|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
66-555 |
3.95e-174 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 506.62 E-value: 3.95e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 66 TNQQSSSGFNSGKEDDKYGRGSDGPKSDSGSRFNEAGRTGPISSNDAASGLGNASSGGSSARGPPSSAAGNELSP----- 140
Cdd:PTZ00110 4 TDGSSSNGSVSSGPSNNYNSYGPYPDSSNPYGNYQANHQDNYGGFRPGYGNYSGGYGGFGMNSYGSSTLGKRLQPidwks 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 141 -------------------------EAYCRKHEIT-VSGGQVPPPLMSFEATGLPNELLREVYSAGFSAPSPIQAQSWPI 194
Cdd:PTZ00110 84 inlvpfeknfykehpevsalsskevDEIRKEKEITiIAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 195 AMQNRDIVAIAKTGSGKTLGYLIPGFMHLQRIHN----DsrmGPTILVLSPTRELATQIQVEALKFGKSSKISCACLYGG 270
Cdd:PTZ00110 164 ALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLlrygD---GPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 271 APKGPQLKEIERGVDIVVATPGRLNDILEMKRISLHQVSYLVLDEADRMLDMGFEPQIRKIVNEVPTKRQTLMYTATWPK 350
Cdd:PTZ00110 241 VPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 351 EVRKIAADLLVN-PAQVNIGNVDeLVANKSITQTIEVLAPMEKHSRLEQIL-RSQEPGSKIIIFCSTKRMCDQLARNLtR 428
Cdd:PTZ00110 321 EVQSLARDLCKEePVHVNVGSLD-LTACHNIKQEVFVVEEHEKRGKLKMLLqRIMRDGDKILIFVETKKGADFLTKEL-R 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 429 TFG--AAAIHGDKSQAERDDVLNQFRSGRTPVLVATDVAARGLDVKDIRVVVNYDFPNGVEDYVHRIGRTGRAGATGLAY 506
Cdd:PTZ00110 399 LDGwpALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASY 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 334187683 507 TFFGDQDAKHASDLIKILEGANQKVPPQVREMATRGGGGmNKFRRWGTP 555
Cdd:PTZ00110 479 TFLTPDKYRLARDLVKVLREAKQPVPPELEKLSNERSNG-TERRRWGGY 526
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
161-535 |
1.32e-171 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 495.44 E-value: 1.32e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 161 MSFEATGLPNELLREVYSAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPgfMhLQRIHNDSRMGPTILVLS 240
Cdd:COG0513 2 MSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLP--L-LQRLDPSRPRAPQALILA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 241 PTRELATQIQVEALKFGKSSKISCACLYGGAPKGPQLKEIERGVDIVVATPGRLNDILEMKRISLHQVSYLVLDEADRML 320
Cdd:COG0513 79 PTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRML 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 321 DMGFEPQIRKIVNEVPTKRQTLMYTATWPKEVRKIAADLLVNPAQVNIGNVDELVANksITQTIEVLAPMEKHSRLEQIL 400
Cdd:COG0513 159 DMGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAET--IEQRYYLVDKRDKLELLRRLL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 401 RSQEPGsKIIIFCSTKRMCDQLARNLTRT-FGAAAIHGDKSQAERDDVLNQFRSGRTPVLVATDVAARGLDVKDIRVVVN 479
Cdd:COG0513 237 RDEDPE-RAIVFCNTKRGADRLAEKLQKRgISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVIN 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 334187683 480 YDFPNGVEDYVHRIGRTGRAGATGLAYTFFGDQDAKHasdLIKILEGANQKVPPQV 535
Cdd:COG0513 316 YDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRL---LRAIEKLIGQKIEEEE 368
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
161-520 |
4.90e-113 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 346.79 E-value: 4.90e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 161 MSFEATGLPNELLREVYSAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKT----LGYLipgfmhlQRIhNDSRMGPTI 236
Cdd:PRK11776 4 TAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTaafgLGLL-------QKL-DVKRFRVQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 237 LVLSPTRELATQIQVEALKFGKSS---KISCAClyGGAPKGPQLKEIERGVDIVVATPGRLNDILEMKRISLHQVSYLVL 313
Cdd:PRK11776 76 LVLCPTRELADQVAKEIRRLARFIpniKVLTLC--GGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 314 DEADRMLDMGFEPQIRKIVNEVPTKRQTLMYTATWPKEVRKIAADLLVNPAQVnigNVDELVANKSITQTIEVLAPMEKH 393
Cdd:PRK11776 154 DEADRMLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEV---KVESTHDLPAIEQRFYEVSPDERL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 394 SRLEQILRSQEPGSkIIIFCSTKRMCDQLARNLT-RTFGAAAIHGDKSQAERDDVLNQFRSGRTPVLVATDVAARGLDVK 472
Cdd:PRK11776 231 PALQRLLLHHQPES-CVVFCNTKKECQEVADALNaQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIK 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 334187683 473 DIRVVVNYDFPNGVEDYVHRIGRTGRAGATGLAYTFFGDQDAKHASDL 520
Cdd:PRK11776 310 ALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAI 357
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
172-367 |
3.53e-103 |
|
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: 311.61 E-value: 3.53e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 172 LLREVYSAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPGFMH------LQRIHndsrmGPTILVLSPTREL 245
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHinaqppLERGD-----GPIVLVLAPTREL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 246 ATQIQVEALKFGKSSKISCACLYGGAPKGPQLKEIERGVDIVVATPGRLNDILEMKRISLHQVSYLVLDEADRMLDMGFE 325
Cdd:cd17966 76 AQQIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 334187683 326 PQIRKIVNEVPTKRQTLMYTATWPKEVRKIAADLLVNPAQVN 367
Cdd:cd17966 156 PQIRKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
172-366 |
5.59e-100 |
|
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: 5.59e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 172 LLREVYSAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPGFMHLQRIHNDSRMGPTILVLSPTRELATQIQV 251
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 252 EALKFGKSSKISCACLYGGAPKGPQLKEIERGVDIVVATPGRLNDILEMKRISLHQVSYLVLDEADRMLDMGFEPQIRKI 331
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 334187683 332 VNEVPTKRQTLMYTATWPKEVRKIAADLLVNPAQV 366
Cdd:cd00268 161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
141-369 |
1.17e-92 |
|
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: 286.13 E-value: 1.17e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 141 EAYCRKHEITVSGGQVPPPLMSFEATGLPNELLREVYSAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPGF 220
Cdd:cd18049 4 EQYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 221 MHLQRI----HNDsrmGPTILVLSPTRELATQIQVEALKFGKSSKISCACLYGGAPKGPQLKEIERGVDIVVATPGRLND 296
Cdd:cd18049 84 VHINHQpfleRGD---GPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLID 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334187683 297 ILEMKRISLHQVSYLVLDEADRMLDMGFEPQIRKIVNEVPTKRQTLMYTATWPKEVRKIAADLLVNPAQVNIG 369
Cdd:cd18049 161 FLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIG 233
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
141-551 |
1.83e-92 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 295.54 E-value: 1.83e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 141 EAYCRKHEITVSGGQVPPPLMSFEATGLPNELLREVYSAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPGF 220
Cdd:PLN00206 101 ELLRRKLEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPII 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 221 MHLQRI---HNDSRMGPTILVLSPTRELATQIQVEALKFGKSSKISCACLYGGAPKGPQLKEIERGVDIVVATPGRLNDI 297
Cdd:PLN00206 181 SRCCTIrsgHPSEQRNPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDL 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 298 LEMKRISLHQVSYLVLDEADRMLDMGFEPQIRKIVNEVPTKrQTLMYTATWPKEVRKIAADLLVNPAQVNIGNVDElvAN 377
Cdd:PLN00206 261 LSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQALSQP-QVLLFSATVSPEVEKFASSLAKDIILISIGNPNR--PN 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 378 KSITQTIEVLAPMEKHSRLEQILRSQE----PGskiIIFCSTKRMCDQLARNLTRTFG--AAAIHGDKSQAERDDVLNQF 451
Cdd:PLN00206 338 KAVKQLAIWVETKQKKQKLFDILKSKQhfkpPA---VVFVSSRLGADLLANAITVVTGlkALSIHGEKSMKERREVMKSF 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 452 RSGRTPVLVATDVAARGLDVKDIRVVVNYDFPNGVEDYVHRIGRTGRAGATGLAYTFFGDQDAKHASDLIKILEGANQKV 531
Cdd:PLN00206 415 LVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKSSGAAI 494
|
410 420
....*....|....*....|
gi 334187683 532 PPQVREMATRGGGGMNKFRR 551
Cdd:PLN00206 495 PRELANSRYLGSGRKRKKKR 514
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
161-505 |
1.73e-91 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 290.94 E-value: 1.73e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 161 MSFEATGLPNELLREVYSAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPGFMHL--QRIHNDSRMGPTILV 238
Cdd:PRK10590 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLitRQPHAKGRRPVRALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 239 LSPTRELATQIQVEALKFGKSSKISCACLYGGAPKGPQLKEIERGVDIVVATPGRLNDILEMKRISLHQVSYLVLDEADR 318
Cdd:PRK10590 81 LTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 319 MLDMGFEPQIRKIVNEVPTKRQTLMYTATWPKEVRKIAADLLVNPAQVNIGNVDelVANKSITQTIEVLAPMEKHSRLEQ 398
Cdd:PRK10590 161 MLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRN--TASEQVTQHVHFVDKKRKRELLSQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 399 ILrSQEPGSKIIIFCSTKRMCDQLARNLTRT-FGAAAIHGDKSQAERDDVLNQFRSGRTPVLVATDVAARGLDVKDIRVV 477
Cdd:PRK10590 239 MI-GKGNWQQVLVFTRTKHGANHLAEQLNKDgIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHV 317
|
330 340
....*....|....*....|....*...
gi 334187683 478 VNYDFPNGVEDYVHRIGRTGRAGATGLA 505
Cdd:PRK10590 318 VNYELPNVPEDYVHRIGRTGRAAATGEA 345
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
130-369 |
9.52e-89 |
|
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or DEAD Box Protein P82) has a wide variety of functions including regulating the alternative splicing of exons exhibiting specific features such as the inclusion of AC-rich alternative exons in CD44 transcripts, playing a role in innate immunity, and promoting mRNA degradation mediated by the antiviral zinc-finger protein ZC3HAV1 in an ATPase-dependent manner. DDX17 synergizes with DDX5 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. DDX17 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350808 [Multi-domain] Cd Length: 271 Bit Score: 277.28 E-value: 9.52e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 130 PSSAAGNELSPEAYCRKHEITVSGGQVPPPLMSFEATGLPNELLREVYSAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGS 209
Cdd:cd18050 31 PEVARMTQYDVEELRRKKEITIRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 210 GKTLGYLIPGFMHL-QRIHNDSRMGPTILVLSPTRELATQIQVEALKFGKSSKISCACLYGGAPKGPQLKEIERGVDIVV 288
Cdd:cd18050 111 GKTLAYLLPAIVHInHQPYLERGDGPICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 289 ATPGRLNDILEMKRISLHQVSYLVLDEADRMLDMGFEPQIRKIVNEVPTKRQTLMYTATWPKEVRKIAADLLVNPAQVNI 368
Cdd:cd18050 191 ATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINI 270
|
.
gi 334187683 369 G 369
Cdd:cd18050 271 G 271
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
161-505 |
6.18e-87 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 278.36 E-value: 6.18e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 161 MSFEATGLPNELLREVYSAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPGFMHLQRIHNDSRMGPTILVLS 240
Cdd:PRK11192 1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRKSGPPRILILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 241 PTRELATQIQVEALKFGKSSKISCACLYGGAPKGPQLKEIERGVDIVVATPGRLNDILEMKRISLHQVSYLVLDEADRML 320
Cdd:PRK11192 81 PTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 321 DMGFEPQIRKIVNEVPTKRQTLMYTATWPKE-VRKIAADLLVNPAQVNignvdelvAN------KSITQTIEvLAPMEKH 393
Cdd:PRK11192 161 DMGFAQDIETIAAETRWRKQTLLFSATLEGDaVQDFAERLLNDPVEVE--------AEpsrrerKKIHQWYY-RADDLEH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 394 SR--LEQILRsQEPGSKIIIFCSTKRMCDQLARNL-TRTFGAAAIHGDKSQAERDDVLNQFRSGRTPVLVATDVAARGLD 470
Cdd:PRK11192 232 KTalLCHLLK-QPEVTRSIVFVRTRERVHELAGWLrKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGID 310
|
330 340 350
....*....|....*....|....*....|....*
gi 334187683 471 VKDIRVVVNYDFPNGVEDYVHRIGRTGRAGATGLA 505
Cdd:PRK11192 311 IDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTA 345
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
162-362 |
1.43e-86 |
|
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: 269.74 E-value: 1.43e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 162 SFEATGLPNELLREVYSAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPGFMHL--QRIHNDSRMG----PT 235
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLleDGPPSVGRGRrkayPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 236 ILVLSPTRELATQIQVEALKFGKSSKISCACLYGGAPKGPQLKEIERGVDIVVATPGRLNDILEMKRISLHQVSYLVLDE 315
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 334187683 316 ADRMLDMGFEPQIRKIVNE----VPTKRQTLMYTATWPKEVRKIAADLLVN 362
Cdd:cd17967 161 ADRMLDMGFEPQIRKIVEHpdmpPKGERQTLMFSATFPREIQRLAADFLKN 211
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
163-514 |
1.57e-83 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 270.63 E-value: 1.57e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 163 FEATGLPNELLREVYSAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPGFMHLQR--IHNDSRMG-PTILVL 239
Cdd:PRK01297 89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQtpPPKERYMGePRALII 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 240 SPTRELATQIQVEALKFGKSSKISCACLYGGAPKGPQLKEIE-RGVDIVVATPGRLNDILEMKRISLHQVSYLVLDEADR 318
Cdd:PRK01297 169 APTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEADR 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 319 MLDMGFEPQIRKIVNEVPTK--RQTLMYTATWPKEVRKIAADLLVNPAQVNIGnvDELVANKSITQTIEVLAPMEKHSRL 396
Cdd:PRK01297 249 MLDMGFIPQVRQIIRQTPRKeeRQTLLFSATFTDDVMNLAKQWTTDPAIVEIE--PENVASDTVEQHVYAVAGSDKYKLL 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 397 EQILRsQEPGSKIIIFCSTKRMCDQLARNLTRT-FGAAAIHGDKSQAERDDVLNQFRSGRTPVLVATDVAARGLDVKDIR 475
Cdd:PRK01297 327 YNLVT-QNPWERVMVFANRKDEVRRIEERLVKDgINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGIS 405
|
330 340 350
....*....|....*....|....*....|....*....
gi 334187683 476 VVVNYDFPNGVEDYVHRIGRTGRAGATGLAYTFFGDQDA 514
Cdd:PRK01297 406 HVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDA 444
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
150-366 |
1.06e-78 |
|
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: 249.22 E-value: 1.06e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 150 TVSGGQVPPPLMSFEATGLPNELLREVYSAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPGFMHL--QRIH 227
Cdd:cd17953 1 KVRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIkdQRPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 228 NDSRmGPTILVLSPTRELATQIQVEALKFGKSSKISCACLYGGAPKGPQLKEIERGVDIVVATPGRLNDILEM---KRIS 304
Cdd:cd17953 81 KPGE-GPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTAnngRVTN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334187683 305 LHQVSYLVLDEADRMLDMGFEPQIRKIVNEVPTKRQTLMYTATWPKEVRKIAADLLVNPAQV 366
Cdd:cd17953 160 LRRVTYVVLDEADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
163-508 |
7.30e-78 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 254.13 E-value: 7.30e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 163 FEATGLPNELLREVYSAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPGFMHL--QRIHNDSRM-GPTILVL 239
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLlsHPAPEDRKVnQPRALIM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 240 SPTRELATQIQVEALKFGKSSKISCACLYGGAPKGPQLKEIERGVDIVVATPGRLNDILEMKRISLHQVSYLVLDEADRM 319
Cdd:PRK04837 90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 320 LDMGFEPQIRKIVNEVP--TKRQTLMYTATWPKEVRKIAADLLVNPAQVNIGnvDELVANKSITQtiEVLAP-MEKHSRL 396
Cdd:PRK04837 170 FDLGFIKDIRWLFRRMPpaNQRLNMLFSATLSYRVRELAFEHMNNPEYVEVE--PEQKTGHRIKE--ELFYPsNEEKMRL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 397 EQILRSQEPGSKIIIFCSTKRMCDQLARNLtrtfgAAAIH------GDKSQAERDDVLNQFRSGRTPVLVATDVAARGLD 470
Cdd:PRK04837 246 LQTLIEEEWPDRAIIFANTKHRCEEIWGHL-----AADGHrvglltGDVAQKKRLRILEEFTRGDLDILVATDVAARGLH 320
|
330 340 350
....*....|....*....|....*....|....*...
gi 334187683 471 VKDIRVVVNYDFPNGVEDYVHRIGRTGRAGATGLAYTF 508
Cdd:PRK04837 321 IPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
151-360 |
2.87e-76 |
|
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: 244.49 E-value: 2.87e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 151 VSGGQVPPPLMSFEATGLPNELLREVYSAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIP---GFMHlQRIH 227
Cdd:cd18052 33 VTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPvltGMMK-EGLT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 228 NDSRMG---PTILVLSPTRELATQIQVEALKFGKSSKISCACLYGGAPKGPQLKEIERGVDIVVATPGRLNDILEMKRIS 304
Cdd:cd18052 112 ASSFSEvqePQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKIS 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 305 LHQVSYLVLDEADRMLDMGFEPQIRKIVNE--VPTK--RQTLMYTATWPKEVRKIAADLL 360
Cdd:cd18052 192 LSKLKYLILDEADRMLDMGFGPEIRKLVSEpgMPSKedRQTLMFSATFPEEIQRLAAEFL 251
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
172-366 |
6.18e-75 |
|
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: 238.47 E-value: 6.18e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 172 LLREVYSAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPGFMHLQrihnDSRM-----GPTILVLSPTRELA 246
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIM----DQRElekgeGPIAVIVAPTRELA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 247 TQIQVEALKFGKSSKISCACLYGGAPKGPQLKEIERGVDIVVATPGRLNDILEMKRISLHQVSYLVLDEADRMLDMGFEP 326
Cdd:cd17952 77 QQIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEY 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 334187683 327 QIRKIVNEVPTKRQTLMYTATWPKEVRKIAADLLVNPAQV 366
Cdd:cd17952 157 QVRSIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
161-508 |
7.99e-75 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 252.08 E-value: 7.99e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 161 MSFEATGLPNELLREVYSAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPGFMHLqrihNDSRMGPTILVLS 240
Cdd:PRK11634 6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNL----DPELKAPQILVLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 241 PTRELATQIQVEALKFGKSSK-ISCACLYGGAPKGPQLKEIERGVDIVVATPGRLNDILEMKRISLHQVSYLVLDEADRM 319
Cdd:PRK11634 82 PTRELAVQVAEAMTDFSKHMRgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 320 LDMGFEPQIRKIVNEVPTKRQTLMYTATWPKEVRKIAADLLVNPAQVNIGNvdELVANKSITQTIEVLAPMEKHSRLEQI 399
Cdd:PRK11634 162 LRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQS--SVTTRPDISQSYWTVWGMRKNEALVRF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 400 LRSqEPGSKIIIFCSTKRMCDQLARNLTRT-FGAAAIHGDKSQAERDDVLNQFRSGRTPVLVATDVAARGLDVKDIRVVV 478
Cdd:PRK11634 240 LEA-EDFDAAIIFVRTKNATLEVAEALERNgYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVV 318
|
330 340 350
....*....|....*....|....*....|
gi 334187683 479 NYDFPNGVEDYVHRIGRTGRAGATGLAYTF 508
Cdd:PRK11634 319 NYDIPMDSESYVHRIGRTGRAGRAGRALLF 348
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
172-366 |
1.67e-74 |
|
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: 237.36 E-value: 1.67e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 172 LLREVYSAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPGFMHL--QRIHNDSRMGPTILVLSPTRELATQI 249
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLdlQPIPREQRNGPGVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 250 QVEALKFgKSSKISCACLYGGAPKGPQLKEIERGVDIVVATPGRLNDILEMKRISLHQVSYLVLDEADRMLDMGFEPQIR 329
Cdd:cd17958 81 EAECSKY-SYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 334187683 330 KIVNEVPTKRQTLMYTATWPKEVRKIAADLLVNPAQV 366
Cdd:cd17958 160 KILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
161-540 |
5.45e-74 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 248.33 E-value: 5.45e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 161 MSFEATGLPNELLREVYSAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPGFMHLQR---IHNDSRMGPTIL 237
Cdd:PRK04537 9 LTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSrpaLADRKPEDPRAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 238 VLSPTRELATQIQVEALKFGKSSKISCACLYGGAPKGPQLKEIERGVDIVVATPGRLNDILEM-KRISLHQVSYLVLDEA 316
Cdd:PRK04537 89 ILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQhKVVSLHACEICVLDEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 317 DRMLDMGFEPQIRKIVNEVP--TKRQTLMYTATWPKEVRKIAADLLVNPAQVNIGNvdELVANKSITQTIEVLAPMEKHS 394
Cdd:PRK04537 169 DRMFDLGFIKDIRFLLRRMPerGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVET--ETITAARVRQRIYFPADEEKQT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 395 RLEQILrSQEPGSKIIIFCSTKRMCDQLARNLTRT-FGAAAIHGDKSQAERDDVLNQFRSGRTPVLVATDVAARGLDVKD 473
Cdd:PRK04537 247 LLLGLL-SRSEGARTMVFVNTKAFVERVARTLERHgYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDG 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334187683 474 IRVVVNYDFPNGVEDYVHRIGRTGRAGATGLAYTFFGDQDAKHASDLIKILEganQKVP--PQVREMAT 540
Cdd:PRK04537 326 VKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIE---QKIPvePVTAELLT 391
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
162-520 |
1.92e-73 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 241.65 E-value: 1.92e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 162 SFEATGLPNELLREVYSAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPGfmhLQRIhNDSRMGPTILVLSP 241
Cdd:PTZ00424 29 SFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAA---LQLI-DYDLNACQALILAP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 242 TRELATQIQVEALKFGKSSKISCACLYGGAPKGPQLKEIERGVDIVVATPGRLNDILEMKRISLHQVSYLVLDEADRMLD 321
Cdd:PTZ00424 105 TRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 322 MGFEPQIRKIVNEVPTKRQTLMYTATWPKEVRKIAADLLVNPAQVNIGNvDELVAnKSITQtIEVLAPMEKHsRLEQILR 401
Cdd:PTZ00424 185 RGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKK-DELTL-EGIRQ-FYVAVEKEEW-KFDTLCD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 402 SQEPGS--KIIIFCSTKRMCDQLARNLT-RTFGAAAIHGDKSQAERDDVLNQFRSGRTPVLVATDVAARGLDVKDIRVVV 478
Cdd:PTZ00424 261 LYETLTitQAIIYCNTRRKVDYLTKKMHeRDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVI 340
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 334187683 479 NYDFPNGVEDYVHRIGRTGRAGATGLAYTFFGDQDAKHASDL 520
Cdd:PTZ00424 341 NYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEI 382
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
172-366 |
6.19e-70 |
|
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and PRP28 homolog) is involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation. Diseases associated with DDX23 include distal hereditary motor neuropathy, type II. DDX23 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350703 [Multi-domain] Cd Length: 220 Bit Score: 226.05 E-value: 6.19e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 172 LLREVYSAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPGFMHLQRI----HNDSRMGPTILVLSPTRELAT 247
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLppldEETKDDGPYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 248 QIQVEALKFGKSSKISCACLYGGAPKGPQLKEIERGVDIVVATPGRLNDILEMKRISLHQVSYLVLDEADRMLDMGFEPQ 327
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 334187683 328 IRKIVNEVPTK--------------------RQTLMYTATWPKEVRKIAADLLVNPAQV 366
Cdd:cd17945 161 VTKILDAMPVSnkkpdteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
151-362 |
2.56e-65 |
|
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: 215.29 E-value: 2.56e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 151 VSGGQVPPPLMSFEATGLPNELLREVYSAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIP----------GF 220
Cdd:cd18051 11 ATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPilsqiyeqgpGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 221 MHLQRIHNDSRMG--PTILVLSPTRELATQIQVEALKFGKSSKISCACLYGGAPKGPQLKEIERGVDIVVATPGRLNDIL 298
Cdd:cd18051 91 SLPSESGYYGRRKqyPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDML 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334187683 299 EMKRISLHQVSYLVLDEADRMLDMGFEPQIRKIVNE---VPT-KRQTLMYTATWPKEVRKIAADLLVN 362
Cdd:cd18051 171 ERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQdtmPPTgERQTLMFSATFPKEIQMLARDFLDN 238
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
380-509 |
2.47e-62 |
|
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: 202.74 E-value: 2.47e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 380 ITQTIEVLAPMEKHSRLEQILRSQEPGSKIIIFCSTKRMCDQLARNLTRT-FGAAAIHGDKSQAERDDVLNQFRSGRTPV 458
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELgIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 334187683 459 LVATDVAARGLDVKDIRVVVNYDFPNGVEDYVHRIGRTGRAGATGLAYTFF 509
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
168-357 |
3.32e-62 |
|
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: 205.51 E-value: 3.32e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 168 LPNELLREVYSAGFSAPSPIQAQSWPIAMQNR-DIVAIAKTGSGKTLGYLIPGFMHLQRIHNDSRMGPT-ILVLSPTREL 245
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILSTGdDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGVsALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 246 ATQIQVEALKF-GKSSKISCACLYGGAPKGPQLKEIER-GVDIVVATPGRLNDILE--MKRISLHQVSYLVLDEADRMLD 321
Cdd:cd17964 81 ALQIAAEAKKLlQGLRKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRLLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 334187683 322 MGFEPQIRKIVNEVPTK----RQTLMYTATWPKEVRKIAA 357
Cdd:cd17964 161 MGFRPDLEQILRHLPEKnadpRQTLLFSATVPDEVQQIAR 200
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
185-355 |
5.72e-62 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 203.24 E-value: 5.72e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 185 SPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPGFMHLQRIHNdsrmGPTILVLSPTRELATQIQVEALKFGKSSKISC 264
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDN----GPQALVLAPTRELAEQIYEELKKLGKGLGLKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 265 ACLYGGAPKGPQLKEIeRGVDIVVATPGRLNDILEmKRISLHQVSYLVLDEADRMLDMGFEPQIRKIVNEVPTKRQTLMY 344
Cdd:pfam00270 77 ASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQ-ERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLL 154
|
170
....*....|.
gi 334187683 345 TATWPKEVRKI 355
Cdd:pfam00270 155 SATLPRNLEDL 165
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
162-366 |
1.33e-57 |
|
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: 192.92 E-value: 1.33e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 162 SFEATGLPNELLREVYSAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPGFMHLqrIHNDSRMgpTILVLSP 241
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQAL--LENPQRF--FALVLAP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 242 TRELATQI--QVEALkfGKSSKISCACLYGGAPKGPQLKEIERGVDIVVATPGRLNDILE-MKRISLHQVSYLVLDEADR 318
Cdd:cd17954 77 TRELAQQIseQFEAL--GSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLEnTKGFSLKSLKFLVMDEADR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 334187683 319 MLDMGFEPQIRKIVNEVPTKRQTLMYTATWPKEVRKIAADLLVNPAQV 366
Cdd:cd17954 155 LLNMDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
162-367 |
3.18e-57 |
|
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: 192.13 E-value: 3.18e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 162 SFEATGLPNELLREVYSAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPGFMHLQRIHndSRMGPTILVLSP 241
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHS--PTVGARALILSP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 242 TRELATQIQVEALKFGKSSKISCACLYGGAPKGPQLKEIERGVDIVVATPGRLNDILEMKRISLHQVSYLVLDEADRMLD 321
Cdd:cd17959 80 TRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 334187683 322 MGFEPQIRKIVNEVPTKRQTLMYTATWPKEVRKIAADLLVNPAQVN 367
Cdd:cd17959 160 MGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
172-367 |
2.96e-56 |
|
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: 189.47 E-value: 2.96e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 172 LLREVYSAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPgfMHLQRIHNDSRM------GPTILVLSPTREL 245
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLP--LIMFALEQEKKLpfikgeGPYGLIVCPSREL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 246 ATQIQ------VEALKFGKSSKISCACLYGGAPKGPQLKEIERGVDIVVATPGRLNDILEMKRISLHQVSYLVLDEADRM 319
Cdd:cd17951 79 ARQTHevieyyCKALQEGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 334187683 320 LDMGFEPQIRKIVNEVPTKRQTLMYTATWPKEVRKIAADLLVNPAQVN 367
Cdd:cd17951 159 IDMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTVN 206
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
172-366 |
3.47e-55 |
|
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: 186.31 E-value: 3.47e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 172 LLREVYSAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPgfmHLQRIHNDSRMGPTI--LVLSPTRELATQI 249
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLP---ILERLLYRPKKKAATrvLVLVPTRELAMQC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 250 QVEALKFGKSSKISCACLYGGAPKGPQLKEIERGVDIVVATPGRLNDILEMKR-ISLHQVSYLVLDEADRMLDMGFEPQI 328
Cdd:cd17947 78 FSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGFADEL 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 334187683 329 RKIVNEVPTKRQTLMYTATWPKEVRKIAADLLVNPAQV 366
Cdd:cd17947 158 KEILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
176-369 |
2.13e-54 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 184.23 E-value: 2.13e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 176 VYSAGFSAPSPIQAQSWPIAMQN-RDIVAIAKTGSGKTLGYLIPGFMHLQRihndsRMGPTILVLSPTRELATQIQVEAL 254
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKR-----GKGGRVLVLVPTRELAEQWAEELK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 255 KFGKSSKISCACLYGGAPKGPQLKEIERGV-DIVVATPGRLNDILEMKRISLHQVSYLVLDEADRMLDMGFEPQIRKIVN 333
Cdd:smart00487 76 KLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLK 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 334187683 334 EVPTKRQTLMYTATWPKEVRKIAADLLVNPAQVNIG 369
Cdd:smart00487 156 LLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVG 191
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
163-367 |
6.87e-54 |
|
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: 182.88 E-value: 6.87e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 163 FEATGLPNELLREVYSAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPgfmHLQRIHNDSRmGPTILVLSPT 242
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIP---ILEKIDPKKD-VIQALILVPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 243 RELATQIQVEALKFGKSSKISCACLYGGAPKGPQLKEIERGVDIVVATPGRLNDILEMKRISLHQVSYLVLDEADRMLDM 322
Cdd:cd17940 77 RELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQ 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 334187683 323 GFEPQIRKIVNEVPTKRQTLMYTATWPKEVRKIAADLLVNPAQVN 367
Cdd:cd17940 157 DFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEIN 201
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
172-369 |
4.71e-53 |
|
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: 180.48 E-value: 4.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 172 LLREVYSAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPGFMHLQRIHNDSrmGPTILVLSPTRELATQIQV 251
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKK--GLRALILAPTRELASQIYR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 252 EALKFGKSSKISCACLYGG-APKGPQLKEIERGVDIVVATPGRLNDILEMKRISLHQVSYLVLDEADRMLDMGFEPQIRK 330
Cdd:cd17957 79 ELLKLSKGTGLRIVLLSKSlEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 334187683 331 IVNEVPTKR-QTLMYTATWPKEVRKIAADLLVNPAQVNIG 369
Cdd:cd17957 159 ILAACTNPNlQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
172-367 |
5.60e-52 |
|
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: 177.77 E-value: 5.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 172 LLREVYSAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPGF-MHLQRIHNDSRMGPTILVLSPTRELATQIQ 250
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLeILLKRKANLKKGQVGALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 251 VEALKFGK--SSKISCACLYGGAPKGPQLKEIER-GVDIVVATPGRLNDILEMK--RISLHQVSYLVLDEADRMLDMGFE 325
Cdd:cd17960 81 EVLQSFLEhhLPKLKCQLLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLSRKadKVKVKSLEVLVLDEADRLLDLGFE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 334187683 326 PQIRKIVNEVPTKRQTLMYTATWPKEVRKIAADLLVNPAQVN 367
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRVV 202
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
163-363 |
5.30e-49 |
|
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: 170.10 E-value: 5.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 163 FEATGLPNELLREVYSAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPgfmHLQRIHNDSrMGPTILVLSPT 242
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALP---ILQRLSEDP-YGIFALVLTPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 243 RELATQIQVEALKFGKSSKISCACLYGGAPKGPQLKEIERGVDIVVATPGRLNDILE---MKRISLHQVSYLVLDEADRM 319
Cdd:cd17955 77 RELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEADRL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 334187683 320 LDMGFEPQIRKIVNEVPTKRQTLMYTATWPKEVRKIAADLLVNP 363
Cdd:cd17955 157 LTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKP 200
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
180-363 |
4.11e-48 |
|
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1. DDX31 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350707 [Multi-domain] Cd Length: 214 Bit Score: 167.76 E-value: 4.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 180 GFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPGFMHLQ----RIHNDSrmGPTILVLSPTRELATQIQVEALK 255
Cdd:cd17949 10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLslepRVDRSD--GTLALVLVPTRELALQIYEVLEK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 256 FGKSSK-ISCACLYGGAPKGPQLKEIERGVDIVVATPGRLNDILEM-KRISLHQVSYLVLDEADRMLDMGFEPQIRKIVN 333
Cdd:cd17949 88 LLKPFHwIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNtQSFDVSNLRWLVLDEADRLLDMGFEKDITKILE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 334187683 334 EV-------------PTKRQTLMYTATWPKEVRKIAADLLVNP 363
Cdd:cd17949 168 LLddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDP 210
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
173-368 |
2.17e-47 |
|
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: 165.16 E-value: 2.17e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 173 LREvysAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPGFMHLQRIHNDSRMGPTILVLSPTRELATQIqVE 252
Cdd:cd17941 5 LKE---AGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTPEDGLGALIISPTRELAMQI-FE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 253 AL-KFGKSSKISCACLYGGAPKGPQLKEIERgVDIVVATPGR-LNDILEMKRISLHQVSYLVLDEADRMLDMGFEPQIRK 330
Cdd:cd17941 81 VLrKVGKYHSFSAGLIIGGKDVKEEKERINR-MNILVCTPGRlLQHMDETPGFDTSNLQMLVLDEADRILDMGFKETLDA 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 334187683 331 IVNEVPTKRQTLMYTATWPKEVRKIAADLLVNPAQVNI 368
Cdd:cd17941 160 IVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
172-366 |
3.94e-47 |
|
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: 164.64 E-value: 3.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 172 LLREVYSAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPGFMHLQRIHNDsrmgPTILVLSPTRELATQIQV 251
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRN----PSALILTPTRELAVQIED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 252 EALKFGKSS-KISCACLYGGAPKGPQLKEIERGVDIVVATPGRLNDILEMKRISLHQVSYLVLDEADRMLDMGFEPQIRK 330
Cdd:cd17962 77 QAKELMKGLpPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLD 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 334187683 331 IVNEVPTKRQTLMYTATWPKEVRKIAADLLVNPAQV 366
Cdd:cd17962 157 ILENISHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
180-356 |
1.62e-45 |
|
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: 160.22 E-value: 1.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 180 GFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPGFMHLQRIHNDSRMGPTILVLSPTRELATQIQVEALKFGKS 259
Cdd:cd17942 9 GFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRNGTGVIIISPTRELALQIYGVAKELLKY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 260 SKISCACLYGGAPKGPQLKEIERGVDIVVATPGRLNDILE-MKRISLHQVSYLVLDEADRMLDMGFEPQIRKIVNEVPTK 338
Cdd:cd17942 89 HSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQnTKGFLYKNLQCLIIDEADRILEIGFEEEMRQIIKLLPKR 168
|
170
....*....|....*...
gi 334187683 339 RQTLMYTATWPKEVRKIA 356
Cdd:cd17942 169 RQTMLFSATQTRKVEDLA 186
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
167-368 |
2.55e-45 |
|
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: 159.80 E-value: 2.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 167 GLPNELLREVYSAGFSAPSPIQAQS-WPIaMQNRDIVAIAKTGSGKTLGYLIpgfMHLQRIHNDSRMgPTILVLSPTREL 245
Cdd:cd17939 3 GLSEDLLRGIYAYGFEKPSAIQQRAiVPI-IKGRDVIAQAQSGTGKTATFSI---GALQRIDTTVRE-TQALVLAPTREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 246 ATQIQVEALKFGKSSKISCACLYGGAPKGPQLKEIERGVDIVVATPGRLNDILEMKRISLHQVSYLVLDEADRMLDMGFE 325
Cdd:cd17939 78 AQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFK 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 334187683 326 PQIRKIVNEVPTKRQTLMYTATWPKEVRKIAADLLVNPaqVNI 368
Cdd:cd17939 158 DQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDP--VRI 198
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
172-347 |
4.78e-44 |
|
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: 157.40 E-value: 4.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 172 LLREVYSAGFSAPSPIQAQSWPIAMQNR-DIVAIAKTGSGKTLGYLIPGFMHL-----QRIHNDSRMGPTILVLSPTREL 245
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRDGkDVIGAAETGSGKTLAFGIPILERLlsqksSNGVGGKQKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 246 ATQIQ--VEALkfGKSSKISCACLYGG--APKgpQLKEIERGVDIVVATPGRLNDILEMKR---ISLHQVSYLVLDEADR 318
Cdd:cd17946 81 AVQVKdhLKAI--AKYTNIKIASIVGGlaVQK--QERLLKKRPEIVVATPGRLWELIQEGNehlANLKSLRFLVLDEADR 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 334187683 319 MLDMG-FEP--QIRKIVNEVPT----KRQTLMYTAT 347
Cdd:cd17946 157 MLEKGhFAEleKILELLNKDRAgkkrKRQTFVFSAT 192
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
168-366 |
8.72e-41 |
|
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: 147.34 E-value: 8.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 168 LPNELLREVYSAGFSAPSPIQAQSWPIAMQN--RDIVAIAKTGSGKTLGYLIPGfmhLQRIHNDSRMgPTILVLSPTREL 245
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAM---LSRVDPTLKS-PQALCLAPTREL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 246 ATQIQVEALKFGKSSKISCAClyggAPKGPQLKEIERGVD-IVVATPGRLNDILEMKRISLHQVSYLVLDEADRMLDM-G 323
Cdd:cd17963 77 ARQIGEVVEKMGKFTGVKVAL----AVPGNDVPRGKKITAqIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqG 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 334187683 324 FEPQIRKIVNEVPTKRQTLMYTATWPKEVRKIAADLLVNPAQV 366
Cdd:cd17963 153 HGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
186-356 |
8.92e-41 |
|
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: 147.30 E-value: 8.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 186 PIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPGFMHLQRIHNDSRMG--PTILVLSPTRELATQIQVEALKFGKssKIS 263
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRGraPKVLVLAPTRELANQVTKDFKDITR--KLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 264 CACLYGGAPKGPQLKEIERGVDIVVATPGRLNDILEMKRISLHQVSYLVLDEADRMLDMGFEPQIRKIVNEVPTKR---- 339
Cdd:cd17944 93 VACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSVSYKKDsedn 172
|
170
....*....|....*...
gi 334187683 340 -QTLMYTATWPKEVRKIA 356
Cdd:cd17944 173 pQTLLFSATCPDWVYNVA 190
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
162-366 |
4.18e-40 |
|
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: 145.95 E-value: 4.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 162 SFEATGLPNELLREVYSAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPGfmhLQRIhNDSRMGPTILVLSP 241
Cdd:cd17950 3 GFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLST---LQQL-EPVDGQVSVLVICH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 242 TRELATQIQVEALKFGKSSK-ISCACLYGGAPKGPQLKEIERGV-DIVVATPGRLNDILEMKRISLHQVSYLVLDEADRM 319
Cdd:cd17950 79 TRELAFQISNEYERFSKYMPnVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 334187683 320 L-DMGFEPQIRKIVNEVPTKRQTLMYTATWPKEVRKIAADLLVNPAQV 366
Cdd:cd17950 159 LeQLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEI 206
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
163-366 |
2.09e-39 |
|
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: 143.76 E-value: 2.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 163 FEATGLPNELLREVYSAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPGfmhLQRIHNDSRmGPTILVLSPT 242
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISV---LQCLDIQVR-ETQALILSPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 243 RELATQIQVEALKFGKSSKISCACLYGGAPKGPQLKEIERGVDIVVATPGRLNDILEMKRISLHQVSYLVLDEADRMLDM 322
Cdd:cd18045 77 RELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 334187683 323 GFEPQIRKIVNEVPTKRQTLMYTATWPKEVRKIAADLLVNPAQV 366
Cdd:cd18045 157 GFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
163-367 |
4.19e-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: 142.85 E-value: 4.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 163 FEATGLPNELLREVYSAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPgfmHLQRIhndsrmgpTILVLSPT 242
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLP---VLQIV--------VALILEPS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 243 RELATQI--QVEALK-FGKSSKISCACLYGGAPKGPQLKEIERGVDIVVATPGRLNDILEMKRISLHQVSYLVLDEADRM 319
Cdd:cd17938 70 RELAEQTynCIENFKkYLDNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 334187683 320 LDMGFEPQIRKIVNEVPT-----KR-QTLMYTATWPK-EVRKIAADLLVNPAQVN 367
Cdd:cd17938 150 LSQGNLETINRIYNRIPKitsdgKRlQVIVCSATLHSfEVKKLADKIMHFPTWVD 204
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
391-500 |
6.55e-39 |
|
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: 138.88 E-value: 6.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 391 EKHSRLEQILRSqEPGSKIIIFCSTKRMCDqlARNLTRTFG--AAAIHGDKSQAERDDVLNQFRSGRTPVLVATDVAARG 468
Cdd:pfam00271 1 EKLEALLELLKK-ERGGKVLIFSQTKKTLE--AELLLEKEGikVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77
|
90 100 110
....*....|....*....|....*....|..
gi 334187683 469 LDVKDIRVVVNYDFPNGVEDYVHRIGRTGRAG 500
Cdd:pfam00271 78 LDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
163-366 |
3.88e-38 |
|
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: 140.27 E-value: 3.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 163 FEATGLPNELLREVYSAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPGfmhLQRIHNDSRmGPTILVLSPT 242
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISI---LQQIDTSLK-ATQALVLAPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 243 RELATQIQVEALKFGKSSKISC-ACLyGGAPKGPQLKEIERGVDIVVATPGRLNDILEMKRISLHQVSYLVLDEADRMLD 321
Cdd:cd18046 77 RELAQQIQKVVMALGDYMGIKChACI-GGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 334187683 322 MGFEPQIRKIVNEVPTKRQTLMYTATWPKEVRKIAADLLVNPAQV 366
Cdd:cd18046 156 RGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
172-364 |
3.94e-37 |
|
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: 137.33 E-value: 3.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 172 LLREVYSAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPgfmHLQRI-----HNDSRMGPTILVLSPTRELA 246
Cdd:cd17961 5 LLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALP---IIQKIlkakaESGEEQGTRALILVPTRELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 247 TQIQVEALKFGK--SSKISCACLYGGAPKGPQLKEIERGVDIVVATPGRLNDILEMKRISL-HQVSYLVLDEADRMLDMG 323
Cdd:cd17961 82 QQVSKVLEQLTAycRKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLlSTLKYLVIDEADLVLSYG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 334187683 324 FEPQIRKIVNEVPTKRQTLMYTATWPKEVRKIAADLLVNPA 364
Cdd:cd17961 162 YEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
172-350 |
6.50e-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: 136.24 E-value: 6.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 172 LLREVYSAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPGFMHLQRihndSRMGPTILVLSPTRELATQIQV 251
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDL----ERRHPQVLILAPTREIAVQIHD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 252 EALKFGKSSK-ISCACLYGGAPKGPQLKEIeRGVDIVVATPGRLNDILEMKRISLHQVSYLVLDEADRMLDMGFEPQIRK 330
Cdd:cd17943 77 VFKKIGKKLEgLKCEVFIGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNW 155
|
170 180
....*....|....*....|
gi 334187683 331 IVNEVPTKRQTLMYTATWPK 350
Cdd:cd17943 156 IFSSLPKNKQVIAFSATYPK 175
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
169-513 |
1.88e-34 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 137.19 E-value: 1.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 169 PNELLREVYsaGFSAPSPIQAQswpI---AMQNRDIVAIAKTGSGKTLGYLIPGFMhlqrihndsRMGPTILVlSPtreL 245
Cdd:COG0514 5 ALEVLKRVF--GYDSFRPGQEE---IieaVLAGRDALVVMPTGGGKSLCYQLPALL---------LPGLTLVV-SP---L 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 246 atqI-----QVEALKfgkSSKISCACLYGGAPKGPQ---LKEIERG-VDIVVATPGRLN-----DILEMKRISLhqvsyL 311
Cdd:COG0514 67 ---IalmkdQVDALR---AAGIRAAFLNSSLSAEERrevLRALRAGeLKLLYVAPERLLnprflELLRRLKISL-----F 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 312 VLDEA--------DrmldmgFEP---QIRKIVNEVPtKRQTLMYTATWPKEVRK-IAADLLVNPAQVNIGNVDElvanKS 379
Cdd:COG0514 136 AIDEAhcisqwghD------FRPdyrRLGELRERLP-NVPVLALTATATPRVRAdIAEQLGLEDPRVFVGSFDR----PN 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 380 ITQTIEVLAPMEKHSRLEQILRSQEPGSkIIIFCSTKRMCDQLARNLT-RTFGAAAIHGDKSQAERDDVLNQFRSGRTPV 458
Cdd:COG0514 205 LRLEVVPKPPDDKLAQLLDFLKEHPGGS-GIVYCLSRKKVEELAEWLReAGIRAAAYHAGLDAEEREANQDRFLRDEVDV 283
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 334187683 459 LVATdVA-ARGLDVKDIRVVVNYDFPNGVEDYVHRIGRTGRAGATGLAYTFFGDQD 513
Cdd:COG0514 284 IVAT-IAfGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPED 338
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
180-367 |
5.72e-32 |
|
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: 123.63 E-value: 5.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 180 GFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPgFMH--LQRIHNDSRMGPTI--LVLSPTRELATQIQVEALK 255
Cdd:cd17948 9 GITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLP-IIQrlLRYKLLAEGPFNAPrgLVITPSRELAEQIGSVAQS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 256 FGKSSKISCACLYGGAPKGpQLKEIERG-VDIVVATPGRLNDILEMKRISLHQVSYLVLDEADRMLDMGFEPQIRKIVNE 334
Cdd:cd17948 88 LTEGLGLKVKVITGGRTKR-QIRNPHFEeVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKLSHFLRR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 334187683 335 VP-------------TKRQTLMYTATWPKEVRKIAADlLVNPAQVN 367
Cdd:cd17948 167 FPlasrrsentdgldPGTQLVLVSATMPSGVGEVLSK-VIDVDSIE 211
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
420-500 |
6.47e-29 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 109.99 E-value: 6.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 420 DQLARNLT-RTFGAAAIHGDKSQAERDDVLNQFRSGRTPVLVATDVAARGLDVKDIRVVVNYDFPNGVEDYVHRIGRTGR 498
Cdd:smart00490 1 EELAELLKeLGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 334187683 499 AG 500
Cdd:smart00490 81 AG 82
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
180-355 |
6.18e-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: 106.56 E-value: 6.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 180 GFSAPSPIQAQSWP--IAMQN-------RDIVAIAKTGSGKTLGYLIPgfmHLQRIHndSRMGPTI--LVLSPTRELATQ 248
Cdd:cd17956 9 GITSAFPVQAAVIPwlLPSSKstppyrpGDLCVSAPTGSGKTLAYVLP---IVQALS--KRVVPRLraLIVVPTKELVQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 249 IQVEALKFGKSSKISCACLYGG---APKGPQLKEIERG-----VDIVVATPGRLNDILEMKR-ISLHQVSYLVLDEADRM 319
Cdd:cd17956 84 VYKVFESLCKGTGLKVVSLSGQksfKKEQKLLLVDTSGrylsrVDILVATPGRLVDHLNSTPgFTLKHLRFLVIDEADRL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 334187683 320 LDMGFEPQIRKIVNEV-------PTKRQTLMYTATWPKEVRKI 355
Cdd:cd17956 164 LNQSFQDWLETVMKALgrptapdLGSFGDANLLERSVRPLQKL 206
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
198-478 |
7.74e-25 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 108.96 E-value: 7.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 198 NRDIVAIAKTGSGKT-LGYLIpgfmhLQRIHNDSRmgptILVLSPTRELATQIQVEALKFgksskiscaclYGGAPKGPQ 276
Cdd:COG1061 100 GGRGLVVAPTGTGKTvLALAL-----AAELLRGKR----VLVLVPRRELLEQWAEELRRF-----------LGDPLAGGG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 277 LKEIERgvDIVVATPGRLNDILEMKRISlHQVSYLVLDEADRmldmGFEPQIRKIVNEVPTKRqTLMYTAT-------WP 349
Cdd:COG1061 160 KKDSDA--PITVATYQSLARRAHLDELG-DRFGLVIIDEAHH----AGAPSYRRILEAFPAAY-RLGLTATpfrsdgrEI 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 350 KEVR------------KIAADLLVNPA--QVNIGNVDELVANKSITQTI-EVLAPME--KHSRLEQILRSQEPGSKIIIF 412
Cdd:COG1061 232 LLFLfdgivyeyslkeAIEDGYLAPPEyyGIRVDLTDERAEYDALSERLrEALAADAerKDKILRELLREHPDDRKTLVF 311
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334187683 413 CSTKRMCDQLARNLTRT-FGAAAIHGDKSQAERDDVLNQFRSGRTPVLVATDVAARGLDVKDIRVVV 478
Cdd:COG1061 312 CSSVDHAEALAELLNEAgIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI 378
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
147-363 |
1.15e-24 |
|
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: 102.79 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 147 HEITVSGGQVPPPLMS---FEATGLPNELLREVYSAGFSAPSPIQAQSWPIAMQN--RDIVAIAKTGSGKTLGYLIPgfm 221
Cdd:cd18048 1 HRVEVLQRDPTSPLFSvksFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 222 HLQRIhNDSRMGPTILVLSPTRELATQIQ--VEAL-KFGKSSKISCACLYGGAPKGPQLKEiergvDIVVATPGRLND-I 297
Cdd:cd18048 78 MLSRV-DALKLYPQCLCLSPTFELALQTGkvVEEMgKFCVGIQVIYAIRGNRPGKGTDIEA-----QIVIGTPGTVLDwC 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334187683 298 LEMKRISLHQVSYLVLDEADRMLDM-GFEPQIRKIVNEVPTKRQTLMYTATWPKEVRKIAADLLVNP 363
Cdd:cd18048 152 FKLRLIDVTNISVFVLDEADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDP 218
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
184-368 |
4.21e-19 |
|
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: 87.05 E-value: 4.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 184 PSPIQ---------------AQSWPIAMQNRDIVAIA-KTGSGKTLGYLIPGFMHLQR---------------IHNDSRM 232
Cdd:cd17965 31 PSPIQtlaikkllktlmrkvTKQTSNEEPKLEVFLLAaETGSGKTLAYLAPLLDYLKRqeqepfeeaeeeyesAKDTGRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 233 GPTILVlsPTRELATQIQVEALKFGKSSKISCACLygGAPKGPQLKEIER----GVDIVVATPGRLNDILEMKRISLHQV 308
Cdd:cd17965 111 RSVILV--PTHELVEQVYSVLKKLSHTVKLGIKTF--SSGFGPSYQRLQLafkgRIDILVTTPGKLASLAKSRPKILSRV 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 309 SYLVLDEADRMLDMGFEPQIRKIVNEVPTKRQTLMYTATWPKEVRKIAADLLvnPAQVNI 368
Cdd:cd17965 187 THLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLRKLF--PDVVRI 244
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
168-513 |
1.37e-18 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 89.77 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 168 LPNELLREVYsaGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPGFMhlqrihndsRMGPTiLVLSPTRELAT 247
Cdd:PRK11057 12 LAKQVLQETF--GYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALV---------LDGLT-LVVSPLISLMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 248 QiQVEALKfgkSSKISCACLYGGAPKGPQLKEIER----GVDIVVATPGRL--NDILEmkRISLHQVSYLVLDEADRMLD 321
Cdd:PRK11057 80 D-QVDQLL---ANGVAAACLNSTQTREQQLEVMAGcrtgQIKLLYIAPERLmmDNFLE--HLAHWNPALLAVDEAHCISQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 322 MG--FEP------QIRKIVNEVPTkrqtLMYTATWPKEVRK-IAADLLVNPAQVNIGNVDElvanKSITQTIevlapMEK 392
Cdd:PRK11057 154 WGhdFRPeyaalgQLRQRFPTLPF----MALTATADDTTRQdIVRLLGLNDPLIQISSFDR----PNIRYTL-----VEK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 393 HSRLEQILR--SQEPGSKIIIFC-STKRMCDQLARNLTRTFGAAAIHGDKSQAERDDVLNQFRSGRTPVLVATDVAARGL 469
Cdd:PRK11057 221 FKPLDQLMRyvQEQRGKSGIIYCnSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGI 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 334187683 470 DVKDIRVVVNYDFPNGVEDYVHRIGRTGRAGATGLAYTFFGDQD 513
Cdd:PRK11057 301 NKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPAD 344
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
395-500 |
2.40e-18 |
|
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: 81.49 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 395 RLEQILRSQEPGSkIIIFCSTKRMCDQLARNL-TRTFGAAAIHGDKSQAERDDVLNQFRSGRTPVLVATdVA-ARGLDVK 472
Cdd:cd18794 20 LLKRIKVEHLGGS-GIIYCLSRKECEQVAARLqSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVAT-VAfGMGIDKP 97
|
90 100
....*....|....*....|....*...
gi 334187683 473 DIRVVVNYDFPNGVEDYVHRIGRTGRAG 500
Cdd:cd18794 98 DVRFVIHYSLPKSMESYYQESGRAGRDG 125
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
202-334 |
4.94e-18 |
|
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: 81.30 E-value: 4.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 202 VAIAKTGSGKTLGYLIPGfmhlqrIHNDSRMGPTILVLSPTRELATQiQVEALKFGKSSKISCACLYGGAPKGPQLKEIE 281
Cdd:cd00046 5 LITAPTGSGKTLAALLAA------LLLLLKKGKKVLVLVPTKALALQ-TAERLRELFGPGIRVAVLVGGSSAEEREKNKL 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 334187683 282 RGVDIVVATPGRL-NDILEMKRISLHQVSYLVLDEADRMLDMGFEPQIRKIVNE 334
Cdd:cd00046 78 GDADIIIATPDMLlNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVR 131
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
162-363 |
2.40e-17 |
|
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both mRNA (mRNA) export from the nucleus into the cytoplasm and in mRNA translation. DDX19 functions in the nucleus in resolving RNA:DNA hybrids (R-loops). Activation of a DNA damage response pathway dependent upon the ATR kinase, a major regulator of replication fork progression, stimulates translocation of DDX19 from the cytoplasm into the nucleus. Only nuclear Ddx19 is competent to resolve R-loops. DDX19 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350805 [Multi-domain] Cd Length: 205 Bit Score: 80.92 E-value: 2.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 162 SFEATGLPNELLREVYSAGFSAPSPIQAQSWPIAMQN--RDIVAIAKTGSGKTLGYLIPGFMHLQRIHNDSRmgptILVL 239
Cdd:cd18047 2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQ----CLCL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 240 SPTRELATQIQVEALKFGK-SSKISCACLYGGapkgpqlKEIERGV----DIVVATPGRLND-ILEMKRISLHQVSYLVL 313
Cdd:cd18047 78 SPTYELALQTGKVIEQMGKfYPELKLAYAVRG-------NKLERGQkiseQIVIGTPGTVLDwCSKLKFIDPKKIKVFVL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 334187683 314 DEADRML-DMGFEPQIRKIVNEVPTKRQTLMYTATWPKEVRKIAADLLVNP 363
Cdd:cd18047 151 DEADVMIaTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
392-501 |
3.18e-17 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 85.55 E-value: 3.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 392 KHSRLEQILRSQ---EPGSKIIIFCSTKRMCDQLARNLTR------TF-GAAAIHGDK--SQAERDDVLNQFRSGRTPVL 459
Cdd:COG1111 336 KLSKLREILKEQlgtNPDSRIIVFTQYRDTAEMIVEFLSEpgikagRFvGQASKEGDKglTQKEQIEILERFRAGEFNVL 415
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 334187683 460 VATDVAARGLDVKDIRVVVNYD-FPNGVEdYVHRIGRTGRAGA 501
Cdd:COG1111 416 VATSVAEEGLDIPEVDLVIFYEpVPSEIR-SIQRKGRTGRKRE 457
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
167-507 |
1.85e-15 |
|
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: 80.26 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 167 GLPNELLREVYSAGFSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPGfmhLQRIHNDSRmgPTILVLSPTRELA 246
Cdd:COG1205 40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPV---LEALLEDPG--ATALYLYPTKALA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 247 tQIQVEAL-KFGKS--SKISCACLYGGAPKGpQLKEIERGVDIVVATPgrlndilEMkrisLHQ---------------V 308
Cdd:COG1205 115 -RDQLRRLrELAEAlgLGVRVATYDGDTPPE-ERRWIREHPDIVLTNP-------DM----LHYgllphhtrwarffrnL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 309 SYLVLDEA---------------DRML----DMGFEPQIrkivnevptkrqtLMYTATW--PKE---------VRKIAAD 358
Cdd:COG1205 182 RYVVIDEAhtyrgvfgshvanvlRRLRricrHYGSDPQF-------------ILASATIgnPAEhaerltgrpVTVVDED 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 359 ---------LLVNPAQVNIGnvdelVANKSITQTIEVLApmekhsrleQILRSqepGSKIIIFCSTKRMCDQLARNLTRT 429
Cdd:COG1205 249 gsprgertfVLWNPPLVDDG-----IRRSALAEAARLLA---------DLVRE---GLRTLVFTRSRRGAELLARYARRA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 430 FgAAAIHGDKSQA--------ERDDVLNQFRSGRTPVLVAT-------DVAarGLDvkdirVVVNYDFPNGVEDYVHRIG 494
Cdd:COG1205 312 L-REPDLADRVAAyragylpeERREIERGLRSGELLGVVSTnalelgiDIG--GLD-----AVVLAGYPGTRASFWQQAG 383
|
410
....*....|...
gi 334187683 495 RTGRAGATGLAYT 507
Cdd:COG1205 384 RAGRRGQDSLVVL 396
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
389-502 |
2.26e-13 |
|
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: 67.62 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 389 PMEKHSRLEQILRSQEPGSKI---IIFCSTKRMCDQLAR-----NLTRTFGAAAI---HGDKSQAERD--------DVLN 449
Cdd:cd18802 5 VIPKLQKLIEILREYFPKTPDfrgIIFVERRATAVVLSRllkehPSTLAFIRCGFligRGNSSQRKRSlmtqrkqkETLD 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 334187683 450 QFRSGRTPVLVATDVAARGLDVKDIRVVVNYDFPNGVEDYVHRIGRTGRAGAT 502
Cdd:cd18802 85 KFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPNSK 137
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
392-509 |
1.01e-12 |
|
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: 66.12 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 392 KHSRLEQILRSQEPGSKIIIFCSTKrmcdQLARNLTRTFGAAAIHGDKSQAERDDVLNQFRSGRTPVLVATDVAARGLDV 471
Cdd:cd18789 35 KLRALEELLKRHEQGDKIIVFTDNV----EALYRYAKRLLKPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDL 110
|
90 100 110
....*....|....*....|....*....|....*....
gi 334187683 472 KDIRVVVNYDFPNGVE-DYVHRIGRTGRAGATGLAYTFF 509
Cdd:cd18789 111 PEANVAIQISGHGGSRrQEAQRLGRILRPKKGGGKNAFF 149
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
170-372 |
4.09e-12 |
|
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.
Pssm-ID: 350776 [Multi-domain] Cd Length: 201 Bit Score: 65.74 E-value: 4.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 170 NELLREVYsaGFSAPSPiqAQSWPIA--MQNRDIVAIAKTGSGKTLGYLIPGFMHLQRihndsRMGPTiLVLSPTRELaT 247
Cdd:cd18018 1 LKLLRRVF--GHPSFRP--GQEEAIArlLSGRSTLVVLPTGAGKSLCYQLPALLLRRR-----GPGLT-LVVSPLIAL-M 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 248 QIQVEALKfgksSKISCACLYGGAPKGPQLKEIER----GVDIVVATPGRLNDilEMKRISLHQ---VSYLVLDEADRML 320
Cdd:cd18018 70 KDQVDALP----RAIKAAALNSSLTREERRRILEKlragEVKILYVSPERLVN--ESFRELLRQtppISLLVVDEAHCIS 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 334187683 321 DMG--FEP---QIRKIVNEVPTKRQTLMYTATWPKEVRK-IAADLLVNPAQVNIGNVD 372
Cdd:cd18018 144 EWShnFRPdylRLCRVLRELLGAPPVLALTATATKRVVEdIASHLGIPESGVVRGPLY 201
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
408-509 |
4.34e-12 |
|
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: 61.95 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 408 KIIIFCSTKRMCDQLARNLTrtfgaaaihgdksqaerddvlnqfrsgrtpVLVATDVAARGLDVKDIRVVVNYDFPNGVE 487
Cdd:cd18785 5 KIIVFTNSIEHAEEIASSLE------------------------------ILVATNVLGEGIDVPSLDTVIFFDPPSSAA 54
|
90 100
....*....|....*....|..
gi 334187683 488 DYVHRIGRTGRAGATGLAYTFF 509
Cdd:cd18785 55 SYIQRVGRAGRGGKDEGEVILF 76
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
396-494 |
1.54e-11 |
|
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: 62.11 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 396 LEQILRSQEPGSKIIIFCSTKRMCDQLARNLTRT-FGAAAIHGDKSQAERDDVLNQFRSGRTP--VLVATDVAARGLDVK 472
Cdd:cd18793 17 LELLEELREPGEKVLIFSQFTDTLDILEEALRERgIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGVGLNLT 96
|
90 100
....*....|....*....|....*...
gi 334187683 473 DIRVVVNYDFP-N-GVE----DYVHRIG 494
Cdd:cd18793 97 AANRVILYDPWwNpAVEeqaiDRAHRIG 124
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
171-366 |
1.68e-11 |
|
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: 63.71 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 171 ELLREVYsaGFSAPSPIQAQSwpI--AMQNRDIVAIAKTGSGKTLGYLIPGFMhlqrihndsRMGPTIlVLSPTRELAtQ 248
Cdd:cd17920 2 QILKEVF--GYDEFRPGQLEA--InaVLAGRDVLVVMPTGGGKSLCYQLPALL---------LDGVTL-VVSPLISLM-Q 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 249 IQVEALkfgKSSKISCACLYGGAPKGPQ---LKEIERG-VDIVVATPGRLNDILEMKRI----SLHQVSYLVLDEADRML 320
Cdd:cd17920 67 DQVDRL---QQLGIRAAALNSTLSPEEKrevLLRIKNGqYKLLYVTPERLLSPDFLELLqrlpERKRLALIVVDEAHCVS 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 334187683 321 DMG--FEPQ------IRKIVNEVPtkrqTLMYTATWPKEVRK-IAADL-LVNPAQV 366
Cdd:cd17920 144 QWGhdFRPDylrlgrLRRALPGVP----ILALTATATPEVREdILKRLgLRNPVIF 195
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
395-496 |
1.21e-10 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 64.48 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 395 RLEQILRS-QEPGSKIIIFCSTKRMCDQLARNLTRT-FGAAAIHGDKSQAERDDVLNQFRSGRTP--VLVATDVAARGLD 470
Cdd:COG0553 537 ALLELLEElLAEGEKVLVFSQFTDTLDLLEERLEERgIEYAYLHGGTSAEERDELVDRFQEGPEApvFLISLKAGGEGLN 616
|
90 100 110
....*....|....*....|....*....|..
gi 334187683 471 VKDIRVVVNYDFP-N-GVE----DYVHRIGRT 496
Cdd:COG0553 617 LTAADHVIHYDLWwNpAVEeqaiDRAHRIGQT 648
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
384-501 |
2.03e-10 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 63.74 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 384 IEVLAPmeKHSRLEQILRSQ---EPGSKIIIFCSTKRMCDQLARNLT-------RTFGAAAIHGDK--SQAERDDVLNQF 451
Cdd:PRK13766 342 LDIEHP--KLEKLREIVKEQlgkNPDSRIIVFTQYRDTAEKIVDLLEkegikavRFVGQASKDGDKgmSQKEQIEILDKF 419
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 334187683 452 RSGRTPVLVATDVAARGLDVKDIRVVVNYD-FPNGVEdYVHRIGRTGRAGA 501
Cdd:PRK13766 420 RAGEFNVLVSTSVAEEGLDIPSVDLVIFYEpVPSEIR-SIQRKGRTGRQEE 469
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
384-498 |
5.03e-10 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350188 [Multi-domain] Cd Length: 143 Bit Score: 58.14 E-value: 5.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 384 IEVLAP-MEKHSRL--EQILRSQEPG-SKIIIFCSTKRMCDQLARNLTR--------TF-GAAAIHGDK--SQAERDDVL 448
Cdd:cd18801 4 VEKIHPkLEKLEEIvkEHFKKKQEGSdTRVIIFSEFRDSAEEIVNFLSKirpgiratRFiGQASGKSSKgmSQKEQKEVI 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 334187683 449 NQFRSGRTPVLVATDVAARGLDVKDIRVVVNYDFPNGVEDYVHRIGRTGR 498
Cdd:cd18801 84 EQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
168-500 |
6.26e-10 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 61.83 E-value: 6.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 168 LPNELLREVYSA-GFSAPSPIQAQSWP-IAMQNRDIVAIAKTGSGKTL-GYLipgfmhlqRIHNDSRMGPTILVLSPTRE 244
Cdd:COG1204 6 LPLEKVIEFLKErGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLiAEL--------AILKALLNGGKALYIVPLRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 245 LATQIQVEALKFGKSSKISCACLYGGAPKGPQlkEIERgVDIVVATPGRLnDILEMKRIS-LHQVSYLVLDEAdRMLDmg 323
Cdd:COG1204 78 LASEKYREFKRDFEELGIKVGVSTGDYDSDDE--WLGR-YDILVATPEKL-DSLLRNGPSwLRDVDLVVVDEA-HLID-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 324 fEPQiRKIVNEVptkrqTLMYTATWPKEVRKIA--AdllvnpaqvNIGNVDEL--------------------------- 374
Cdd:COG1204 151 -DES-RGPTLEV-----LLARLRRLNPEAQIVAlsA---------TIGNAEEIaewldaelvksdwrpvplnegvlydgv 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 375 --VANKSITQTIEVLAPMEKHSrleqilrsqEPGSKIIIFCSTKRMCDQLARNLTRTF---------------------- 430
Cdd:COG1204 215 lrFDDGSRRSKDPTLALALDLL---------EEGGQVLVFVSSRRDAESLAKKLADELkrrltpeereeleelaeellev 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 431 ----------------GAAAIHGDKSQAERDDVLNQFRSGRTPVLVATD-------VAARGLDVKDIRVVVNYDFPngVE 487
Cdd:COG1204 286 seethtnekladclekGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPtlaagvnLPARRVIIRDTKRGGMVPIP--VL 363
|
410
....*....|...
gi 334187683 488 DYVHRIGRTGRAG 500
Cdd:COG1204 364 EFKQMAGRAGRPG 376
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
396-500 |
1.09e-09 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350182 [Multi-domain] Cd Length: 154 Bit Score: 57.56 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 396 LEQILRSQEPGSKIIIFCSTKRMCDQLARNLTrtfGAAAIHGDKSQAERDDVLNQFRSGRTPVLVATDVAARGLD----- 470
Cdd:cd18795 33 VLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNlpart 109
|
90 100 110
....*....|....*....|....*....|...
gi 334187683 471 --VKDIRVVVNYDFPN-GVEDYVHRIGRTGRAG 500
Cdd:cd18795 110 viIKGTQRYDGKGYRElSPLEYLQMIGRAGRPG 142
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
181-521 |
5.42e-09 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 59.35 E-value: 5.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 181 FSAPSPIQAQSWPIAMQNRDIVAIAKTGSGKTL-GYLIPgfmhLQRIHNDSRMGPT-----ILVLSPTRELATQIQ---- 250
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTLaAFLPA----LDELARRPRPGELpdglrVLYISPLKALANDIErnlr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 251 --VEALkfgksskiscaclygGAPKGPQLKEIERGV------------------DIVVATPgrlndilEmkriSLhqvsY 310
Cdd:COG1201 98 apLEEI---------------GEAAGLPLPEIRVGVrtgdtpaserqrqrrrppHILITTP-------E----SL----A 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 311 LVL--DEADRMLdmgfepqiRK----IVNEV----PTKRQTLM------YTATWPKEVRKI-----------AADLLV-- 361
Cdd:COG1201 148 LLLtsPDARELL--------RGvrtvIVDEIhalaGSKRGVHLalslerLRALAPRPLQRIglsatvgpleeVARFLVgy 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 362 -NPAQVNIGNVDelvANKSItqTIEVLAPMEKHSRLeqILRSQEPGSKI--------------IIFCSTKRMCDQLARNL 426
Cdd:COG1201 220 eDPRPVTIVDAG---AGKKP--DLEVLVPVEDLIER--FPWAGHLWPHLyprvldlieahrttLVFTNTRSQAERLFQRL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 427 TRTFG-----AAAIHGDKSQAERDDVLNQFRSGRTPVLVAT---DVaarGLDVKDIRVVVNYDFPNGVEDYVHRIGRTG- 497
Cdd:COG1201 293 NELNPedalpIAAHHGSLSREQRLEVEEALKAGELRAVVATsslEL---GIDIGDVDLVIQVGSPKSVARLLQRIGRAGh 369
|
410 420
....*....|....*....|....
gi 334187683 498 RAGATGLAYTFfgdqdAKHASDLI 521
Cdd:COG1201 370 RVGEVSKGRLV-----PTHRDELV 388
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
188-316 |
6.68e-09 |
|
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: 55.67 E-value: 6.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 188 QAQSWPIAMQNRDIVAIAKTGSGKTLGYLIPGFMHLQRIHndsrmGPTILVLSPTRELAtQIQVEALK---FGKSSKISC 264
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDP-----GSRALYLYPTKALA-QDQLRSLRellEQLGLGIRV 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 334187683 265 ACLYGGAPKGPQLKEIERGVDIVVATPGRLNDIL----EMKRISLHQVSYLVLDEA 316
Cdd:cd17923 79 ATYDGDTPREERRAIIRNPPRILLTNPDMLHYALlphhDRWARFLRNLRYVVLDEA 134
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
184-316 |
8.27e-09 |
|
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: 55.74 E-value: 8.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 184 PSPIQAQSWPIAMQnRDIVAIAKTGSGKTL--GYLIPGFMHLQRIHNDSrmGPTILVLSPTRELATQiQVEALKFGksSK 261
Cdd:cd18034 3 PRSYQLELFEAALK-RNTIVVLPTGSGKTLiaVMLIKEMGELNRKEKNP--KKRAVFLVPTVPLVAQ-QAEAIRSH--TD 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 334187683 262 ISCACLYGGA----PKGPQLKEIERGVDIVVATPGRLNDILEMKRISLHQVSYLVLDEA 316
Cdd:cd18034 77 LKVGEYSGEMgvdkWTKERWKEELEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
395-498 |
1.52e-07 |
|
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: 51.11 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 395 RLEQILRSQEPGSKIIIFCSTKRMCDQLARNLTRTFGAAAI-------HGDKSQAERDDVLNQFRSGRTPVLVATDVAAR 467
Cdd:cd18796 27 AYAEVIFLLERHKSTLVFTNTRSQAERLAQRLRELCPDRVPpdfialhHGSLSRELREEVEAALKRGDLKVVVATSSLEL 106
|
90 100 110
....*....|....*....|....*....|.
gi 334187683 468 GLDVKDIRVVVNYDFPNGVEDYVHRIGRTGR 498
Cdd:cd18796 107 GIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
186-316 |
1.88e-07 |
|
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: 51.49 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 186 PIQAQSWPIAMQNRDIVAI-AKTGSGKTlgyLIPGFMHLQRIhndSRMGPTILVLSPTRELATQIQVEALKFGKSSKISC 264
Cdd:cd17921 4 PIQREALRALYLSGDSVLVsAPTSSGKT---LIAELAILRAL---ATSGGKAVYIAPTRALVNQKEADLRERFGPLGKNV 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 334187683 265 ACLYGGAPKGPQLkeiERGVDIVVATPGRLnDILEMKRISLH--QVSYLVLDEA 316
Cdd:cd17921 78 GLLTGDPSVNKLL---LAEADILVATPEKL-DLLLRNGGERLiqDVRLVVVDEA 127
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
406-505 |
4.38e-07 |
|
C-terminal helicase domain of HrQ family helicases; 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. HrQ 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: 350184 [Multi-domain] Cd Length: 146 Bit Score: 49.56 E-value: 4.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 406 GSKIIIFCSTKRMCDQLARNLTRTFGAAAIHGDKSQA--------ERDDVLNQFRSGRTPVLVATDVAARGLDVKDIRVV 477
Cdd:cd18797 35 GVKTIVFCRSRKLAELLLRYLKARLVEEGPLASKVASyragylaeDRREIEAELFNGELLGVVATNALELGIDIGGLDAV 114
|
90 100
....*....|....*....|....*...
gi 334187683 478 VNYDFPNGVEDYVHRIGRTGRAGATGLA 505
Cdd:cd18797 115 VLAGYPGSLASLWQQAGRAGRRGKDSLV 142
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
196-500 |
5.68e-07 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 52.98 E-value: 5.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 196 MQNRDIVAIAKTGSGKTLGYLIPGFMhlqrihndsrmGPTI-LVLSPtreLATQIQVEALKFGKSSkISCACLYGGAPKG 274
Cdd:PLN03137 473 MSGYDVFVLMPTGGGKSLTYQLPALI-----------CPGItLVISP---LVSLIQDQIMNLLQAN-IPAASLSAGMEWA 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 275 PQLkEIERGVD-------IVVATPGRL--NDILEMKRISLHQVSYL---VLDEADRMLDMG--FEPQIRK--IVNEVPTK 338
Cdd:PLN03137 538 EQL-EILQELSseyskykLLYVTPEKVakSDSLLRHLENLNSRGLLarfVIDEAHCVSQWGhdFRPDYQGlgILKQKFPN 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 339 RQTLMYTATWPKEVRKIAADLLvnpaqvniGNVDELVANKS----------ITQTIEVLAPMEKHSRLEQIlrsQEPGsk 408
Cdd:PLN03137 617 IPVLALTATATASVKEDVVQAL--------GLVNCVVFRQSfnrpnlwysvVPKTKKCLEDIDKFIKENHF---DECG-- 683
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 409 iIIFCSTKRMCDQLARNLtRTFG--AAAIHGDKSQAERDDVLNQFRSGRTPVLVATDVAARGLDVKDIRVVVNYDFPNGV 486
Cdd:PLN03137 684 -IIYCLSRMDCEKVAERL-QEFGhkAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSI 761
|
330
....*....|....
gi 334187683 487 EDYVHRIGRTGRAG 500
Cdd:PLN03137 762 EGYHQECGRAGRDG 775
|
|
| WW |
pfam00397 |
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
17-47 |
8.15e-06 |
|
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.
Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 42.88 E-value: 8.15e-06
10 20 30
....*....|....*....|....*....|.
gi 334187683 17 LPKPWKGLVDSrTGYLYFWNPETNVTQYERP 47
Cdd:pfam00397 1 LPPGWEERWDP-DGRVYYYNHETGETQWEKP 30
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
408-478 |
1.11e-05 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350186 [Multi-domain] Cd Length: 116 Bit Score: 44.86 E-value: 1.11e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334187683 408 KIIIFCSTKRMCDQLARNLTRTFG-AAAIHGDKSQAERDDV---LNQFRSGRTPVLVATDVAARGLDVKDIRVVV 478
Cdd:cd18799 8 KTLIFCVSIEHAEFMAEAFNEAGIdAVALNSDYSDRERGDEaliLLFFGELKPPILVTVDLLTTGVDIPEVDNVV 82
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
392-526 |
1.82e-05 |
|
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: 45.41 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 392 KHSRLEQILRSQE----PGSKIIIFC------------STKRMCDQLARNLTRTFGAAAIHGDKSQAERDDVLNQFRSGR 455
Cdd:cd18811 8 FHTRLDKVYEFVReeiaKGRQAYVIYplieesekldlkAAVAMYEYLKERFRPELNVGLLHGRLKSDEKDAVMAEFREGE 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334187683 456 TPVLVATDVAARGLDVKDIRVVVnydfpngVED-------YVHRI-GRTGRAGATGLAYTFFGDQDAKHASDLIKILEG 526
Cdd:cd18811 88 VDILVSTTVIEVGVDVPNATVMV-------IEDaerfglsQLHQLrGRVGRGDHQSYCLLVYKDPLTETAKQRLRVMTE 159
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
204-318 |
2.44e-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: 45.20 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 204 IAKTGSGKTLGYLIPGFMHLQRihndsrMGPTILVLSPTRELATQiQVEALKFGKSSKISCACLyGGAPKGPQLKEIERG 283
Cdd:cd18035 22 VLPTGLGKTIIAILVAADRLTK------KGGKVLILAPSRPLVEQ-HAENLKRVLNIPDKITSL-TGEVKPEERAERWDA 93
|
90 100 110
....*....|....*....|....*....|....*.
gi 334187683 284 VDIVVATPGRL-NDILEmKRISLHQVSYLVLDEADR 318
Cdd:cd18035 94 SKIIVATPQVIeNDLLA-GRITLDDVSLLIFDEAHH 128
|
|
| WW |
smart00456 |
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
17-49 |
9.24e-05 |
|
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.
Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 39.89 E-value: 9.24e-05
10 20 30
....*....|....*....|....*....|...
gi 334187683 17 LPKPWKGLVDsRTGYLYFWNPETNVTQYERPAS 49
Cdd:smart00456 2 LPPGWEERKD-PDGRPYYYNHETKETQWEKPRE 33
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
207-318 |
1.57e-04 |
|
DEAH-box helicase domain of FANCM; 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. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM 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: 350791 [Multi-domain] Cd Length: 182 Bit Score: 43.08 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 207 TGSGKTlgylipgFMHLQRIHNDSRMGPT--ILVLSPTRELATQiQVEA-LKFGKSSKISCACLYGGAPKgPQLKEIERG 283
Cdd:cd18033 25 TGLGKT-------FIAAVVMLNYYRWFPKgkIVFMAPTKPLVSQ-QIEAcYKITGIPSSQTAELTGSVPP-TKRAELWAS 95
|
90 100 110
....*....|....*....|....*....|....*.
gi 334187683 284 VDIVVATPGRL-NDILEmKRISLHQVSYLVLDEADR 318
Cdd:cd18033 96 KRVFFLTPQTLeNDLKE-GDCDPKSIVCLVIDEAHR 130
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
195-318 |
1.60e-04 |
|
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: 43.19 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 195 AMQNRDIVAIAKTGSGKTLGYLIPGFMHLQRIHndSRMGPTILVLSPTRELATQiQVEALK--FGKSsKISCACLYGG-A 271
Cdd:cd17927 14 ALKGKNTIICLPTGSGKTFVAVLICEHHLKKFP--AGRKGKVVFLANKVPLVEQ-QKEVFRkhFERP-GYKVTGLSGDtS 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 334187683 272 PKGPQLKEIERGvDIVVATPGRL-NDILEMKRISLHQVSYLVLDEADR 318
Cdd:cd17927 90 ENVSVEQIVESS-DVIIVTPQILvNDLKSGTIVSLSDFSLLVFDECHN 136
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
396-503 |
3.42e-04 |
|
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: 41.75 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 396 LEQILRSQEPGSkIIIFCST----KRMCDQLARNLTRTFGAAAI----HGDKSQAERDDVLNQFRSGRTPVLVATDVAAR 467
Cdd:cd18791 34 ILQIHRTEEPGD-ILVFLPGqeeiERLCELLREELLSPDLGKLLvlplHSSLPPEEQQRVFEPPPPGVRKVVLATNIAET 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 334187683 468 GLDVKDIRVVVnyDFpnGVE---DYVHRIG----------------RTGRAGATG 503
Cdd:cd18791 113 SITIPGVVYVI--DS--GLVkekVYDPRTGlsslvtvwiskasaeqRAGRAGRTR 163
|
|
| WW |
cd00201 |
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
18-47 |
3.78e-04 |
|
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.
Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 37.89 E-value: 3.78e-04
10 20 30
....*....|....*....|....*....|
gi 334187683 18 PKPWKGLVDsRTGYLYFWNPETNVTQYERP 47
Cdd:cd00201 1 PPGWEERWD-PDGRVYYYNHNTKETQWEDP 29
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
198-315 |
3.94e-04 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 41.41 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 198 NRDIVAIAKTGSGKTLGYLIPGfmhLQRIHNDSRMGPTILVLSPTRELATQIQ--VEALKFGKSSKISCACLYGGAPKGP 275
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPA---LSSLADEPEKGVQVLYISPLKALINDQErrLEEPLDEIDLEIPVAVRHGDTSQSE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 334187683 276 QLKEIERGVDIVVATPGRLNDILEMKRIS--LHQVSYLVLDE 315
Cdd:cd17922 78 KAKQLKNPPGILITTPESLELLLVNKKLRelFAGLRYVVVDE 119
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
200-471 |
4.23e-04 |
|
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: 43.19 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 200 DIVAIAKTGSGKTLGYLIPGFMHLQRIHNDSrmgpTILVLsPTRELATQIQVEALK-FGKSSKISCACLYGGAPKGPQLK 278
Cdd:cd09639 1 LLVIEAPTGYGKTEAALLWALHSLKSQKADR----VIIAL-PTRATINAMYRRAKEaFGETGLYHSSILSSRIKEMGDSE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 279 EIER-------GVDIVVATPGRLNDILEMKRISLHQVSY------------LVLDEADRMLD--MGFEPQIRKIVNEVPT 337
Cdd:cd09639 76 EFEHlfplyihSNDTLFLDPITVCTIDQVLKSVFGEFGHyeftlasianslLIFDEVHFYDEytLALILAVLEVLKDNDV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 338 KrqTLMYTATWPKevrkiaadLLVNPAQvNIGNVDE-----LVANKSITQTIEVLAPMEKHSRLEQILRSQEPGSKIIIF 412
Cdd:cd09639 156 P--ILLMSATLPK--------FLKEYAE-KIGYVEEnepldLKPNERAPFIKIESDKVGEISSLERLLEFIKKGGSVAII 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334187683 413 CST---KRMCDQLARNLTRTFGAAAIHGDKSQAERDD----VLNQFRSGRTPVLVATDVAARGLDV 471
Cdd:cd09639 225 VNTvdrAQEFYQQLKEKGPEEEIMLIHSRFTEKDRAKkeaeLLLEFKKSEKFVIVATQVIEASLDI 290
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
207-347 |
4.35e-04 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 41.14 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 207 TGSGKTLgylipgfMHLQRIHNdsRMGPTILVLSPTRELATQIQVEALKFGKSSKIscaclygGAPKGPQLKEIErGVDI 286
Cdd:cd17926 27 TGSGKTL-------TALALIAY--LKELRTLIVVPTDALLDQWKERFEDFLGDSSI-------GLIGGGKKKDFD-DANV 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334187683 287 VVATPGRLNDILEMKRISLHQVSYLVLDEADRmldmGFEPQIRKIVNEVPTKRQtLMYTAT 347
Cdd:cd17926 90 VVATYQSLSNLAEEEKDLFDQFGLLIVDEAHH----LPAKTFSEILKELNAKYR-LGLTAT 145
|
|
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
421-464 |
8.40e-04 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 42.34 E-value: 8.40e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 334187683 421 QLARNLTRTFGAAAI---HGDKSQAERDDVLNQFRSGRTPVLVATDV 464
Cdd:COG1200 492 ETYEELREAFPGLRVgllHGRMKPAEKDAVMAAFKAGEIDVLVATTV 538
|
|
| DEXQc_arch_SWI2_SNF2 |
cd18012 |
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ... |
208-316 |
1.04e-03 |
|
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging to SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprises a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. Archaeal SWI2 and SNF2 are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350770 [Multi-domain] Cd Length: 218 Bit Score: 41.01 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 208 GSGKTLGYLIpgfmHLQRIHNDSRMGPTiLVLSPTrELATQIQVEALKFgkSSKISCACLYGGAPKGPQLKEIErGVDIV 287
Cdd:cd18012 33 GLGKTLQTLA----LLLSRKEEGRKGPS-LVVAPT-SLIYNWEEEAAKF--APELKVLVIHGTKRKREKLRALE-DYDLV 103
|
90 100 110
....*....|....*....|....*....|
gi 334187683 288 VATPGRL-NDILEMKRISLHqvsYLVLDEA 316
Cdd:cd18012 104 ITSYGLLrRDIELLKEVKFH---YLVLDEA 130
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
417-512 |
1.44e-03 |
|
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: 39.94 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 417 RMCDQLaRNLTRTFGAAAIHGDKSQAERDDVLNQFRSGRTPVLVATDVAARGLDVKDIRVVVnydfpngVED-------Y 489
Cdd:cd18792 49 ALAEEL-KELVPEARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMI-------IEDadrfglsQ 120
|
90 100
....*....|....*....|....
gi 334187683 490 VHRI-GRTGRAGATGLAYTFFGDQ 512
Cdd:cd18792 121 LHQLrGRVGRGKHQSYCYLLYPDP 144
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
396-498 |
2.23e-03 |
|
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350177 [Multi-domain] Cd Length: 171 Bit Score: 39.54 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 396 LEQILRSQEPGSKIIIFCSTKRMCDQLARNLT-RTFGAAAIHGDKSQAERDDVLNQFRSGRTPVLVATDVAARGLDVKDI 474
Cdd:cd18790 17 LGEIRKRVARGERVLVTTLTKRMAEDLTEYLQeLGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEV 96
|
90 100
....*....|....*....|....*....
gi 334187683 475 RVVVNYD-----FPNGVEDYVHRIGRTGR 498
Cdd:cd18790 97 SLVAILDadkegFLRSETSLIQTIGRAAR 125
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
197-347 |
2.35e-03 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 39.19 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 197 QNRDIVAIAKTGSGKTLGYLipGFM-HLQRIHNDSRmgptILVLSPTRELATQIQVEALKFGKSSKISCACLYGGApkgp 275
Cdd:pfam04851 22 GQKRGLIVMATGSGKTLTAA--KLIaRLFKKGPIKK----VLFLVPRKDLLEQALEEFKKFLPNYVEIGEIISGDK---- 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334187683 276 qLKEIERGVDIVVATPGRLN--DILEMKRISLHQVSYLVLDEADRmldmGFEPQIRKIVNEVPTKRQtLMYTAT 347
Cdd:pfam04851 92 -KDESVDDNKIVVTTIQSLYkaLELASLELLPDFFDVIIIDEAHR----SGASSYRNILEYFKPAFL-LGLTAT 159
|
|
| SF2_C_priA |
cd18804 |
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ... |
395-506 |
3.87e-03 |
|
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA 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: 350191 [Multi-domain] Cd Length: 238 Bit Score: 39.54 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187683 395 RLEQILRSQEPGSKIIifcstkRMcDqlaRNLTRTFGAaaihgdksqaeRDDVLNQFRSGRTPVLVATDVAARGLDVKDI 474
Cdd:cd18804 105 RVEEELKTLFPEARIA------RI-D---RDTTRKKGA-----------LEKLLDQFERGEIDILIGTQMIAKGLDFPNV 163
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 334187683 475 R--VVVNYDFPNGVEDY---------VHRI-GRTGRAGATGLAY 506
Cdd:cd18804 164 TlvGILNADSGLNSPDFraserafqlLTQVsGRAGRGDKPGKVI 207
|
|
| DinG |
COG1199 |
Rad3-related DNA helicase DinG [Replication, recombination and repair]; |
195-252 |
8.23e-03 |
|
Rad3-related DNA helicase DinG [Replication, recombination and repair];
Pssm-ID: 440812 [Multi-domain] Cd Length: 629 Bit Score: 39.14 E-value: 8.23e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 334187683 195 AMQNRDIVAI-AKTGSGKTLGYLIPGFMHLQRihNDSRmgptILVLSPTRelATQIQVE 252
Cdd:COG1199 29 ALAEGRHLLIeAGTGTGKTLAYLVPALLAARE--TGKK----VVISTATK--ALQEQLV 79
|
|
| |
