|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
269-634 |
8.33e-160 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 470.40 E-value: 8.33e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 269 TSFGHFGFDEQLIKAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMHVMDQKQlkpgDGPIGLIL 348
Cdd:COG0513 2 MSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP----RAPQALIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 349 APTRELSLQIYNEAKKFGKVYNLNVVCCYGGGSKWEQSKALEQGAEIIVATPGRMIDMVKMKATNLRRVTFLVLDEADRM 428
Cdd:COG0513 78 APTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 429 FHMGFEPQVRSICNHVRPDRQCLMFSATFKKRIERLARDVLSDPVRIVQGDLNEANQDITQSVYvFPNPLQKWNwLLCHL 508
Cdd:COG0513 158 LDMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYY-LVDKRDKLE-LLRRL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 509 VKFLSEGSVLIFVTKKVDAETVSNNLLIKEYNCLLLHGDMDQADRNKVITQFKRKECDILVATDVAARGLDIPHIRNVVN 588
Cdd:COG0513 236 LRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVIN 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 24662330 589 YDTARDIETHTHRIGRTGRAGEKGNAYTLVTDKDKefagHLVRNLE 634
Cdd:COG0513 316 YDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDER----RLLRAIE 357
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
214-670 |
2.03e-147 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 443.45 E-value: 2.03e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 214 DPLPPIYHSEIEYEPFEKNFYTQHDDIAALDDEQVRELRRTLGVK-VTGPSPPKPVTSFGHFGFDEQLIKAVRKAEYTQP 292
Cdd:PTZ00110 74 KRLQPIDWKSINLVPFEKNFYKEHPEVSALSSKEVDEIRKEKEITiIAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 293 TPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMHVMDQKQLKPGDGPIGLILAPTRELSLQIYNEAKKFGKVYNLN 372
Cdd:PTZ00110 154 TPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIR 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 373 VVCCYGGGSKWEQSKALEQGAEIIVATPGRMIDMVKMKATNLRRVTFLVLDEADRMFHMGFEPQVRSICNHVRPDRQCLM 452
Cdd:PTZ00110 234 NTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLM 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 453 FSATFKKRIERLARDVLSD-PVRIVQGDLN-EANQDITQSVYVFpNPLQKWNWLLCHLVKFLSEGS-VLIFVTKKVDAET 529
Cdd:PTZ00110 314 WSATWPKEVQSLARDLCKEePVHVNVGSLDlTACHNIKQEVFVV-EEHEKRGKLKMLLQRIMRDGDkILIFVETKKGADF 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 530 VSNNLLIKEYNCLLLHGDMDQADRNKVITQFKRKECDILVATDVAARGLDIPHIRNVVNYDTARDIETHTHRIGRTGRAG 609
Cdd:PTZ00110 393 LTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAG 472
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24662330 610 EKGNAYTLVTDKDKEFAGHLVRNLEGADQLVPDDLMELAMKSSWFRSSRFKQGKGKRPTNT 670
Cdd:PTZ00110 473 AKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSNERSNGTERRRWGGYGRFSNNV 533
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
280-476 |
2.76e-140 |
|
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor 3B-Associated 125 kDa Protein, RHELP, or RNAHP) is an NTPase with a preference for ATP, the hydrolysis of which is enhanced by various RNA substrates. It acts as a non-processive RNA helicase with protein displacement and RNA annealing activities. DDX42 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350710 [Multi-domain] Cd Length: 197 Bit Score: 411.42 E-value: 2.76e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 280 LIKAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMHVMDQKQLKPGDGPIGLILAPTRELSLQIY 359
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGEGPIAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 360 NEAKKFGKVYNLNVVCCYGGGSKWEQSKALEQGAEIIVATPGRMIDMVKMKATNLRRVTFLVLDEADRMFHMGFEPQVRS 439
Cdd:cd17952 81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 24662330 440 ICNHVRPDRQCLMFSATFKKRIERLARDVLSDPVRIV 476
Cdd:cd17952 161 IVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRVV 197
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
258-475 |
4.14e-111 |
|
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: 337.43 E-value: 4.14e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 258 KVTGPSPPKPVTSFGHFGFDEQLIKAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMHVMDQKQL 337
Cdd:cd17953 1 KVRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 338 KPGDGPIGLILAPTRELSLQIYNEAKKFGKVYNLNVVCCYGGGSKWEQSKALEQGAEIIVATPGRMIDMVKM---KATNL 414
Cdd:cd17953 81 KPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTAnngRVTNL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24662330 415 RRVTFLVLDEADRMFHMGFEPQVRSICNHVRPDRQCLMFSATFKKRIERLARDVLSDPVRI 475
Cdd:cd17953 161 RRVTYVVLDEADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
280-475 |
1.99e-98 |
|
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: 303.21 E-value: 1.99e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 280 LIKAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMHVMDQKQLKPGdGPIGLILAPTRELSLQIY 359
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGR-GPQALVLAPTRELAMQIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 360 NEAKKFGKVYNLNVVCCYGGGSKWEQSKALEQGAEIIVATPGRMIDMVKMKATNLRRVTFLVLDEADRMFHMGFEPQVRS 439
Cdd:cd00268 80 EVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 24662330 440 ICNHVRPDRQCLMFSATFKKRIERLARDVLSDPVRI 475
Cdd:cd00268 160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
269-634 |
4.74e-98 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 311.11 E-value: 4.74e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 269 TSFGHFGFDEQLIKAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMHVMDQKQLKPGDGPIgLIL 348
Cdd:PRK11192 1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRKSGPPRI-LIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 349 APTRELSLQIYNEAKKFGKVYNLNVVCCYGGGSKWEQSKALEQGAEIIVATPGRMIDMVKMKATNLRRVTFLVLDEADRM 428
Cdd:PRK11192 80 TPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 429 FHMGFEPQVRSICNHVRPDRQCLMFSATFK-KRIERLARDVLSDPVRIvqgdlnEAN------QDITQSVYVFPNPLQKW 501
Cdd:PRK11192 160 LDMGFAQDIETIAAETRWRKQTLLFSATLEgDAVQDFAERLLNDPVEV------EAEpsrrerKKIHQWYYRADDLEHKT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 502 NwLLCHLVKFLSEGSVLIFVTKKVDAETVSNNLLIKEYNCLLLHGDMDQADRNKVITQFKRKECDILVATDVAARGLDIP 581
Cdd:PRK11192 234 A-LLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDID 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 24662330 582 HIRNVVNYDTARDIETHTHRIGRTGRAGEKGNAYTLVTDKDKEFAGHLVRNLE 634
Cdd:PRK11192 313 DVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIE 365
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
289-634 |
2.23e-97 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 310.19 E-value: 2.23e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 289 YTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMHVmDQKQLKPGdgpiGLILAPTRELSLQIYNEAKKFGK- 367
Cdd:PRK11776 24 YTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL-DVKRFRVQ----ALVLCPTRELADQVAKEIRRLARf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 368 VYNLNVVCCYGGGSKWEQSKALEQGAEIIVATPGRMIDMVKMKATNLRRVTFLVLDEADRMFHMGFEPQVRSICNHVRPD 447
Cdd:PRK11776 99 IPNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMGFQDAIDAIIRQAPAR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 448 RQCLMFSATFKKRIERLARDVLSDPVRIVQGDLNEANQdITQSVY-VFPNplQKWNWLLCHLVKFLSEgSVLIFVTKKVD 526
Cdd:PRK11776 179 RQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPA-IEQRFYeVSPD--ERLPALQRLLLHHQPE-SCVVFCNTKKE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 527 AETVSNNLLIKEYNCLLLHGDMDQADRNKVITQFKRKECDILVATDVAARGLDIPHIRNVVNYDTARDIETHTHRIGRTG 606
Cdd:PRK11776 255 CQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTG 334
|
330 340
....*....|....*....|....*...
gi 24662330 607 RAGEKGNAYTLVTDKDkefaGHLVRNLE 634
Cdd:PRK11776 335 RAGSKGLALSLVAPEE----MQRANAIE 358
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
280-476 |
4.43e-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: 299.67 E-value: 4.43e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 280 LIKAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMHVMDQKQLKPGDGPIGLILAPTRELSLQIY 359
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGDGPIVLVLAPTRELAQQIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 360 NEAKKFGKVYNLNVVCCYGGGSKWEQSKALEQGAEIIVATPGRMIDMVKMKATNLRRVTFLVLDEADRMFHMGFEPQVRS 439
Cdd:cd17966 81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 24662330 440 ICNHVRPDRQCLMFSATFKKRIERLARDVLSDPVRIV 476
Cdd:cd17966 161 IVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
202-475 |
1.45e-88 |
|
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or DEAD Box Protein P82) has a wide variety of functions including regulating the alternative splicing of exons exhibiting specific features such as the inclusion of AC-rich alternative exons in CD44 transcripts, playing a role in innate immunity, and promoting mRNA degradation mediated by the antiviral zinc-finger protein ZC3HAV1 in an ATPase-dependent manner. DDX17 synergizes with DDX5 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. DDX17 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350808 [Multi-domain] Cd Length: 271 Bit Score: 280.36 E-value: 1.45e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 202 GNPIAPPKKK--DIDPLPPiyhseieyepFEKNFYTQHDDIAALDDEQVRELRRTLGVKVTGPSPPKPVTSFGHFGFDEQ 279
Cdd:cd18050 3 GNPGERLRKKkwDLSELPK----------FEKNFYVEHPEVARMTQYDVEELRRKKEITIRGVGCPKPVFAFHQANFPQY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 280 LIKAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMHVMDQKQLKPGDGPIGLILAPTRELSLQIY 359
Cdd:cd18050 73 VMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDGPICLVLAPTRELAQQVQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 360 NEAKKFGKVYNLNVVCCYGGGSKWEQSKALEQGAEIIVATPGRMIDMVKMKATNLRRVTFLVLDEADRMFHMGFEPQVRS 439
Cdd:cd18050 153 QVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRK 232
|
250 260 270
....*....|....*....|....*....|....*.
gi 24662330 440 ICNHVRPDRQCLMFSATFKKRIERLARDVLSDPVRI 475
Cdd:cd18050 233 IVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQI 268
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
246-475 |
5.81e-81 |
|
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: 259.17 E-value: 5.81e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 246 EQVRELRRTLGVKVTGPSPPKPVTSFGHFGFDEQLIKAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIW 325
Cdd:cd18049 1 QEVEQYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 326 PMLMHVMDQKQLKPGDGPIGLILAPTRELSLQIYNEAKKFGKVYNLNVVCCYGGGSKWEQSKALEQGAEIIVATPGRMID 405
Cdd:cd18049 81 PAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLID 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 406 MVKMKATNLRRVTFLVLDEADRMFHMGFEPQVRSICNHVRPDRQCLMFSATFKKRIERLARDVLSDPVRI 475
Cdd:cd18049 161 FLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHI 230
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
270-471 |
1.72e-80 |
|
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: 257.03 E-value: 1.72e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 270 SFGHFGFDEQLIKAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMHVMDQKQLKPGDG-----PI 344
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGrrkayPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 345 GLILAPTRELSLQIYNEAKKFgkVYN--LNVVCCYGGGSKWEQSKALEQGAEIIVATPGRMIDMVKMKATNLRRVTFLVL 422
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKF--SYRsgVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 24662330 423 DEADRMFHMGFEPQVRSICNH----VRPDRQCLMFSATFKKRIERLARDVLSD 471
Cdd:cd17967 159 DEADRMLDMGFEPQIRKIVEHpdmpPKGERQTLMFSATFPREIQRLAADFLKN 211
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
269-634 |
2.67e-79 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 267.48 E-value: 2.67e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 269 TSFGHFGFDEQLIKAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLmHVMDQkQLKpgdGPIGLIL 348
Cdd:PRK11634 6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLL-HNLDP-ELK---APQILVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 349 APTRELSLQIYNEAKKFGK-VYNLNVVCCYGGGSKWEQSKALEQGAEIIVATPGRMIDMVKMKATNLRRVTFLVLDEADR 427
Cdd:PRK11634 81 APTRELAVQVAEAMTDFSKhMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 428 MFHMGFEPQVRSICNHVRPDRQCLMFSATFKKRIERLARDVLSDP--VRIvQGDLNeANQDITQSvYVFPNPLQKWNwll 505
Cdd:PRK11634 161 MLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPqeVRI-QSSVT-TRPDISQS-YWTVWGMRKNE--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 506 cHLVKFLSE---GSVLIFVTKKVDAETVSNNLLIKEYNCLLLHGDMDQADRNKVITQFKRKECDILVATDVAARGLDIPH 582
Cdd:PRK11634 235 -ALVRFLEAedfDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVER 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 24662330 583 IRNVVNYDTARDIETHTHRIGRTGRAGEKGNAYTLVTDKDKEfaghLVRNLE 634
Cdd:PRK11634 314 ISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERR----LLRNIE 361
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
266-621 |
1.13e-78 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 264.12 E-value: 1.13e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 266 KPVT--SFGHFGFDEQLIKAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMHVMDQKQL---KPG 340
Cdd:PRK04537 4 KPLTdlTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALadrKPE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 341 DgPIGLILAPTRELSLQIYNEAKKFGKVYNLNVVCCYGGGSKWEQSKALEQGAEIIVATPGRMIDMVKM-KATNLRRVTF 419
Cdd:PRK04537 84 D-PRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQhKVVSLHACEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 420 LVLDEADRMFHMGFEPQVRSICNHV--RPDRQCLMFSATFKKRIERLARDVLSDPVRIVQGDLNEANQDITQSVYvFPNP 497
Cdd:PRK04537 163 CVLDEADRMFDLGFIKDIRFLLRRMpeRGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIY-FPAD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 498 LQKWNWLLCHLVKflSEGS-VLIFVTKKVDAETVSNNLLIKEYNCLLLHGDMDQADRNKVITQFKRKECDILVATDVAAR 576
Cdd:PRK04537 242 EEKQTLLLGLLSR--SEGArTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAAR 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 24662330 577 GLDIPHIRNVVNYDTARDIETHTHRIGRTGRAGEKGNAYTLVTDK 621
Cdd:PRK04537 320 GLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACER 364
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
205-469 |
1.56e-77 |
|
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: 251.04 E-value: 1.56e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 205 IAPPKKKDIDPLPPIYHSEIEyepFEKnfytqHDDIAalddeqvrelrrtlgVKVTGPSPPKPVTSFGHFGFDEQLIKAV 284
Cdd:cd18052 2 IPPPPPEDEDEIFATIQTGIN---FDK-----YDEIP---------------VEVTGRNPPPAILTFEEANLCETLLKNI 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 285 RKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMHVMDQ----KQLKPGDGPIGLILAPTRELSLQIYN 360
Cdd:cd18052 59 RKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEgltaSSFSEVQEPQALIVAPTRELANQIFL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 361 EAKKFGKVYNLNVVCCYGGGSKWEQSKALEQGAEIIVATPGRMIDMVKMKATNLRRVTFLVLDEADRMFHMGFEPQVRSI 440
Cdd:cd18052 139 EARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKL 218
|
250 260 270
....*....|....*....|....*....|...
gi 24662330 441 CNHV----RPDRQCLMFSATFKKRIERLARDVL 469
Cdd:cd18052 219 VSEPgmpsKEDRQTLMFSATFPEEIQRLAAEFL 251
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
233-644 |
1.58e-75 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 254.33 E-value: 1.58e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 233 FY-TQHDDIAALDDEQVRELRRTLGVKVTGPSPPKPVTSFGHFGFDEQLIKAVRKAEYTQPTPIQAQAVPTALSGRDIIG 311
Cdd:PLN00206 84 FYvRDPGSTSGLSSSQAELLRRKLEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 312 IAKTGSGKTAAFIWPMLMHVMDQKQLKPGD--GPIGLILAPTRELSLQIYNEAKKFGKVYNLNVVCCYGGGSKWEQSKAL 389
Cdd:PLN00206 164 SADTGSGKTASFLVPIISRCCTIRSGHPSEqrNPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRI 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 390 EQGAEIIVATPGRMIDMVKMKATNLRRVTFLVLDEADRMFHMGFEPQVRSICNHVrPDRQCLMFSATFKKRIERLARDVL 469
Cdd:PLN00206 244 QQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQAL-SQPQVLLFSATVSPEVEKFASSLA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 470 SDPVRIVQGDLNEANQDITQ-SVYVFP-NPLQKWNWLLCHLVKFLSEGSVliFVTKKVDAETVSNNL-LIKEYNCLLLHG 546
Cdd:PLN00206 323 KDIILISIGNPNRPNKAVKQlAIWVETkQKKQKLFDILKSKQHFKPPAVV--FVSSRLGADLLANAItVVTGLKALSIHG 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 547 DMDQADRNKVITQFKRKECDILVATDVAARGLDIPHIRNVVNYDTARDIETHTHRIGRTGRAGEKGNAYTLVTDKDKEFA 626
Cdd:PLN00206 401 EKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLF 480
|
410
....*....|....*...
gi 24662330 627 GHLVRNLEGADQLVPDDL 644
Cdd:PLN00206 481 PELVALLKSSGAAIPREL 498
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
270-634 |
3.38e-75 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 251.65 E-value: 3.38e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 270 SFGHFGFDEQLIKAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMHVMDQKQLKPGDGPI-GLIL 348
Cdd:PRK10590 2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVrALIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 349 APTRELSLQIYNEAKKFGKVYNLNVVCCYGGGSKWEQSKALEQGAEIIVATPGRMIDMVKMKATNLRRVTFLVLDEADRM 428
Cdd:PRK10590 82 TPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 429 FHMGFEPQVRSICNHVRPDRQCLMFSATFKKRIERLARDVLSDPVRIVQGDLNEANQDITQSVYvFPNPLQKWNwLLCHL 508
Cdd:PRK10590 162 LDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVH-FVDKKRKRE-LLSQM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 509 VKFLSEGSVLIFVTKKVDAETVSNNLLIKEYNCLLLHGDMDQADRNKVITQFKRKECDILVATDVAARGLDIPHIRNVVN 588
Cdd:PRK10590 240 IGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVN 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 24662330 589 YDTARDIETHTHRIGRTGRAGEKGNAYTLV-TDKDKefaghLVRNLE 634
Cdd:PRK10590 320 YELPNVPEDYVHRIGRTGRAAATGEALSLVcVDEHK-----LLRDIE 361
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
264-622 |
9.31e-75 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 250.99 E-value: 9.31e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 264 PPKPVTSFGHFGFDEQLIKAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAF---IWPMLMHVMDQKQLKPG 340
Cdd:PRK01297 82 PQEGKTRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFlisIINQLLQTPPPKERYMG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 341 DgPIGLILAPTRELSLQIYNEAKKFGKVYNLNVVCCYGGGSKWEQSKALE-QGAEIIVATPGRMIDMVKMKATNLRRVTF 419
Cdd:PRK01297 162 E-PRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMVEV 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 420 LVLDEADRMFHMGFEPQVRSICNHVRP--DRQCLMFSATFKKRIERLARDVLSDPVRIVQGDLNEANQDITQSVYVFPNP 497
Cdd:PRK01297 241 MVLDEADRMLDMGFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGS 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 498 lQKWNwLLCHLVKFLSEGSVLIFVTKKVDAETVSNNLLIKEYNCLLLHGDMDQADRNKVITQFKRKECDILVATDVAARG 577
Cdd:PRK01297 321 -DKYK-LLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRG 398
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 24662330 578 LDIPHIRNVVNYDTARDIETHTHRIGRTGRAGEKGNAYTLVTDKD 622
Cdd:PRK01297 399 IHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDD 443
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
269-617 |
5.37e-74 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 247.19 E-value: 5.37e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 269 TSFGHFGFDEQLIKAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMHVMD--QKQLKPGDGPIGL 346
Cdd:PRK04837 8 QKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLShpAPEDRKVNQPRAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 347 ILAPTRELSLQIYNEAKKFGKVYNLNVVCCYGGGSKWEQSKALEQGAEIIVATPGRMIDMVKMKATNLRRVTFLVLDEAD 426
Cdd:PRK04837 88 IMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEAD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 427 RMFHMGFEPQVRSICNHVRP--DRQCLMFSATFKKRIERLARDVLSDPVRIVQGDLNEANQDITQSVYvFPNPLQKWNWL 504
Cdd:PRK04837 168 RMFDLGFIKDIRWLFRRMPPanQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELF-YPSNEEKMRLL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 505 LCHLVKFLSEGSVlIFVTKKVDAETVSNNLLIKEYNCLLLHGDMDQADRNKVITQFKRKECDILVATDVAARGLDIPHIR 584
Cdd:PRK04837 247 QTLIEEEWPDRAI-IFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVT 325
|
330 340 350
....*....|....*....|....*....|...
gi 24662330 585 NVVNYDTARDIETHTHRIGRTGRAGEKGNAYTL 617
Cdd:PRK04837 326 HVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
280-475 |
2.24e-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: 235.68 E-value: 2.24e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 280 LIKAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLM------HVMDQKQLkpgDGPIGLILAPTRE 353
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVyisrlpPLDEETKD---DGPYALILAPTRE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 354 LSLQIYNEAKKFGKVYNLNVVCCYGGGSKWEQSKALEQGAEIIVATPGRMIDMVKMKATNLRRVTFLVLDEADRMFHMGF 433
Cdd:cd17945 78 LAQQIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24662330 434 EPQVRSICNHV-----RPD---------------RQCLMFSATFKKRIERLARDVLSDPVRI 475
Cdd:cd17945 158 EPQVTKILDAMpvsnkKPDteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
257-471 |
1.70e-66 |
|
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: 221.07 E-value: 1.70e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 257 VKVTGPSPPKPVTSFGHFGFDEQLIKAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMHVMDQ-- 334
Cdd:cd18051 9 VEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQgp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 335 -KQLKPGDG--------PIGLILAPTRELSLQIYNEAKKFgkVYNLNVVCC--YGGGSKWEQSKALEQGAEIIVATPGRM 403
Cdd:cd18051 89 gESLPSESGyygrrkqyPLALVLAPTRELASQIYDEARKF--AYRSRVRPCvvYGGADIGQQMRDLERGCHLLVATPGRL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24662330 404 IDMVKMKATNLRRVTFLVLDEADRMFHMGFEPQVRSIC--NHVRP--DRQCLMFSATFKKRIERLARDVLSD 471
Cdd:cd18051 167 VDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVeqDTMPPtgERQTLMFSATFPKEIQMLARDFLDN 238
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
280-476 |
3.91e-66 |
|
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: 218.10 E-value: 3.91e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 280 LIKAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMHVMDQKQLK-PGDGPIGLILAPTRELSLQI 358
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPReQRNGPGVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 359 YNEAKKFgKVYNLNVVCCYGGGSKWEQSKALEQGAEIIVATPGRMIDMVKMKATNLRRVTFLVLDEADRMFHMGFEPQVR 438
Cdd:cd17958 81 EAECSKY-SYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 24662330 439 SICNHVRPDRQCLMFSATFKKRIERLARDVLSDPVRIV 476
Cdd:cd17958 160 KILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIVY 197
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
270-475 |
2.12e-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: 213.72 E-value: 2.12e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 270 SFGHFGFDEQLIKAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMHVMDQKQlkpgdGPIGLILA 349
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQ-----RFFALVLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 350 PTRELSLQIYNEAKKFGKVYNLNVVCCYGGGSKWEQSKALEQGAEIIVATPGRMID-MVKMKATNLRRVTFLVLDEADRM 428
Cdd:cd17954 76 PTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDhLENTKGFSLKSLKFLVMDEADRL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 24662330 429 FHMGFEPQVRSICNHVRPDRQCLMFSATFKKRIERLARDVLSDPVRI 475
Cdd:cd17954 156 LNMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
280-475 |
4.36e-64 |
|
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: 212.97 E-value: 4.36e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 280 LIKAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMHVMDQKQLKP---GDGPIGLILAPTRELSL 356
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEKKLPfikGEGPYGLIVCPSRELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 357 QIYNEAKKFGKVYN------LNVVCCYGGGSKWEQSKALEQGAEIIVATPGRMIDMVKMKATNLRRVTFLVLDEADRMFH 430
Cdd:cd17951 81 QTHEVIEYYCKALQeggypqLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 24662330 431 MGFEPQVRSICNHVRPDRQCLMFSATFKKRIERLARDVLSDPVRI 475
Cdd:cd17951 161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
270-475 |
5.55e-62 |
|
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350717 [Multi-domain] Cd Length: 205 Bit Score: 207.16 E-value: 5.55e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 270 SFGHFGFDEQLIKAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMHVmdqKQLKPGDGPIGLILA 349
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKL---KAHSPTVGARALILS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 350 PTRELSLQIYNEAKKFGKVYNLNVVCCYGGGSKWEQSKALEQGAEIIVATPGRMID-MVKMKaTNLRRVTFLVLDEADRM 428
Cdd:cd17959 79 PTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHlLVEMN-LKLSSVEYVVFDEADRL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 24662330 429 FHMGFEPQVRSICNHVRPDRQCLMFSATFKKRIERLARDVLSDPVRI 475
Cdd:cd17959 158 FEMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
280-478 |
6.20e-62 |
|
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: 206.67 E-value: 6.20e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 280 LIKAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMHVMDQKQLKpgdGPIGLILAPTRELSLQIY 359
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKK---GLRALILAPTRELASQIY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 360 NEAKKFGKVYNLNVVCCYGGGS-KWEQSKALEQGAEIIVATPGRMIDMVKMKATNLRRVTFLVLDEADRMFHMGFEPQVR 438
Cdd:cd17957 78 RELLKLSKGTGLRIVLLSKSLEaKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 24662330 439 SI---CNHvrPDRQCLMFSATFKKRIERLARDVLSDPVRIVQG 478
Cdd:cd17957 158 EIlaaCTN--PNLQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
293-464 |
2.20e-61 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 204.01 E-value: 2.20e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 293 TPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMHVMDQKqlkpgDGPIGLILAPTRELSLQIYNEAKKFGKVYNLN 372
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLD-----NGPQALVLAPTRELAEQIYEELKKLGKGLGLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 373 VVCCYGGGSKWEQSKALeQGAEIIVATPGRMIDMVKmKATNLRRVTFLVLDEADRMFHMGFEPQVRSICNHVRPDRQCLM 452
Cdd:pfam00270 76 VASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQ-ERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILL 153
|
170
....*....|..
gi 24662330 453 FSATFKKRIERL 464
Cdd:pfam00270 154 LSATLPRNLEDL 165
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
268-624 |
2.63e-59 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 206.60 E-value: 2.63e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 268 VTSFGHFGFDEQLIKAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMHV---MDQKQLkpgdgpi 344
Cdd:PTZ00424 27 VDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIdydLNACQA------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 345 gLILAPTRELSLQIYNEAKKFGKVYNLNVVCCYGGGSKWEQSKALEQGAEIIVATPGRMIDMVKMKATNLRRVTFLVLDE 424
Cdd:PTZ00424 100 -LILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 425 ADRMFHMGFEPQVRSICNHVRPDRQCLMFSATFKKRIERLARDVLSDPVRI-VQGDlnEANQDITQSVYVfpnPLQKWNW 503
Cdd:PTZ00424 179 ADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRIlVKKD--ELTLEGIRQFYV---AVEKEEW 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 504 ---LLCHLVKFLSEGSVLIFVTKKVDAETVSNNLLIKEYNCLLLHGDMDQADRNKVITQFKRKECDILVATDVAARGLDI 580
Cdd:PTZ00424 254 kfdTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDV 333
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 24662330 581 PHIRNVVNYDTARDIETHTHRIGRTGRAGEKGNAYTLVTDKDKE 624
Cdd:PTZ00424 334 QQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIE 377
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
280-475 |
1.90e-57 |
|
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: 194.40 E-value: 1.90e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 280 LIKAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPmlmhVMDQKQLKPGDGPI--GLILAPTRELSLQ 357
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLP----ILERLLYRPKKKAAtrVLVLVPTRELAMQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 358 IYNEAKKFGKVYNLNVVCCYGGGSKWEQSKALEQGAEIIVATPGRMIDMVK-MKATNLRRVTFLVLDEADRMFHMGFEPQ 436
Cdd:cd17947 77 CFSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRnSPSFDLDSIEILVLDEADRMLEEGFADE 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 24662330 437 VRSICNHVRPDRQCLMFSATFKKRIERLARDVLSDPVRI 475
Cdd:cd17947 157 LKEILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
284-489 |
6.02e-57 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 193.48 E-value: 6.02e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 284 VRKAEYTQPTPIQAQAVPTALSG-RDIIGIAKTGSGKTAAFIWPMLMHvmdqkqLKPGDGPIGLILAPTRELSLQIYNEA 362
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEA------LKRGKGGRVLVLVPTRELAEQWAEEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 363 KKFGKVYNLNVVCCYGGGSKWEQSKALEQG-AEIIVATPGRMIDMVKMKATNLRRVTFLVLDEADRMFHMGFEPQVRSIC 441
Cdd:smart00487 75 KKLGPSLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 24662330 442 NHVRPDRQCLMFSATFKKRIERLARDVLSDPVRIVQGDLneANQDITQ 489
Cdd:smart00487 155 KLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFT--PLEPIEQ 200
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
271-473 |
3.32e-55 |
|
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350713 [Multi-domain] Cd Length: 204 Bit Score: 188.59 E-value: 3.32e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 271 FGHFGFDEQLIKAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLmhvmdQKQLKPGDGPIGLILAP 350
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPIL-----QRLSEDPYGIFALVLTP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 351 TRELSLQIYNEAKKFGKVYNLNVVCCYGGGSKWEQSKALEQGAEIIVATPGRMIDMVK---MKATNLRRVTFLVLDEADR 427
Cdd:cd17955 76 TRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEADR 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 24662330 428 MFHMGFEPQVRSICNHVRPDRQCLMFSATFKKRIERLARDVLSDPV 473
Cdd:cd17955 156 LLTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPF 201
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
487-618 |
1.50e-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: 181.17 E-value: 1.50e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 487 ITQSvYVFPNPLQKWNWLLCHLVKFLSEGSVLIFVTKKVDAETVSNNLLIKEYNCLLLHGDMDQADRNKVITQFKRKECD 566
Cdd:cd18787 1 IKQL-YVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 24662330 567 ILVATDVAARGLDIPHIRNVVNYDTARDIETHTHRIGRTGRAGEKGNAYTLV 618
Cdd:cd18787 80 VLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
276-469 |
4.68e-51 |
|
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: 177.39 E-value: 4.68e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 276 FDEQLIKAVRKAEYTQPTPIQAQAVPTALS-GRDIIGIAKTGSGKTAAFIWPMLMHVMDQKQLKPGDGPIGLILAPTREL 354
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGVSALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 355 SLQIYNEAKKF-GKVYNLNVVCCYGGGSKWEQSKALE-QGAEIIVATPGRMIDMVK--MKATNLRRVTFLVLDEADRMFH 430
Cdd:cd17964 81 ALQIAAEAKKLlQGLRKLRVQSAVGGTSRRAELNRLRrGRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRLLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 24662330 431 MGFEPQVRSICNHVRP----DRQCLMFSATFKKRIERLARDVL 469
Cdd:cd17964 161 MGFRPDLEQILRHLPEknadPRQTLLFSATVPDEVQQIARLTL 203
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
282-475 |
1.10e-50 |
|
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin gene, NUP98, by inversion 11 (p15q22) chromosome translocation is found in the patients with de novo or therapy-related myeloid malignancies. Diseases associated with DDX10 (also known as DDX10-NUP98 Fusion Protein Type 2) include myelodysplastic syndrome and leukemia, acute myeloid. DDX10 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350699 [Multi-domain] Cd Length: 198 Bit Score: 175.94 E-value: 1.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 282 KAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMHVMdQKQLKPGDGPIGLILAPTRELSLQIYNE 361
Cdd:cd17941 3 KGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLY-RERWTPEDGLGALIISPTRELAMQIFEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 362 AKKFGKVYNLNVVCCYGG-GSKWEQSKAleQGAEIIVATPGRMI----DMVKMKATNLRrvtFLVLDEADRMFHMGFEPQ 436
Cdd:cd17941 82 LRKVGKYHSFSAGLIIGGkDVKEEKERI--NRMNILVCTPGRLLqhmdETPGFDTSNLQ---MLVLDEADRILDMGFKET 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 24662330 437 VRSICNHVRPDRQCLMFSATFKKRIERLARDVLSDPVRI 475
Cdd:cd17941 157 LDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYI 195
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
280-457 |
2.16e-50 |
|
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: 176.66 E-value: 2.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 280 LIKAVRKAEYTQPTPIQAQAVPTALS-GRDIIGIAKTGSGKTAAFIWPMLMHVMDQKQ----LKPGDGPIGLILAPTREL 354
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLLSQKSsngvGGKQKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 355 SLQIYNEAKKFGKVYNLNVVCCYGGGSKWEQSKALEQGAEIIVATPGRMIDMVKMK---ATNLRRVTFLVLDEADRMFHM 431
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGnehLANLKSLRFLVLDEADRMLEK 160
|
170 180 190
....*....|....*....|....*....|....
gi 24662330 432 G-FEpQVRSICNHV-------RPDRQCLMFSATF 457
Cdd:cd17946 161 GhFA-ELEKILELLnkdragkKRKRQTFVFSATL 193
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
280-475 |
3.55e-50 |
|
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: 174.66 E-value: 3.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 280 LIKAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMHVMDQKqlkpgDGPIGLILAPTRELSLQIY 359
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEH-----RNPSALILTPTRELAVQIE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 360 NEAKKFGK-VYNLNVVCCYGGGSKWEQSKALEQGAEIIVATPGRMIDMVKMKATNLRRVTFLVLDEADRMFHMGFEPQVR 438
Cdd:cd17962 76 DQAKELMKgLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVL 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 24662330 439 SICNHVRPDRQCLMFSATFKKRIERLARDVLSDPVRI 475
Cdd:cd17962 156 DILENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
286-476 |
4.06e-49 |
|
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: 172.39 E-value: 4.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 286 KAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMHVM-DQKQLKPGDGPIGLILAPTRELSLQIYNEAKK 364
Cdd:cd17949 8 KMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLsLEPRVDRSDGTLALVLVPTRELALQIYEVLEK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 365 FGKVYNLNVVCCYGGGSKWEQSKA-LEQGAEIIVATPGRMIDMVKM-KATNLRRVTFLVLDEADRMFHMGFEPQVRSICN 442
Cdd:cd17949 88 LLKPFHWIVPGYLIGGEKRKSEKArLRKGVNILIATPGRLLDHLKNtQSFDVSNLRWLVLDEADRLLDMGFEKDITKILE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 24662330 443 HVR-------------PDRQCLMFSATFKKRIERLARDVLSDPVRIV 476
Cdd:cd17949 168 LLDdkrskaggekskpSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
280-476 |
1.09e-48 |
|
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: 170.45 E-value: 1.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 280 LIKAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMHVMDQKQLKPGDGPIGLILAPTRELSLQIY 359
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKKGQVGALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 360 NEAKKFGKVY--NLNVVCCYGGGSKWEQSKAL-EQGAEIIVATPGRMIDMVKMKAT--NLRRVTFLVLDEADRMFHMGFE 434
Cdd:cd17960 81 EVLQSFLEHHlpKLKCQLLIGGTNVEEDVKKFkRNGPNILVGTPGRLEELLSRKADkvKVKSLEVLVLDEADRLLDLGFE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 24662330 435 PQVRSICNHVRPDRQCLMFSATFKKRIERLARDVLSDPVRIV 476
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRVV 202
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
271-475 |
4.02e-47 |
|
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: 166.32 E-value: 4.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 271 FGHFGFDEQLIKAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLmhvmdqKQLKPGDGPI-GLILA 349
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPIL------EKIDPKKDVIqALILV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 350 PTRELSLQIYNEAKKFGKVYNLNVVCCYGGGSKWEQSKALEQGAEIIVATPGRMIDMVKMKATNLRRVTFLVLDEADRMF 429
Cdd:cd17940 75 PTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 24662330 430 HMGFEPQVRSICNHVRPDRQCLMFSATFKKRIERLARDVLSDPVRI 475
Cdd:cd17940 155 SQDFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
282-466 |
4.00e-46 |
|
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: 163.30 E-value: 4.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 282 KAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPmLMHVMDQKQLKPGDGPIGLILAPTRELSLQIYNE 361
Cdd:cd17942 3 KAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIP-AIELLYKLKFKPRNGTGVIIISPTRELALQIYGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 362 AKKFGKVYNLNVVCCYGGGSKWEQSKALEQGAEIIVATPGRMIDMVKMKA----TNLRrvtFLVLDEADRMFHMGFEPQV 437
Cdd:cd17942 82 AKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKgflyKNLQ---CLIIDEADRILEIGFEEEM 158
|
170 180
....*....|....*....|....*....
gi 24662330 438 RSICNHVRPDRQCLMFSATFKKRIERLAR 466
Cdd:cd17942 159 RQIIKLLPKRRQTMLFSATQTRKVEDLAR 187
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
277-473 |
4.24e-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: 163.52 E-value: 4.24e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 277 DEQLIKAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMHVMDQKQ-LKPGDGPIGLILAPTRELS 355
Cdd:cd17961 2 DPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAeSGEEQGTRALILVPTRELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 356 LQIYNEAKKF-----GKVYNLNVVccyGGGSKWEQSKALEQGAEIIVATPGRMIDMVKMKAT-NLRRVTFLVLDEADRMF 429
Cdd:cd17961 82 QQVSKVLEQLtaycrKDVRVVNLS---ASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLlLLSTLKYLVIDEADLVL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 24662330 430 HMGFEPQVRSICNHVRPDRQCLMFSATFKKRIERLARDVLSDPV 473
Cdd:cd17961 159 SYGYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
275-475 |
2.06e-43 |
|
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: 155.95 E-value: 2.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 275 GFDEQLIKAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMHV-MDQKQLKpgdgpiGLILAPTRE 353
Cdd:cd17939 3 GLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIdTTVRETQ------ALVLAPTRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 354 LSLQIYNEAKKFGKVYNLNVVCCYGGGSKWEQSKALEQGAEIIVATPGRMIDMVKMKATNLRRVTFLVLDEADRMFHMGF 433
Cdd:cd17939 77 LAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 24662330 434 EPQVRSICNHVRPDRQCLMFSATFKKRIERLARDVLSDPVRI 475
Cdd:cd17939 157 KDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
277-475 |
7.42e-42 |
|
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: 151.19 E-value: 7.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 277 DEQLIKAVRKAEYTQPTPIQAQAVPTALSG--RDIIGIAKTGSGKTAAFIWPMLMHVMDQKQLkpgdgPIGLILAPTREL 354
Cdd:cd17963 2 KPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKS-----PQALCLAPTREL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 355 SLQIYNEAKKFGKVYNLNVVCCYGGGSKWEQSKALEQgaeIIVATPGRMIDMVKMKATNLRRVTFLVLDEADRMFHM-GF 433
Cdd:cd17963 77 ARQIGEVVEKMGKFTGVKVALAVPGNDVPRGKKITAQ---IVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGH 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 24662330 434 EPQVRSICNHVRPDRQCLMFSATFKKRIERLARDVLSDPVRI 475
Cdd:cd17963 154 GDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
268-475 |
3.47e-41 |
|
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: 149.80 E-value: 3.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 268 VTSFGHFGFDEQLIKAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLmhvmdqKQLKPGDGPIG-L 346
Cdd:cd17950 1 SSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTL------QQLEPVDGQVSvL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 347 ILAPTRELSLQIYNEAKKFGK-VYNLNVVCCYGGGSKWEQSKALEQGA-EIIVATPGRMIDMVKMKATNLRRVTFLVLDE 424
Cdd:cd17950 75 VICHTRELAFQISNEYERFSKyMPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 24662330 425 ADRMFH-MGFEPQVRSICNHVRPDRQCLMFSATFKKRIERLARDVLSDPVRI 475
Cdd:cd17950 155 CDKMLEqLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEI 206
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
271-456 |
4.25e-39 |
|
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: 143.62 E-value: 4.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 271 FGHFGFDEQLIKAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMHVMdqkqlkpgdgpiGLILAP 350
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIVV------------ALILEP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 351 TRELSLQIYNEAKKFGKVYN---LNVVCCYGGGSKWEQSKALEQGAEIIVATPGRMIDMVKMKATNLRRVTFLVLDEADR 427
Cdd:cd17938 69 SRELAEQTYNCIENFKKYLDnpkLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADR 148
|
170 180 190
....*....|....*....|....*....|....*
gi 24662330 428 MFHMGFEPQVRSICNH-----VRPDR-QCLMFSAT 456
Cdd:cd17938 149 LLSQGNLETINRIYNRipkitSDGKRlQVIVCSAT 183
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
280-475 |
8.14e-37 |
|
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: 137.01 E-value: 8.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 280 LIKAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMHVMDQKQlkpgdGPIGLILAPTRELSLQIY 359
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERR-----HPQVLILAPTREIAVQIH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 360 NEAKKFGKVYNLNVVCCYGGGSKWEQSKALEQGAEIIVATPGRMIDMVKMKATNLRRVTFLVLDEADRMFHMGFEPQVRS 439
Cdd:cd17943 76 DVFKKIGKKLEGLKCEVFIGGTPVKEDKKKLKGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNW 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 24662330 440 ICNHVRPDRQCLMFSATFKKR-IERLARdVLSDPVRI 475
Cdd:cd17943 156 IFSSLPKNKQVIAFSATYPKNlDNLLAR-YMRKPVLV 191
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
271-476 |
2.87e-36 |
|
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: 135.65 E-value: 2.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 271 FGHFGFDEQLIKAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMHVmdQKQLKpgdGPIGLILAP 350
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQI--DTSLK---ATQALVLAP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 351 TRELSLQIYNEAKKFGKVYNLNVVCCYGGGSKWEQSKALEQGAEIIVATPGRMIDMVKMKATNLRRVTFLVLDEADRMFH 430
Cdd:cd18046 76 TRELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 24662330 431 MGFEPQVRSICNHVRPDRQCLMFSATFKKRIERLARDVLSDPVRIV 476
Cdd:cd18046 156 RGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRIL 201
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
271-476 |
4.13e-36 |
|
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: 135.29 E-value: 4.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 271 FGHFGFDEQLIKAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMhvMDQKQLKPgdgPIGLILAP 350
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQ--CLDIQVRE---TQALILSP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 351 TRELSLQIYNEAKKFGKVYNLNVVCCYGGGSKWEQSKALEQGAEIIVATPGRMIDMVKMKATNLRRVTFLVLDEADRMFH 430
Cdd:cd18045 76 TRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 24662330 431 MGFEPQVRSICNHVRPDRQCLMFSATFKKRIERLARDVLSDPVRIV 476
Cdd:cd18045 156 KGFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRIL 201
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
504-609 |
7.63e-34 |
|
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: 125.40 E-value: 7.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 504 LLCHLVKFLSEGSVLIFVTKKVDAETvsNNLLIKE-YNCLLLHGDMDQADRNKVITQFKRKECDILVATDVAARGLDIPH 582
Cdd:pfam00271 5 ALLELLKKERGGKVLIFSQTKKTLEA--ELLLEKEgIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPD 82
|
90 100
....*....|....*....|....*..
gi 24662330 583 IRNVVNYDTARDIETHTHRIGRTGRAG 609
Cdd:pfam00271 83 VDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
280-479 |
5.88e-33 |
|
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350706 [Multi-domain] Cd Length: 231 Bit Score: 127.10 E-value: 5.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 280 LIKAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMHVMDQKQLKPG--DGPIGLILAPTRELSLQ 357
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGpfNAPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 358 IYNEAKKFGKVYNLNVVCCYGGGSKWEQSKALEQGAEIIVATPGRMIDMVKMKATNLRRVTFLVLDEADRMFHMGFEPQV 437
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 24662330 438 RSICNH-----VRPDR--------QCLMFSATFKKRIERLARDVLS-DPVRIVQGD 479
Cdd:cd17948 161 SHFLRRfplasRRSENtdgldpgtQLVLVSATMPSGVGEVLSKVIDvDSIETVTSD 216
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
294-456 |
3.59e-32 |
|
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: 123.80 E-value: 3.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 294 PIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMHVM-DQKQLKPGDGPIGLILAPTRELSLQIYNEAKKFGKvyNLN 372
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQeDQQPRKRGRAPKVLVLAPTRELANQVTKDFKDITR--KLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 373 VVCCYGGGSKWEQSKALEQGAEIIVATPGRMIDMVKMKATNLRRVTFLVLDEADRMFHMGFEPQVRSICnHVR------P 446
Cdd:cd17944 93 VACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEIL-SVSykkdseD 171
|
170
....*....|
gi 24662330 447 DRQCLMFSAT 456
Cdd:cd17944 172 NPQTLLFSAT 181
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
528-609 |
1.28e-27 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 106.53 E-value: 1.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 528 ETVSNNLLIKEYNCLLLHGDMDQADRNKVITQFKRKECDILVATDVAARGLDIPHIRNVVNYDTARDIETHTHRIGRTGR 607
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 24662330 608 AG 609
Cdd:smart00490 81 AG 82
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
280-466 |
1.79e-26 |
|
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: 108.49 E-value: 1.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 280 LIKAVRKAEYTQPTPIQAQAVPTALSG---------RDIIGIAKTGSGKTAAFIWPMLmhvmdQKqLKPGDGPI--GLIL 348
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIV-----QA-LSKRVVPRlrALIV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 349 APTRELSLQIYNEAKKFGKVYNLNVVCCYGGGSKWEQSKALEQG--------AEIIVATPGRMIDMVKMKAT-NLRRVTF 419
Cdd:cd17956 75 VPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRLVDHLNSTPGfTLKHLRF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24662330 420 LVLDEADRMFHMGFE---PQV-RSICNHVRPDRQC----------------LMFSATFKKRIERLAR 466
Cdd:cd17956 155 LVIDEADRLLNQSFQdwlETVmKALGRPTAPDLGSfgdanllersvrplqkLLFSATLTRDPEKLSS 221
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
257-472 |
1.82e-23 |
|
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: 99.71 E-value: 1.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 257 VKVTGPSPPKP---VTSFGHFGFDEQLIKAVRKAEYTQPTPIQAQAVPTALSG--RDIIGIAKTGSGKTAAFIWPMLMHV 331
Cdd:cd18048 3 VEVLQRDPTSPlfsVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 332 mDQKQLKPGdgpiGLILAPTRELSLQIYNEAKKFGKVYNLNVVCCYGGGSKWEQSKALEqgAEIIVATPGRMID-MVKMK 410
Cdd:cd18048 83 -DALKLYPQ----CLCLSPTFELALQTGKVVEEMGKFCVGIQVIYAIRGNRPGKGTDIE--AQIVIGTPGTVLDwCFKLR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24662330 411 ATNLRRVTFLVLDEADRMFHM-GFEPQVRSICNHVRPDRQCLMFSATFKKRIERLARDVLSDP 472
Cdd:cd18048 156 LIDVTNISVFVLDEADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDP 218
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
285-629 |
3.54e-22 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 101.64 E-value: 3.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 285 RKAEYTQPTPIQAQAVPTALS-----GRDIIGIAKTGSGKTAafiwpMLMHVMDQKQLKpgdGPIgLILAPTRELSLQIY 359
Cdd:COG1061 74 ASGTSFELRPYQQEALEALLAalergGGRGLVVAPTGTGKTV-----LALALAAELLRG---KRV-LVLVPRRELLEQWA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 360 NEAKKFGKVYNLnvvccyGGGSKweqskalEQGAEIIVATpgrmIDMVKMKATN---LRRVTFLVLDEAdrmfHMGFEPQ 436
Cdd:COG1061 145 EELRRFLGDPLA------GGGKK-------DSDAPITVAT----YQSLARRAHLdelGDRFGLVIIDEA----HHAGAPS 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 437 VRSICNHVRPDRqCLMFSAT------------------FKKRIERLARD-VLSDP-VRIVQGDLNEANQD---ITQSVY- 492
Cdd:COG1061 204 YRRILEAFPAAY-RLGLTATpfrsdgreillflfdgivYEYSLKEAIEDgYLAPPeYYGIRVDLTDERAEydaLSERLRe 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 493 -VFPNPLQKWNWLLCHLVKFLSEGSVLIFVTKKVDAETVSNNLLIKEYNCLLLHGDMDQADRNKVITQFKRKECDILVAT 571
Cdd:COG1061 283 aLAADAERKDKILRELLREHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTV 362
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24662330 572 DVAARGLDIPHIRNVVnydTARDIETHTH---RIGRTGRAGE-KGNA--YTLVTDKDKEFAGHL 629
Cdd:COG1061 363 DVLNEGVDVPRLDVAI---LLRPTGSPREfiqRLGRGLRPAPgKEDAlvYDFVGNDVPVLEELA 423
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
276-476 |
2.83e-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: 93.98 E-value: 2.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 276 FDE-QLIKAVRKA-------------EYTQPTPIQAQAVPtALSGRDIIGI-----------------AKTGSGKTAAFI 324
Cdd:cd17965 1 FDQlKLLPSVREAiikeilkgsnktdEEIKPSPIQTLAIK-KLLKTLMRKVtkqtsneepklevfllaAETGSGKTLAYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 325 WPML-----MHVMDQKQLKPGDGPIG-------LILAPTRELSLQIYNEAKKFGKV--YNLNVVCCYGGGSKWEQSKALE 390
Cdd:cd17965 80 APLLdylkrQEQEPFEEAEEEYESAKdtgrprsVILVPTHELVEQVYSVLKKLSHTvkLGIKTFSSGFGPSYQRLQLAFK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 391 QGAEIIVATPGRMIDMVKMKATNLRRVTFLVLDEADRMFHMGFEPQVRSICNHVRPDRQCLMFSATFKKRIERLARDVLS 470
Cdd:cd17965 160 GRIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLRKLFP 239
|
....*.
gi 24662330 471 DPVRIV 476
Cdd:cd17965 240 DVVRIA 245
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
270-472 |
1.40e-20 |
|
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: 90.55 E-value: 1.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 270 SFGHFGFDEQLIKAVRKAEYTQPTPIQAQAVPTALSG--RDIIGIAKTGSGKTAAFIWPMLMHVMDQKQLKPgdgpiGLI 347
Cdd:cd18047 2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQ-----CLC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 348 LAPTRELSLQIYNEAKKFGKVYNLNVVCCYGGGSKWEQSKALEQgaEIIVATPGRMID-MVKMKATNLRRVTFLVLDEAD 426
Cdd:cd18047 77 LSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISE--QIVIGTPGTVLDwCSKLKFIDPKKIKVFVLDEAD 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 24662330 427 RMFH-MGFEPQVRSICNHVRPDRQCLMFSATFKKRIERLARDVLSDP 472
Cdd:cd18047 155 VMIAtQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
280-624 |
6.92e-17 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 84.56 E-value: 6.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 280 LIKAVRKAEYTQPTPIQAQAVPTAL-SGRDIIGIAKTGSGKTA-AFIWpMLMHVMDqkqlkpgdGPIGLILAPTRELSLQ 357
Cdd:COG1204 11 VIEFLKERGIEELYPPQAEALEAGLlEGKNLVVSAPTASGKTLiAELA-ILKALLN--------GGKALYIVPLRALASE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 358 IYNEAKKFGKVYNLNVVCCYGGgskWEQSKALEQGAEIIVATPGRMIDMVKMKATNLRRVTFLVLDEAdrmfHM------ 431
Cdd:COG1204 82 KYREFKRDFEELGIKVGVSTGD---YDSDDEWLGRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEA----HLiddesr 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 432 GfePQVRSICNHVR---PDRQCLMFSATFKKrIERLAR-----DVLSD--PVRIVQGDLNEANQDITQSVYVfpnPLQKW 501
Cdd:COG1204 155 G--PTLEVLLARLRrlnPEAQIVALSATIGN-AEEIAEwldaeLVKSDwrPVPLNEGVLYDGVLRFDDGSRR---SKDPT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 502 NWLLCHLVKflSEGSVLIFVTKKVDAET--------VSNNLLIKEYNCLLL----------------------------- 544
Cdd:COG1204 229 LALALDLLE--EGGQVLVFVSSRRDAESlakkladeLKRRLTPEEREELEElaeellevseethtnekladclekgvafh 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 545 HGDMDQADRNKVITQFKRKECDILVATDVAARGLDIPhIRNVVNYDTARDIETH-THR-----IGRTGRAG--EKGNAYt 616
Cdd:COG1204 307 HAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLP-ARRVIIRDTKRGGMVPiPVLefkqmAGRAGRPGydPYGEAI- 384
|
....*...
gi 24662330 617 LVTDKDKE 624
Cdd:COG1204 385 LVAKSSDE 392
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
296-650 |
5.07e-14 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 75.18 E-value: 5.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 296 QAQAVPTALSGRDIIGIAKTGSGKTAAFiwpmlmhvmdqkQLkPG---DGPiGLILAPTreLSL---QIyNEAKKFGkvy 369
Cdd:COG0514 22 QEEIIEAVLAGRDALVVMPTGGGKSLCY------------QL-PAlllPGL-TLVVSPL--IALmkdQV-DALRAAG--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 370 nLNVVCCYGGGSKWEQS---KALEQGA-EIIVATP-----GRMIDMVKmkatnLRRVTFLVLDEA--------Drmfhmg 432
Cdd:COG0514 82 -IRAAFLNSSLSAEERRevlRALRAGElKLLYVAPerllnPRFLELLR-----RLKISLFAIDEAhcisqwghD------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 433 FEPQVRSIcNHVR---PDRQCLMFSATFKKR-----IERLArdvLSDPVRIVQGdLNEANqdITQSVyVFPNPLQKWNWL 504
Cdd:COG0514 150 FRPDYRRL-GELRerlPNVPVLALTATATPRvradiAEQLG---LEDPRVFVGS-FDRPN--LRLEV-VPKPPDDKLAQL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 505 LcHLVKFLSEGSVLIFVTKKVDAETVSNNLLIKEYNCLLLHGDMDQADRNKVITQFKRKECDILVATdVA-ARGLDIPHI 583
Cdd:COG0514 222 L-DFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDV 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24662330 584 RNVVNYDTARDIETHTHRIGRTGRAGEKGNAYTLVTDKDKEFAGHLVRNLEGADQLVPDDLMEL-AMK 650
Cdd:COG0514 300 RFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEERKRVERAKLdAML 367
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
313-456 |
4.53e-12 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 64.35 E-value: 4.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 313 AKTGSGKT-AAFIWpmLMHVMDQKQLKPgdgpigLILAPTRELSLQIYNEAKKFGKvYNLNVVCCYGGGSKWEQSKALEQ 391
Cdd:cd00046 8 APTGSGKTlAALLA--ALLLLLKKGKKV------LVLVPTKALALQTAERLRELFG-PGIRVAVLVGGSSAEEREKNKLG 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24662330 392 GAEIIVATPGrMI--DMVKMKATNLRRVTFLVLDEADRMFHMGFEPQV--RSICNHVRPDRQCLMFSAT 456
Cdd:cd00046 79 DADIIIATPD-MLlnLLLREDRLFLKDLKLIIVDEAHALLIDSRGALIldLAVRKAGLKNAQVILLSAT 146
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
548-619 |
7.14e-12 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 68.99 E-value: 7.14e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24662330 548 MDQADRNKVITQFKRKECDILVATDVAARGLDIPHIRNVVNYD---TA-RDIEththRIGRTGRAGEkGNAYTLVT 619
Cdd:COG1111 395 LTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYEpvpSEiRSIQ----RKGRTGRKRE-GRVVVLIA 465
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
293-431 |
3.08e-11 |
|
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: 63.05 E-value: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 293 TPIQAQAVPTALSGRDIIGI-AKTGSGKTAAFIWPMLMHVMDQKQLKpgdgpigLILAPTRELSLQIYNEAKKFGKVYNL 371
Cdd:cd17921 3 NPIQREALRALYLSGDSVLVsAPTSSGKTLIAELAILRALATSGGKA-------VYIAPTRALVNQKEADLRERFGPLGK 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24662330 372 NVVCCYGGGSKweqSKALEQGAEIIVATPGRMIDMV-KMKATNLRRVTFLVLDEAdrmfHM 431
Cdd:cd17921 76 NVGLLTGDPSV---NKLLLAEADILVATPEKLDLLLrNGGERLIQDVRLVVVDEA----HL 129
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
533-635 |
3.36e-10 |
|
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: 59.28 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 533 NLLIKEYNCLLLHGDMDQADRNKVITQFKRKECDILVATDVAARGLDIPHIRNVVNYDTARDIETHTHRI-GRTGRAGEK 611
Cdd:cd18811 56 ERFRPELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLHQLrGRVGRGDHQ 135
|
90 100
....*....|....*....|....
gi 24662330 612 GNAYTLVTDKDKEFAGHLVRNLEG 635
Cdd:cd18811 136 SYCLLVYKDPLTETAKQRLRVMTE 159
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
289-580 |
1.70e-09 |
|
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: 61.25 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 289 YTQPTPIQAQAVPTALSGRDIIG-----IAKTGSGKT-AAFIWpMLmhvmdqKQLKPGDGPiGLILA-PTRELSLQIYNE 361
Cdd:COG1203 125 RTPINPLQNEALELALEAAEEEPglfilTAPTGGGKTeAALLF-AL------RLAAKHGGR-RIIYAlPFTSIINQTYDR 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 362 AKKFG-----------KVYNLNVVCCYGGGSKWEQ--SKALEqgAEIIVATPGRMIDMV--KMKATNLRRVTF----LVL 422
Cdd:COG1203 197 LRDLFgedvllhhslaDLDLLEEEEEYESEARWLKllKELWD--APVVVTTIDQLFESLfsNRKGQERRLHNLansvIIL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 423 DEAD----RMFHmgfePQVRSICNHVRPDRQCLMFSATF-KKRIERL--ARDVLSDPVrivqGDLNE-ANQDITQSVYVF 494
Cdd:COG1203 275 DEVQayppYMLA----LLLRLLEWLKNLGGSVILMTATLpPLLREELleAYELIPDEP----EELPEyFRAFVRKRVELK 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 495 PNPLqKWNWLLCHLVKFLSEG-SVLIFV-TKKvDAETVSNNL--LIKEYNCLLLHGDMDQADRNKVITQ----FKRKECD 566
Cdd:COG1203 347 EGPL-SDEELAELILEALHKGkSVLVIVnTVK-DAQELYEALkeKLPDEEVYLLHSRFCPADRSEIEKEikerLERGKPC 424
|
330
....*....|....
gi 24662330 567 ILVATDVAARGLDI 580
Cdd:COG1203 425 ILVSTQVVEAGVDI 438
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
514-610 |
4.39e-09 |
|
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: 55.29 E-value: 4.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 514 EGSVLIFVTKKVDAETVSNNLLIKEYNCLLLHGDMDQADRNKVITQFKRKECDILVATdVA-ARGLDIPHIRNVVNYDTA 592
Cdd:cd18794 30 GGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVAT-VAfGMGIDKPDVRFVIHYSLP 108
|
90
....*....|....*...
gi 24662330 593 RDIETHTHRIGRTGRAGE 610
Cdd:cd18794 109 KSMESYYQESGRAGRDGL 126
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
518-624 |
6.61e-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: 55.74 E-value: 6.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 518 LIFVTKKVDAETVSN-----NLLIKEYNCLLLHGDMDQADRNKVITQFKRKECDILVATDVAARGLDIPHIRNVVNYDTA 592
Cdd:cd18792 35 RIEESEKLDLKSIEAlaeelKELVPEARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIEDAD 114
|
90 100 110
....*....|....*....|....*....|...
gi 24662330 593 RDIETHTHRI-GRTGRAGEKGNAYTLVTDKDKE 624
Cdd:cd18792 115 RFGLSQLHQLrGRVGRGKHQSYCYLLYPDPKKL 147
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
548-617 |
1.12e-08 |
|
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: 54.67 E-value: 1.12e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24662330 548 MDQADRNKVITQFKRKECDILVATDVAARGLDIPHIRNVVNYDTA----RDIEththRIGRTGRaGEKGNAYTL 617
Cdd:cd18801 74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASpspiRMIQ----RMGRTGR-KRQGRVVVL 142
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
517-619 |
2.70e-08 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 57.58 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 517 VLIFVTKKVDAETVSNNLLIKEYNCLLLHGdmdQADRN-----------KVITQFKRKECDILVATDVAARGLDIPHIRN 585
Cdd:PRK13766 368 IIVFTQYRDTAEKIVDLLEKEGIKAVRFVG---QASKDgdkgmsqkeqiEILDKFRAGEFNVLVSTSVAEEGLDIPSVDL 444
|
90 100 110
....*....|....*....|....*....|....*...
gi 24662330 586 VVNYD---TA-RDIEththRIGRTGRaGEKGNAYTLVT 619
Cdd:PRK13766 445 VIFYEpvpSEiRSIQ----RKGRTGR-QEEGRVVVLIA 477
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
518-619 |
2.83e-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: 53.36 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 518 LIFVTKKVDAETVS-----NNLLIKEYNCLLLHG----------DMDQADRNKVITQFKRKECDILVATDVAARGLDIPH 582
Cdd:cd18802 29 IIFVERRATAVVLSrllkeHPSTLAFIRCGFLIGrgnssqrkrsLMTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPA 108
|
90 100 110
....*....|....*....|....*....|....*..
gi 24662330 583 IRNVVNYDTARDIETHthrIGRTGRAGEKGNAYTLVT 619
Cdd:cd18802 109 CNLVIRFDLPKTLRSY---IQSRGRARAPNSKYILMV 142
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
567-619 |
4.52e-08 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 50.78 E-value: 4.52e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 24662330 567 ILVATDVAARGLDIPHIRNVVNYDTARDIETHTHRIGRTGRAGEKGNAYTLVT 619
Cdd:cd18785 25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILFV 77
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
313-650 |
7.73e-08 |
|
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: 55.13 E-value: 7.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 313 AKTGSGKT-AAFIWPMlmhvmdqKQLKPGDGPIGLILAPTRELSLQIYNEAKK-FGKVYNLNVVCCYGGGSKWEQSKALE 390
Cdd:cd09639 6 APTGYGKTeAALLWAL-------HSLKSQKADRVIIALPTRATINAMYRRAKEaFGETGLYHSSILSSRIKEMGDSEEFE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 391 Q-------GAEIIVATPGRMIDMVKMKATNLRRVTF------------LVLDEADrmfhmGFEPQVRSICNHV-----RP 446
Cdd:cd09639 79 HlfplyihSNDTLFLDPITVCTIDQVLKSVFGEFGHyeftlasianslLIFDEVH-----FYDEYTLALILAVlevlkDN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 447 DRQCLMFSATFKKRIERLARDVLSDpvrivqgDLNEANQDITQSVYVFPNPLQKW----NWLLCHLVKFLSEGSVLIFVT 522
Cdd:cd09639 154 DVPILLMSATLPKFLKEYAEKIGYV-------EENEPLDLKPNERAPFIKIESDKvgeiSSLERLLEFIKKGGSVAIIVN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 523 KKVDAETVSNNL--LIKEYNCLLLHGDMDQADRNK----VITQFKRKECDILVATDVAARGLDIPHirNVVNYDTArDIE 596
Cdd:cd09639 227 TVDRAQEFYQQLkeKGPEEEIMLIHSRFTEKDRAKkeaeLLLEFKKSEKFVIVATQVIEASLDISV--DVMITELA-PID 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 24662330 597 THTHRIGRTGRAGEKGNAYTLVTDKDKEFAGHLVRnlegadqlvPDDLMELAMK 650
Cdd:cd09639 304 SLIQRLGRLHRYGEKNGEEVYIITDAPDGKGQKPY---------PYDLVERTIE 348
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
500-603 |
1.45e-07 |
|
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: 50.94 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 500 KWNWLLCHLVKFLSEGS-VLIFVTKKVDAETVSNNLLIKEYNCLLLHGDMDQADRNKVITQFKR--KECDILVATDVAAR 576
Cdd:cd18793 12 KLEALLELLEELREPGEkVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEdpDIRVFLLSTKAGGV 91
|
90 100 110
....*....|....*....|....*....|....*...
gi 24662330 577 GLDIPHIRNVVNYD-----------TARdiethTHRIG 603
Cdd:cd18793 92 GLNLTAANRVILYDpwwnpaveeqaIDR-----AHRIG 124
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
316-605 |
1.89e-07 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 54.85 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 316 GSGKTAAfiwpMLMHVMDQKQLKPgDGPIgLILAPTrelSLqIYN---EAKKFGkvYNLNVVCCYGGGSKWEQSKALEQg 392
Cdd:COG0553 270 GLGKTIQ----ALALLLELKERGL-ARPV-LIVAPT---SL-VGNwqrELAKFA--PGLRVLVLDGTRERAKGANPFED- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 393 AEIIVATpgrmIDMVKMKATNLRRVTF--LVLDEAdrmfHMGFEPQ------VRSIC-------------NHVRpDRQCL 451
Cdd:COG0553 337 ADLVITS----YGLLRRDIELLAAVDWdlVILDEA----QHIKNPAtkrakaVRALKarhrlaltgtpveNRLE-ELWSL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 452 M-------------FSATFKKRIE--------------------RLARDVLSD-PVRIVQG---DLNEANQDITQSVY-- 492
Cdd:COG0553 408 LdflnpgllgslkaFRERFARPIEkgdeealerlrrllrpfllrRTKEDVLKDlPEKTEETlyvELTPEQRALYEAVLey 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 493 ----------------VFP----------NPLQ-------------KWNWLLCHLVKFLSEG-SVLIFvTKKVD-AETVS 531
Cdd:COG0553 488 lrrelegaegirrrglILAaltrlrqicsHPALlleegaelsgrsaKLEALLELLEELLAEGeKVLVF-SQFTDtLDLLE 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 532 NNLLIKEYNCLLLHGDMDQADRNKVITQFKRK-ECD-ILVATDVAARGLDIPHIRNVVNYD-----------TARdieth 598
Cdd:COG0553 567 ERLEERGIEYAYLHGGTSAEERDELVDRFQEGpEAPvFLISLKAGGEGLNLTAADHVIHYDlwwnpaveeqaIDR----- 641
|
....*..
gi 24662330 599 THRIGRT 605
Cdd:COG0553 642 AHRIGQT 648
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
545-609 |
2.76e-07 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 53.95 E-value: 2.76e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24662330 545 HGDMDQADRNKVITQFKRKECDILVATDVAARGLDIPHIRNVVNYDTARDIETHTHRIGRTGRAG 609
Cdd:PRK11057 267 HAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDG 331
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
504-618 |
3.07e-07 |
|
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: 50.99 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 504 LLCHLVKFLSEGSVLIFVTKKVDAETVSNNLL-------IKEYNCLLLHGDMDQADRNKVIT---QFKRKecdILVATDV 573
Cdd:cd18791 33 LILQIHRTEEPGDILVFLPGQEEIERLCELLReellspdLGKLLVLPLHSSLPPEEQQRVFEpppPGVRK---VVLATNI 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24662330 574 AARGLDIPHIRNVV--------NYDTARDIET-HTHRIG------RTGRAG--EKGNAYTLV 618
Cdd:cd18791 110 AETSITIPGVVYVIdsglvkekVYDPRTGLSSlVTVWISkasaeqRAGRAGrtRPGKCYRLY 171
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
296-456 |
4.77e-07 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 50.66 E-value: 4.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 296 QAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMHVMDQKQLKpgdgpiGLILAPTRELSLQIYNEAKKFGKVYNLNVVC 375
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDPGSR------ALYLYPTKALAQDQLRSLRELLEQLGLGIRV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 376 -CYGGGSKWEQSKAL-EQGAEIIVATPgrmiDMV--------KMKATNLRRVTFLVLDEAdrmfHM---GFEPQV----- 437
Cdd:cd17923 79 aTYDGDTPREERRAIiRNPPRILLTNP----DMLhyallphhDRWARFLRNLRYVVLDEA----HTyrgVFGSHValllr 150
|
170 180
....*....|....*....|.
gi 24662330 438 --RSICNHVRPDRQCLMFSAT 456
Cdd:cd17923 151 rlRRLCRRYGADPQFILTSAT 171
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
275-479 |
7.59e-07 |
|
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: 52.92 E-value: 7.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 275 GFDEQLIKAVRKAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMHVMDqkqlkpGDGPIGLILAPTREL 354
Cdd:COG1205 40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLE------DPGATALYLYPTKAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 355 SLQIYNEAKKFGKVYNLNV-VCCYGGGSKWEQSKALEQGAEIIVATPgrmiDMVKMK--------ATNLRRVTFLVLDEA 425
Cdd:COG1205 114 ARDQLRRLRELAEALGLGVrVATYDGDTPPEERRWIREHPDIVLTNP----DMLHYGllphhtrwARFFRNLRYVVIDEA 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24662330 426 ---------------DRMfhmgfepqvRSICNHVRPDRQCLMFSATfkkrI---ERLARDVLSDPVRIVQGD 479
Cdd:COG1205 190 htyrgvfgshvanvlRRL---------RRICRHYGSDPQFILASAT----IgnpAEHAERLTGRPVTVVDED 248
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
510-611 |
7.98e-07 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 52.98 E-value: 7.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 510 KFLSEGSV----LIFVTKKVDAETVSNNLLIKEYNCLLLHGDMDQADRNKVITQFKRKECDILVATDVAARGLDIPHIRN 585
Cdd:PLN03137 672 KFIKENHFdecgIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRF 751
|
90 100
....*....|....*....|....*.
gi 24662330 586 VVNYDTARDIETHTHRIGRTGRAGEK 611
Cdd:PLN03137 752 VIHHSLPKSIEGYHQECGRAGRDGQR 777
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
307-425 |
8.19e-07 |
|
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: 50.34 E-value: 8.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 307 RDIIGIAKTGSGKTaaFIWPMLMHVMDQKQLKPG-DGPIGLILAPTRELSLQiynEAKKFGKVYNLNVVCCYG--GGSKW 383
Cdd:cd18034 17 RNTIVVLPTGSGKT--LIAVMLIKEMGELNRKEKnPKKRAVFLVPTVPLVAQ---QAEAIRSHTDLKVGEYSGemGVDKW 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 24662330 384 EQSKALE--QGAEIIVATPGRMID-----MVKMKATNLrrvtfLVLDEA 425
Cdd:cd18034 92 TKERWKEelEKYDVLVMTAQILLDalrhgFLSLSDINL-----LIFDEC 135
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
278-481 |
2.81e-06 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 48.68 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 278 EQLIKAVRKaeYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMhvmdqkqlkpgDGPIGLILAPTreLSL- 356
Cdd:cd17920 1 EQILKEVFG--YDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALL-----------LDGVTLVVSPL--ISLm 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 357 --QIynEAKKfgkvyNLNVVCCY-GGGSKWEQSKALEQGAE-----IIVATP-----GRMIDMVKmKATNLRRVTFLVLD 423
Cdd:cd17920 66 qdQV--DRLQ-----QLGIRAAAlNSTLSPEEKREVLLRIKngqykLLYVTPerllsPDFLELLQ-RLPERKRLALIVVD 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24662330 424 EAdrmfHM------GFEPQVRSICNHVR--PDRQCLMFSATFKKRIERLARDVLS-DPVRIVQGDLN 481
Cdd:cd17920 138 EA----HCvsqwghDFRPDYLRLGRLRRalPGVPILALTATATPEVREDILKRLGlRNPVIFRASFD 200
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
535-623 |
5.42e-06 |
|
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: 46.95 E-value: 5.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 535 LIKEYNCLLLHGDMDQADRNKVITQFKRKECDILVATDVAARGLDIPHIRNVV--NYDTARDIETHTHRiGRTGRAGEKG 612
Cdd:cd18810 48 LVPEARIAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIieRADKFGLAQLYQLR-GRVGRSKERA 126
|
90
....*....|.
gi 24662330 613 NAYTLVTDKDK 623
Cdd:cd18810 127 YAYFLYPDQKK 137
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
278-342 |
5.65e-06 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 50.10 E-value: 5.65e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24662330 278 EQLIKAVR---KAEYTQPTPIQAQAVPTALSGRDIIGIAKTGSGKT-AAFIWPMLMHVMDQKQLKPGDG 342
Cdd:COG1201 8 SLLHPAVRawfAARFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAFLPALDELARRPRPGELPDG 76
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
277-456 |
2.66e-05 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 45.48 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 277 DEQLIKAVRKAEYTQPTPIQAQAVptalsgRDIIG------------IAKTGSGKTAAFIWPMLMHVMDQKQLkpgdgpi 344
Cdd:cd17918 1 DRALIQELCKSLPFSLTKDQAQAI------KDIEKdlhspepmdrllSGDVGSGKTLVALGAALLAYKNGKQV------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 345 gLILAPTRELSLQIYNEAKKFGKVYNLNVVCcyggGSKWEQskaLEQGAEIIVATPGRMIDMVKMKAtnlrrVTFLVLDE 424
Cdd:cd17918 68 -AILVPTEILAHQHYEEARKFLPFINVELVT----GGTKAQ---ILSGISLLVGTHALLHLDVKFKN-----LDLVIVDE 134
|
170 180 190
....*....|....*....|....*....|..
gi 24662330 425 ADRmfhMGFEpQVRSICNHVRPDrqCLMFSAT 456
Cdd:cd17918 135 QHR---FGVA-QREALYNLGATH--FLEATAT 160
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
291-427 |
2.99e-05 |
|
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: 45.58 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 291 QPTPIQAQAVPTALSGRDIIgIAKTGSGKTAAFIWPMLmhvmdqKQLKPGDGPIgLILAPTRELSLQIYNeakKFGKVYN 370
Cdd:cd18035 2 ERRLYQVLIAAVALNGNTLI-VLPTGLGKTIIAILVAA------DRLTKKGGKV-LILAPSRPLVEQHAE---NLKRVLN 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 24662330 371 LNVVCCYGGGSKWEQSKA-LEQGAEIIVATPGRMIDMVKMKATNLRRVTFLVLDEADR 427
Cdd:cd18035 71 IPDKITSLTGEVKPEERAeRWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
|
|
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
537-573 |
3.09e-05 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 47.35 E-value: 3.09e-05
10 20 30
....*....|....*....|....*....|....*..
gi 24662330 537 KEYNCLLLHGDMDQADRNKVITQFKRKECDILVATDV 573
Cdd:COG1200 502 PGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTV 538
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
294-456 |
4.20e-05 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 45.02 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 294 PIQAQAVPTAL-SGRDIIGIAKTGSGKTAAFIWPMLMHVMDQKQlkpgdgpiGLILAPTRELSLQIYNEAKKFgkvYNLN 372
Cdd:cd18028 4 PPQAEAVRAGLlKGENLLISIPTASGKTLIAEMAMVNTLLEGGK--------ALYLVPLRALASEKYEEFKKL---EEIG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 373 VVCCYGGGSKWEQSKALEQgAEIIVATPGRMIDMVKMKATNLRRVTFLVLDEadrmFHMGFE----PQVRSICNHVR--- 445
Cdd:cd18028 73 LKVGISTGDYDEDDEWLGD-YDIIVATYEKFDSLLRHSPSWLRDVGVVVVDE----IHLISDeergPTLESIVARLRrln 147
|
170
....*....|.
gi 24662330 446 PDRQCLMFSAT 456
Cdd:cd18028 148 PNTQIIGLSAT 158
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
291-427 |
8.32e-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: 44.35 E-value: 8.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 291 QPTPIQAQAVPTALSGRDIIGIAKTGSGKTaaFIWPMLM-HVMDQKQLKPGdGPIgLILAPTRELSLQiynEAKKFGKVY 369
Cdd:cd17927 2 KPRNYQLELAQPALKGKNTIICLPTGSGKT--FVAVLICeHHLKKFPAGRK-GKV-VFLANKVPLVEQ---QKEVFRKHF 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24662330 370 N---LNVVCCYGGGSKWEQSKALEQGAEIIVATPGRMI-DMVKMKATNLRRVTFLVLDEADR 427
Cdd:cd17927 75 ErpgYKVTGLSGDTSENVSVEQIVESSDVIIVTPQILVnDLKSGTIVSLSDFSLLVFDECHN 136
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
295-424 |
1.01e-04 |
|
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: 44.27 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 295 IQAQAVPTAL-SGRDIIGIAKTGSGKTAAFIWPMLMHVMDQKQLKPGDgPIGLILAPTRELSLQIYNEAK-KFGKvynLN 372
Cdd:cd18023 5 IQSEVFPDLLySDKNFVVSAPTGSGKTVLFELAILRLLKERNPLPWGN-RKVVYIAPIKALCSEKYDDWKeKFGP---LG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 373 VVCC-----YGGGSKWEQskaleQGAEIIVATPGRMIDMVKMKATN---LRRVTFLVLDE 424
Cdd:cd18023 81 LSCAeltgdTEMDDTFEI-----QDADIILTTPEKWDSMTRRWRDNgnlVQLVALVLIDE 135
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
313-611 |
1.24e-04 |
|
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: 45.14 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 313 AKTGSGKT-AAFIWpmLMHVMD-QKQLKpgdgpigLILA-PTRELSLQIYNEAKK-FGkvyNLNVVccYGGGSKWEQSKA 388
Cdd:TIGR01587 6 APTGYGKTeAALLW--ALHSIKsQKADR-------VIIAlPTRATINAMYRRAKElFG---SELVG--LHHSSSFSRIKE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 389 LEQGAEIIVATPGRMIDMVKMKATNLRRVTF-------------------------LVLDEADrmfhmGFEPQVRSICNH 443
Cdd:TIGR01587 72 MGDSEEFEHLFPLYIHSNDKLFLDPITVCTIdqvlksvfgefghyeftlasianslLIFDEVH-----FYDEYTLALILA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 444 V-----RPDRQCLMFSATFKKRIERLARDVlsDPVRIVQG-DLNEANQditQSVYVFPNPLQKW----NWLLCHLVKFLS 513
Cdd:TIGR01587 147 VlevlkDNDVPILLMSATLPKFLKEYAEKI--GYVEFNEPlDLKEERR---FENHRFILIESDKvgeiSSLERLLEFIKK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 514 EGSVLIFVTKKVDAETVSNNLLIK--EYNCLLLHGDMDQADRNK----VITQFKR-KECDILVATDVAARGLDIPHirNV 586
Cdd:TIGR01587 222 GGSIAIIVNTVDRAQEFYQQLKEKapEEEIILYHSRFTEKDRAKkeaeLLREMKKsNEKFVIVATQVIEASLDISA--DV 299
|
330 340
....*....|....*....|....*
gi 24662330 587 VNYDTArDIETHTHRIGRTGRAGEK 611
Cdd:TIGR01587 300 MITELA-PIDSLIQRLGRLHRYGRK 323
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
536-581 |
1.46e-04 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 45.14 E-value: 1.46e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 24662330 536 IKEYNCLLLHGDMDQADRNKVITQFKRKECDILVATDVAARGLDIP 581
Cdd:PRK10917 503 FPELRVGLLHGRMKPAEKDAVMAAFKAGEIDILVATTVIEVGVDVP 548
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
507-607 |
2.78e-04 |
|
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: 41.87 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 507 HLVKFLSEGSVLIFVTKKVDAETVSNNLL-IKEYNCLLL-----HGDMDQADRNKVITQFKRKECDILVATDVAARGLDI 580
Cdd:cd18796 31 VIFLLERHKSTLVFTNTRSQAERLAQRLReLCPDRVPPDfialhHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDI 110
|
90 100
....*....|....*....|....*..
gi 24662330 581 PHIRNVVNYDTARDIETHTHRIGRTGR 607
Cdd:cd18796 111 GDVDLVIQIGSPKSVARLLQRLGRSGH 137
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
292-424 |
5.10e-04 |
|
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: 42.08 E-value: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 292 PTPIQAQAVPTALSGRDIIGIAKTGSGKTAAFIWPMLMHVmdQKQLKPGDGPIGLILAPTREL-SLQIYNEAKKFGKVYN 370
Cdd:cd18036 3 LRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHL--EKRRSAGEKGRVVVLVNKVPLvEQQLEKFFKYFRKGYK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 24662330 371 LNVVccYGGGSKWEQSKALEQGAEIIVATPGRMIDMVKmKATNLRRV-----TFLVLDE 424
Cdd:cd18036 81 VTGL--SGDSSHKVSFGQIVKASDVIICTPQILINNLL-SGREEERVylsdfSLLIFDE 136
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
508-622 |
6.89e-04 |
|
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: 41.14 E-value: 6.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 508 LVKFLSEGsVLIFVTK---KVDAETVSNNLLIKEYNCLLLHgdmdqADRNKVITQFKRKECDILVAT----DVAARGLDI 580
Cdd:cd18798 19 LVKKLGDG-GLIFVSIdygKEYAEELKEFLERHGIKAELAL-----SSTEKNLEKFEEGEIDVLIGVasyyGVLVRGIDL 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 24662330 581 PH-IRNVVNYDTArdIETHTHRIGRTGR--AGE--KGNAYTLVTDKD 622
Cdd:cd18798 93 PErIKYAIFYGVP--VTTYIQASGRTSRlyAGGltKGLSVVLVDDPE 137
|
|
| VirD4 |
COG3505 |
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ... |
312-372 |
8.25e-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: 42.66 E-value: 8.25e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24662330 312 IAKTGSGKTAAFIWPMLMhvmdqkQLKPGDGpiGLILAPTRELSLQIYNEAKKFG-KVYNLN 372
Cdd:COG3505 5 IGPTGSGKTVGLVIPNLT------QLARGES--VVVTDPKGDLAELTAGFRRRAGyDVYVFD 58
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
315-458 |
9.49e-04 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 40.73 E-value: 9.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 315 TGSGKTAafiwpMLMHVMDQKQLKPGDGPIgLILAPTRELSLQIYNEAKKFGKvynlnvvCCYGGGSKWEQSKALEQ--G 392
Cdd:pfam04851 32 TGSGKTL-----TAAKLIARLFKKGPIKKV-LFLVPRKDLLEQALEEFKKFLP-------NYVEIGEIISGDKKDESvdD 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24662330 393 AEIIVATP---GRMIDMVKMKATNLRRVTFLVlDEAdrmfHMGFEPQVRSICNHVRPDRQcLMFSATFK 458
Cdd:pfam04851 99 NKIVVTTIqslYKALELASLELLPDFFDVIII-DEA----HRSGASSYRNILEYFKPAFL-LGLTATPE 161
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
507-618 |
1.64e-03 |
|
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: 39.93 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662330 507 HLVKFLSEGS-VLIFVTKKVDAETVSNNLLIkeyncLLLHGDMDQADRNKVITQFKRKECDILVATDVAARGLDIPHIrN 585
Cdd:cd18789 41 ELLKRHEQGDkIIVFTDNVEALYRYAKRLLK-----PFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPEA-N 114
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 24662330 586 VV-----NYDTARDietHTHRIGRTGRAGEKGNA----YTLV 618
Cdd:cd18789 115 VAiqisgHGGSRRQ---EAQRLGRILRPKKGGGKnaffYSLV 153
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