|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
91-515 |
1.03e-159 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 469.24 E-value: 1.03e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 91 SFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKElepgDGPIAVIVC 170
Cdd:COG0513 3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP----RAPQALILA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 171 PTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMF 250
Cdd:COG0513 79 PTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRML 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 251 DMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVvqgDIGEANEDVTQIVEILH--SGPSKWNwLTRR 328
Cdd:COG0513 159 DMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRI---EVAPENATAETIEQRYYlvDKRDKLE-LLRR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 329 LVEFTSSGSVLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVI 408
Cdd:COG0513 235 LLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 409 NYDVARDIDTHTHRIGRTGRAGEKGVAYTLLTPKDSNfagdLVRNLEGA-NQHVSKELLDLAMQNAWFRKSRFKGGKGKK 487
Cdd:COG0513 315 NYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERR----LLRAIEKLiGQKIEEEELPGFEPVEEKRLERLKPKIKEK 390
|
410 420
....*....|....*....|....*...
gi 1907083232 488 LNIGGGGLGYRERPGlGSENSDRGNNNN 515
Cdd:COG0513 391 LKGKKAGRGGRPGPK-GERKARRGKRRR 417
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
30-489 |
5.99e-149 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 446.53 E-value: 5.99e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 30 SKKIIDPLPPIDHSEIDYPPFEKNFYNEHEEITNLTPQQLIDLR--HKLNLrVSGAAPPRPGSSFAHFGFDEQLMHQIRK 107
Cdd:PTZ00110 69 SSTLGKRLQPIDWKSINLVPFEKNFYKEHPEVSALSSKEVDEIRkeKEITI-IAGENVPKPVVSFEYTSFPDYILKSLKN 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 108 SEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIHAECKRFG 187
Cdd:PTZ00110 148 AGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGDGPIVLVLAPTRELAEQIREQCNKFG 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 188 KAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASHVRP 267
Cdd:PTZ00110 228 ASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRP 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 268 DRQTLLFSATFRKKIEKLARDILID-PIRVVQGDIG-EANEDVTQIVEIL--HSGPSKWNWLTRRLveFTSSGSVLLFVT 343
Cdd:PTZ00110 308 DRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSLDlTACHNIKQEVFVVeeHEKRGKLKMLLQRI--MRDGDKILIFVE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 344 KKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRI 423
Cdd:PTZ00110 386 TKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRI 465
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083232 424 GRTGRAGEKGVAYTLLTPKDSNFAGDLVRNLEGANQHVSKELLDLAMQNAWFRKSRFKGGKGKKLN 489
Cdd:PTZ00110 466 GRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSNERSNGTERRRWGGYGRFSN 531
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
101-297 |
5.77e-142 |
|
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: 5.77e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 101 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIH 180
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGEGPIAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 181 AECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRS 260
Cdd:cd17952 81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1907083232 261 IASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVV 297
Cdd:cd17952 161 IVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRVV 197
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
110-450 |
4.00e-106 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 332.54 E-value: 4.00e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 110 YTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHImDQKELepgdGPIAVIVCPTRELCQQIHAECKRFGKA 189
Cdd:PRK11776 24 YTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL-DVKRF----RVQALVLCPTRELADQVAKEIRRLARF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 190 -YNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASHVRPD 268
Cdd:PRK11776 99 iPNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMGFQDAIDAIIRQAPAR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 269 RQTLLFSATFRKKIEKLARDILIDPIRVvqgdIGEANEDVTQI----VEILHSGpsKWNWLTRRLVEFTSSgSVLLFVTK 344
Cdd:PRK11776 179 RQTLLFSATYPEGIAAISQRFQRDPVEV----KVESTHDLPAIeqrfYEVSPDE--RLPALQRLLLHHQPE-SCVVFCNT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 345 KANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRIG 424
Cdd:PRK11776 252 KKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRIG 331
|
330 340
....*....|....*....|....*.
gi 1907083232 425 RTGRAGEKGVAYTLLTPKDSNFAGDL 450
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) ... |
79-296 |
1.29e-102 |
|
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) is a component of the 17S U2 snRNP complex. It plays an important role in pre-mRNA splicing and has a role in antiviral innate immunity. DDX46 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350711 [Multi-domain] Cd Length: 222 Bit Score: 314.70 E-value: 1.29e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 79 RVSGAAPPRPGSSFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKEL 158
Cdd:cd17953 1 KVRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 159 EPGDGPIAVIVCPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHV---KKKATNL 235
Cdd:cd17953 81 KPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtanNGRVTNL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907083232 236 QRVSYLVFDEADRMFDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 296
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 ... |
101-297 |
6.46e-97 |
|
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: 6.46e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 101 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIH 180
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGDGPIVLVLAPTRELAQQIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 181 AECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRS 260
Cdd:cd17966 81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1907083232 261 IASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVV 297
Cdd:cd17966 161 IVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
101-296 |
1.04e-96 |
|
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350669 [Multi-domain] Cd Length: 196 Bit Score: 298.20 E-value: 1.04e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 101 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKElEPGDGPIAVIVCPTRELCQQIH 180
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPK-KKGRGPQALVLAPTRELAMQIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 181 AECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRS 260
Cdd:cd00268 80 EVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907083232 261 IASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 296
Cdd:cd00268 160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
92-438 |
1.69e-93 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 298.78 E-value: 1.69e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 92 FAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDgPIAVIVCP 171
Cdd:PRK11192 3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRKSGP-PRILILTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 172 TRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFD 251
Cdd:PRK11192 82 TRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 252 MGFEYQVRSIASHVRPDRQTLLFSATFR-KKIEKLARDILIDPIRVvqgdigEAN------EDVTQIVEILHSGPSKWNW 324
Cdd:PRK11192 162 MGFAQDIETIAAETRWRKQTLLFSATLEgDAVQDFAERLLNDPVEV------EAEpsrrerKKIHQWYYRADDLEHKTAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 325 LTRRLVEFTSSGSVLlFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSI 404
Cdd:PRK11192 236 LCHLLKQPEVTRSIV-FVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDV 314
|
330 340 350
....*....|....*....|....*....|....
gi 1907083232 405 KTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTL 438
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 ... |
41-296 |
1.60e-89 |
|
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or DEAD Box Protein P82) has a wide variety of functions including regulating the alternative splicing of exons exhibiting specific features such as the inclusion of AC-rich alternative exons in CD44 transcripts, playing a role in innate immunity, and promoting mRNA degradation mediated by the antiviral zinc-finger protein ZC3HAV1 in an ATPase-dependent manner. DDX17 synergizes with DDX5 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. DDX17 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350808 [Multi-domain] Cd Length: 271 Bit Score: 282.28 E-value: 1.60e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 41 DHSEIdyPPFEKNFYNEHEEITNLTPQQLIDLRHKLNLRVSGAAPPRPGSSFAHFGFDEQLMHQIRKSEYTQPTPIQCQG 120
Cdd:cd18050 15 DLSEL--PKFEKNFYVEHPEVARMTQYDVEELRRKKEITIRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 121 VPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIHAECKRFGKAYNLRSVAVYGG 200
Cdd:cd18050 93 FPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 201 GSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASHVRPDRQTLLFSATFRK 280
Cdd:cd18050 173 APKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPK 252
|
250
....*....|....*.
gi 1907083232 281 KIEKLARDILIDPIRV 296
Cdd:cd18050 253 EVRQLAEDFLRDYVQI 268
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
91-515 |
8.49e-81 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 265.90 E-value: 8.49e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 91 SFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPI-AVIV 169
Cdd:PRK10590 2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVrALIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 170 CPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRM 249
Cdd:PRK10590 82 TPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 250 FDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIGEANEDVTQIV---------EILHSGPS 320
Cdd:PRK10590 162 LDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVhfvdkkrkrELLSQMIG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 321 KWNWltrrlveftssGSVLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLD 400
Cdd:PRK10590 242 KGNW-----------QQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 401 IPSIKTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTLLTPKDSNFAGDLVRNLEganqhvsKELLDLAM---------- 470
Cdd:PRK10590 311 IEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLK-------KEIPRIAIpgyepdpsik 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1907083232 471 ----QNAwfRKSRFKGGKGKKLNIGGGGLGYRERPGLGSENSDRGNNNN 515
Cdd:PRK10590 384 aepiQNG--RQQRGGGGRGQGGGRGQQQGQPRRGEGGAKSASAKPAEKP 430
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
91-302 |
1.05e-79 |
|
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes Drosophila melanogaster Vasa, which is essential for development. DEAD box protein 3 (DDX3) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DDX3 and DDX4 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350725 [Multi-domain] Cd Length: 221 Bit Score: 254.72 E-value: 1.05e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 91 SFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDG-----PI 165
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGrrkayPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 166 AVIVCPTRELCQQIHAECKRFgkAYN--LRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVF 243
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKF--SYRsgVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907083232 244 DEADRMFDMGFEYQVRSIASH----VRPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIG 302
Cdd:cd17967 159 DEADRMLDMGFEPQIRKIVEHpdmpPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVGRVG 221
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
27-467 |
2.78e-79 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 263.57 E-value: 2.78e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 27 IAPSKKIIDPLPPIDHSEIDyppfeKNFYNEHEEITN-LTPQQLIDLRHKLNLRVSGAAPPRPGSSFAHFGFDEQLMHQI 105
Cdd:PLN00206 62 VAKSRVAVGAPKPKRLPATD-----ECFYVRDPGSTSgLSSSQAELLRRKLEIHVKGEAVPPPILSFSSCGLPPKLLLNL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 106 RKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGD--GPIAVIVCPTRELCQQIHAEC 183
Cdd:PLN00206 137 ETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTIRSGHPSEqrNPLAMVLTPTRELCVQVEDQA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 184 KRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIAS 263
Cdd:PLN00206 217 KVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQ 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 264 HVrPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIGEANEDVTQIVEILHSGPSKwnwltRRLVEFTSSGS-----V 338
Cdd:PLN00206 297 AL-SQPQVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKK-----QKLFDILKSKQhfkppA 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 339 LLFVTKKANAEELASNL-KQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDID 417
Cdd:PLN00206 371 VVFVSSRLGADLLANAItVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIK 450
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1907083232 418 THTHRIGRTGRAGEKGVAYTLLTPKDSNFAGDLVRNLEGANQHVSKELLD 467
Cdd:PLN00206 451 EYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKSSGAAIPRELAN 500
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
67-296 |
2.67e-77 |
|
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, G17P1, or HUMP68) is involved in pathways that include the alteration of RNA structures, plays a role as a coregulator of transcription, a regulator of splicing, and in the processing of small noncoding RNAs. It synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. Dysregulation of this gene may play a role in cancer development. DDX5 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350807 [Multi-domain] Cd Length: 234 Bit Score: 248.77 E-value: 2.67e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 67 QQLIDLRHKLNLRVSGAAPPRPGSSFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIW 146
Cdd:cd18049 1 QEVEQYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 147 PMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLID 226
Cdd:cd18049 81 PAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLID 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 227 HVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 296
Cdd:cd18049 161 FLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHI 230
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
86-444 |
1.25e-76 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 255.22 E-value: 1.25e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 86 PRPGSS-FAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAF---IWPMLIHIMDQKELEPG 161
Cdd:PRK01297 82 PQEGKTrFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFlisIINQLLQTPPPKERYMG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 162 DgPIAVIVCPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEG-AEIVVCTPGRLIDHVKKKATNLQRVSY 240
Cdd:PRK01297 162 E-PRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfCDILVATPGRLLDFNQRGEVHLDMVEV 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 241 LVFDEADRMFDMGFEYQVRSIASHVRP--DRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIGEANEDVTQIVEILhSG 318
Cdd:PRK01297 241 MVLDEADRMLDMGFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAV-AG 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 319 PSKWNwLTRRLVEFTSSGSVLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARG 398
Cdd:PRK01297 320 SDKYK-LLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRG 398
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1907083232 399 LDIPSIKTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTLLTPKDS 444
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 ... |
34-302 |
2.54e-74 |
|
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DEAD-box helicases are a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350810 [Multi-domain] Cd Length: 264 Bit Score: 242.18 E-value: 2.54e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 34 IDPLPPIDHSEIdYPPFEK--NFyNEHEEItnltpqqLIDlrhklnlrVSGAAPPRPGSSFAHFGFDEQLMHQIRKSEYT 111
Cdd:cd18052 2 IPPPPPEDEDEI-FATIQTgiNF-DKYDEI-------PVE--------VTGRNPPPAILTFEEANLCETLLKNIRKAGYE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 112 QPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIM-------DQKELEPgdgPIAVIVCPTRELCQQIHAECK 184
Cdd:cd18052 65 KPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMkegltasSFSEVQE---PQALIVAPTRELANQIFLEAR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 185 RFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASH 264
Cdd:cd18052 142 KFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSE 221
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1907083232 265 V----RPDRQTLLFSATFRKKIEKLARDIL-IDPIRVVQGDIG 302
Cdd:cd18052 222 PgmpsKEDRQTLMFSATFPEEIQRLAAEFLkEDYLFLTVGRVG 264
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
92-438 |
1.72e-73 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 245.27 E-value: 1.72e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 92 FAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPG--DGPIAVIV 169
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPAPEDRkvNQPRALIM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 170 CPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRM 249
Cdd:PRK04837 90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 250 FDMGFeyqVRSIASHVR--PD---RQTLLFSATFRKKIEKLARDILIDPIRVVqgdIGEANEDVTQIVEILH--SGPSKW 322
Cdd:PRK04837 170 FDLGF---IKDIRWLFRrmPPanqRLNMLFSATLSYRVRELAFEHMNNPEYVE---VEPEQKTGHRIKEELFypSNEEKM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 323 NwLTRRLVEFTSSGSVLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIP 402
Cdd:PRK04837 244 R-LLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIP 322
|
330 340 350
....*....|....*....|....*....|....*.
gi 1907083232 403 SIKTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTL 438
Cdd:PRK04837 323 AVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
90-455 |
3.19e-73 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 250.54 E-value: 3.19e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 90 SSFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHImdQKELEpgdGPIAVIV 169
Cdd:PRK11634 6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNL--DPELK---APQILVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 170 CPTRELCQQIHAECKRFGK-AYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADR 248
Cdd:PRK11634 81 APTRELAVQVAEAMTDFSKhMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 249 MFDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV-VQGDIgEANEDVTQIVEILHsGPSKWNWLTR 327
Cdd:PRK11634 161 MLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVrIQSSV-TTRPDISQSYWTVW-GMRKNEALVR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 328 RLvEFTSSGSVLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTV 407
Cdd:PRK11634 239 FL-EAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLV 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1907083232 408 INYDVARDIDTHTHRIGRTGRAGEKGVAYTLLTPKDSNfagdLVRNLE 455
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 ... |
101-296 |
1.89e-72 |
|
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and PRP28 homolog) is involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation. Diseases associated with DDX23 include distal hereditary motor neuropathy, type II. DDX23 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350703 [Multi-domain] Cd Length: 220 Bit Score: 235.29 E-value: 1.89e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 101 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMD---QKELEPGDGPIAVIVCPTRELCQ 177
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRlppLDEETKDDGPYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 178 QIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQ 257
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083232 258 VRSIASHV-----RPD---------------RQTLLFSATFRKKIEKLARDILIDPIRV 296
Cdd:cd17945 161 VTKILDAMpvsnkKPDteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
91-435 |
7.29e-71 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 242.55 E-value: 7.29e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 91 SFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKEL---EPGDgPIAV 167
Cdd:PRK04537 10 TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALadrKPED-PRAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 168 IVCPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKK-KATNLQRVSYLVFDEA 246
Cdd:PRK04537 89 ILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQhKVVSLHACEICVLDEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 247 DRMFDMGFEYQVRSIASHV--RPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIGEANEDVTQivEILHSGPSKWNW 324
Cdd:PRK04537 169 DRMFDLGFIKDIRFLLRRMpeRGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQ--RIYFPADEEKQT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 325 LTRRLVEFTSSGSVLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSI 404
Cdd:PRK04537 247 LLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGV 326
|
330 340 350
....*....|....*....|....*....|.
gi 1907083232 405 KTVINYDVARDIDTHTHRIGRTGRAGEKGVA 435
Cdd:PRK04537 327 KYVYNYDLPFDAEDYVHRIGRTARLGEEGDA 357
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
112-296 |
3.88e-69 |
|
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts with several spliceosomal proteins and may recognize the bacterial second messengers cyclic di-GMP and cyclic di-AMP, resulting in the induction of genes involved in the innate immune response. Diseases associated with DDX41 include "myeloproliferative/lymphoproliferative neoplasms, familial" and "Ddx41-related susceptibility to familial myeloproliferative/lymphoproliferative neoplasms". DDX41 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350709 [Multi-domain] Cd Length: 206 Bit Score: 226.07 E-value: 3.88e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 112 QPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKE---LEPGDGPIAVIVCPTRELCQQIHAECKRFGK 188
Cdd:cd17951 12 KPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEKklpFIKGEGPYGLIVCPSRELARQTHEVIEYYCK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 189 AYN------LRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIA 262
Cdd:cd17951 92 ALQeggypqLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMIDMGFEEDIRTIF 171
|
170 180 190
....*....|....*....|....*....|....
gi 1907083232 263 SHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 296
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 ... |
101-297 |
8.56e-69 |
|
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: 224.65 E-value: 8.56e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 101 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKEL-EPGDGPIAVIVCPTRELCQQI 179
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPrEQRNGPGVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 180 HAECKRFgKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVR 259
Cdd:cd17958 81 EAECSKY-SYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907083232 260 SIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVV 297
Cdd:cd17958 160 KILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIVY 197
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
101-299 |
2.85e-65 |
|
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350715 [Multi-domain] Cd Length: 198 Bit Score: 215.53 E-value: 2.85e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 101 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKElepGDGPIAVIVCPTRELCQQIH 180
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRK---KKGLRALILAPTRELASQIY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 181 AECKRFGKAYNLRSVAVygGGSMWEQAKALQE---GAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQ 257
Cdd:cd17957 78 RELLKLSKGTGLRIVLL--SKSLEAKAKDGPKsitKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQ 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907083232 258 VRSI-ASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVVQG 299
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 ... |
91-296 |
1.17e-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: 1.17e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 91 SFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKElepgdGPIAVIVC 170
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQ-----RFFALVLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 171 PTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKK-KATNLQRVSYLVFDEADRM 249
Cdd:cd17954 76 PTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENtKGFSLKSLKFLVMDEADRL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907083232 250 FDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 296
Cdd:cd17954 156 LNMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
90-296 |
2.07e-63 |
|
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350717 [Multi-domain] Cd Length: 205 Bit Score: 210.62 E-value: 2.07e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 90 SSFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHImdqKELEPGDGPIAVIV 169
Cdd:cd17959 1 GGFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKL---KAHSPTVGARALIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 170 CPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRM 249
Cdd:cd17959 78 SPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907083232 250 FDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 296
Cdd:cd17959 158 FEMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
114-285 |
6.97e-63 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 207.87 E-value: 6.97e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 114 TPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKelepgDGPIAVIVCPTRELCQQIHAECKRFGKAYNLR 193
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLD-----NGPQALVLAPTRELAEQIYEELKKLGKGLGLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 194 SVAVYGGGSMWEQAKALQeGAEIVVCTPGRLIDHVKKKaTNLQRVSYLVFDEADRMFDMGFEYQVRSIASHVRPDRQTLL 273
Cdd:pfam00270 76 VASLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQER-KLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILL 153
|
170
....*....|..
gi 1907083232 274 FSATFRKKIEKL 285
Cdd:pfam00270 154 LSATLPRNLEDL 165
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
91-443 |
9.57e-59 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 204.68 E-value: 9.57e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 91 SFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLiHIMDQKELEPGdgpiAVIVC 170
Cdd:PTZ00424 29 SFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAAL-QLIDYDLNACQ----ALILA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 171 PTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMF 250
Cdd:PTZ00424 104 PTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEML 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 251 DMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIGEANEDVTQIVEILHSGPSKWNWLTRrLV 330
Cdd:PTZ00424 184 SRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCD-LY 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 331 EFTSSGSVLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINY 410
Cdd:PTZ00424 263 ETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINY 342
|
330 340 350
....*....|....*....|....*....|...
gi 1907083232 411 DVARDIDTHTHRIGRTGRAGEKGVAYTLLTPKD 443
Cdd:PTZ00424 343 DLPASPENYIHRIGRSGRFGRKGVAINFVTPDD 375
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
80-302 |
1.39e-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: 1.39e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 80 VSGAAPPRPGSSFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQ---K 156
Cdd:cd18051 11 ATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQgpgE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 157 ELEPGDG--------PIAVIVCPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHV 228
Cdd:cd18051 91 SLPSESGyygrrkqyPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDML 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083232 229 KKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIASH-VRP---DRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIG 302
Cdd:cd18051 171 ERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQdTMPptgERQTLMFSATFPKEIQMLARDFLDNYIFLAVGRVG 248
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
105-311 |
4.04e-58 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 196.17 E-value: 4.04e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 105 IRKSEYTQPTPIQCQGVPVALSG-RDMIGIAKTGSGKTAAFIWPMLIHIMdqkelePGDGPIAVIVCPTRELCQQIHAEC 183
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALK------RGKGGRVLVLVPTRELAEQWAEEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 184 KRFGKAYNLRSVAVYGGGSMWEQAKALQEG-AEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIA 262
Cdd:smart00487 75 KKLGPSLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1907083232 263 SHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDigEANEDVTQI 311
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 ... |
92-293 |
3.50e-56 |
|
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350713 [Multi-domain] Cd Length: 204 Bit Score: 190.90 E-value: 3.50e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 92 FAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLihimdQKELEPGDGPIAVIVCP 171
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPIL-----QRLSEDPYGIFALVLTP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 172 TRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVK---KKATNLQRVSYLVFDEADR 248
Cdd:cd17955 76 TRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEADR 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907083232 249 MFDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDP 293
Cdd:cd17955 156 LLTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
101-296 |
1.39e-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: 1.39e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 101 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPmlihIMDQKELEPGDGPI--AVIVCPTRELCQQ 178
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLP----ILERLLYRPKKKAAtrVLVLVPTRELAMQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 179 IHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKAT-NLQRVSYLVFDEADRMFDMGFEYQ 257
Cdd:cd17947 77 CFSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSfDLDSIEILVLDEADRMLEEGFADE 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907083232 258 VRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 296
Cdd:cd17947 157 LKEILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
308-439 |
6.04e-53 |
|
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350174 [Multi-domain] Cd Length: 131 Bit Score: 179.24 E-value: 6.04e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 308 VTQIVEILHSGpSKWNWLTRRLVEFTSSGSVLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIP 387
Cdd:cd18787 1 IKQLYVVVEEE-EKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1907083232 388 VLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTLL 439
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 ... |
101-296 |
1.40e-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: 1.40e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 101 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKelepgDGPIAVIVCPTRELCQQIH 180
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEH-----RNPSALILTPTRELAVQIE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 181 AECKRFGKAY-NLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVR 259
Cdd:cd17962 76 DQAKELMKGLpPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVL 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 1907083232 260 SIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 296
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 ... |
105-296 |
1.02e-49 |
|
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin gene, NUP98, by inversion 11 (p15q22) chromosome translocation is found in the patients with de novo or therapy-related myeloid malignancies. Diseases associated with DDX10 (also known as DDX10-NUP98 Fusion Protein Type 2) include myelodysplastic syndrome and leukemia, acute myeloid. DDX10 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350699 [Multi-domain] Cd Length: 198 Bit Score: 173.24 E-value: 1.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 105 IRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKeLEPGDGPIAVIVCPTRELCQQIHAECK 184
Cdd:cd17941 5 LKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRER-WTPEDGLGALIISPTRELAMQIFEVLR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 185 RFGKAYNLRSVAVYGGGSMWEQAKALQEgAEIVVCTPGRLIDHVKKK----ATNLQrvsYLVFDEADRMFDMGFEYQVRS 260
Cdd:cd17941 84 KVGKYHSFSAGLIIGGKDVKEEKERINR-MNILVCTPGRLLQHMDETpgfdTSNLQ---MLVLDEADRILDMGFKETLDA 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907083232 261 IASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 296
Cdd:cd17941 160 IVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYI 195
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
97-290 |
8.40e-49 |
|
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: 8.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 97 FDEQLMHQIRKSEYTQPTPIQCQGVPVALS-GRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTREL 175
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGVSALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 176 CQQIHAECKR---FGKAYNLRSvaVYGGGSMWEQAKALQ-EGAEIVVCTPGRLIDHVK--KKATNLQRVSYLVFDEADRM 249
Cdd:cd17964 81 ALQIAAEAKKllqGLRKLRVQS--AVGGTSRRAELNRLRrGRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907083232 250 FDMGFEYQVRSIASHVRP----DRQTLLFSATFRKKIEKLARDIL 290
Cdd:cd17964 159 LDMGFRPDLEQILRHLPEknadPRQTLLFSATVPDEVQQIARLTL 203
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
107-297 |
4.65e-48 |
|
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1. DDX31 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350707 [Multi-domain] Cd Length: 214 Bit Score: 168.92 E-value: 4.65e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 107 KSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIM-DQKELEPGDGPIAVIVCPTRELCQQIHAECKR 185
Cdd:cd17949 8 KMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLsLEPRVDRSDGTLALVLVPTRELALQIYEVLEK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 186 FGK-AYNLRSVAVYGGgsmwEQAKA----LQEGAEIVVCTPGRLIDHVKK-KATNLQRVSYLVFDEADRMFDMGFEYQVR 259
Cdd:cd17949 88 LLKpFHWIVPGYLIGG----EKRKSekarLRKGVNILIATPGRLLDHLKNtQSFDVSNLRWLVLDEADRLLDMGFEKDIT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1907083232 260 SIASHVR-------------PDRQTLLFSATFRKKIEKLARDILIDPIRVV 297
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, ... |
105-297 |
9.71e-47 |
|
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350718 [Multi-domain] Cd Length: 202 Bit Score: 165.06 E-value: 9.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 105 IRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDGPIAVIVCPTRELCQQIHAECK 184
Cdd:cd17960 5 VAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKKGQVGALIISPTRELATQIYEVLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 185 RFGKAY--NLRSVAVYGGGSMWEQ-AKALQEGAEIVVCTPGRLIDHVKKKAT--NLQRVSYLVFDEADRMFDMGFEYQVR 259
Cdd:cd17960 85 SFLEHHlpKLKCQLLIGGTNVEEDvKKFKRNGPNILVGTPGRLEELLSRKADkvKVKSLEVLVLDEADRLLDLGFEADLN 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907083232 260 SIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVV 297
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 ... |
98-294 |
1.25e-46 |
|
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of infectious West Nile virus particles. New research suggests that DDX56 relocalizes to the site of virus assembly during WNV infection and that its interaction with WNV capsid in the cytoplasm may occur transiently during virion morphogenesis. DDX56 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350719 [Multi-domain] Cd Length: 206 Bit Score: 164.68 E-value: 1.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 98 DEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGD-GPIAVIVCPTRELC 176
Cdd:cd17961 2 DPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGEEqGTRALILVPTRELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 177 QQIHAE-------CKRFgkaynLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKAT-NLQRVSYLVFDEADR 248
Cdd:cd17961 82 QQVSKVleqltayCRKD-----VRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLlLLSTLKYLVIDEADL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907083232 249 MFDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPI 294
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 ... |
92-296 |
1.51e-45 |
|
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or p54) participates in mRNA regulation mediated by miRNA-mediated silencing. It also plays a role in global and transcript-specific messenger RNA (mRNA) storage, translational repression, and decay. It is a member of the DEAD-box helicase family, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350698 [Multi-domain] Cd Length: 201 Bit Score: 161.70 E-value: 1.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 92 FAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHImDQKElepgDGPIAVIVCP 171
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKI-DPKK----DVIQALILVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 172 TRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFD 251
Cdd:cd17940 76 TRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907083232 252 MGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 296
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 ... |
101-278 |
1.83e-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: 1.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 101 LMHQIRKSEYTQPTPIQCQGVPVALS-GRDMIGIAKTGSGKTAAFIWPMLIHIMDQKE----LEPGDGPIAVIVCPTREL 175
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLLSQKSsngvGGKQKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 176 CQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKK---ATNLQRVSYLVFDEADRMFDM 252
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGnehLANLKSLRFLVLDEADRMLEK 160
|
170 180 190
....*....|....*....|....*....|....
gi 1907083232 253 G-FEyQVRSIASHV-------RPDRQTLLFSATF 278
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 ... |
102-287 |
5.00e-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: 5.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 102 MHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPmLIHIMDQKELEPGDGPIAVIVCPTRELCQQIHA 181
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIP-AIELLYKLKFKPRNGTGVIIISPTRELALQIYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 182 ECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKA----TNLQrvsYLVFDEADRMFDMGFEYQ 257
Cdd:cd17942 81 VAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKgflyKNLQ---CLIIDEADRILEIGFEEE 157
|
170 180 190
....*....|....*....|....*....|
gi 1907083232 258 VRSIASHVRPDRQTLLFSATFRKKIEKLAR 287
Cdd:cd17942 158 MRQIIKLLPKRRQTMLFSATQTRKVEDLAR 187
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
98-294 |
6.63e-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: 6.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 98 DEQLMHQIRKSEYTQPTPIQCQGVPVALSG--RDMIGIAKTGSGKTAAFIWPMLIHImDQKELEPGdgpiAVIVCPTREL 175
Cdd:cd17963 2 KPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRV-DPTLKSPQ----ALCLAPTREL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 176 CQQIHAECKRFGK------AYNLRSVAVYGGGSMWEQakalqegaeIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRM 249
Cdd:cd17963 77 ARQIGEVVEKMGKftgvkvALAVPGNDVPRGKKITAQ---------IVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVM 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907083232 250 FDM-GFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPI 294
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 ... |
89-296 |
1.02e-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: 1.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 89 GSSFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLihimdqKELEPGDGPIAVI 168
Cdd:cd17950 1 SSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTL------QQLEPVDGQVSVL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 169 V-CPTRELCQQIHAECKRFGKaY--NLRSVAVYGGGSMWEQAKALQ-EGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFD 244
Cdd:cd17950 75 ViCHTRELAFQISNEYERFSK-YmpNVKTAVFFGGVPIKKDIEVLKnKCPHIVVGTPGRILALVREKKLKLSHVKHFVLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907083232 245 EADRMF-DMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 296
Cdd:cd17950 154 ECDKMLeQLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEI 206
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
96-296 |
3.24e-37 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation factor-4A (eIF4A) family consists of 3 proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA. EIF4A proteins are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350697 [Multi-domain] Cd Length: 199 Bit Score: 138.23 E-value: 3.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 96 GFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHI-MDQKELEpgdgpiAVIVCPTRE 174
Cdd:cd17939 3 GLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIdTTVRETQ------ALVLAPTRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 175 LCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGF 254
Cdd:cd17939 77 LAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907083232 255 EYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRV 296
Cdd:cd17939 157 KDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
101-300 |
1.78e-33 |
|
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350706 [Multi-domain] Cd Length: 231 Bit Score: 128.64 E-value: 1.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 101 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPG--DGPIAVIVCPTRELCQQ 178
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGpfNAPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 179 IHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQV 258
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083232 259 RSIASH-----VRPDR--------QTLLFSATFRKKIEKLARDIL-IDPIRVVQGD 300
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 ... |
92-296 |
2.69e-33 |
|
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350696 [Multi-domain] Cd Length: 204 Bit Score: 127.05 E-value: 2.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 92 FAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMdqkelepgdgpiAVIVCP 171
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIVV------------ALILEP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 172 TRELCQQIHAECKRFgKAY----NLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEAD 247
Cdd:cd17938 69 SRELAEQTYNCIENF-KKYldnpKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEAD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083232 248 RMFDMGFEYQVRSIASH-----VRPDR-QTLLFSATFRK-KIEKLARDILIDPIRV 296
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 ... |
92-297 |
3.31e-33 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation factor 4A-I (DDX2A) and eukaryotic initiation factor 4A-II (DDX2B) are involved in cap recognition and are required for mRNA binding to ribosome. They are DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350804 [Multi-domain] Cd Length: 201 Bit Score: 126.79 E-value: 3.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 92 FAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIwpmlIHIMDQKELEPgDGPIAVIVCP 171
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFS----ISILQQIDTSL-KATQALVLAP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 172 TRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFD 251
Cdd:cd18046 76 TRELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907083232 252 MGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVV 297
Cdd:cd18046 156 RGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRIL 201
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
320-430 |
7.66e-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: 119.62 E-value: 7.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 320 SKWNWLtRRLVEFTSSGSVLLFV--TKKANAEELasnLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAAR 397
Cdd:pfam00271 1 EKLEAL-LELLKKERGGKVLIFSqtKKTLEAELL---LEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAER 76
|
90 100 110
....*....|....*....|....*....|...
gi 1907083232 398 GLDIPSIKTVINYDVARDIDTHTHRIGRTGRAG 430
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, ... |
101-287 |
2.01e-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: 2.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 101 LMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLiHIMDqkeLEPGdGPIAVIVCPTRELCQQIH 180
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIAL-ESLD---LERR-HPQVLILAPTREIAVQIH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 181 AECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRS 260
Cdd:cd17943 76 DVFKKIGKKLEGLKCEVFIGGTPVKEDKKKLKGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNW 155
|
170 180
....*....|....*....|....*...
gi 1907083232 261 IASHVRPDRQTLLFSATFRKK-IEKLAR 287
Cdd:cd17943 156 IFSSLPKNKQVIAFSATYPKNlDNLLAR 183
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
101-287 |
6.44e-31 |
|
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350714 [Multi-domain] Cd Length: 231 Bit Score: 121.20 E-value: 6.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 101 LMHQIRKSEYTQPTPIQCQGVPVALSG---------RDMIGIAKTGSGKTAAFIWPMLihimdQKeLEPGDGPI--AVIV 169
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIV-----QA-LSKRVVPRlrALIV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 170 CPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEG--------AEIVVCTPGRLIDHVKKKAT-NLQRVSY 240
Cdd:cd17956 75 VPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRLVDHLNSTPGfTLKHLRF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907083232 241 LVFDEADRMFDMGFEY---QV-RSIASHVRPDR----------------QTLLFSATFRKKIEKLAR 287
Cdd:cd17956 155 LVIDEADRLLNQSFQDwleTVmKALGRPTAPDLgsfgdanllersvrplQKLLFSATLTRDPEKLSS 221
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
92-297 |
6.48e-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: 6.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 92 FAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLiHIMDQKELEPGdgpiAVIVCP 171
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVL-QCLDIQVRETQ----ALILSP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 172 TRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFD 251
Cdd:cd18045 76 TRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907083232 252 MGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVV 297
Cdd:cd18045 156 KGFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRIL 201
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
115-277 |
1.03e-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: 119.57 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 115 PIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIM-DQKELEPGDGPIAVIVCPTRELCQQIHAECKRFGKayNLR 193
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQeDQQPRKRGRAPKVLVLAPTRELANQVTKDFKDITR--KLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 194 SVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFEYQVRSIAS-----HVRPD 268
Cdd:cd17944 93 VACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSvsykkDSEDN 172
|
....*....
gi 1907083232 269 RQTLLFSAT 277
Cdd:cd17944 173 PQTLLFSAT 181
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
349-430 |
6.84e-29 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 109.99 E-value: 6.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 349 EELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRIGRTGR 428
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 1907083232 429 AG 430
Cdd:smart00490 81 AG 82
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
127-425 |
5.19e-26 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 113.20 E-value: 5.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 127 GRDMIGIAKTGSGKTAafiwpMLIHIMDQKelepGDGPIAVIVCPTRELCQQIHAECKRFgkaynLRSVAVYGGgsmweq 206
Cdd:COG1061 100 GGRGLVVAPTGTGKTV-----LALALAAEL----LRGKRVLVLVPRRELLEQWAEELRRF-----LGDPLAGGG------ 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 207 akALQEGAEIVVCTPGRLIDHVKKKATNlQRVSYLVFDEADRMFDMGFeyqvRSIASHVRPDRqTLLFSAT--------- 277
Cdd:COG1061 160 --KKDSDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHHAGAPSY----RRILEAFPAAY-RLGLTATpfrsdgrei 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 278 ---------FRKKIEKLARDILIDPIRVV---------QGDIGEANEDVTQivEILHSGPSKWNWLTRRLVEFTSSGSVL 339
Cdd:COG1061 232 llflfdgivYEYSLKEAIEDGYLAPPEYYgirvdltdeRAEYDALSERLRE--ALAADAERKDKILRELLREHPDDRKTL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 340 LFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVInydVARDIDTH 419
Cdd:COG1061 310 VFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI---LLRPTGSP 386
|
....*....
gi 1907083232 420 TH---RIGR 425
Cdd:COG1061 387 REfiqRLGR 395
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
108-297 |
4.16e-21 |
|
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 (MRH4) plays an essential role during the late stages of mitochondrial ribosome or mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions. MRH4 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350723 [Multi-domain] Cd Length: 251 Bit Score: 93.21 E-value: 4.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 108 SEYTQPTPIQCQGVPvALSGRDMIGI-----------------AKTGSGKTAAFIWPMLIHIMDQKELEPGDG------- 163
Cdd:cd17965 26 DEEIKPSPIQTLAIK-KLLKTLMRKVtkqtsneepklevfllaAETGSGKTLAYLAPLLDYLKRQEQEPFEEAeeeyesa 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 164 -----PIAVIVCPTRELCQQIHAECKRFGKA--YNLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQ 236
Cdd:cd17965 105 kdtgrPRSVILVPTHELVEQVYSVLKKLSHTvkLGIKTFSSGFGPSYQRLQLAFKGRIDILVTTPGKLASLAKSRPKILS 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907083232 237 RVSYLVFDEADRMFDMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDPIRVV 297
Cdd:cd17965 185 RVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLRKLFPDVVRIA 245
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
77-293 |
1.64e-18 |
|
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH) is a testis-specific protein essential for completion of spermatogenesis. DDX25 is also a novel negative regulator of IFN pathway and facilitates RNA virus infection. Diseases associated with DDX25 include hydrolethalus syndrome, an autosomal recessive lethal malformation syndrome characterized by multiple developmental defects of fetus.. DDX25 (also called gonadotropin-regulated testicular RNA helicase) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350806 [Multi-domain] Cd Length: 229 Bit Score: 85.46 E-value: 1.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 77 NLRVSGAAPPRP---GSSFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSG--RDMIGIAKTGSGKTAAFIWPMLIH 151
Cdd:cd18048 2 RVEVLQRDPTSPlfsVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 152 ImDQKELEPGdgpiAVIVCPTRELCQQIHAECKRFGKAYNLRSV--AVYGGgsmwEQAKALQEGAEIVVCTPGRLIDHV- 228
Cdd:cd18048 82 V-DALKLYPQ----CLCLSPTFELALQTGKVVEEMGKFCVGIQViyAIRGN----RPGKGTDIEAQIVIGTPGTVLDWCf 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083232 229 KKKATNLQRVSYLVFDEADRMFDM-GFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDP 293
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 ... |
91-293 |
1.74e-17 |
|
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both mRNA (mRNA) export from the nucleus into the cytoplasm and in mRNA translation. DDX19 functions in the nucleus in resolving RNA:DNA hybrids (R-loops). Activation of a DNA damage response pathway dependent upon the ATR kinase, a major regulator of replication fork progression, stimulates translocation of DDX19 from the cytoplasm into the nucleus. Only nuclear Ddx19 is competent to resolve R-loops. DDX19 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350805 [Multi-domain] Cd Length: 205 Bit Score: 81.69 E-value: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 91 SFAHFGFDEQLMHQIRKSEYTQPTPIQCQGVPVALSG--RDMIGIAKTGSGKTAAFIWPMLIHImdqkelEPG-DGPIAV 167
Cdd:cd18047 2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV------EPAnKYPQCL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 168 IVCPTRELCQQIHAECKRFGKAYNLRSVAVYGGGSMWEQAKALQEgaEIVVCTPGRLIDH-VKKKATNLQRVSYLVFDEA 246
Cdd:cd18047 76 CLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISE--QIVIGTPGTVLDWcSKLKFIDPKKIKVFVLDEA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907083232 247 DRMF-DMGFEYQVRSIASHVRPDRQTLLFSATFRKKIEKLARDILIDP 293
Cdd:cd18047 154 DVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
125-436 |
1.12e-16 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 83.79 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 125 LSGRDMIGIAKTGSGKTA-AFIWpMLIHIMDqkelepgdGPIAVIVCPTRELCQQIHAECKRFGKAYNLRSVAVYGGgsm 203
Cdd:COG1204 36 LEGKNLVVSAPTASGKTLiAELA-ILKALLN--------GGKALYIVPLRALASEKYREFKRDFEELGIKVGVSTGD--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 204 WEQAKALQEGAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEA------DRmfdmGFEYQVrsIASHVR---PDRQTLLF 274
Cdd:COG1204 104 YDSDDEWLGRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAhliddeSR----GPTLEV--LLARLRrlnPEAQIVAL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 275 SATFrKKIEKLAR----DILIDPIRVVQGDIGEANEDVTQIVEILHSGPSKWNWLTRRLVEftSSGSVLLFVTKKANAEE 350
Cdd:COG1204 178 SATI-GNAEEIAEwldaELVKSDWRPVPLNEGVLYDGVLRFDDGSRRSKDPTLALALDLLE--EGGQVLVFVSSRRDAES 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 351 LASNLKQE------GHNLGLL-------------------------------HGDMDQSERNKVISDFKKKDIPVLVATD 393
Cdd:COG1204 255 LAKKLADElkrrltPEEREELeelaeellevseethtnekladclekgvafhHAGLPSELRRLVEDAFREGLIKVLVATP 334
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1907083232 394 VAARGLDIPSiKTVINYDVAR----DIDTHTHR--IGRTGRAG--EKGVAY 436
Cdd:COG1204 335 TLAAGVNLPA-RRVIIRDTKRggmvPIPVLEFKqmAGRAGRPGydPYGEAI 384
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
313-444 |
5.69e-14 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 75.54 E-value: 5.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 313 EILHSGPSKwnwlTRRLVEFT----SSGSVLLFVTKKANAEELASNLKQEGHNLGLLHGD--------MDQSERNKVISD 380
Cdd:COG1111 331 DIEHPKLSK----LREILKEQlgtnPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQaskegdkgLTQKEQIEILER 406
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083232 381 FKKKDIPVLVATDVAARGLDIPSIKTVINYD-VA---RDIdthtHRIGRTGRAGEKGVaYTLLTpKDS 444
Cdd:COG1111 407 FRAGEFNVLVATSVAEEGLDIPEVDLVIFYEpVPseiRSI----QRKGRTGRKREGRV-VVLIA-KGT 468
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
321-443 |
1.03e-11 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 67.86 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 321 KWNWLTRRLVEFTSsGSVLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATdVA-ARGL 399
Cdd:COG0514 217 KLAQLLDFLKEHPG-GSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGI 294
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1907083232 400 DIPSIKTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTLLTPKD 443
Cdd:COG0514 295 DKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPED 338
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
134-432 |
1.38e-11 |
|
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
Pssm-ID: 187770 [Multi-domain] Cd Length: 353 Bit Score: 66.68 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 134 AKTGSGKT-AAFIWpmLIHIMDQKELEPGdgpiaVIVCPTRELCQQIHAECKR-FGKAYNLRSVAVYGGGSMWEQAKALQ 211
Cdd:cd09639 6 APTGYGKTeAALLW--ALHSLKSQKADRV-----IIALPTRATINAMYRRAKEaFGETGLYHSSILSSRIKEMGDSEEFE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 212 E-------------GAEIVVCTP-------GRLIDHVKKKATNLQRvSYLVFDEADRMFD---MGFEYQVRSIAshvRPD 268
Cdd:cd09639 79 HlfplyihsndtlfLDPITVCTIdqvlksvFGEFGHYEFTLASIAN-SLLIFDEVHFYDEytlALILAVLEVLK---DND 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 269 RQTLLFSATFRKKIEKLARDILIDpirvvqgdigEANE-------DVTQIVEILHSGPSKWNWLTRRLVEFTSSGSVLLF 341
Cdd:cd09639 155 VPILLMSATLPKFLKEYAEKIGYV----------EENEpldlkpnERAPFIKIESDKVGEISSLERLLEFIKKGGSVAII 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 342 VTKKANAEELASNLKQEGH--NLGLLHGDMDQSERNK----VISDFKKKDIPVLVATDVAARGLDIPSikTVINYDVArD 415
Cdd:cd09639 225 VNTVDRAQEFYQQLKEKGPeeEIMLIHSRFTEKDRAKkeaeLLLEFKKSEKFVIVATQVIEASLDISV--DVMITELA-P 301
|
330
....*....|....*..
gi 1907083232 416 IDTHTHRIGRTGRAGEK 432
Cdd:cd09639 302 IDSLIQRLGRLHRYGEK 318
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
129-426 |
1.83e-11 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 67.56 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 129 DMigiaktGSGKTA---AFIwpmlihimdQKELEPGDGPIAVIVCPTReLCQQIHAECKRFgkAYNLRSVAVYGGGSMWE 205
Cdd:COG0553 268 DM------GLGKTIqalALL---------LELKERGLARPVLIVAPTS-LVGNWQRELAKF--APGLRVLVLDGTRERAK 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 206 QAKALQEgAEIVVCTpgrlIDHVKKKATNLQRV--SYLVFDEADRMFDMG-FEYQ-VRSIASHVR--------------- 266
Cdd:COG0553 330 GANPFED-ADLVITS----YGLLRRDIELLAAVdwDLVILDEAQHIKNPAtKRAKaVRALKARHRlaltgtpvenrleel 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 267 ------------PDRQTllFSATFRKKIEK--------LAR------------DILID-PIRVVQ--------------- 298
Cdd:COG0553 405 wslldflnpgllGSLKA--FRERFARPIEKgdeealerLRRllrpfllrrtkeDVLKDlPEKTEEtlyveltpeqralye 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 299 -------GDIGEANEDVTQIV----------------------EILHSGPSKWNWLTRRLVEFTSSG-SVLLFVTKKANA 348
Cdd:COG0553 483 avleylrRELEGAEGIRRRGLilaaltrlrqicshpallleegAELSGRSAKLEALLELLEELLAEGeKVLVFSQFTDTL 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 349 EELASNLKQEGHNLGLLHGDMDQSERNKVISDFK-KKDIPV-LVATDVAARGLDIPSIKTVINYD-----------VARd 415
Cdd:COG0553 563 DLLEERLEERGIEYAYLHGGTSAEERDELVDRFQeGPEAPVfLISLKAGGEGLNLTAADHVIHYDlwwnpaveeqaIDR- 641
|
410
....*....|.
gi 1907083232 416 idthTHRIGRT 426
Cdd:COG0553 642 ----AHRIGQT 648
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
134-277 |
3.28e-11 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 61.65 E-value: 3.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 134 AKTGSGKT-AAFIWpmLIHIMDQKelepgdGPIAVIVCPTRELCQQIHAECKRFGKaYNLRSVAVYGGGSMWEQAKALQE 212
Cdd:cd00046 8 APTGSGKTlAALLA--ALLLLLKK------GKKVLVLVPTKALALQTAERLRELFG-PGIRVAVLVGGSSAEEREKNKLG 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083232 213 GAEIVVCTPGRLIDHVK-KKATNLQRVSYLVFDEADRM-FDMGFEYQVR-SIASHVRPDRQTLLFSAT 277
Cdd:cd00046 79 DADIIIATPDMLLNLLLrEDRLFLKDLKLIIVDEAHALlIDSRGALILDlAVRKAGLKNAQVILLSAT 146
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
136-445 |
6.90e-11 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 65.49 E-value: 6.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 136 TGSGKT-AAFIWpMLIHimdqkeLEPGDGPIAVIVCPTRELCQQIHaecKRFGKAYNLrSVAVYGGGSMWEQAKALQEG- 213
Cdd:COG1203 156 TGGGKTeAALLF-ALRL------AAKHGGRRIIYALPFTSIINQTY---DRLRDLFGE-DVLLHHSLADLDLLEEEEEYe 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 214 --------------AEIVVCTPGRLIDHV-------KKKATNLQRvSYLVFDEADrMFDMgfEYQ---VRSIASHVRPDR 269
Cdd:COG1203 225 searwlkllkelwdAPVVVTTIDQLFESLfsnrkgqERRLHNLAN-SVIILDEVQ-AYPP--YMLallLRLLEWLKNLGG 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 270 QTLLFSATFRKKIeklaRDILIDPIRVVQGDIGEANEDVTQIVE---ILHSGPSKWNWLTRRLVE-FTSSGSVLLFVTKK 345
Cdd:COG1203 301 SVILMTATLPPLL----REELLEAYELIPDEPEELPEYFRAFVRkrvELKEGPLSDEELAELILEaLHKGKSVLVIVNTV 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 346 ANAEELASNLKQEGHNLG--LLHGDMDQSERNKVISD----FKKKDIPVLVATDVAARGLDipsiktvINYDVA-RD--- 415
Cdd:COG1203 377 KDAQELYEALKEKLPDEEvyLLHSRFCPADRSEIEKEikerLERGKPCILVSTQVVEAGVD-------IDFDVViRDlap 449
|
330 340 350
....*....|....*....|....*....|...
gi 1907083232 416 IDTHTHRIGRT---GRAGEKGVAYtLLTPKDSN 445
Cdd:COG1203 450 LDSLIQRAGRCnrhGRKEEEGNVY-VFDPEDEG 481
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
134-432 |
7.04e-11 |
|
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.
Pssm-ID: 273707 [Multi-domain] Cd Length: 359 Bit Score: 64.78 E-value: 7.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 134 AKTGSGKT-AAFIWpmLIHIMDQKELEPGdgpiaVIVCPTRELCQQIHaecKRFGKAYNLRSVAVYGGGSMWEQAKALQE 212
Cdd:TIGR01587 6 APTGYGKTeAALLW--ALHSIKSQKADRV-----IIALPTRATINAMY---RRAKELFGSELVGLHHSSSFSRIKEMGDS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 213 GA------------------EIVVCTP-------GRLIDHVKKKATNLQRvSYLVFDEADRMFD---MGFEYQVRSIAsh 264
Cdd:TIGR01587 76 EEfehlfplyihsndklfldPITVCTIdqvlksvFGEFGHYEFTLASIAN-SLLIFDEVHFYDEytlALILAVLEVLK-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 265 vRPDRQTLLFSATFRKKIEKLARDILIDPIRVVQGDIGEANEDVTQIVEILHSGPSKWNWLTRRLVEFTSSGSVLLFVTK 344
Cdd:TIGR01587 153 -DNDVPILLMSATLPKFLKEYAEKIGYVEFNEPLDLKEERRFENHRFILIESDKVGEISSLERLLEFIKKGGSIAIIVNT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 345 KANAEELASNLKQEGHNLG--LLHGDMDQSERNK----VISDFKKKDIP-VLVATDVAARGLDIPSikTVINYDVArDID 417
Cdd:TIGR01587 232 VDRAQEFYQQLKEKAPEEEiiLYHSRFTEKDRAKkeaeLLREMKKSNEKfVIVATQVIEASLDISA--DVMITELA-PID 308
|
330
....*....|....*
gi 1907083232 418 THTHRIGRTGRAGEK 432
Cdd:TIGR01587 309 SLIQRLGRLHRYGRK 323
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
136-246 |
1.47e-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: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 136 TGSGKTaaFIWPMLIHIM-DQKELEPGDGPIAVIVCPTRELCQQihaECKRFGKAYNLRSVAVYG--GGSMWEQAKALQE 212
Cdd:cd18034 25 TGSGKT--LIAVMLIKEMgELNRKEKNPKKRAVFLVPTVPLVAQ---QAEAIRSHTDLKVGEYSGemGVDKWTKERWKEE 99
|
90 100 110
....*....|....*....|....*....|....*.
gi 1907083232 213 --GAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEA 246
Cdd:cd18034 100 leKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
312-424 |
5.35e-10 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 57.87 E-value: 5.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 312 VEILHSGpsKWNWLTRRLVEFTSSGS-VLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKK-KDIPV- 388
Cdd:cd18793 5 IEEVVSG--KLEALLELLEELREPGEkVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEdPDIRVf 82
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1907083232 389 LVATDVAARGLDIPSIKTVINYDV----ARD---IDtHTHRIG 424
Cdd:cd18793 83 LLSTKAGGVGLNLTAANRVILYDPwwnpAVEeqaID-RAHRIG 124
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
114-246 |
5.86e-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: 5.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 114 TPIQCQGV-PVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQkelepgdGPIAVIVCPTRELCQQIHAECKRFGKAYNL 192
Cdd:cd17921 3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRALATS-------GGKAVYIAPTRALVNQKEADLRERFGPLGK 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083232 193 RSVAVYGGGSMweqAKALQEGAEIVVCTP----GRLIDHvkkKATNLQRVSYLVFDEA 246
Cdd:cd17921 76 NVGLLTGDPSV---NKLLLAEADILVATPekldLLLRNG---GERLIQDVRLVVVDEA 127
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
85-439 |
7.38e-10 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 62.55 E-value: 7.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 85 PPRPGSsFAHF--GFDEQLMHQIRKSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDqkelepGD 162
Cdd:COG1205 28 PAREAR-YAPWpdWLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLE------DP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 163 GPIAVIVCPTRELCQQIHAECKRFGKAYNLR-SVAVYGGGSMWEQAKALQEGAEIVVCTP-----GrLIDHVKKKATNLQ 236
Cdd:COG1205 101 GATALYLYPTKALARDQLRRLRELAEALGLGvRVATYDGDTPPEERRWIREHPDIVLTNPdmlhyG-LLPHHTRWARFFR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 237 RVSYLVFDEA---------------DRMfdmgfeyqvRSIASHVRPDRQTLLFSATfrkkI---EKLARDILIDPIRVVQ 298
Cdd:COG1205 180 NLRYVVIDEAhtyrgvfgshvanvlRRL---------RRICRHYGSDPQFILASAT----IgnpAEHAERLTGRPVTVVD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 299 GDiGEAnedvTQIVEILHSGPSKWNWLTRR---------LVEFTSSG-SVLLFVTKKANAEELASNLKQEGHNLGLL--- 365
Cdd:COG1205 247 ED-GSP----RGERTFVLWNPPLVDDGIRRsalaeaarlLADLVREGlRTLVFTRSRRGAELLARYARRALREPDLAdrv 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907083232 366 ---HGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTLL 439
Cdd:COG1205 322 aayRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVLVA 398
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
345-470 |
1.08e-09 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 61.65 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 345 KANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRIG 424
Cdd:PRK11057 246 RAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETG 325
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1907083232 425 RTGRAGEKGVAYTLLTPKDSNFagdLVRNLE----GANQHVSKELLDlAM 470
Cdd:PRK11057 326 RAGRDGLPAEAMLFYDPADMAW---LRRCLEekpaGQQQDIERHKLN-AM 371
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
369-439 |
1.22e-09 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350188 [Multi-domain] Cd Length: 143 Bit Score: 57.37 E-value: 1.22e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907083232 369 MDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYD-VARDIDThTHRIGRTGRaGEKGVAYTLL 439
Cdd:cd18801 74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDaSPSPIRM-IQRMGRTGR-KRQGRVVVLL 143
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
325-428 |
1.34e-09 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 57.27 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 325 LTRRLVEFTSSGSVLLFVTKKANAEELASNLKQ------EGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARG 398
Cdd:cd18796 28 YAEVIFLLERHKSTLVFTNTRSQAERLAQRLRElcpdrvPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELG 107
|
90 100 110
....*....|....*....|....*....|
gi 1907083232 399 LDIPSIKTVINYDVARDIDTHTHRIGRTGR 428
Cdd:cd18796 108 IDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
347-441 |
2.69e-09 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350179 [Multi-domain] Cd Length: 160 Bit Score: 56.51 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 347 NAEELASNLKQE--GHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRI- 423
Cdd:cd18792 46 SIEALAEELKELvpEARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFGLSQLHQLr 125
|
90
....*....|....*...
gi 1907083232 424 GRTGRAGEKGVAYtLLTP 441
Cdd:cd18792 126 GRVGRGKHQSYCY-LLYP 142
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
331-455 |
4.79e-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: 55.81 E-value: 4.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 331 EFTSSGSVLLFVTKKANAEELASNLKQ--EGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVI 408
Cdd:cd18810 21 ELLRGGQVFYVHNRIESIEKLATQLRQlvPEARIAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTII 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1907083232 409 --NYDVARDIDTHTHRiGRTGRAGEKGVAYtLLTPKDSNFAGDLVRNLE 455
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 ... |
388-440 |
1.43e-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: 1.43e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1907083232 388 VLVATDVAARGLDIPSIKTVINYDVARDIDTHTHRIGRTGRAGEKGVAYTLLT 440
Cdd:cd18785 25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILFV 77
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
344-456 |
1.59e-08 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 54.27 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 344 KKANA--EELASNLKQEgHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDTHTH 421
Cdd:cd18811 45 KAAVAmyEYLKERFRPE-LNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLH 123
|
90 100 110
....*....|....*....|....*....|....*.
gi 1907083232 422 RI-GRTGRAGEKGVAYTLLTPKDSNFAGDLVRNLEG 456
Cdd:cd18811 124 QLrGRVGRGDHQSYCLLVYKDPLTETAKQRLRVMTE 159
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
327-431 |
1.87e-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: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 327 RRLVEFTSSGSVLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKT 406
Cdd:cd18794 22 KRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRF 101
|
90 100
....*....|....*....|....*
gi 1907083232 407 VINYDVARDIDTHTHRIGRTGRAGE 431
Cdd:cd18794 102 VIHYSLPKSMESYYQESGRAGRDGL 126
|
|
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
346-408 |
4.08e-08 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 56.60 E-value: 4.08e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907083232 346 ANAEELASNLKQE--GHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATdvaargldipsikTVI 408
Cdd:COG1200 488 QAAEETYEELREAfpGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVAT-------------TVI 539
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
339-440 |
4.18e-08 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350189 [Multi-domain] Cd Length: 142 Bit Score: 52.59 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 339 LLFVTKKANAEELASNLKQEGHNLGLLHGD---------------MDQSERNKVISDFKKKDIPVLVATDVAARGLDIPS 403
Cdd:cd18802 29 IIFVERRATAVVLSRLLKEHPSTLAFIRCGfligrgnssqrkrslMTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPA 108
|
90 100 110
....*....|....*....|....*....|....*..
gi 1907083232 404 IKTVINYDVARDIdthTHRIGRTGRAGEKGVAYTLLT 440
Cdd:cd18802 109 CNLVIRFDLPKTL---RSYIQSRGRARAPNSKYILMV 142
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
369-440 |
4.62e-08 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 56.81 E-value: 4.62e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907083232 369 MDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYD-VARDIDThTHRIGRTGRaGEKGVAYTLLT 440
Cdd:PRK13766 407 MSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEpVPSEIRS-IQRKGRTGR-QEEGRVVVLIA 477
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
107-451 |
1.19e-07 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 55.49 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 107 KSEYTQPTPIQCQGVPVALSGRDMIGIAKTGSGKT-AAFIWPmLIHIMDQKELEPGDGPIAVI-VCPTRELCQQIHaeck 184
Cdd:COG1201 19 AARFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAFLPA-LDELARRPRPGELPDGLRVLyISPLKALANDIE---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 185 RfgkayNLR-----------------SVAV-YGGGSMWEQAKALQEGAEIVVCTPGRLidHV----KKKATNLQRVSYLV 242
Cdd:COG1201 94 R-----NLRapleeigeaaglplpeiRVGVrTGDTPASERQRQRRRPPHILITTPESL--ALlltsPDARELLRGVRTVI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 243 FDEadrmfdmgfeyqVRSIAS---------------HVRPDR-QTLLFSATFRkKIEKLAR----DILIDPIRVVQGDIG 302
Cdd:COG1201 167 VDE------------IHALAGskrgvhlalslerlrALAPRPlQRIGLSATVG-PLEEVARflvgYEDPRPVTIVDAGAG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 303 -----EANEDVTQIVEILHSGPSKWNWLTRRLVEF-TSSGSVLLFVTKKANAEELASNLKQ----EGHNLGLLHGDMDQS 372
Cdd:COG1201 234 kkpdlEVLVPVEDLIERFPWAGHLWPHLYPRVLDLiEAHRTTLVFTNTRSQAERLFQRLNElnpeDALPIAAHHGSLSRE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 373 ERNKVISDFKKKDIPVLVAT---DVaarGLDIPSIKTVINYD----VARDIdthtHRIGRTG-RAGEKGVAYtlLTPKDs 444
Cdd:COG1201 314 QRLEVEEALKAGELRAVVATsslEL---GIDIGDVDLVIQVGspksVARLL----QRIGRAGhRVGEVSKGR--LVPTH- 383
|
....*..
gi 1907083232 445 nfAGDLV 451
Cdd:COG1201 384 --RDELV 388
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
337-408 |
2.23e-07 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350186 [Multi-domain] Cd Length: 116 Bit Score: 49.87 E-value: 2.23e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907083232 337 SVLLFVTKKANAEELASNLKQEGHNLGLLHGD--MDQSERNKVISDFK-KKDIPVLVATDVAARGLDIPSIKTVI 408
Cdd:cd18799 8 KTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDysDRERGDEALILLFFgELKPPILVTVDLLTTGVDIPEVDNVV 82
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
331-438 |
1.12e-06 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350182 [Multi-domain] Cd Length: 154 Bit Score: 49.09 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 331 EFTSSGSVLLFVTKKANAEELASNLKqeghNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSiKTVI-- 408
Cdd:cd18795 39 TVSEGKPVLVFCSSRKECEKTAKDLA----GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPA-RTVIik 113
|
90 100 110
....*....|....*....|....*....|....*....
gi 1907083232 409 -----NYDVARDIDTHTHR--IGRTGRAG--EKGVAYTL 438
Cdd:cd18795 114 gtqryDGKGYRELSPLEYLqmIGRAGRPGfdTRGEAIIM 152
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
347-402 |
1.45e-06 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 51.69 E-value: 1.45e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083232 347 NAEELASNLKQE--GHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIP 402
Cdd:PRK10917 491 SAEETYEELQEAfpELRVGLLHGRMKPAEKDAVMAAFKAGEIDILVATTVIEVGVDVP 548
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
136-278 |
1.74e-06 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 48.07 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 136 TGSGKT---AAFIWpmliHIMDQKELepgdgpiavIVCPTRELCQQIHAECKRFGKAynlRSVAVYGGGSmweqaKALQE 212
Cdd:cd17926 27 TGSGKTltaLALIA----YLKELRTL---------IVVPTDALLDQWKERFEDFLGD---SSIGLIGGGK-----KKDFD 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083232 213 GAEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADRMFDMGFeyqvRSIASHVRPDRQtLLFSATF 278
Cdd:cd17926 86 DANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHHLPAKTF----SEILKELNAKYR-LGLTATP 146
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
113-245 |
2.15e-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: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 113 PTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIHImdQKELEPGDGPIAVIVCPTRELC-QQIHAECKRFGKAYN 191
Cdd:cd18036 3 LRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHL--EKRRSAGEKGRVVVLVNKVPLVeQQLEKFFKYFRKGYK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083232 192 LrsVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKKKATN----LQRVSYLVFDE 245
Cdd:cd18036 81 V--TGLSGDSSHKVSFGQIVKASDVIICTPQILINNLLSGREEervyLSDFSLLIFDE 136
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
339-432 |
3.47e-06 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 50.66 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 339 LLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYDVARDIDT 418
Cdd:PLN03137 684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEG 763
|
90
....*....|....
gi 1907083232 419 HTHRIGRTGRAGEK 432
Cdd:PLN03137 764 YHQECGRAGRDGQR 777
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
127-245 |
3.78e-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: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 127 GRDMIGIAKTGSGKT-AAFIWPmLIHIMDQKElepgdGPIAVI-VCPTRELCQQIHAECKRFGKAYNL-RSVAV-YGGGS 202
Cdd:cd17922 1 GRNVLIAAPTGSGKTeAAFLPA-LSSLADEPE-----KGVQVLyISPLKALINDQERRLEEPLDEIDLeIPVAVrHGDTS 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1907083232 203 MWEQAKALQEGAEIVVCTP---GRLIDHvKKKATNLQRVSYLVFDE 245
Cdd:cd17922 75 QSEKAKQLKNPPGILITTPeslELLLVN-KKLRELFAGLRYVVVDE 119
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
338-411 |
5.38e-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: 47.24 E-value: 5.38e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907083232 338 VLLFVTKKANAEELASNLKQEGHNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVINYD 411
Cdd:cd18790 30 VLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILD 103
|
|
| PRK10689 |
PRK10689 |
transcription-repair coupling factor; Provisional |
366-455 |
1.02e-05 |
|
transcription-repair coupling factor; Provisional
Pssm-ID: 182649 [Multi-domain] Cd Length: 1147 Bit Score: 49.36 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 366 HGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIKTVI-----NYDVARdidTHTHRiGRTGRAGEKGVAYtLLT 440
Cdd:PRK10689 842 HGQMRERELERVMNDFHHQRFNVLVCTTIIETGIDIPTANTIIieradHFGLAQ---LHQLR-GRVGRSHHQAYAW-LLT 916
|
90
....*....|....*
gi 1907083232 441 PKDSNFAGDLVRNLE 455
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 ... |
112-248 |
1.52e-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: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 112 QPTPIQCQGVPVALSGRDMIGIAKTGSGKTaaFIwPMLI--HIMDQKELEPGdGPIAVIVcPTRELC-QQIHAECKRFGK 188
Cdd:cd17927 2 KPRNYQLELAQPALKGKNTIICLPTGSGKT--FV-AVLIceHHLKKFPAGRK-GKVVFLA-NKVPLVeQQKEVFRKHFER 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907083232 189 AYnLRSVAVYGGGSMWEQAKALQEGAEIVVCTPGRLIDHVKK-KATNLQRVSYLVFDEADR 248
Cdd:cd17927 77 PG-YKVTGLSGDTSENVSVEQIVESSDVIIVTPQILVNDLKSgTIVSLSDFSLLVFDECHN 136
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
116-221 |
5.46e-05 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350781 [Multi-domain] Cd Length: 206 Bit Score: 45.04 E-value: 5.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 116 IQCQGVPVAL-SGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKELEPGDgPIAVIVCPTRELCQQIHAECK-RFGKaYNLR 193
Cdd:cd18023 5 IQSEVFPDLLySDKNFVVSAPTGSGKTVLFELAILRLLKERNPLPWGN-RKVVYIAPIKALCSEKYDDWKeKFGP-LGLS 82
|
90 100
....*....|....*....|....*...
gi 1907083232 194 SVAVYGGGSMWEQAKAlqEGAEIVVCTP 221
Cdd:cd18023 83 CAELTGDTEMDDTFEI--QDADIILTTP 108
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
339-445 |
5.78e-05 |
|
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350185 [Multi-domain] Cd Length: 174 Bit Score: 44.22 E-value: 5.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 339 LLFVTK---KANAEELASNLKQEGHNLGLLHgdmdqSERNKVISDFKKKDIPVLVAT----DVAARGLDIP-SIKTVINY 410
Cdd:cd18798 28 LIFVSIdygKEYAEELKEFLERHGIKAELAL-----SSTEKNLEKFEEGEIDVLIGVasyyGVLVRGIDLPeRIKYAIFY 102
|
90 100 110
....*....|....*....|....*....|....*....
gi 1907083232 411 DVArdIDTHTHRIGRTGR--AGE--KGVAYTLLTPKDSN 445
Cdd:cd18798 103 GVP--VTTYIQASGRTSRlyAGGltKGLSVVLVDDPELF 139
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
334-438 |
8.74e-05 |
|
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family members are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350178 [Multi-domain] Cd Length: 171 Bit Score: 43.68 E-value: 8.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 334 SSGSVLLFVTKKANAEELASNLKQEGHNLGL-------LHGDMDQSERNKVI---SDFKKKdipVLVATDVAARGLDIPS 403
Cdd:cd18791 42 EPGDILVFLPGQEEIERLCELLREELLSPDLgkllvlpLHSSLPPEEQQRVFeppPPGVRK---VVLATNIAETSITIPG 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1907083232 404 IKTVI--------NYDVARDIDT-HTHRIG------RTGRAG--EKGVAYTL 438
Cdd:cd18791 119 VVYVIdsglvkekVYDPRTGLSSlVTVWISkasaeqRAGRAGrtRPGKCYRL 170
|
|
| VirD4 |
COG3505 |
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ... |
133-188 |
1.47e-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: 1.47e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083232 133 IAKTGSGKTAAFIWPMLIHimdqkeLEPGDGpiAVIVCPTRELCQQIHAECKRFGK 188
Cdd:COG3505 5 IGPTGSGKTVGLVIPNLTQ------LARGES--VVVTDPKGDLAELTAGFRRRAGY 52
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
123-248 |
1.51e-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: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 123 VALSGRDMIgIAKTGSGKTAAFIWPMLihimdqKELEPGDGPIaVIVCPTRELCQQiHAEckRFGKAYNL--RSVAVYGG 200
Cdd:cd18035 13 VALNGNTLI-VLPTGLGKTIIAILVAA------DRLTKKGGKV-LILAPSRPLVEQ-HAE--NLKRVLNIpdKITSLTGE 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1907083232 201 GSMWEQAKALQEGaEIVVCTPGRLIDHVKKKATNLQRVSYLVFDEADR 248
Cdd:cd18035 82 VKPEERAERWDAS-KIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
246-430 |
1.96e-04 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 44.87 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 246 ADRMFDMGFEYQ------VRSIASHVRPDRQTLLFSATFRKKIEK---LARDILIDPIRVVQGDIGEANEDVTQIVEILH 316
Cdd:PRK01172 141 ADEIHIIGDEDRgptletVLSSARYVNPDARILALSATVSNANELaqwLNASLIKSNFRPVPLKLGILYRKRLILDGYER 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 317 SGPSKwNWLTRRLVEftSSGSVLLFVTKKANAEELASNLKQE-------------------------GHNLGLLHGDMDQ 371
Cdd:PRK01172 221 SQVDI-NSLIKETVN--DGGQVLVFVSSRKNAEDYAEMLIQHfpefndfkvssennnvyddslnemlPHGVAFHHAGLSN 297
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083232 372 SERNKVISDFKKKDIPVLVATDVAARGLDIPSiKTVINYDVARDIDTHT---------HRIGRTGRAG 430
Cdd:PRK01172 298 EQRRFIEEMFRNRYIKVIVATPTLAAGVNLPA-RLVIVRDITRYGNGGIrylsnmeikQMIGRAGRPG 364
|
|
| secA |
PRK12898 |
preprotein translocase subunit SecA; Reviewed |
320-479 |
2.22e-04 |
|
preprotein translocase subunit SecA; Reviewed
Pssm-ID: 237253 [Multi-domain] Cd Length: 656 Bit Score: 44.62 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 320 SKWNWLTRRLVEFTSSGSVLLFVTKK-ANAEELASNLKQEGHNLGLLHGDMDQSErNKVISDFKKKDiPVLVATDVAARG 398
Cdd:PRK12898 457 AKWAAVAARVRELHAQGRPVLVGTRSvAASERLSALLREAGLPHQVLNAKQDAEE-AAIVARAGQRG-RITVATNMAGRG 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 399 LDIPsiktvINYDVARD-----IDTHTHR--------IGRTGRAGEKGVAYTLLTPKD---SNFAGDLVRNLEGANQHVS 462
Cdd:PRK12898 535 TDIK-----LEPGVAARgglhvILTERHDsaridrqlAGRCGRQGDPGSYEAILSLEDdllQSFLGSRGLAIRRMELLGP 609
|
170
....*....|....*..
gi 1907083232 463 KELLDLAMQNAWFRKSR 479
Cdd:PRK12898 610 RGGRALGALLLRRAQRR 626
|
|
| dermokine |
cd21118 |
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ... |
481-726 |
5.93e-04 |
|
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.
Pssm-ID: 411053 [Multi-domain] Cd Length: 495 Bit Score: 43.06 E-value: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 481 KGGKGKKLNIGGGGLGYRERPGLGSEnsdRGNNNNVMSNYeayKPSTGAMGdrltamkaafqsqykshfvaaSLSNQKAG 560
Cdd:cd21118 168 QGGNGGPLNYGTNSQGAVAQPGYGTV---RGNNQNSGCTN---PPPSGSHE---------------------SFSNSGGS 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 561 TSSAGASGWTSAGSLNSVPTNSAQQGHNSPDNPMTSSTKNIPGFNNSGNISSAPVTYPSIGAQGVNNTASGNNSREGIGG 640
Cdd:cd21118 221 SSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSGGSNGGSSGNSGSGSGGSSSGGSNGWGGSSSSGGSGGS 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 641 GNGKRERYTENRGGSRHSHGDGGNRhgdggrhgdgyrYPESGSRHTDGHRHGEtrhggsagrhGESRGANDGRNGESRKE 720
Cdd:cd21118 301 GGGNKPECNNPGNDVRMAGGGGSQG------------SKESSGSHGSNGGNGQ----------AEAVGGLNTLNSDASTL 358
|
....*.
gi 1907083232 721 GFNREN 726
Cdd:cd21118 359 PFNFDT 364
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
338-433 |
7.14e-04 |
|
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350176 [Multi-domain] Cd Length: 153 Bit Score: 40.70 E-value: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 338 VLLFVTKKANAEELASNLkqeghNLGLLHGDMDQSERNKVISDFKKKDIPVLVATDVAARGLDIPSIktvinyDVARDID 417
Cdd:cd18789 52 IIVFTDNVEALYRYAKRL-----LKPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPEA------NVAIQIS 120
|
90 100
....*....|....*....|...
gi 1907083232 418 TH-------THRIGRTGRAGEKG 433
Cdd:cd18789 121 GHggsrrqeAQRLGRILRPKKGG 143
|
|
| DEXQc_arch_SWI2_SNF2 |
cd18012 |
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ... |
129-246 |
1.07e-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: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 129 DMigiaktGSGKTAAfiwpMLIHIMDQKElEPGDGPiAVIVCPTrELCQQIHAECKRFgkAYNLRSVAVYGGGSMWEQAK 208
Cdd:cd18012 31 DM------GLGKTLQ----TLALLLSRKE-EGRKGP-SLVVAPT-SLIYNWEEEAAKF--APELKVLVIHGTKRKREKLR 95
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1907083232 209 ALqEGAEIVVCTPG---RLIDHVKKkatnlQRVSYLVFDEA 246
Cdd:cd18012 96 AL-EDYDLVITSYGllrRDIELLKE-----VKFHYLVLDEA 130
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
136-278 |
1.15e-03 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 40.35 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 136 TGSGKTAafiwpMLIHIMDQKeLEPGDGPIAVIVCPTRELCQQIHAECKRFGKAYNLRSvAVYGGGSMweqaKALQEGAE 215
Cdd:pfam04851 32 TGSGKTL-----TAAKLIARL-FKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYVEIG-EIISGDKK----DESVDDNK 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907083232 216 IVVCTP---GRLIDHVKKKATNLQRVsYLVFDEADRMFDMGFeyqvRSIASHVRPdrQTLL-FSATF 278
Cdd:pfam04851 101 IVVTTIqslYKALELASLELLPDFFD-VIIIDEAHRSGASSY----RNILEYFKP--AFLLgLTATP 160
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
124-246 |
1.86e-03 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 39.88 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 124 ALSGRDMIGIAKTGSGKTAAFIWPMLIHIMDQKelepgdGPIAVIVCPTRELCQQIHAECKRFGKAYNLR-SVAVYGG-G 201
Cdd:cd17923 12 ARAGRSVVVTTGTASGKSLCYQLPILEALLRDP------GSRALYLYPTKALAQDQLRSLRELLEQLGLGiRVATYDGdT 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1907083232 202 SMWEQAKALQEGAEIVVCTPGRL----IDHVKKKATNLQRVSYLVFDEA 246
Cdd:cd17923 86 PREERRAIIRNPPRILLTNPDMLhyalLPHHDRWARFLRNLRYVVLDEA 134
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
115-246 |
5.05e-03 |
|
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.
Pssm-ID: 350776 [Multi-domain] Cd Length: 201 Bit Score: 39.16 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 115 PIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIhimdQKELEPGdgpIAVIVCPTRELCQ-QIHAeCKRFGKAYNLR 193
Cdd:cd18018 15 PGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALL----LRRRGPG---LTLVVSPLIALMKdQVDA-LPRAIKAAALN 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1907083232 194 SVAvyGGGSMWEQAKALQEG-AEIVVCTPGRLID-HVKKKATNLQRVSYLVFDEA 246
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 ... |
110-246 |
6.66e-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: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083232 110 YTQPTPIQCQGVPVALSGRDMIGIAKTGSGKTAAFIWPMLIhimdqkelepgDGPIAVIVCPTRELCQ-QIHaECKRFGK 188
Cdd:cd17920 10 YDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALL-----------LDGVTLVVSPLISLMQdQVD-RLQQLGI 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083232 189 aynlRSVAVYGGGSMWEQAKALQEGAE----IVVCTPGRLI-DHVKK---KATNLQRVSYLVFDEA 246
Cdd:cd17920 78 ----RAAALNSTLSPEEKREVLLRIKNgqykLLYVTPERLLsPDFLEllqRLPERKRLALIVVDEA 139
|
|
| |
