
4.53e-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: 4.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 259 GFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHI-MDQKELEpgdgpiAVIVCPTRE 337
Cdd:cd17939 3 GLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIdTTVRETQ------ALVLAPTRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 338 LCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGF 417
Cdd:cd17939 77 LAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 45446743 418 EYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 459
Cdd:cd17939 157 KDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
264-463 |
2.38e-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: 2.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 264 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPG--DGPIAVIVCPTRELCQQ 341
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGpfNAPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 342 IHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQV 421
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 45446743 422 RSIASH-----VRPDR--------QTLLFSATFRKKIEKLARDIL-IDPIRVVQGD 463
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 ... |
255-459 |
3.54e-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: 3.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 255 FAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMdqkelepgdgpiAVIVCP 334
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIVV------------ALILEP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 335 TRELCQQIHAECKRFgKAY----NLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEAD 410
Cdd:cd17938 69 SRELAEQTYNCIENF-KKYldnpKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEAD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 45446743 411 RMFDMGFEYQVRSIASH-----VRPDR-QTLLFSATFRK-KIEKLARDILIDPIRV 459
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 ... |
255-460 |
4.35e-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: 4.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 255 FAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIwpmlIHIMDQKELEPgDGPIAVIVCP 334
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFS----ISILQQIDTSL-KATQALVLAP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 335 TRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFD 414
Cdd:cd18046 76 TRELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 45446743 415 MGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVV 460
Cdd:cd18046 156 RGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRIL 201
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
483-593 |
4.18e-32 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 120.39 E-value: 4.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 483 SKWNWLtRRLVEFTSSGSVLLFV--TKKANAEELannLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAAR 560
Cdd:pfam00271 1 EKLEAL-LELLKKERGGKVLIFSqtKKTLEAELL---LEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAER 76
|
90 100 110
....*....|....*....|....*....|...
gi 45446743 561 GLDIPSIKTVINYDVARDIDTHTHRIGRTGRAG 593
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, ... |
264-450 |
2.60e-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: 2.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 264 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLiHIMDqkeLEPGdGPIAVIVCPTRELCQQIH 343
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIAL-ESLD---LERR-HPQVLILAPTREIAVQIH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 344 AECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRS 423
Cdd:cd17943 76 DVFKKIGKKLEGLKCEVFIGGTPVKEDKKKLKGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNW 155
|
170 180
....*....|....*....|....*...
gi 45446743 424 IASHVRPDRQTLLFSATFRKK-IEKLAR 450
Cdd:cd17943 156 IFSSLPKNKQVIAFSATYPKNlDNLLAR 183
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
255-460 |
8.36e-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: 8.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 255 FAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLiHIMDQKELEPGdgpiAVIVCP 334
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVL-QCLDIQVRETQ----ALILSP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 335 TRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFD 414
Cdd:cd18045 76 TRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 45446743 415 MGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVV 460
Cdd:cd18045 156 KGFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRIL 201
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
264-450 |
8.40e-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: 8.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 264 LMHQIRKSEYTQPTPIQCQGVPVALSG---------RDMIGIAKTGSGKTAAFIWPMLihimdQKeLEPGDGPI--AVIV 332
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIV-----QA-LSKRVVPRlrALIV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 333 CPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEG--------AEIVVCTPGRLIDHVKKKAT-NLQRVSY 403
Cdd:cd17956 75 VPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRLVDHLNSTPGfTLKHLRF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45446743 404 LVFDEADRMFDMGFEY---QV-RSIASHVRPDR----------------QTLLFSATFRKKIEKLAR 450
Cdd:cd17956 155 LVIDEADRLLNQSFQDwleTVmKALGRPTAPDLgsfgdanllersvrplQKLLFSATLTRDPEKLSS 221
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
278-440 |
1.96e-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: 1.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 278 PIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIM-DQKELEPGDGPIAVIVCPTRELCQQIHAECKRFGKayNLR 356
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQeDQQPRKRGRAPKVLVLAPTRELANQVTKDFKDITR--KLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 357 SVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIAS-----HVRPD 431
Cdd:cd17944 93 VACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSvsykkDSEDN 172
|
....*....
gi 45446743 432 RQTLLFSAT 440
Cdd:cd17944 173 PQTLLFSAT 181
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
512-593 |
1.95e-29 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 111.92 E-value: 1.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 512 EELANNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRIGRTGR 591
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 45446743 592 AG 593
Cdd:smart00490 81 AG 82
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
290-588 |
7.02e-26 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 113.58 E-value: 7.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 290 GRDMIGIAKTGSGKTAafiwpMLIHIMDQKelepGDGPIAVIVCPTRELCQQIHAECKRFgkaynLRSVAVYGGgsmweq 369
Cdd:COG1061 100 GGRGLVVAPTGTGKTV-----LALALAAEL----LRGKRVLVLVPRRELLEQWAEELRRF-----LGDPLAGGG------ 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 370 akALQEGAEIVVCTPGRLIDHVKKKATNlQRVSYLVFDEADRMFDMGFeyqvRSIASHVRPDRqTLLFSAT--------- 440
Cdd:COG1061 160 --KKDSDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHHAGAPSY----RRILEAFPAAY-RLGLTATpfrsdgrei 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 441 ---------FRKKIEKLARDILIDPIRVV---------QGDIGEANEDVTQivEILHSGPSKWNWLTRRLVEFTSSGSVL 502
Cdd:COG1061 232 llflfdgivYEYSLKEAIEDGYLAPPEYYgirvdltdeRAEYDALSERLRE--ALAADAERKDKILRELLREHPDDRKTL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 503 LFVTKKANAEELANNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVInydVARDIDTH 582
Cdd:COG1061 310 VFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI---LLRPTGSP 386
|
....*....
gi 45446743 583 TH---RIGR 588
Cdd:COG1061 387 REfiqRLGR 395
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
271-460 |
5.37e-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: 5.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 271 SEYTQPTPIQCQGVPvALSGRDMIGI-----------------AKTGSGKTAAFIWPMLIHIMDQKELEPGDG------- 326
Cdd:cd17965 26 DEEIKPSPIQTLAIK-KLLKTLMRKVtkqtsneepklevfllaAETGSGKTLAYLAPLLDYLKRQEQEPFEEAeeeyesa 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 327 -----PIAVIVCPTRELCQQIHAECKRFGKA--YNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQ 399
Cdd:cd17965 105 kdtgrPRSVILVPTHELVEQVYSVLKKLSHTvkLGIKTFSSGFGPSYQRLQLAFKGRIDILVTTPGKLASLAKSRPKILS 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45446743 400 RVSYLVFDEADRMFDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVV 460
Cdd:cd17965 185 RVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLRKLFPDVVRIA 245
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
240-456 |
2.10e-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: 2.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 240 NLRVSGAAPPRP---GSSFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSG--RDMIGIAKTGSGKTAAFIWPMLIH 314
Cdd:cd18048 2 RVEVLQRDPTSPlfsVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 315 ImDQKELEPGdgpiAVIVCPTRELCQQIHAECKRFGKAYNLRSV--AVYGGgsmwEQAKALQEGAEIVVCTPGRLIDHV- 391
Cdd:cd18048 82 V-DALKLYPQ----CLCLSPTFELALQTGKVVEEMGKFCVGIQViyAIRGN----RPGKGTDIEAQIVIGTPGTVLDWCf 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45446743 392 KKKATNLQRVSYLVFDEADRMFDM-GFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDP 456
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 ... |
254-456 |
2.21e-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: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 254 SFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSG--RDMIGIAKTGSGKTAAFIWPMLIHImdqkelEPG-DGPIAV 330
Cdd:cd18047 2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV------EPAnKYPQCL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 331 IVCPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEgaEIVVCTPGRLIDH-VKKKATNLQRVSYLVFDEA 409
Cdd:cd18047 76 CLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISE--QIVIGTPGTVLDWcSKLKFIDPKKIKVFVLDEA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 45446743 410 DRMF-DMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDP 456
Cdd:cd18047 154 DVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
288-599 |
1.43e-16 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 83.79 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 288 LSGRDMIGIAKTGSGKTA-AFIWpMLIHIMDqkelepgdGPIAVIVCPTRELCQQIHAECKRFGKAYNLRSVAVYGGgsm 366
Cdd:COG1204 36 LEGKNLVVSAPTASGKTLiAELA-ILKALLN--------GGKALYIVPLRALASEKYREFKRDFEELGIKVGVSTGD--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 367 WEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEA------DRmfdmGFEYQVrsIASHVR---PDRQTLLF 437
Cdd:COG1204 104 YDSDDEWLGRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAhliddeSR----GPTLEV--LLARLRrlnPEAQIVAL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 438 SATFrKKIEKLAR----DILIDPIRVVQGDIGEANEDVTQIVEILHSGPSKWNWLTRRLVEftSSGSVLLFVTKKANAEE 513
Cdd:COG1204 178 SATI-GNAEEIAEwldaELVKSDWRPVPLNEGVLYDGVLRFDDGSRRSKDPTLALALDLLE--EGGQVLVFVSSRRDAES 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 514 LANNLKQE------GHNLGLL-------------------------------HGDMDQSERNKVISDFKKKDIPVLVATD 556
Cdd:COG1204 255 LAKKLADElkrrltPEEREELeelaeellevseethtnekladclekgvafhHAGLPSELRRLVEDAFREGLIKVLVATP 334
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 45446743 557 VAARGLDIPSiKTVINYDVAR----DIDTHTHR--IGRTGRAG--EKGVAY 599
Cdd:COG1204 335 TLAAGVNLPA-RRVIIRDTKRggmvPIPVLEFKqmAGRAGRPGydPYGEAI 384
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
476-607 |
6.21e-14 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 75.92 E-value: 6.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 476 EILHSGPSKwnwlTRRLVEFT----SSGSVLLFVTKKANAEELANNLKQEGHNLGLLHGD--------MDQSERNKVISD 543
Cdd:COG1111 331 DIEHPKLSK----LREILKEQlgtnPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQaskegdkgLTQKEQIEILER 406
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45446743 544 FKKKDIPVLVATDVAARGLDIPSIKTVINYD-VA---RDIdthtHRIGRTGRAGEKGVaYTLLTpKDS 607
Cdd:COG1111 407 FRAGEFNVLVATSVAEEGLDIPEVDLVIFYEpVPseiRSI----QRKGRTGRKREGRV-VVLIA-KGT 468
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
297-595 |
1.22e-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: 67.45 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 297 AKTGSGKT-AAFIWpmLIHIMDQKELEPGdgpiaVIVCPTRELCQQIHAECKR-FGKAYNLRSVAVYGGGSMWEQAKALQ 374
Cdd:cd09639 6 APTGYGKTeAALLW--ALHSLKSQKADRV-----IIALPTRATINAMYRRAKEaFGETGLYHSSILSSRIKEMGDSEEFE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 375 E-------------GAEIVVCTP-------GRLIDHVKKKATNLQRvSYLVFDEADRMFD---MGFEYQVRSIAshvRPD 431
Cdd:cd09639 79 HlfplyihsndtlfLDPITVCTIdqvlksvFGEFGHYEFTLASIAN-SLLIFDEVHFYDEytlALILAVLEVLK---DND 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 432 RQTLLFSATFRKKIEKLARDILIDpirvvqgdigEANE-------DVTQIVEILHSGPSKWNWLTRRLVEFTSSGSVLLF 504
Cdd:cd09639 155 VPILLMSATLPKFLKEYAEKIGYV----------EENEpldlkpnERAPFIKIESDKVGEISSLERLLEFIKKGGSVAII 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 505 VTKKANAEELANNLKQEGH--NLGLLHGDMDQSERNK----VISDFKKKDIPVLVATDVAARGLDIPSikTVINYDVArD 578
Cdd:cd09639 225 VNTVDRAQEFYQQLKEKGPeeEIMLIHSRFTEKDRAKkeaeLLLEFKKSEKFVIVATQVIEASLDISV--DVMITELA-P 301
|
330
....*....|....*..
gi 45446743 579 IDTHTHRIGRTGRAGEK 595
Cdd:cd09639 302 IDSLIQRLGRLHRYGEK 318
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
484-606 |
1.44e-11 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 67.86 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 484 KWNWLTRRLVEFTSsGSVLLFVTKKANAEELANNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATdVA-ARGL 562
Cdd:COG0514 217 KLAQLLDFLKEHPG-GSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGI 294
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 45446743 563 DIPSIKTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTLLTPKD 606
Cdd:COG0514 295 DKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPED 338
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
292-589 |
2.42e-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: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 292 DMigiaktGSGKTA---AFIwpmlihimdQKELEPGDGPIAVIVCPTReLCQQIHAECKRFgkAYNLRSVAVYGGGSMWE 368
Cdd:COG0553 268 DM------GLGKTIqalALL---------LELKERGLARPVLIVAPTS-LVGNWQRELAKF--APGLRVLVLDGTRERAK 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 369 QAKALQEgAEIVVCTpgrlIDHVKKKATNLQRV--SYLVFDEADRMFDMG-FEYQ-VRSIASHVR--------------- 429
Cdd:COG0553 330 GANPFED-ADLVITS----YGLLRRDIELLAAVdwDLVILDEAQHIKNPAtKRAKaVRALKARHRlaltgtpvenrleel 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 430 ------------PDRQTllFSATFRKKIEK--------LAR------------DILID-PIRVVQ--------------- 461
Cdd:COG0553 405 wslldflnpgllGSLKA--FRERFARPIEKgdeealerLRRllrpfllrrtkeDVLKDlPEKTEEtlyveltpeqralye 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 462 -------GDIGEANEDVTQIV----------------------EILHSGPSKWNWLTRRLVEFTSSG-SVLLFVTKKANA 511
Cdd:COG0553 483 avleylrRELEGAEGIRRRGLilaaltrlrqicshpallleegAELSGRSAKLEALLELLEELLAEGeKVLVFSQFTDTL 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 512 EELANNLKQEGHNLGLLHGDMDQSERNKVISDFK-KKDIPV-LVATDVAARGLDIPSIKTVINYD-----------VARd 578
Cdd:COG0553 563 DLLEERLEERGIEYAYLHGGTSAEERDELVDRFQeGPEAPVfLISLKAGGEGLNLTAADHVIHYDlwwnpaveeqaIDR- 641
|
410
....*....|.
gi 45446743 579 idthTHRIGRT 589
Cdd:COG0553 642 ----AHRIGQT 648
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
297-440 |
4.11e-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: 4.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 297 AKTGSGKT-AAFIWpmLIHIMDQKelepgdGPIAVIVCPTRELCQQIHAECKRFGKaYNLRSVAVYGGGSMWEQAKALQE 375
Cdd:cd00046 8 APTGSGKTlAALLA--ALLLLLKK------GKKVLVLVPTKALALQTAERLRELFG-PGIRVAVLVGGSSAEEREKNKLG 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45446743 376 GAEIVVCTPGRLIDHVK-KKATNLQRVSYLVFDEADRM-FDMGFEYQVR-SIASHVRPDRQTLLFSAT 440
Cdd:cd00046 79 DADIIIATPDMLLNLLLrEDRLFLKDLKLIIVDEAHALlIDSRGALILDlAVRKAGLKNAQVILLSAT 146
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
299-608 |
5.98e-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: 65.87 E-value: 5.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 299 TGSGKT-AAFIWpMLIHimdqkeLEPGDGPIAVIVCPTRELCQQIHaecKRFGKAYNLrSVAVYGGGSMWEQAKALQEG- 376
Cdd:COG1203 156 TGGGKTeAALLF-ALRL------AAKHGGRRIIYALPFTSIINQTY---DRLRDLFGE-DVLLHHSLADLDLLEEEEEYe 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 377 --------------AEIVVCTPGRLIDHV-------KKKATNLQRvSYLVFDEADrMFDMgfEYQ---VRSIASHVRPDR 432
Cdd:COG1203 225 searwlkllkelwdAPVVVTTIDQLFESLfsnrkgqERRLHNLAN-SVIILDEVQ-AYPP--YMLallLRLLEWLKNLGG 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 433 QTLLFSATFRKKIeklaRDILIDPIRVVQGDIGEANEDVTQIVE---ILHSGPSKWNWLTRRLVE-FTSSGSVLLFVTKK 508
Cdd:COG1203 301 SVILMTATLPPLL----REELLEAYELIPDEPEELPEYFRAFVRkrvELKEGPLSDEELAELILEaLHKGKSVLVIVNTV 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 509 ANAEELANNLKQEGHNLG--LLHGDMDQSERNKVISD----FKKKDIPVLVATDVAARGLDipsiktvINYDVA-RD--- 578
Cdd:COG1203 377 KDAQELYEALKEKLPDEEvyLLHSRFCPADRSEIEKEikerLERGKPCILVSTQVVEAGVD-------IDFDVViRDlap 449
|
330 340 350
....*....|....*....|....*....|...
gi 45446743 579 IDTHTHRIGRT---GRAGEKGVAYtLLTPKDSN 608
Cdd:COG1203 450 LDSLIQRAGRCnrhGRKEEEGNVY-VFDPEDEG 481
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
297-595 |
6.13e-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: 65.17 E-value: 6.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 297 AKTGSGKT-AAFIWpmLIHIMDQKELEPGdgpiaVIVCPTRELCQQIHaecKRFGKAYNLRSVAVYGGGSMWEQAKALQE 375
Cdd:TIGR01587 6 APTGYGKTeAALLW--ALHSIKSQKADRV-----IIALPTRATINAMY---RRAKELFGSELVGLHHSSSFSRIKEMGDS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 376 GA------------------EIVVCTP-------GRLIDHVKKKATNLQRvSYLVFDEADRMFD---MGFEYQVRSIAsh 427
Cdd:TIGR01587 76 EEfehlfplyihsndklfldPITVCTIdqvlksvFGEFGHYEFTLASIAN-SLLIFDEVHFYDEytlALILAVLEVLK-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 428 vRPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIGEANEDVTQIVEILHSGPSKWNWLTRRLVEFTSSGSVLLFVTK 507
Cdd:TIGR01587 153 -DNDVPILLMSATLPKFLKEYAEKIGYVEFNEPLDLKEERRFENHRFILIESDKVGEISSLERLLEFIKKGGSIAIIVNT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 508 KANAEELANNLKQEGHNLG--LLHGDMDQSERNK----VISDFKKKDIP-VLVATDVAARGLDIPSikTVINYDVArDID 580
Cdd:TIGR01587 232 VDRAQEFYQQLKEKAPEEEiiLYHSRFTEKDRAKkeaeLLREMKKSNEKfVIVATQVIEASLDISA--DVMITELA-PID 308
|
330
....*....|....*
gi 45446743 581 THTHRIGRTGRAGEK 595
Cdd:TIGR01587 309 SLIQRLGRLHRYGRK 323
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
299-409 |
1.86e-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: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 299 TGSGKTaaFIWPMLIHIM-DQKELEPGDGPIAVIVCPTRELCQQihaECKRFGKAYNLRSVAVYG--GGSMWEQAKALQE 375
Cdd:cd18034 25 TGSGKT--LIAVMLIKEMgELNRKEKNPKKRAVFLVPTVPLVAQ---QAEAIRSHTDLKVGEYSGemGVDKWTKERWKEE 99
|
90 100 110
....*....|....*....|....*....|....*.
gi 45446743 376 --GAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEA 409
Cdd:cd18034 100 leKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
501-602 |
4.29e-10 |
|
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: 58.91 E-value: 4.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 501 VLLFVTKKANAEELANNLKQE----------GHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTV 570
Cdd:cd18801 33 VIIFSEFRDSAEEIVNFLSKIrpgiratrfiGQASGKSSKGMSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLI 112
|
90 100 110
....*....|....*....|....*....|...
gi 45446743 571 INYD-VARDIDThTHRIGRTGRaGEKGVAYTLL 602
Cdd:cd18801 113 ICYDaSPSPIRM-IQRMGRTGR-KRQGRVVVLL 143
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
475-587 |
4.95e-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: 58.26 E-value: 4.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 475 VEILHSGpsKWNWLTRRLVEFTSSGS-VLLFVTKKANAEELANNLKQEGHNLGLLHGDMDQSERNKVISDFKK-KDIPV- 551
Cdd:cd18793 5 IEEVVSG--KLEALLELLEELREPGEkVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEdPDIRVf 82
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 45446743 552 LVATDVAARGLDIPSIKTVINYDV----ARD---IDtHTHRIG 587
Cdd:cd18793 83 LLSTKAGGVGLNLTAANRVILYDPwwnpAVEeqaID-RAHRIG 124
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
277-409 |
7.40e-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: 7.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 277 TPIQCQGV-PVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQkelepgdGPIAVIVCPTRELCQQIHAECKRFGKAYNL 355
Cdd:cd17921 3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRALATS-------GGKAVYIAPTRALVNQKEADLRERFGPLGK 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 45446743 356 RSVAVYGGGSMweqAKALQEGAEIVVCTP----GRLIDHvkkKATNLQRVSYLVFDEA 409
Cdd:cd17921 76 NVGLLTGDPSV---NKLLLAEADILVATPekldLLLRNG---GERLIQDVRLVVVDEA 127
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
510-604 |
1.78e-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: 57.66 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 510 NAEELANNLKQE--GHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRI- 586
Cdd:cd18792 46 SIEALAEELKELvpEARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFGLSQLHQLr 125
|
90
....*....|....*...
gi 45446743 587 GRTGRAGEKGVAYtLLTP 604
Cdd:cd18792 126 GRVGRGKHQSYCY-LLYP 142
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
248-602 |
2.20e-09 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 61.39 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 248 PPRPGSsFAHF--GFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDqkelepGD 325
Cdd:COG1205 28 PAREAR-YAPWpdWLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLE------DP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 326 GPIAVIVCPTRELCQQIHAECKRFGKAYNLR-SVAVYGGGSMWEQAKALQEGAEIVVCTP-----GrLIDHVKKKATNLQ 399
Cdd:COG1205 101 GATALYLYPTKALARDQLRRLRELAEALGLGvRVATYDGDTPPEERRWIREHPDIVLTNPdmlhyG-LLPHHTRWARFFR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 400 RVSYLVFDEA---------------DRMfdmgfeyqvRSIASHVRPDRQTLLFSATfrkkI---EKLARDILIDPIRVVQ 461
Cdd:COG1205 180 NLRYVVIDEAhtyrgvfgshvanvlRRL---------RRICRHYGSDPQFILASAT----IgnpAEHAERLTGRPVTVVD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 462 GDiGEAnedvTQIVEILHSGPSKWNWLTRR---------LVEFTSSG-SVLLFVTKKANAEELANNLKQEGHNLGLL--- 528
Cdd:COG1205 247 ED-GSP----RGERTFVLWNPPLVDDGIRRsalaeaarlLADLVREGlRTLVFTRSRRGAELLARYARRALREPDLAdrv 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45446743 529 ---HGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTLL 602
Cdd:COG1205 322 aayRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVLVA 398
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
508-633 |
2.23e-09 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 61.27 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 508 KANAEELANNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRIG 587
Cdd:PRK11057 246 RAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETG 325
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 45446743 588 RTGRAGEKGVAYTLLTPKDSNFagdLVRNLE----GANQHVSKELLDlAM 633
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 ... |
488-591 |
5.33e-09 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 55.73 E-value: 5.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 488 LTRRLVEFTSSGSVLLFVTKKANAEELANNLKQ------EGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARG 561
Cdd:cd18796 28 YAEVIFLLERHKSTLVFTNTRSQAERLAQRLRElcpdrvPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELG 107
|
90 100 110
....*....|....*....|....*....|
gi 45446743 562 LDIPSIKTVINYDVARDIDTHTHRIGRTGR 591
Cdd:cd18796 108 IDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
510-619 |
7.09e-09 |
|
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: 55.81 E-value: 7.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 510 NAEELANNLKQE---GHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRI 586
Cdd:cd18811 46 AAVAMYEYLKERfrpELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLHQL 125
|
90 100 110
....*....|....*....|....*....|....
gi 45446743 587 -GRTGRAGEKGVAYTLLTPKDSNFAGDLVRNLEG 619
Cdd:cd18811 126 rGRVGRGDHQSYCLLVYKDPLTETAKQRLRVMTE 159
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
494-618 |
7.78e-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: 7.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 494 EFTSSGSVLLFVTKKANAEELANNLKQ--EGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVI 571
Cdd:cd18810 21 ELLRGGQVFYVHNRIESIEKLATQLRQlvPEARIAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTII 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 45446743 572 --NYDVARDIDTHTHRiGRTGRAGEKGVAYtLLTPKDSNFAGDLVRNLE 618
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 ... |
551-603 |
1.77e-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: 1.77e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 45446743 551 VLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTLLT 603
Cdd:cd18785 25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILFV 77
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
490-594 |
2.65e-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: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 490 RRLVEFTSSGSVLLFVTKKANAEELANNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATdVA-ARGLDIPSIK 568
Cdd:cd18794 22 KRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVAT-VAfGMGIDKPDVR 100
|
90 100
....*....|....*....|....*.
gi 45446743 569 TVINYDVARDIDTHTHRIGRTGRAGE 594
Cdd:cd18794 101 FVIHYSLPKSMESYYQESGRAGRDGL 126
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
511-603 |
4.40e-08 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 57.19 E-value: 4.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 511 AEELANNLKQEGHNLGLLHGD--------MDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYD-VARDIDT 581
Cdd:PRK13766 378 AEKIVDLLEKEGIKAVRFVGQaskdgdkgMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEpVPSEIRS 457
|
90 100
....*....|....*....|..
gi 45446743 582 hTHRIGRTGRaGEKGVAYTLLT 603
Cdd:PRK13766 458 -IQRKGRTGR-QEEGRVVVLIA 477
|
|
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
509-571 |
4.57e-08 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 56.98 E-value: 4.57e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45446743 509 ANAEELANNLKQE--GHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATdvaargldipsikTVI 571
Cdd:COG1200 488 QAAEETYEELREAfpGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVAT-------------TVI 539
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
502-603 |
5.32e-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: 5.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 502 LLFVTKKANAEELANNLKQEGHNLGLLHGD---------------MDQSERNKVISDFKKKDIPVLVATDVAARGLDIPS 566
Cdd:cd18802 29 IIFVERRATAVVLSRLLKEHPSTLAFIRCGfligrgnssqrkrslMTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPA 108
|
90 100 110
....*....|....*....|....*....|....*..
gi 45446743 567 IKTVINYDVARDIdthTHRIGRTGRAGEKGVAYTLLT 603
Cdd:cd18802 109 CNLVIRFDLPKTL---RSYIQSRGRARAPNSKYILMV 142
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
500-571 |
1.30e-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: 51.02 E-value: 1.30e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45446743 500 SVLLFVTKKANAEELANNLKQEGHNLGLLHGD--MDQSERNKVISDFK-KKDIPVLVATDVAARGLDIPSIKTVI 571
Cdd:cd18799 8 KTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDysDRERGDEALILLFFgELKPPILVTVDLLTTGVDIPEVDNVV 82
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
270-614 |
2.26e-07 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 54.72 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 270 KSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKT-AAFIWPmLIHIMDQKELEPGDGPIAVI-VCPTRELCQQIHaeck 347
Cdd:COG1201 19 AARFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAFLPA-LDELARRPRPGELPDGLRVLyISPLKALANDIE---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 348 RfgkayNLR-----------------SVAV-YGGGSMWEQAKALQEGAEIVVCTPGRLidHV----KKKATNLQRVSYLV 405
Cdd:COG1201 94 R-----NLRapleeigeaaglplpeiRVGVrTGDTPASERQRQRRRPPHILITTPESL--ALlltsPDARELLRGVRTVI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 406 FDEadrmfdmgfeyqVRSIAS---------------HVRPDR-QTLLFSATFRkKIEKLAR----DILIDPIRVVQGDIG 465
Cdd:COG1201 167 VDE------------IHALAGskrgvhlalslerlrALAPRPlQRIGLSATVG-PLEEVARflvgYEDPRPVTIVDAGAG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 466 -----EANEDVTQIVEILHSGPSKWNWLTRRLVEF-TSSGSVLLFVTKKANAEELANNLKQ----EGHNLGLLHGDMDQS 535
Cdd:COG1201 234 kkpdlEVLVPVEDLIERFPWAGHLWPHLYPRVLDLiEAHRTTLVFTNTRSQAERLFQRLNElnpeDALPIAAHHGSLSRE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 536 ERNKVISDFKKKDIPVLVAT---DVaarGLDIPSIKTVINYD----VARDIdthtHRIGRTG-RAGEKGVAYtlLTPKDs 607
Cdd:COG1201 314 QRLEVEEALKAGELRAVVATsslEL---GIDIGDVDLVIQVGspksVARLL----QRIGRAGhRVGEVSKGR--LVPTH- 383
|
....*..
gi 45446743 608 nfAGDLV 614
Cdd:COG1201 384 --RDELV 388
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
494-601 |
1.51e-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: 48.70 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 494 EFTSSGSVLLFVTKKANAEELANNLKqeghNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSiKTVI-- 571
Cdd:cd18795 39 TVSEGKPVLVFCSSRKECEKTAKDLA----GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPA-RTVIik 113
|
90 100 110
....*....|....*....|....*....|....*....
gi 45446743 572 -----NYDVARDIDTHTHR--IGRTGRAG--EKGVAYTL 601
Cdd:cd18795 114 gtqryDGKGYRELSPLEYLqmIGRAGRPGfdTRGEAIIM 152
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
299-441 |
2.18e-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: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 299 TGSGKT---AAFIWpmliHIMDQKELepgdgpiavIVCPTRELCQQIHAECKRFGKAynlRSVAVYGGGSmweqaKALQE 375
Cdd:cd17926 27 TGSGKTltaLALIA----YLKELRTL---------IVVPTDALLDQWKERFEDFLGD---SSIGLIGGGK-----KKDFD 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45446743 376 GAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFeyqvRSIASHVRPDRQtLLFSATF 441
Cdd:cd17926 86 DANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHHLPAKTF----SEILKELNAKYR-LGLTATP 146
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
510-565 |
2.60e-06 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 51.30 E-value: 2.60e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 45446743 510 NAEELANNLKQE--GHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIP 565
Cdd:PRK10917 491 SAEETYEELQEAfpELRVGLLHGRMKPAEKDAVMAAFKAGEIDILVATTVIEVGVDVP 548
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
276-408 |
2.72e-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: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 276 PTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHImdQKELEPGDGPIAVIVCPTRELC-QQIHAECKRFGKAYN 354
Cdd:cd18036 3 LRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHL--EKRRSAGEKGRVVVLVNKVPLVeQQLEKFFKYFRKGYK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 45446743 355 LrsVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATN----LQRVSYLVFDE 408
Cdd:cd18036 81 V--TGLSGDSSHKVSFGQIVKASDVIICTPQILINNLLSGREEervyLSDFSLLIFDE 136
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
290-408 |
4.75e-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: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 290 GRDMIGIAKTGSGKT-AAFIWPmLIHIMDQKElepgdGPIAVI-VCPTRELCQQIHAECKRFGKAYNL-RSVAV-YGGGS 365
Cdd:cd17922 1 GRNVLIAAPTGSGKTeAAFLPA-LSSLADEPE-----KGVQVLyISPLKALINDQERRLEEPLDEIDLeIPVAVrHGDTS 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 45446743 366 MWEQAKALQEGAEIVVCTP---GRLIDHvKKKATNLQRVSYLVFDE 408
Cdd:cd17922 75 QSEKAKQLKNPPGILITTPeslELLLVN-KKLRELFAGLRYVVVDE 119
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
502-595 |
5.23e-06 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 50.66 E-value: 5.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 502 LLFVTKKANAEELANNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDT 581
Cdd:PLN03137 684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEG 763
|
90
....*....|....
gi 45446743 582 HTHRIGRTGRAGEK 595
Cdd:PLN03137 764 YHQECGRAGRDGQR 777
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
501-574 |
8.65e-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: 8.65e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45446743 501 VLLFVTKKANAEELANNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYD 574
Cdd:cd18790 30 VLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILD 103
|
|
| PRK10689 |
PRK10689 |
transcription-repair coupling factor; Provisional |
529-618 |
1.59e-05 |
|
transcription-repair coupling factor; Provisional
Pssm-ID: 182649 [Multi-domain] Cd Length: 1147 Bit Score: 48.97 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 529 HGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVI-----NYDVARdidTHTHRiGRTGRAGEKGVAYtLLT 603
Cdd:PRK10689 842 HGQMRERELERVMNDFHHQRFNVLVCTTIIETGIDIPTANTIIieradHFGLAQ---LHQLR-GRVGRSHHQAYAW-LLT 916
|
90
....*....|....*
gi 45446743 604 PKDSNFAGDLVRNLE 618
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 ... |
275-411 |
1.92e-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: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 275 QPTPIQCQGVPVALSGRDMIGIAKTGSGKTaaFIwPMLI--HIMDQKELEPGdGPIAVIVcPTRELC-QQIHAECKRFGK 351
Cdd:cd17927 2 KPRNYQLELAQPALKGKNTIICLPTGSGKT--FV-AVLIceHHLKKFPAGRK-GKVVFLA-NKVPLVeQQKEVFRKHFER 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45446743 352 AYnLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKK-KATNLQRVSYLVFDEADR 411
Cdd:cd17927 77 PG-YKVTGLSGDTSENVSVEQIVESSDVIIVTPQILVNDLKSgTIVSLSDFSLLVFDECHN 136
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
502-608 |
3.72e-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: 45.37 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 502 LLFVTK---KANAEELANNLKQEGHNLGLLHgdmdqSERNKVISDFKKKDIPVLVAT----DVAARGLDIP-SIKTVINY 573
Cdd:cd18798 28 LIFVSIdygKEYAEELKEFLERHGIKAELAL-----SSTEKNLEKFEEGEIDVLIGVasyyGVLVRGIDLPeRIKYAIFY 102
|
90 100 110
....*....|....*....|....*....|....*....
gi 45446743 574 DVArdIDTHTHRIGRTGR--AGE--KGVAYTLLTPKDSN 608
Cdd:cd18798 103 GVP--VTTYIQASGRTSRlyAGGltKGLSVVLVDDPELF 139
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
279-384 |
6.90e-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: 6.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 279 IQCQGVPVAL-SGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDgPIAVIVCPTRELCQQIHAECK-RFGKaYNLR 356
Cdd:cd18023 5 IQSEVFPDLLySDKNFVVSAPTGSGKTVLFELAILRLLKERNPLPWGN-RKVVYIAPIKALCSEKYDDWKeKFGP-LGLS 82
|
90 100
....*....|....*....|....*...
gi 45446743 357 SVAVYGGGSMWEQAKAlqEGAEIVVCTP 384
Cdd:cd18023 83 CAELTGDTEMDDTFEI--QDADIILTTP 108
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
497-601 |
9.99e-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: 44.06 E-value: 9.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 497 SSGSVLLFVTKKANAEELANNLKQEGHNLGL-------LHGDMDQSERNKVI---SDFKKKdipVLVATDVAARGLDIPS 566
Cdd:cd18791 42 EPGDILVFLPGQEEIERLCELLREELLSPDLgkllvlpLHSSLPPEEQQRVFeppPPGVRK---VVLATNIAETSITIPG 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 45446743 567 IKTVI--------NYDVARDIDT-HTHRIG------RTGRAG--EKGVAYTL 601
Cdd:cd18791 119 VVYVIdsglvkekVYDPRTGLSSlVTVWISkasaeqRAGRAGrtRPGKCYRL 170
|
|
| VirD4 |
COG3505 |
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ... |
296-351 |
1.89e-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: 1.89e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 45446743 296 IAKTGSGKTAAFIWPMLIHimdqkeLEPGDGpiAVIVCPTRELCQQIHAECKRFGK 351
Cdd:COG3505 5 IGPTGSGKTVGLVIPNLTQ------LARGES--VVVTDPKGDLAELTAGFRRRAGY 52
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
286-411 |
1.98e-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: 43.27 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 286 VALSGRDMIgIAKTGSGKTAAFIWPMLihimdqKELEPGDGPIaVIVCPTRELCQQiHAEckRFGKAYNL--RSVAVYGG 363
Cdd:cd18035 13 VALNGNTLI-VLPTGLGKTIIAILVAA------DRLTKKGGKV-LILAPSRPLVEQ-HAE--NLKRVLNIpdKITSLTGE 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 45446743 364 GSMWEQAKALQEGaEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADR 411
Cdd:cd18035 82 VKPEERAERWDAS-KIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
409-593 |
2.54e-04 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 44.87 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 409 ADRMFDMGFEYQ------VRSIASHVRPDRQTLLFSATFRKKIEK---LARDILIDPIRVVQGDIGEANEDvTQIVEILH 479
Cdd:PRK01172 141 ADEIHIIGDEDRgptletVLSSARYVNPDARILALSATVSNANELaqwLNASLIKSNFRPVPLKLGILYRK-RLILDGYE 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 480 SGPSKWNWLTRRLVEftSSGSVLLFVTKKANAEELANNLKQE-------------------------GHNLGLLHGDMDQ 534
Cdd:PRK01172 220 RSQVDINSLIKETVN--DGGQVLVFVSSRKNAEDYAEMLIQHfpefndfkvssennnvyddslnemlPHGVAFHHAGLSN 297
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45446743 535 SERNKVISDFKKKDIPVLVATDVAARGLDIPSiKTVINYDVARDIDTHT---------HRIGRTGRAG 593
Cdd:PRK01172 298 EQRRFIEEMFRNRYIKVIVATPTLAAGVNLPA-RLVIVRDITRYGNGGIrylsnmeikQMIGRAGRPG 364
|
|
| secA |
PRK12898 |
preprotein translocase subunit SecA; Reviewed |
483-642 |
5.15e-04 |
|
preprotein translocase subunit SecA; Reviewed
Pssm-ID: 237253 [Multi-domain] Cd Length: 656 Bit Score: 43.85 E-value: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 483 SKWNWLTRRLVEFTSSGSVLLFVTKK-ANAEELANNLKQEGHNLGLLHGDMDQSErNKVISDFKKKDiPVLVATDVAARG 561
Cdd:PRK12898 457 AKWAAVAARVRELHAQGRPVLVGTRSvAASERLSALLREAGLPHQVLNAKQDAEE-AAIVARAGQRG-RITVATNMAGRG 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 562 LDIPsiktvINYDVARD-----IDTHTHR--------IGRTGRAGEKGVAYTLLTPKD---SNFAGDLVRNLEGANQHVS 625
Cdd:PRK12898 535 TDIK-----LEPGVAARgglhvILTERHDsaridrqlAGRCGRQGDPGSYEAILSLEDdllQSFLGSRGLAIRRMELLGP 609
|
170
....*....|....*..
gi 45446743 626 KELLDLAMQNAWFRKSR 642
Cdd:PRK12898 610 RGGRALGALLLRRAQRR 626
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
501-596 |
9.46e-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: 9.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 501 VLLFVTKKANAEELANNLkqeghNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIktvinyDVARDID 580
Cdd:cd18789 52 IIVFTDNVEALYRYAKRL-----LKPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPEA------NVAIQIS 120
|
90 100
....*....|....*....|...
gi 45446743 581 TH-------THRIGRTGRAGEKG 596
Cdd:cd18789 121 GHggsrrqeAQRLGRILRPKKGG 143
|
|
| DEXQc_arch_SWI2_SNF2 |
cd18012 |
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ... |
292-409 |
1.35e-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: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 292 DMigiaktGSGKTAAfiwpMLIHIMDQKElEPGDGPiAVIVCPTrELCQQIHAECKRFgkAYNLRSVAVYGGGSMWEQAK 371
Cdd:cd18012 31 DM------GLGKTLQ----TLALLLSRKE-EGRKGP-SLVVAPT-SLIYNWEEEAAKF--APELKVLVIHGTKRKREKLR 95
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 45446743 372 ALqEGAEIVVCTPG---RLIDHVKKkatnlQRVSYLVFDEA 409
Cdd:cd18012 96 AL-EDYDLVITSYGllrRDIELLKE-----VKFHYLVLDEA 130
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
299-441 |
1.44e-03 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 40.35 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 299 TGSGKTAafiwpMLIHIMDQKeLEPGDGPIAVIVCPTRELCQQIHAECKRFGKAYNLRSvAVYGGGSMweqaKALQEGAE 378
Cdd:pfam04851 32 TGSGKTL-----TAAKLIARL-FKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYVEIG-EIISGDKK----DESVDDNK 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45446743 379 IVVCTP---GRLIDHVKKKATNLQRVsYLVFDEADRMFDMGFeyqvRSIASHVRPdrQTLL-FSATF 441
Cdd:pfam04851 101 IVVTTIqslYKALELASLELLPDFFD-VIIIDEAHRSGASSY----RNILEYFKP--AFLLgLTATP 160
|
|
| dermokine |
cd21118 |
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ... |
733-891 |
2.13e-03 |
|
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: 41.52 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 733 SAGSLNSvpTNSAQQGHNSPDSPVTSAAKGIPGFGNTGNiSGAPVTYPSAGAQGVNntaSGNNSREGTGGSNGKRERYTE 812
Cdd:cd21118 217 SGGSSSS--GSSGSQGSHGSNGQGSSGSSGGQGNGGNNG-SSSSNSGNSGGSNGGS---SGNSGSGSGGSSSGGSNGWGG 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 813 NRGSSRHSHGETGNRHS-DSPRHGDggrhgdgyRHPESSSRHTDGHRHGENRHGGSAGRhGENRGANDGRNGESRKEAFN 891
Cdd:cd21118 291 SSSSGGSGGSGGGNKPEcNNPGNDV--------RMAGGGGSQGSKESSGSHGSNGGNGQ-AEAVGGLNTLNSDASTLPFN 361
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
287-409 |
2.33e-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: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 287 ALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKelepgdGPIAVIVCPTRELCQQIHAECKRFGKAYNLR-SVAVYGG-G 364
Cdd:cd17923 12 ARAGRSVVVTTGTASGKSLCYQLPILEALLRDP------GSRALYLYPTKALAQDQLRSLRELLEQLGLGiRVATYDGdT 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 45446743 365 SMWEQAKALQEGAEIVVCTPGRL----IDHVKKKATNLQRVSYLVFDEA 409
Cdd:cd17923 86 PREERRAIIRNPPRILLTNPDMLhyalLPHHDRWARFLRNLRYVVLDEA 134
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
278-409 |
6.36e-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: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 278 PIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIhimdQKELEPGdgpIAVIVCPTRELCQ-QIHAeCKRFGKAYNLR 356
Cdd:cd18018 15 PGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALL----LRRRGPG---LTLVVSPLIALMKdQVDA-LPRAIKAAALN 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 45446743 357 SVAvyGGGSMWEQAKALQEG-AEIVVCTPGRLID-HVKKKATNLQRVSYLVFDEA 409
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 ... |
273-409 |
8.39e-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: 8.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446743 273 YTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIhimdqkelepgDGPIAVIVCPTRELCQ-QIHaECKRFGK 351
Cdd:cd17920 10 YDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALL-----------LDGVTLVVSPLISLMQdQVD-RLQQLGI 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45446743 352 aynlRSVAVYGGGSMWEQAKALQEGAE----IVVCTPGRLI-DHVKK---KATNLQRVSYLVFDEA 409
Cdd:cd17920 78 ----RAAALNSTLSPEEKREVLLRIKNgqykLLYVTPERLLsPDFLEllqRLPERKRLALIVVDEA 139
|
|
| |
