|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
141-526 |
1.59e-167 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 485.42 E-value: 1.59e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 141 FNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAGGPDMVKppaftngrrt 220
Cdd:COG0513 4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAPQ---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 221 yypcALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGrENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRY 300
Cdd:COG0513 74 ----ALILAPTRELALQVAEELRKLAKYLGLRVATVYGG-VSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVET 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 301 LVLDEADRMLDMGFEPQIRKIVGQgMPPKtaRTTAMFSATFPKEIQVLAKDFLKdNYIFLAVGRVGSTSENIEQRLLWVN 380
Cdd:COG0513 149 LVLDEADRMLDMGFIEDIERILKL-LPKE--RQTLLFSATMPPEIRKLAKRYLK-NPVRIEVAPENATAETIEQRYYLVD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 381 EMEKRSNLMEILmNEHSENLVLVFVETKRGANELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQCPILVATAVAAR 460
Cdd:COG0513 225 KRDKLELLRRLL-RDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAAR 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71995514 461 GLDIPNVRHVINYDLPGDSDEYVHRIGRTGRCGNLGIATSFFNDKNRGIGRDLKNLIvesNQEVPE 526
Cdd:COG0513 304 GIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLI---GQKIEE 366
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
141-366 |
5.04e-137 |
|
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: 399.94 E-value: 5.04e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 141 FNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAGGpdmvkPPAFTNGRRT 220
Cdd:cd17967 2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDG-----PPSVGRGRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 221 YYPCALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGREnYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRY 300
Cdd:cd17967 77 AYPSALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGAD-VVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71995514 301 LVLDEADRMLDMGFEPQIRKIV-GQGMPPKTARTTAMFSATFPKEIQVLAKDFLKdNYIFLAVGRVG 366
Cdd:cd17967 156 LVLDEADRMLDMGFEPQIRKIVeHPDMPPKGERQTLMFSATFPREIQRLAADFLK-NYIFLTVGRVG 221
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
101-366 |
7.79e-134 |
|
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: 393.56 E-value: 7.79e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 101 PAEySESNLFHRTDSGINFDKYENIPVEVSGDSVPAAIEHFNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLM 180
Cdd:cd18052 6 PPE-DEDEIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 181 SCAQTGSGKTAAFLLPIIQHILAGGpdmVKPPAFTNGRRtyyPCALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGr 260
Cdd:cd18052 85 ACAQTGSGKTAAFLLPVLTGMMKEG---LTASSFSEVQE---PQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGG- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 261 ENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRYLVLDEADRMLDMGFEPQIRKIVGQ-GMPPKTARTTAMFSA 339
Cdd:cd18052 158 VSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEpGMPSKEDRQTLMFSA 237
|
250 260
....*....|....*....|....*..
gi 71995514 340 TFPKEIQVLAKDFLKDNYIFLAVGRVG 366
Cdd:cd18052 238 TFPEEIQRLAAEFLKEDYLFLTVGRVG 264
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
119-367 |
5.94e-132 |
|
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: 387.86 E-value: 5.94e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 119 FDKYENIPVEVSGDSVPAAIEHFNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPII 198
Cdd:cd18051 1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 199 QHILAGGP-DMVKPPAFTNGRRTYYPCALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGrENYRDQVNRLRAGTHIL 277
Cdd:cd18051 81 SQIYEQGPgESLPSESGYYGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGG-ADIGQQMRDLERGCHLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 278 IATPGRLIDIIEQGFIGLAGCRYLVLDEADRMLDMGFEPQIRKIVGQ-GMPPKTARTTAMFSATFPKEIQVLAKDFLkDN 356
Cdd:cd18051 160 VATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQdTMPPTGERQTLMFSATFPKEIQMLARDFL-DN 238
|
250
....*....|.
gi 71995514 357 YIFLAVGRVGS 367
Cdd:cd18051 239 YIFLAVGRVGS 249
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
61-534 |
1.19e-131 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 398.38 E-value: 1.19e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 61 GYSENFENFDENGSSGYNNFADSG-------NGFNNNGAESNQWGG--APAEYSESNLF---------HRTDSGINFDKY 122
Cdd:PTZ00110 29 DSSNPYGNYQANHQDNYGGFRPGYgnysggyGGFGMNSYGSSTLGKrlQPIDWKSINLVpfeknfykeHPEVSALSSKEV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 123 ENIPVE-----VSGDSVPAAIEHFNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPI 197
Cdd:PTZ00110 109 DEIRKEkeitiIAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 198 IQHILAggpdmvkPPAFTNGRRtyyPCALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGRENyRDQVNRLRAGTHIL 277
Cdd:PTZ00110 189 IVHINA-------QPLLRYGDG---PIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPK-RGQIYALRRGVEIL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 278 IATPGRLIDIIEQGFIGLAGCRYLVLDEADRMLDMGFEPQIRKIVGQGMPPktaRTTAMFSATFPKEIQVLAKDFLKDNY 357
Cdd:PTZ00110 258 IACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPD---RQTLMWSATWPKEVQSLARDLCKEEP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 358 IFLAVGRVG-STSENIEQRLLWVNEMEKRSNLMEIL---MNEHSEnlVLVFVETKRGANELAYFLNRQQIRSVSIHGDLK 433
Cdd:PTZ00110 335 VHVNVGSLDlTACHNIKQEVFVVEEHEKRGKLKMLLqriMRDGDK--ILIFVETKKGADFLTKELRLDGWPALCIHGDKK 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 434 QIERERNLELFRSGQCPILVATAVAARGLDIPNVRHVINYDLPGDSDEYVHRIGRTGRCGNLGIATSFFN-DKNRgIGRD 512
Cdd:PTZ00110 413 QEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTpDKYR-LARD 491
|
490 500
....*....|....*....|..
gi 71995514 513 LKNLIVESNQEVPEWLHQVAAE 534
Cdd:PTZ00110 492 LVKVLREAKQPVPPELEKLSNE 513
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
148-505 |
1.98e-102 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 319.82 E-value: 1.98e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 148 PAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHIlaggpdmvkppaftNGRRtYYPCALV 227
Cdd:PRK11776 13 PALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL--------------DVKR-FRVQALV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 228 LSPTRELAIQIHKEATKFS-YKSNIQTAILYGGrENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRYLVLDEA 306
Cdd:PRK11776 78 LCPTRELADQVAKEIRRLArFIPNIKVLTLCGG-VPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 307 DRMLDMGFEPQIRKIVGQgMPPKtaRTTAMFSATFPKEIQVLAKDFLKDNyifLAVgRVGSTSEN--IEQRLLWVNEmEK 384
Cdd:PRK11776 157 DRMLDMGFQDAIDAIIRQ-APAR--RQTLLFSATYPEGIAAISQRFQRDP---VEV-KVESTHDLpaIEQRFYEVSP-DE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 385 RSNLMEILMNEHSENLVLVFVETKRGANELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQCPILVATAVAARGLDI 464
Cdd:PRK11776 229 RLPALQRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDI 308
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 71995514 465 PNVRHVINYDLPGDSDEYVHRIGRTGRCGNLGIATSFFNDK 505
Cdd:PRK11776 309 KALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPE 349
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
141-525 |
4.08e-96 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 303.27 E-value: 4.08e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 141 FNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHilaggpdMVKPPAFTNGRRT 220
Cdd:PRK10590 3 FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQH-------LITRQPHAKGRRP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 221 YYpcALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGrENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRY 300
Cdd:PRK10590 76 VR--ALILTPTRELAAQIGENVRDYSKYLNIRSLVVFGG-VSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 301 LVLDEADRMLDMGFEPQIRKIVGQgMPPKtaRTTAMFSATFPKEIQVLAKDFLkDNYIFLAVGRVGSTSENIEQRLLWVN 380
Cdd:PRK10590 153 LVLDEADRMLDMGFIHDIRRVLAK-LPAK--RQNLLFSATFSDDIKALAEKLL-HNPLEIEVARRNTASEQVTQHVHFVD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 381 EMEKRSnLMEILMNEHSENLVLVFVETKRGANELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQCPILVATAVAAR 460
Cdd:PRK10590 229 KKRKRE-LLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAAR 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71995514 461 GLDIPNVRHVINYDLPGDSDEYVHRIGRTGRCGNLGIATSFFNDKNRGIGRDLKNLIvesNQEVP 525
Cdd:PRK10590 308 GLDIEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLL---KKEIP 369
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
150-355 |
9.45e-91 |
|
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: 279.71 E-value: 9.45e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 150 VMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAGGPDMVKPPAftngrrtyypcALVLS 229
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRGPQ-----------ALVLA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 230 PTRELAIQIHKEATKFSYKSNIQTAILYGGrENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRYLVLDEADRM 309
Cdd:cd00268 70 PTRELAMQIAEVARKLGKGTGLKVAAIYGG-APIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRM 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 71995514 310 LDMGFEPQIRKIVGQgMPPKtaRTTAMFSATFPKEIQVLAKDFLKD 355
Cdd:cd00268 149 LDMGFEEDVEKILSA-LPKD--RQTLLFSATLPEEVKELAKKFLKN 191
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
140-501 |
3.49e-90 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 286.87 E-value: 3.49e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 140 HFNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAggpdmvKPPAftNGRR 219
Cdd:PRK04837 9 KFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLS------HPAP--EDRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 220 TYYPCALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGrENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCR 299
Cdd:PRK04837 81 VNQPRALIMAPTRELAVQIHADAEPLAQATGLKLGLAYGG-DGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 300 YLVLDEADRMLDMGFEPQIRKIVgQGMPPKTARTTAMFSATFPKEIQVLAKDFLKD-NYIFLAVGRvgSTSENIEQRLLW 378
Cdd:PRK04837 160 VVVLDEADRMFDLGFIKDIRWLF-RRMPPANQRLNMLFSATLSYRVRELAFEHMNNpEYVEVEPEQ--KTGHRIKEELFY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 379 VNeMEKRSNLMEILMNEHSENLVLVFVETKRGANELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQCPILVATAVA 458
Cdd:PRK04837 237 PS-NEEKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVA 315
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 71995514 459 ARGLDIPNVRHVINYDLPGDSDEYVHRIGRTGRCGNLGIATSF 501
Cdd:PRK04837 316 ARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
123-528 |
7.02e-88 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 283.99 E-value: 7.02e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 123 ENIPVEVSGDSVPAAIEHFNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQH-- 200
Cdd:PLN00206 105 RKLEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRcc 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 201 -ILAGGPDMVKPPaftngrrtyypCALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGRENYRdQVNRLRAGTHILIA 279
Cdd:PLN00206 185 tIRSGHPSEQRNP-----------LAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQ-QLYRIQQGVELIVG 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 280 TPGRLIDIIEQGFIGLAGCRYLVLDEADRMLDMGFEPQIRKIVGQGMPPKTArttaMFSATFPKEIQVLAKDFLKDnYIF 359
Cdd:PLN00206 253 TPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQALSQPQVL----LFSATVSPEVEKFASSLAKD-IIL 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 360 LAVGRVGSTSENIEQRLLWVNEMEKRSNLMEILMN-EHSENLVLVFVETKRGANELAYFLNR-QQIRSVSIHGDLKQIER 437
Cdd:PLN00206 328 ISIGNPNRPNKAVKQLAIWVETKQKKQKLFDILKSkQHFKPPAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKER 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 438 ERNLELFRSGQCPILVATAVAARGLDIPNVRHVINYDLPGDSDEYVHRIGRTGRCGNLGIATSFFNDKNRGIGRDLKNLI 517
Cdd:PLN00206 408 REVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALL 487
|
410
....*....|.
gi 71995514 518 VESNQEVPEWL 528
Cdd:PLN00206 488 KSSGAAIPREL 498
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
141-501 |
1.04e-83 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 270.28 E-value: 1.04e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 141 FNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHIL-----AGGPdmvkppaft 215
Cdd:PRK11192 3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLdfprrKSGP--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 216 ngrrtyyPCALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGReNYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGL 295
Cdd:PRK11192 74 -------PRILILTPTRELAMQVADQARELAKHTHLDIATITGGV-AYMNHAEVFSENQDIVVATPGRLLQYIKEENFDC 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 296 AGCRYLVLDEADRMLDMGFEPQIRKIVGQgmppktAR---TTAMFSATFPKE-IQVLAKDFLKDNyIFLAVGrvGSTSE- 370
Cdd:PRK11192 146 RAVETLILDEADRMLDMGFAQDIETIAAE------TRwrkQTLLFSATLEGDaVQDFAERLLNDP-VEVEAE--PSRREr 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 371 -NIEQRLLWVNEME-KRSNLMEILMNEHSENLVlVFVETKRGANELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQ 448
Cdd:PRK11192 217 kKIHQWYYRADDLEhKTALLCHLLKQPEVTRSI-VFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGR 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 71995514 449 CPILVATAVAARGLDIPNVRHVINYDLPGDSDEYVHRIGRTGRCGNLGIATSF 501
Cdd:PRK11192 296 VNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
141-501 |
2.99e-82 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 267.55 E-value: 2.99e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 141 FNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILaggpdMVKPPAftnGRRT 220
Cdd:PRK01297 89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLL-----QTPPPK---ERYM 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 221 YYPCALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGREnYRDQVNRLRAG-THILIATPGRLIDIIEQGFIGLAGCR 299
Cdd:PRK01297 161 GEPRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMD-FDKQLKQLEARfCDILVATPGRLLDFNQRGEVHLDMVE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 300 YLVLDEADRMLDMGFEPQIRKIVGQgMPPKTARTTAMFSATFPKEIQVLAKDFLKDNYIfLAVGRVGSTSENIEQRLLWV 379
Cdd:PRK01297 240 VMVLDEADRMLDMGFIPQVRQIIRQ-TPRKEERQTLLFSATFTDDVMNLAKQWTTDPAI-VEIEPENVASDTVEQHVYAV 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 380 NEMEKRSNLMEILMNEHSENlVLVFVETKRGANELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQCPILVATAVAA 459
Cdd:PRK01297 318 AGSDKYKLLYNLVTQNPWER-VMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAG 396
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 71995514 460 RGLDIPNVRHVINYDLPGDSDEYVHRIGRTGRCGNLGIATSF 501
Cdd:PRK01297 397 RGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISF 438
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
148-501 |
7.72e-82 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 269.51 E-value: 7.72e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 148 PAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAggpdmvkPPAFTNgRRTYYPCALV 227
Cdd:PRK04537 18 PALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLS-------RPALAD-RKPEDPRALI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 228 LSPTRELAIQIHKEATKFSYKSNIQTAILYGGREnYRDQVNRLRAGTHILIATPGRLIDIIEQ-GFIGLAGCRYLVLDEA 306
Cdd:PRK04537 90 LAPTRELAIQIHKDAVKFGADLGLRFALVYGGVD-YDKQRELLQQGVDVIIATPGRLIDYVKQhKVVSLHACEICVLDEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 307 DRMLDMGFEPQIRKIVGQgMPPKTARTTAMFSATFPKEIQVLAKDFLKDNYIfLAVGRVGSTSENIEQRLLWVNEMEKRS 386
Cdd:PRK04537 169 DRMFDLGFIKDIRFLLRR-MPERGTRQTLLFSATLSHRVLELAYEHMNEPEK-LVVETETITAARVRQRIYFPADEEKQT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 387 NLMEILmnEHSENL-VLVFVETKRGANELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQCPILVATAVAARGLDIP 465
Cdd:PRK04537 247 LLLGLL--SRSEGArTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHID 324
|
330 340 350
....*....|....*....|....*....|....*.
gi 71995514 466 NVRHVINYDLPGDSDEYVHRIGRTGRCGNLGIATSF 501
Cdd:PRK04537 325 GVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISF 360
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
150-360 |
3.25e-79 |
|
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: 249.98 E-value: 3.25e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 150 VMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAggpdmvKPPAftngRRTYYPCALVLS 229
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINA------QPPL----ERGDGPIVLVLA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 230 PTRELAIQIHKEATKFSYKSNIQTAILYGGRENYrDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRYLVLDEADRM 309
Cdd:cd17966 71 PTRELAQQIQQEANKFGGSSRLRNTCVYGGAPKG-PQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRM 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 71995514 310 LDMGFEPQIRKIVGQGMPPktaRTTAMFSATFPKEIQVLAKDFLKDnYIFL 360
Cdd:cd17966 150 LDMGFEPQIRKIVDQIRPD---RQTLMWSATWPKEVRRLAEDFLKD-YIQV 196
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
141-526 |
4.73e-79 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 263.63 E-value: 4.73e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 141 FNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHIlagGPDMVKPPAftngrrt 220
Cdd:PRK11634 8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNL---DPELKAPQI------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 221 yypcaLVLSPTRELAIQIHKEATKFS-YKSNIQTAILYGGrENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCR 299
Cdd:PRK11634 78 -----LVLAPTRELAVQVAEAMTDFSkHMRGVNVVALYGG-QRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 300 YLVLDEADRMLDMGFEPQIRKIVGQgMPPKtaRTTAMFSATFPKEIQVLAKDFLKDNYIFLAVGRVgSTSENIEQRLLWV 379
Cdd:PRK11634 152 GLVLDEADEMLRMGFIEDVETIMAQ-IPEG--HQTALFSATMPEAIRRITRRFMKEPQEVRIQSSV-TTRPDISQSYWTV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 380 NEMEKRSNLMEILMNEHSEnLVLVFVETKRGANELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQCPILVATAVAA 459
Cdd:PRK11634 228 WGMRKNEALVRFLEAEDFD-AAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAA 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71995514 460 RGLDIPNVRHVINYDLPGDSDEYVHRIGRTGRCGNLGIATSFFNDKNRgigRDLKNLIVESNQEVPE 526
Cdd:PRK11634 307 RGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRER---RLLRNIERTMKLTIPE 370
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
150-354 |
1.58e-68 |
|
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: 222.97 E-value: 1.58e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 150 VMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILaggpdmvKPPAFTNGRRTYYPCALVLS 229
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYIS-------RLPPLDEETKDDGPYALILA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 230 PTRELAIQIHKEATKFSYKSNIQTAILYGGReNYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRYLVLDEADRM 309
Cdd:cd17945 74 PTRELAQQIEEETQKFAKPLGIRVVSIVGGH-SIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71995514 310 LDMGFEPQIRKIVGQgMPP------------------KTARTTAMFSATFPKEIQVLAKDFLK 354
Cdd:cd17945 153 IDMGFEPQVTKILDA-MPVsnkkpdteeaeklaasgkHRYRQTMMFTATMPPAVEKIAKGYLR 214
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
150-355 |
5.99e-67 |
|
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: 217.67 E-value: 5.99e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 150 VMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAGgPDMVKPPAftngrrtyyPCALVLS 229
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQ-RELEKGEG---------PIAVIVA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 230 PTRELAIQIHKEATKFSYKSNIQTAILYGGrENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRYLVLDEADRM 309
Cdd:cd17952 71 PTRELAQQIYLEAKKFGKAYNLRVVAVYGG-GSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRM 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 71995514 310 LDMGFEPQIRKIVGQGMPPktaRTTAMFSATFPKEIQVLAKDFLKD 355
Cdd:cd17952 150 FDMGFEYQVRSIVGHVRPD---RQTLLFSATFKKKIEQLARDILSD 192
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
129-355 |
4.03e-66 |
|
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: 216.47 E-value: 4.03e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 129 VSGDSVPAAIEHFNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAGGPdm 208
Cdd:cd17953 2 VRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRP-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 209 VKPpafTNGrrtyyPCALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGrENYRDQVNRLRAGTHILIATPGRLIDII 288
Cdd:cd17953 80 VKP---GEG-----PIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGG-SGISEQIAELKRGAEIVVCTPGRMIDIL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 289 --EQGFI-GLAGCRYLVLDEADRMLDMGFEPQIRKIVGQGMPPktaRTTAMFSATFPKEIQVLAKDFLKD 355
Cdd:cd17953 151 taNNGRVtNLRRVTYVVLDEADRMFDMGFEPQIMKIVNNIRPD---RQTVLFSATFPRKVEALARKVLHK 217
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
127-363 |
1.28e-63 |
|
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: 210.64 E-value: 1.28e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 127 VEVSGDSVPAAIEHFNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHIlaggp 206
Cdd:cd18049 12 ITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHI----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 207 dmVKPPAFTNGRRtyyPCALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGRENyRDQVNRLRAGTHILIATPGRLID 286
Cdd:cd18049 87 --NHQPFLERGDG---PICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPK-GPQIRDLERGVEICIATPGRLID 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71995514 287 IIEQGFIGLAGCRYLVLDEADRMLDMGFEPQIRKIVGQGMPPktaRTTAMFSATFPKEIQVLAKDFLKDnYIFLAVG 363
Cdd:cd18049 161 FLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPD---RQTLMWSATWPKEVRQLAEDFLKD-YIHINIG 233
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
372-502 |
2.16e-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: 203.12 E-value: 2.16e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 372 IEQRLLWVNEMEKRSNLMEILMNEHSENLVLVFVETKRGANELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQCPI 451
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 71995514 452 LVATAVAARGLDIPNVRHVINYDLPGDSDEYVHRIGRTGRCGNLGIATSFF 502
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
137-528 |
1.10e-61 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 210.84 E-value: 1.10e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 137 AIEHFNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHIlagGPDMVKppaftn 216
Cdd:PTZ00424 26 IVDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLI---DYDLNA------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 217 grrtyypC-ALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGrENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGL 295
Cdd:PTZ00424 97 -------CqALILAPTRELAQQIQKVVLALGDYLKVRCHACVGG-TVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 296 AGCRYLVLDEADRMLDMGFEPQIRKIVgQGMPPKTarTTAMFSATFPKEIQVLAKDFLKDNYIFLaVGRVGSTSENIEQR 375
Cdd:PTZ00424 169 DDLKLFILDEADEMLSRGFKGQIYDVF-KKLPPDV--QVALFSATMPNEILELTTKFMRDPKRIL-VKKDELTLEGIRQF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 376 LLWVNEMEKRSNLMEILMNEHSENLVLVFVETKRGANELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQCPILVAT 455
Cdd:PTZ00424 245 YVAVEKEEWKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITT 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71995514 456 AVAARGLDIPNVRHVINYDLPGDSDEYVHRIGRTGRCGNLGIATSFFNDKN----RGIGRDLKNLIVESNQEVPEWL 528
Cdd:PTZ00424 325 DLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDieqlKEIERHYNTQIEEMPMEVADYL 401
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
150-355 |
1.91e-60 |
|
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: 200.77 E-value: 1.91e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 150 VMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAGGPDMVKPPAftngrrtyyPCALVLS 229
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPREQRNG---------PGVLVLT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 230 PTRELAIQIHKEATKFSYKsNIQTAILYGGReNYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRYLVLDEADRM 309
Cdd:cd17958 72 PTRELALQIEAECSKYSYK-GLKSVCVYGGG-NRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRM 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 71995514 310 LDMGFEPQIRKIVGQGMPPktaRTTAMFSATFPKEIQVLAKDFLKD 355
Cdd:cd17958 150 LDMGFEPQIRKILLDIRPD---RQTIMTSATWPDGVRRLAQSYLKD 192
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
150-363 |
1.09e-59 |
|
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: 198.58 E-value: 1.09e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 150 VMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAggpdmvkpPAFTNGRRtyypcALVLS 229
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGK--------PRKKKGLR-----ALILA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 230 PTRELAIQIHKEATKFSYKSNIQTAILYGGRENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRYLVLDEADRM 309
Cdd:cd17957 68 PTRELASQIYRELLKLSKGTGLRIVLLSKSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 71995514 310 LDMGFEPQIRKIVGQGMPPKTarTTAMFSATFPKEIQVLAKDFLKDnYIFLAVG 363
Cdd:cd17957 148 FEPGFREQTDEILAACTNPNL--QRSLFSATIPSEVEELARSVMKD-PIRIIVG 198
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
127-363 |
1.56e-59 |
|
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: 201.01 E-value: 1.56e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 127 VEVSGDSVPAAIEHFNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHIlaggp 206
Cdd:cd18050 50 ITIRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHI----- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 207 dmVKPPAFTNGRRtyyPCALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGRENyRDQVNRLRAGTHILIATPGRLID 286
Cdd:cd18050 125 --NHQPYLERGDG---PICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPK-GPQIRDLERGVEICIATPGRLID 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71995514 287 IIEQGFIGLAGCRYLVLDEADRMLDMGFEPQIRKIVGQGMPPktaRTTAMFSATFPKEIQVLAKDFLKDnYIFLAVG 363
Cdd:cd18050 199 FLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPD---RQTLMWSATWPKEVRQLAEDFLRD-YVQINIG 271
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
148-360 |
3.98e-58 |
|
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: 194.72 E-value: 3.98e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 148 PAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSC-AQTGSGKTAAFLLPIIQHILAGgpdmvkPPAFTNGRRTyypcAL 226
Cdd:cd17964 3 PSLLKALTRMGFETMTPVQQKTLKPILSTGDDVLArAKTGTGKTLAFLLPAIQSLLNT------KPAGRRSGVS----AL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 227 VLSPTRELAIQIHKEATKFSYKS---NIQTAIlyGGRENYRDQVNRLRAGTHILIATPGRLIDIIE-QGFIG-LAGCRYL 301
Cdd:cd17964 73 IISPTRELALQIAAEAKKLLQGLrklRVQSAV--GGTSRRAELNRLRRGRPDILVATPGRLIDHLEnPGVAKaFTDLDYL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71995514 302 VLDEADRMLDMGFEPQIRKIVgQGMPPKTA--RTTAMFSATFPKEIQVLAKDFLKDNYIFL 360
Cdd:cd17964 151 VLDEADRLLDMGFRPDLEQIL-RHLPEKNAdpRQTLLFSATVPDEVQQIARLTLKKDYKFI 210
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
158-354 |
1.14e-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: 187.85 E-value: 1.14e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 158 GYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILaggpdmVKPPAFTNGRrtyypcALVLSPTRELAIQ 237
Cdd:cd17947 9 GFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLL------YRPKKKAATR------VLVLVPTRELAMQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 238 IHKEATKFSYKSNIQTAILYGGReNYRDQVNRLRAGTHILIATPGRLIDIIEQGF-IGLAGCRYLVLDEADRMLDMGFEP 316
Cdd:cd17947 77 CFSVLQQLAQFTDITFALAVGGL-SLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGFAD 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 71995514 317 QIRKIVgqGMPPKTaRTTAMFSATFPKEIQVLAKDFLK 354
Cdd:cd17947 156 ELKEIL--RLCPRT-RQTMLFSATMTDEVKDLAKLSLN 190
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
163-346 |
4.00e-55 |
|
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: 185.14 E-value: 4.00e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 163 TPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAGGpdmvkppaftNGRRtyypcALVLSPTRELAIQIHKEA 242
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLD----------NGPQ-----ALVLAPTRELAEQIYEEL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 243 TKFSYKSNIQTAILYGGrENYRDQVNRLRaGTHILIATPGRLIDIIEQGFiGLAGCRYLVLDEADRMLDMGFEPQIRKIV 322
Cdd:pfam00270 66 KKLGKGLGLKVASLLGG-DSRKEQLEKLK-GPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEIL 142
|
170 180
....*....|....*....|....
gi 71995514 323 GQgMPPKtaRTTAMFSATFPKEIQ 346
Cdd:pfam00270 143 RR-LPKK--RQILLLSATLPRNLE 163
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
141-360 |
1.23e-54 |
|
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: 185.51 E-value: 1.23e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 141 FNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQhILAGGPdmvkppaftngrrt 220
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQ-RLSEDP-------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 221 YYPCALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGRENYRdQVNRLRAGTHILIATPGRLIDIIE---QGFIGLAG 297
Cdd:cd17955 66 YGIFALVLTPTRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVK-QALELSKRPHIVVATPGRLADHLRssdDTTKVLSR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71995514 298 CRYLVLDEADRMLDMGFEPQIRKIVGQgMPPKtaRTTAMFSATFPKEIQVLAKDFLKDNYIFL 360
Cdd:cd17955 145 VKFLVLDEADRLLTGSFEDDLATILSA-LPPK--RQTLLFSATLTDALKALKELFGNKPFFWE 204
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
154-356 |
5.01e-54 |
|
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: 183.94 E-value: 5.01e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 154 VNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAggpdmvKPPAFTngrRTYYPCALVLSPTRE 233
Cdd:cd17949 6 KSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLS------LEPRVD---RSDGTLALVLVPTRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 234 LAIQIHKEATKF-SYKSNIQTAILYGGrENYRDQVNRLRAGTHILIATPGRLIDIIE--QGFiGLAGCRYLVLDEADRML 310
Cdd:cd17949 77 LALQIYEVLEKLlKPFHWIVPGYLIGG-EKRKSEKARLRKGVNILIATPGRLLDHLKntQSF-DVSNLRWLVLDEADRLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 71995514 311 DMGFEPQIRKIV----------GQGMPPKTARTTAMFSATFPKEIQVLAKDFLKDN 356
Cdd:cd17949 155 DMGFEKDITKILellddkrskaGGEKSKPSRRQTVLVSATLTDGVKRLAGLSLKDP 210
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
141-355 |
5.67e-54 |
|
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: 183.67 E-value: 5.67e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 141 FNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILaggpdmvkppaftNGRRT 220
Cdd:cd17954 2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALL-------------ENPQR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 221 YYpcALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGReNYRDQVNRLRAGTHILIATPGRLIDIIEQ--GFiGLAGC 298
Cdd:cd17954 69 FF--ALVLAPTRELAQQISEQFEALGSSIGLKSAVLVGGM-DMMAQAIALAKKPHVIVATPGRLVDHLENtkGF-SLKSL 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 71995514 299 RYLVLDEADRMLDMGFEPQIRKIVGQgMPpkTARTTAMFSATFPKEIQVLAKDFLKD 355
Cdd:cd17954 145 KFLVMDEADRLLNMDFEPEIDKILKV-IP--RERTTYLFSATMTTKVAKLQRASLKN 198
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
141-355 |
9.89e-54 |
|
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: 182.89 E-value: 9.89e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 141 FNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHIlaggpdmvKPPAFTNGRRt 220
Cdd:cd17959 3 FQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKL--------KAHSPTVGAR- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 221 yypcALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGrENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRY 300
Cdd:cd17959 74 ----ALILSPTRELALQTLKVTKELGKFTDLRTALLVGG-DSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEY 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 71995514 301 LVLDEADRMLDMGFEPQIRKIVGQgMPPktARTTAMFSATFPKEIQVLAKDFLKD 355
Cdd:cd17959 149 VVFDEADRLFEMGFAEQLHEILSR-LPE--NRQTLLFSATLPKLLVEFAKAGLNE 200
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
150-353 |
2.23e-51 |
|
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: 176.61 E-value: 2.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 150 VMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAGGPDMvKPPAFTngrrtyypcALVLS 229
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANL-KKGQVG---------ALIIS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 230 PTRELAIQIHKEATKF--SYKSNIQTAILYGGRENYRDQVNRLRAGTHILIATPGRLIDIIE--QGFIGLAGCRYLVLDE 305
Cdd:cd17960 71 PTRELATQIYEVLQSFleHHLPKLKCQLLIGGTNVEEDVKKFKRNGPNILVGTPGRLEELLSrkADKVKVKSLEVLVLDE 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 71995514 306 ADRMLDMGFEPQIRKIVGQgmPPKTaRTTAMFSATFPKEIQVLAKDFL 353
Cdd:cd17960 151 ADRLLDLGFEADLNRILSK--LPKQ-RRTGLFSATQTDAVEELIKAGL 195
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
154-375 |
1.77e-50 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 174.22 E-value: 1.77e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 154 VNRSGYSKPTPVQKHSIPTLLAN-RDLMSCAQTGSGKTAAFLLPIIQHIlaggpdmvkppaftngRRTYYPCALVLSPTR 232
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAL----------------KRGKGGRVLVLVPTR 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 233 ELAIQIHKEATKFSYKSNIQTAILYGGrENYRDQVNRLRAG-THILIATPGRLIDIIEQGFIGLAGCRYLVLDEADRMLD 311
Cdd:smart00487 65 ELAEQWAEELKKLGPSLGLKVVGLYGG-DSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLD 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71995514 312 MGFEPQIRKIVGQgMPPKtaRTTAMFSATFPKEIQVLAKDFLKdNYIFLAVGRvgSTSENIEQR 375
Cdd:smart00487 144 GGFGDQLEKLLKL-LPKN--VQLLLLSATPPEEIENLLELFLN-DPVFIDVGF--TPLEPIEQF 201
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
141-357 |
1.85e-47 |
|
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or p54) participates in mRNA regulation mediated by miRNA-mediated silencing. It also plays a role in global and transcript-specific messenger RNA (mRNA) storage, translational repression, and decay. It is a member of the DEAD-box helicase family, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350698 [Multi-domain] Cd Length: 201 Bit Score: 165.93 E-value: 1.85e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 141 FNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHIlaggpDMVKppaftngrrt 220
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKI-----DPKK---------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 221 YYPCALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGrENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRY 300
Cdd:cd17940 66 DVIQALILVPTRELALQTSQVCKELGKHMGVKVMVTTGG-TSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKT 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 71995514 301 LVLDEADRMLDMGFEPQIRKIVGQgMPPKtaRTTAMFSATFPKEIQVLAKDFLKDNY 357
Cdd:cd17940 145 LVLDEADKLLSQDFQPIIEKILNF-LPKE--RQILLFSATFPLTVKNFMDRHMHNPY 198
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
158-353 |
3.07e-47 |
|
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: 165.59 E-value: 3.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 158 GYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAggPDMVKPPAFTNGrrtyyPCALVLSPTRELAIQ 237
Cdd:cd17951 9 GIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALE--QEKKLPFIKGEG-----PYGLIVCPSRELARQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 238 IHKEATKFSYK------SNIQTAILYGGrENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRYLVLDEADRMLD 311
Cdd:cd17951 82 THEVIEYYCKAlqeggyPQLRCLLCIGG-MSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 71995514 312 MGFEPQIRKIV----GQgmppktaRTTAMFSATFPKEIQVLAKDFL 353
Cdd:cd17951 161 MGFEEDIRTIFsyfkGQ-------RQTLLFSATMPKKIQNFAKSAL 199
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
155-360 |
8.64e-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: 164.00 E-value: 8.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 155 NRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILA---GGPDMVKppaftngrrtyypcALVLSPT 231
Cdd:cd17941 6 KEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRerwTPEDGLG--------------ALIISPT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 232 RELAIQIHKEATKFSYKSNIQTAILYGGReNYRDQVNRLrAGTHILIATPGRLIDIIEQ--GFiGLAGCRYLVLDEADRM 309
Cdd:cd17941 72 RELAMQIFEVLRKVGKYHSFSAGLIIGGK-DVKEEKERI-NRMNILVCTPGRLLQHMDEtpGF-DTSNLQMLVLDEADRI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 71995514 310 LDMGFEPQIRKIVGQgMPPKtaRTTAMFSATFPKEIQVLAKDFLKD-NYIFL 360
Cdd:cd17941 149 LDMGFKETLDAIVEN-LPKS--RQTLLFSATQTKSVKDLARLSLKNpEYISV 197
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
153-355 |
1.67e-45 |
|
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: 160.41 E-value: 1.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 153 NVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQhilaggpdmvkppaftngRRTYY---PCALVLS 229
Cdd:cd17962 4 NLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVII------------------RCLTEhrnPSALILT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 230 PTRELAIQIHKEATKF-SYKSNIQTAILYGGrENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRYLVLDEADR 308
Cdd:cd17962 66 PTRELAVQIEDQAKELmKGLPPMKTALLVGG-LPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADT 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 71995514 309 MLDMGFEPQIRKIVgQGMPPKtaRTTAMFSATFPKEIQVLAKDFLKD 355
Cdd:cd17962 145 MLKMGFQQQVLDIL-ENISHD--HQTILVSATIPRGIEQLAGQLLQN 188
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
141-340 |
1.33e-42 |
|
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: 152.48 E-value: 1.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 141 FNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAggpdmvkppaftngrrt 220
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIVVA----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 221 yypcaLVLSPTRELAIQIHKEATKFSY---KSNIQTAILYGGrENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAG 297
Cdd:cd17938 64 -----LILEPSRELAEQTYNCIENFKKyldNPKLRVALLIGG-VKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSS 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 71995514 298 CRYLVLDEADRMLDMGFEPQIRKIVGQgMPPKTAR----TTAMFSAT 340
Cdd:cd17938 138 VRFFVLDEADRLLSQGNLETINRIYNR-IPKITSDgkrlQVIVCSAT 183
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
158-355 |
2.02e-40 |
|
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: 146.32 E-value: 2.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 158 GYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHIlaggpdmvkppaftnGRRTYYPCALVLSPTRELAIQ 237
Cdd:cd17939 16 GFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRI---------------DTTVRETQALVLAPTRELAQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 238 IHKEATKFSYKSNIQTAILYGGrENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRYLVLDEADRMLDMGFEPQ 317
Cdd:cd17939 81 IQKVVKALGDYMGVKVHACIGG-TSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQ 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 71995514 318 IRKIVgQGMPPKTarTTAMFSATFPKEIQVLAKDFLKD 355
Cdd:cd17939 160 IYDIF-QFLPPET--QVVLFSATMPHEVLEVTKKFMRD 194
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
158-355 |
3.37e-40 |
|
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: 146.19 E-value: 3.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 158 GYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILaggpdMVKppafTNGRRTYYPCALVLSPTRELAIQ 237
Cdd:cd17961 13 GWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIL-----KAK----AESGEEQGTRALILVPTRELAQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 238 IHKEATKFSYKSNIQTAIL-YGGRENYRDQVNRLRAGTHILIATPGRLIDIIEQG-FIGLAGCRYLVLDEADRMLDMGFE 315
Cdd:cd17961 84 VSKVLEQLTAYCRKDVRVVnLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGsLLLLSTLKYLVIDEADLVLSYGYE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 71995514 316 PQIRKIVGQGmpPKTARTTAMfSATFPKEIQVLAKDFLKD 355
Cdd:cd17961 164 EDLKSLLSYL--PKNYQTFLM-SATLSEDVEALKKLVLHN 200
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
158-360 |
6.89e-40 |
|
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: 144.81 E-value: 6.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 158 GYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAggpdmVKppaFTNGRRTyypCALVLSPTRELAIQ 237
Cdd:cd17942 9 GFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYK-----LK---FKPRNGT---GVIIISPTRELALQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 238 IH---KEATKFsyksNIQTAILYGGRENYRDQVNRLRAGTHILIATPGRLIDIIE--QGFIgLAGCRYLVLDEADRMLDM 312
Cdd:cd17942 78 IYgvaKELLKY----HSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQntKGFL-YKNLQCLIIDEADRILEI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 71995514 313 GFEPQIRKIVgqGMPPKTaRTTAMFSATFPKEIQVLAKDFLKDNYIFL 360
Cdd:cd17942 153 GFEEEMRQII--KLLPKR-RQTMLFSATQTRKVEDLARISLKKKPLYV 197
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
150-346 |
2.04e-39 |
|
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: 145.07 E-value: 2.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 150 VMENVNRSGYSKPTPVQKHSIPTLLANR-DLMSCAQTGSGKTAAFLLPIIQHILAGGPDMVKPPAFTngrrtyYPCALVL 228
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRDGkDVIGAAETGSGKTLAFGIPILERLLSQKSSNGVGGKQK------PLRALIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 229 SPTRELAIQI--H-KEATKFsykSNIQTAILYGGRENYRdQVNRLRAGTHILIATPGRLIDIIEQG--FIG-LAGCRYLV 302
Cdd:cd17946 75 TPTRELAVQVkdHlKAIAKY---TNIKIASIVGGLAVQK-QERLLKKRPEIVVATPGRLWELIQEGneHLAnLKSLRFLV 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 71995514 303 LDEADRMLDMG-FEP--QIRKIVGQGMP-PKTARTTAMFSATFPKEIQ 346
Cdd:cd17946 151 LDEADRMLEKGhFAEleKILELLNKDRAgKKRKRQTFVFSATLTLDHQ 198
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
383-493 |
3.71e-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: 139.65 E-value: 3.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 383 EKRSNLMEILmNEHSENLVLVFVETKRGAnELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQCPILVATAVAARGL 462
Cdd:pfam00271 1 EKLEALLELL-KKERGGKVLIFSQTKKTL-EAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
|
90 100 110
....*....|....*....|....*....|.
gi 71995514 463 DIPNVRHVINYDLPGDSDEYVHRIGRTGRCG 493
Cdd:pfam00271 79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
150-350 |
4.41e-36 |
|
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: 135.57 E-value: 4.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 150 VMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAggpDMVKPpaftnGRRTYYPCALVLS 229
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLR---YKLLA-----EGPFNAPRGLVIT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 230 PTRELAIQIHKEATKFSYKSNIQTAILYGGReNYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRYLVLDEADRM 309
Cdd:cd17948 73 PSRELAEQIGSVAQSLTEGLGLKVKVITGGR-TKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 71995514 310 LDMGFEPQIRKIVGQ------------GMPPKTARTTAmfSATFPKEI-QVLAK 350
Cdd:cd17948 152 LDDSFNEKLSHFLRRfplasrrsentdGLDPGTQLVLV--SATMPSGVgEVLSK 203
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
164-358 |
5.04e-35 |
|
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: 131.51 E-value: 5.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 164 PVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAGGPDMvkppaftngRRTYYPCALVLSPTRELAIQIHKEAT 243
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPR---------KRGRAPKVLVLAPTRELANQVTKDFK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 244 KFSYKSNIqtAILYGGrENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRYLVLDEADRMLDMGFEPQIRKI-- 321
Cdd:cd17944 86 DITRKLSV--ACFYGG-TPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEIls 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 71995514 322 VGQGMPPKTARTTAMFSATFPKEIQVLAKDFLKDNYI 358
Cdd:cd17944 163 VSYKKDSEDNPQTLLFSATCPDWVYNVAKKYMKSQYE 199
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
158-355 |
8.24e-35 |
|
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: 131.03 E-value: 8.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 158 GYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAGGPDmvkppaftngrrtyyPCALVLSPTRELAIQ 237
Cdd:cd18046 18 GFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKA---------------TQALVLAPTRELAQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 238 IHKEATKFSYKSNIQTAILYGGrENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRYLVLDEADRMLDMGFEPQ 317
Cdd:cd18046 83 IQKVVMALGDYMGIKCHACIGG-TSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKDQ 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 71995514 318 IRKIVgQGMPPKTarTTAMFSATFPKEIQVLAKDFLKD 355
Cdd:cd18046 162 IYDIF-QKLPPDT--QVVLLSATMPNDVLEVTTKFMRD 196
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
141-355 |
8.99e-35 |
|
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: 130.93 E-value: 8.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 141 FNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHIlaggpdmVKPPAFTNgrrt 220
Cdd:cd17950 4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQL-------EPVDGQVS---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 221 yypcALVLSPTRELAIQIHKEATKFS-YKSNIQTAILYGGReNYRDQVNRLRAGT-HILIATPGRLIDIIEQGFIGLAGC 298
Cdd:cd17950 73 ----VLVICHTRELAFQISNEYERFSkYMPNVKTAVFFGGV-PIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHV 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 71995514 299 RYLVLDEADRML-DMGFEPQIRKIVgqGMPPKTaRTTAMFSATFPKEIQVLAKDFLKD 355
Cdd:cd17950 148 KHFVLDECDKMLeQLDMRRDVQEIF--RATPHD-KQVMMFSATLSKEIRPVCKKFMQD 202
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
148-355 |
2.65e-33 |
|
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: 126.54 E-value: 2.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 148 PAVMENVNRSGYSKPTPVQKHSIPTLLAN--RDLMSCAQTGSGKTAAFLLPIIQHIlaggpDMVKPpaftngrrtyYPCA 225
Cdd:cd17963 3 PELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRV-----DPTLK----------SPQA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 226 LVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGRENYRDQvnrlRAGTHILIATPGRLIDIIEQGFIGLAGCRYLVLDE 305
Cdd:cd17963 68 LCLAPTRELARQIGEVVEKMGKFTGVKVALAVPGNDVPRGK----KITAQIVIGTPGTVLDWLKKRQLDLKKIKILVLDE 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 71995514 306 ADRMLDM-GFEPQIRKIvgQGMPPKTARTTaMFSATFPKEIQVLAKDFLKD 355
Cdd:cd17963 144 ADVMLDTqGHGDQSIRI--KRMLPRNCQIL-LFSATFPDSVRKFAEKIAPN 191
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
150-343 |
5.67e-33 |
|
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: 125.45 E-value: 5.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 150 VMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAGgpdmvkppaftngRRTyyPCALVLS 229
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLE-------------RRH--PQVLILA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 230 PTRELAIQIHKEATKF-SYKSNIQTAILYGGRENYRDqVNRLRaGTHILIATPGRLIDIIEQGFIGLAGCRYLVLDEADR 308
Cdd:cd17943 66 PTREIAVQIHDVFKKIgKKLEGLKCEVFIGGTPVKED-KKKLK-GCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADK 143
|
170 180 190
....*....|....*....|....*....|....*
gi 71995514 309 MLDMGFEPQIRKIVGQgMPPKtaRTTAMFSATFPK 343
Cdd:cd17943 144 LMEGSFQKDVNWIFSS-LPKN--KQVIAFSATYPK 175
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
150-315 |
2.68e-32 |
|
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: 124.67 E-value: 2.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 150 VMENVNRSGYSKPTPVQKHSIPTLLAN---------RDLMSCAQTGSGKTAAFLLPIIQhILAGGPDmvkppaftngRRT 220
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQ-ALSKRVV----------PRL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 221 YypcALVLSPTRELAIQIHKEATKFSYKSNIQTAILyGGRENYRDQVNRLRAGTH--------ILIATPGRLIDIIEQ-- 290
Cdd:cd17956 70 R---ALIVVPTKELVQQVYKVFESLCKGTGLKVVSL-SGQKSFKKEQKLLLVDTSgrylsrvdILVATPGRLVDHLNStp 145
|
170 180
....*....|....*....|....*
gi 71995514 291 GFIgLAGCRYLVLDEADRMLDMGFE 315
Cdd:cd17956 146 GFT-LKHLRFLVIDEADRLLNQSFQ 169
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
141-355 |
2.97e-32 |
|
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: 123.73 E-value: 2.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 141 FNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILaggpdmvkppafTNGRRT 220
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLD------------IQVRET 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 221 YypcALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGReNYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRY 300
Cdd:cd18045 69 Q---ALILSPTRELAVQIQKVLLALGDYMNVQCHACIGGT-SVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKM 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 71995514 301 LVLDEADRMLDMGFEPQIRKIVgQGMPPKTarTTAMFSATFPKEIQVLAKDFLKD 355
Cdd:cd18045 145 LVLDEADEMLNKGFKEQIYDVY-RYLPPAT--QVVLVSATLPQDILEMTNKFMTD 196
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
413-493 |
1.64e-30 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 114.62 E-value: 1.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 413 ELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQCPILVATAVAARGLDIPNVRHVINYDLPGDSDEYVHRIGRTGRC 492
Cdd:smart00490 2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRA 81
|
.
gi 71995514 493 G 493
Cdd:smart00490 82 G 82
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
152-344 |
3.50e-24 |
|
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: 102.07 E-value: 3.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 152 ENVNRSGYSKPTPVQKHSIPTLLANR----------------DLMSCAQTGSGKTAAFLLPIIQHILAG--GPDMVKPPA 213
Cdd:cd17965 21 GSNKTDEEIKPSPIQTLAIKKLLKTLmrkvtkqtsneepkleVFLLAAETGSGKTLAYLAPLLDYLKRQeqEPFEEAEEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 214 FTNGRRTYYPCALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGR-ENYRDQVNRLRAGTHILIATPGRLIDIIEQGF 292
Cdd:cd17965 101 YESAKDTGRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFgPSYQRLQLAFKGRIDILVTTPGKLASLAKSRP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 71995514 293 IGLAGCRYLVLDEADRMLDMGFEPQIRKIVGQGMPPKTArttAMFSATFPKE 344
Cdd:cd17965 181 KILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHL---ILCSATIPKE 229
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
185-488 |
2.07e-20 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 95.48 E-value: 2.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 185 TGSGKTAAFLLpIIQHILAGGPdmvkppaftngrrtyypcALVLSPTRELAIQIHKEATKFSYKsniqtAILYGGRENyr 264
Cdd:COG1061 109 TGTGKTVLALA-LAAELLRGKR------------------VLVLVPRRELLEQWAEELRRFLGD-----PLAGGGKKD-- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 265 dqvnrlrAGTHILIATPGRLIDIIEQGFIGlAGCRYLVLDEADRmldmGFEPQIRKIVGQGMPPK----TA---RTTA-- 335
Cdd:COG1061 163 -------SDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHH----AGAPSYRRILEAFPAAYrlglTAtpfRSDGre 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 336 MFSATFPKEI------QVLAKDFLKDnYIFLAV--------GRVGSTSENIEQRLLWVNEMeKRSNLMEILMNEHSENLV 401
Cdd:COG1061 231 ILLFLFDGIVyeyslkEAIEDGYLAP-PEYYGIrvdltderAEYDALSERLREALAADAER-KDKILRELLREHPDDRKT 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 402 LVFVETKRGANELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQCPILVATAVAARGLDIPNVRHVINYDLPGDSDE 481
Cdd:COG1061 309 LVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPRE 388
|
....*..
gi 71995514 482 YVHRIGR 488
Cdd:COG1061 389 FIQRLGR 395
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
137-355 |
2.98e-19 |
|
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: 87.38 E-value: 2.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 137 AIEHFNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLAN--RDLMSCAQTGSGKTAAFLLPIIQHIlaggpdmvkppaf 214
Cdd:cd18048 16 SVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRV------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 215 tNGRRTYYPCaLVLSPTRELAIQIHK---EATKFSykSNIQtaILYGGRENYRDQVNRLRAgtHILIATPGRLID-IIEQ 290
Cdd:cd18048 83 -DALKLYPQC-LCLSPTFELALQTGKvveEMGKFC--VGIQ--VIYAIRGNRPGKGTDIEA--QIVIGTPGTVLDwCFKL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71995514 291 GFIGLAGCRYLVLDEADRMLDM-GFEPQIRKIvgQGMPPKTARTTaMFSATFPKEIQVLAKDFLKD 355
Cdd:cd18048 155 RLIDVTNISVFVLDEADVMINVqGHSDHSVRV--KRSMPKECQML-LFSATFEDSVWAFAERIVPD 217
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
141-355 |
8.22e-18 |
|
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: 82.46 E-value: 8.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 141 FNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLAN--RDLMSCAQTGSGKTAAFLLPIIQHIlaggpdmvkPPAftngr 218
Cdd:cd18047 3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV---------EPA----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 219 rTYYPCALVLSPTRELAIQIHKEATKFSyKSNIQTAILYGGRENYRDQVNRLRagTHILIATPGRLID-IIEQGFIGLAG 297
Cdd:cd18047 69 -NKYPQCLCLSPTYELALQTGKVIEQMG-KFYPELKLAYAVRGNKLERGQKIS--EQIVIGTPGTVLDwCSKLKFIDPKK 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 71995514 298 CRYLVLDEADRML-DMGFEPQIRKIvgQGMPPKTARTTaMFSATFPKEIQVLAKDFLKD 355
Cdd:cd18047 145 IKVFVLDEADVMIaTQGHQDQSIRI--QRMLPRNCQML-LFSATFEDSVWKFAQKVVPD 200
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
264-509 |
2.64e-16 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 82.11 E-value: 2.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 264 RDQV-NRLRAG-THILIATPGRL-----IDIIEQGFIGLagcryLVLDEA--------DrmldmgFEP---QIRKIVGQ- 324
Cdd:COG0514 96 RREVlRALRAGeLKLLYVAPERLlnprfLELLRRLKISL-----FAIDEAhcisqwghD------FRPdyrRLGELRERl 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 325 GMPPktartTAMFSATFPKEIQ--VLAKDFLKDNYIFLA-VGRvgstsENIEQRLLWVNEMEKRSNLMEILmNEHSENLV 401
Cdd:COG0514 165 PNVP-----VLALTATATPRVRadIAEQLGLEDPRVFVGsFDR-----PNLRLEVVPKPPDDKLAQLLDFL-KEHPGGSG 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 402 LVFVETKRGANELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQCPILVATaVA-ARGLDIPNVRHVINYDLPGDSD 480
Cdd:COG0514 234 IVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLPKSIE 312
|
250 260
....*....|....*....|....*....
gi 71995514 481 EYVHRIGRTGRCGNLGIATSFFNDKNRGI 509
Cdd:COG0514 313 AYYQEIGRAGRDGLPAEALLLYGPEDVAI 341
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
374-491 |
2.58e-15 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 79.77 E-value: 2.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 374 QRLLW---VNEMEKRSN-----------LMEIL---MNEHSENLVLVFVETKRGANELAYFLNRQQIRSV------SIHG 430
Cdd:COG1111 312 KRLVSdprFRKAMRLAEeadiehpklskLREILkeqLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGrfvgqaSKEG 391
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71995514 431 D--LKQIERERNLELFRSGQCPILVATAVAARGLDIPNVRHVINYDlPGDSD-EYVHRIGRTGR 491
Cdd:COG1111 392 DkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYE-PVPSEiRSIQRKGRTGR 454
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
147-491 |
2.11e-13 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 73.01 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 147 GPAVMENVNRSGYSKPTPVQKHSIP-TLLANRDLMSCAQTGSGKTAAFLLPIIQHILAGGpdmvkppaftngrrtyypCA 225
Cdd:COG1204 8 LEKVIEFLKERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKALLNGG------------------KA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 226 LVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGREnyrdqVNRLRAGTH-ILIATPGRLIDIIEQGFIGLAGCRYLVLD 304
Cdd:COG1204 70 LYIVPLRALASEKYREFKRDFEELGIKVGVSTGDYD-----SDDEWLGRYdILVATPEKLDSLLRNGPSWLRDVDLVVVD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 305 EA----------------DRMLDMGFEPQirkIVGqgmppktarttamFSATF--PKEI-QVLAKDFLKDNY--IFLAVG 363
Cdd:COG1204 145 EAhliddesrgptlevllARLRRLNPEAQ---IVA-------------LSATIgnAEEIaEWLDAELVKSDWrpVPLNEG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 364 RVgstsenIEQRLLWVNEMEKRSNLMEILMNEHSENL--VLVFVETKRGANELA-----------YFLNRQQIRSVSI-- 428
Cdd:COG1204 209 VL------YDGVLRFDDGSRRSKDPTLALALDLLEEGgqVLVFVSSRRDAESLAkkladelkrrlTPEEREELEELAEel 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 429 ------------------------HGDLKQIERERNLELFRSGQCPILVATAVAARGLDIPnVRHVI--NYDLPGDSD-- 480
Cdd:COG1204 283 levseethtnekladclekgvafhHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLP-ARRVIirDTKRGGMVPip 361
|
410
....*....|...
gi 71995514 481 --EYVHRIGRTGR 491
Cdd:COG1204 362 vlEFKQMAGRAGR 374
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
182-340 |
7.16e-13 |
|
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: 66.27 E-value: 7.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 182 CAQTGSGKTAAFLLPIIQHILAGGPDmvkppaftngrrtyypcALVLSPTRELAIQiHKEATKFSYKSNIQTAILYGGRE 261
Cdd:cd00046 7 TAPTGSGKTLAALLAALLLLLKKGKK-----------------VLVLVPTKALALQ-TAERLRELFGPGIRVAVLVGGSS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 262 NYRDQVNRLRAgTHILIATPGRLIDIIEQ-GFIGLAGCRYLVLDEADRMLDMGFEPQIRKIVGQGMPPKTARTTAMfSAT 340
Cdd:cd00046 69 AEEREKNKLGD-ADIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQVILL-SAT 146
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
369-502 |
1.12e-12 |
|
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: 65.31 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 369 SENIEQRLLWVNEMEKRSNLMEILMNEHSENLVLVFVETKRGANELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQ 448
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 71995514 449 CPILVATAVAARGLDIPNVRHVINYDLPGDSDEYVHRIGRTGRCGNLGIATSFF 502
Cdd:cd18794 81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
388-488 |
1.62e-12 |
|
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: 65.31 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 388 LMEILMNE--HSENLV-LVFVETKRGANELAYFLNRQQIRSVSIHGD---------------LKQIERERNLELFRSGQC 449
Cdd:cd18802 12 LIEILREYfpKTPDFRgIIFVERRATAVVLSRLLKEHPSTLAFIRCGfligrgnssqrkrslMTQRKQKETLDKFRDGEL 91
|
90 100 110
....*....|....*....|....*....|....*....
gi 71995514 450 PILVATAVAARGLDIPNVRHVINYDLPGDSDEYVHRIGR 488
Cdd:cd18802 92 NLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR 130
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
384-491 |
7.73e-11 |
|
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: 60.45 E-value: 7.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 384 KRSNLMEIL------MNEHSENLVLVFVETKRGANELAYFLNRQ-----------QIRSVSIHGdLKQIERERNLELFRS 446
Cdd:cd18801 10 KLEKLEEIVkehfkkKQEGSDTRVIIFSEFRDSAEEIVNFLSKIrpgiratrfigQASGKSSKG-MSQKEQKEVIEQFRK 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 71995514 447 GQCPILVATAVAARGLDIPNVRHVINYDLPGDSDEYVHRIGRTGR 491
Cdd:cd18801 89 GGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
148-498 |
2.33e-10 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 63.70 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 148 PAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAgGPDmvkppaftngrrtyyPCALV 227
Cdd:COG1205 43 PELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLE-DPG---------------ATALY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 228 LSPTRELAiQ-----IHKEATKFSykSNIQTAILYGG-RENYRDQVnrlRAGTHILIATPgrliDIIEQGFIG------- 294
Cdd:COG1205 107 LYPTKALA-RdqlrrLRELAEALG--LGVRVATYDGDtPPEERRWI---REHPDIVLTNP----DMLHYGLLPhhtrwar 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 295 -LAGCRYLVLDEA---------------DRML----DMGFEPQIrkivgqgmppktarttAMFSATF--PKEiqvLAKDF 352
Cdd:COG1205 177 fFRNLRYVVIDEAhtyrgvfgshvanvlRRLRricrHYGSDPQF----------------ILASATIgnPAE---HAERL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 353 LKDNyiFLAVGRVGSTSeNIEQRLLW----VNEMEKRSNLME---ILMNEHSENL-VLVFVETKRGANELAYFLNRQ--- 421
Cdd:COG1205 238 TGRP--VTVVDEDGSPR-GERTFVLWnpplVDDGIRRSALAEaarLLADLVREGLrTLVFTRSRRGAELLARYARRAlre 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 422 QIRSVSI---HGDLKQIEReRNLE-LFRSGQCPILVAT-AVAArGLDIPNVRHVINYDLPGDSDEYVHRIGRTGRCGNLG 496
Cdd:COG1205 315 PDLADRVaayRAGYLPEER-REIErGLRSGELLGVVSTnALEL-GIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDS 392
|
..
gi 71995514 497 IA 498
Cdd:COG1205 393 LV 394
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
451-491 |
6.07e-09 |
|
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: 53.09 E-value: 6.07e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 71995514 451 ILVATAVAARGLDIPNVRHVINYDLPGDSDEYVHRIGRTGR 491
Cdd:cd18785 25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGR 65
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
388-489 |
8.61e-09 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 58.70 E-value: 8.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 388 LMEILMNEHSENL-VLVFVETKRGANELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQ-CP-ILVATAVAARGLDI 464
Cdd:COG0553 538 LLELLEELLAEGEkVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeAPvFLISLKAGGEGLNL 617
|
90 100 110
....*....|....*....|....*....|....*.
gi 71995514 465 PNVRHVINYDLPgdsdeY-----------VHRIGRT 489
Cdd:COG0553 618 TAADHVIHYDLW-----WnpaveeqaidrAHRIGQT 648
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
373-502 |
8.98e-09 |
|
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: 54.95 E-value: 8.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 373 EQRLLWVNEMEKRSNLMEILMNEHSENLVLVFVETKRGANELAYFLNRQqirsvSIHGDLKQIERERNLELFRSGQCPIL 452
Cdd:cd18789 24 KRRLLAAMNPNKLRALEELLKRHEQGDKIIVFTDNVEALYRYAKRLLKP-----FITGETPQSEREEILQNFREGEYNTL 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 71995514 453 VATAVAARGLDIP--NVRHVINYdLPGDSDEYVHRIGRTGRCGNLGIATSFF 502
Cdd:cd18789 99 VVSKVGDEGIDLPeaNVAIQISG-HGGSRRQEAQRLGRILRPKKGGGKNAFF 149
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
166-306 |
1.03e-08 |
|
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: 55.28 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 166 QKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILaggpdmvkppaftngrRTYYPCALVLSPTRELAIQIHKEATKF 245
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALL----------------RDPGSRALYLYPTKALAQDQLRSLREL 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71995514 246 --SYKSNIqTAILYGGRENYRDQVNRLRAGTHILIATPgrliDIIEQGFIG--------LAGCRYLVLDEA 306
Cdd:cd17923 69 leQLGLGI-RVATYDGDTPREERRAIIRNPPRILLTNP----DMLHYALLPhhdrwarfLRNLRYVVLDEA 134
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
159-490 |
1.11e-08 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 58.58 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 159 YSKPTPVQKHSIPTLLANRDLMSCAQTGSGKT-AAFLLPIIQhiLAGGPDMVKPPaftngRRTYypcALVLSPTRELAIQ 237
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAFLPALDE--LARRPRPGELP-----DGLR---VLYISPLKALAND 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 238 IHKeatkfsyksNIQTAILyGGRENYRDQVNRLRAGT------------------HILIATPgrlidiiEQGFI------ 293
Cdd:COG1201 92 IER---------NLRAPLE-EIGEAAGLPLPEIRVGVrtgdtpaserqrqrrrppHILITTP-------ESLALlltspd 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 294 ---GLAGCRYLVLDE----AD--R--MLDMGFEpQIRKIVgqgmpPKTARTTAMfSATF--PKEI-QVLAKDFLKDNYIF 359
Cdd:COG1201 155 areLLRGVRTVIVDEihalAGskRgvHLALSLE-RLRALA-----PRPLQRIGL-SATVgpLEEVaRFLVGYEDPRPVTI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 360 LAVG-------RVGSTSENIEQRLLWVNE----MEKRsnLMEILMNEHSenlVLVFVETKRGANELAYFLNRQ------Q 422
Cdd:COG1201 228 VDAGagkkpdlEVLVPVEDLIERFPWAGHlwphLYPR--VLDLIEAHRT---TLVFTNTRSQAERLFQRLNELnpedalP 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71995514 423 IRSVsiHGDLKQIER---ERNLelfRSGQCPILVATAVAARGLDIPNVRHVINYDLPGDSDEYVHRIGRTG 490
Cdd:COG1201 303 IAAH--HGSLSREQRlevEEAL---KAGELRAVVATSSLELGIDIGDVDLVIQVGSPKSVARLLQRIGRAG 368
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
388-487 |
1.18e-08 |
|
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: 54.02 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 388 LMEILMNEHSENL-VLVFVETKRGANELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQCP--ILVATAVAARGLDI 464
Cdd:cd18793 16 LLELLEELREPGEkVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGVGLNL 95
|
90 100
....*....|....*....|....*....
gi 71995514 465 PNVRHVINYDLPGDS--DEY----VHRIG 487
Cdd:cd18793 96 TAANRVILYDPWWNPavEEQaidrAHRIG 124
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
384-491 |
1.30e-08 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 57.96 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 384 KRSNLMEIL---MNEHSENLVLVFVETKRGANELAYFLNRQQIRSV------SIHGD--LKQIERERNLELFRSGQCPIL 452
Cdd:PRK13766 348 KLEKLREIVkeqLGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVrfvgqaSKDGDkgMSQKEQIEILDKFRAGEFNVL 427
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 71995514 453 VATAVAARGLDIPNVRHVINYDlPGDSD-EYVHRIGRTGR 491
Cdd:PRK13766 428 VSTSVAEEGLDIPSVDLVIFYE-PVPSEiRSIQRKGRTGR 466
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
402-491 |
1.85e-07 |
|
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350185 [Multi-domain] Cd Length: 174 Bit Score: 51.54 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 402 LVFVETKRG---ANELAYFLNRQQIRSVSIHGDlkqieRERNLELFRSGQCPILVATA----VAARGLDIPN-VRHVINY 473
Cdd:cd18798 28 LIFVSIDYGkeyAEELKEFLERHGIKAELALSS-----TEKNLEKFEEGEIDVLIGVAsyygVLVRGIDLPErIKYAIFY 102
|
90
....*....|....*...
gi 71995514 474 DLPGDSdeYVHRIGRTGR 491
Cdd:cd18798 103 GVPVTT--YIQASGRTSR 118
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
401-491 |
3.12e-07 |
|
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: 50.71 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 401 VLVFVETKRGANELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQCPILVATAVAARGLDIPNVRHV--INYDLPG- 477
Cdd:cd18790 30 VLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVaiLDADKEGf 109
|
90
....*....|....*.
gi 71995514 478 --DSDEYVHRIGRTGR 491
Cdd:cd18790 110 lrSETSLIQTIGRAAR 125
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
402-471 |
8.96e-07 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350186 [Multi-domain] Cd Length: 116 Bit Score: 47.94 E-value: 8.96e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71995514 402 LVFVETKRGANELAYFLNRQQIRSVSIHGDLKQIERERN-LELFRSGQ--CPILVATAVAARGLDIPNVRHVI 471
Cdd:cd18799 10 LIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDEaLILLFFGElkPPILVTVDLLTTGVDIPEVDNVV 82
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
158-493 |
1.39e-06 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 51.64 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 158 GYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIqhILAGgpdmvkppaftngrrtyypCALVLSPTrelaIQ 237
Cdd:PRK11057 22 GYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPAL--VLDG-------------------LTLVVSPL----IS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 238 IHKEATKFSYKSNIQTAILYG--GRENYRDQVNRLRAGT-HILIATPGRLI--DIIEQgfigLAGCR--YLVLDEADRML 310
Cdd:PRK11057 77 LMKDQVDQLLANGVAAACLNStqTREQQLEVMAGCRTGQiKLLYIAPERLMmdNFLEH----LAHWNpaLLAVDEAHCIS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 311 DMG--FEPQIRKIvGQgmppktarttamFSATFPkEIQVLAKDFLKDNyiflavgrvgSTSENIEQRLLWVNEMEK---- 384
Cdd:PRK11057 153 QWGhdFRPEYAAL-GQ------------LRQRFP-TLPFMALTATADD----------TTRQDIVRLLGLNDPLIQissf 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 385 -RSNLMEILMNEHS--ENLVLvFVETKRG------------ANELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQC 449
Cdd:PRK11057 209 dRPNIRYTLVEKFKplDQLMR-YVQEQRGksgiiycnsrakVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDL 287
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 71995514 450 PILVATAVAARGLDIPNVRHVINYDLPGDSDEYVHRIGRTGRCG 493
Cdd:PRK11057 288 QIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDG 331
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
173-306 |
1.51e-06 |
|
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: 48.80 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 173 LLANRDLMSCAQTGSGKTAAFLLPIIQHILaggpdmvkppafTNGRRTYYpcalvLSPTRELAIQIHKEATKFSYKSNIQ 252
Cdd:cd17921 14 YLSGDSVLVSAPTSSGKTLIAELAILRALA------------TSGGKAVY-----IAPTRALVNQKEADLRERFGPLGKN 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 71995514 253 TAILYGGrenyrDQVNRLR-AGTHILIATP----GRLIDIIEQGFIGLagcRYLVLDEA 306
Cdd:cd17921 77 VGLLTGD-----PSVNKLLlAEADILVATPekldLLLRNGGERLIQDV---RLVVVDEA 127
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
161-279 |
1.71e-06 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 48.95 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 161 KPTPVQKHSIPTLLAN------RDLMSCAQTGSGKTAAFLLPIIQhilaggpdmvkppAFTNGRRTyypcaLVLSPTREL 234
Cdd:cd17918 15 SLTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAALL-------------AYKNGKQV-----AILVPTEIL 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 71995514 235 AIQIHKEATKfsYKSNIQTAILYGGRENYRDQVNRLRAGTHILIA 279
Cdd:cd17918 77 AHQHYEEARK--FLPFINVELVTGGTKAQILSGISLLVGTHALLH 119
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
428-491 |
1.11e-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: 45.80 E-value: 1.11e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71995514 428 IHGDLKQIERERNLELFRSGQCPILVATAVAARGLDIPN--VRHVINYDLPGDSDeyVHRI-GRTGR 491
Cdd:cd18811 67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNatVMVIEDAERFGLSQ--LHQLrGRVGR 131
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
156-305 |
2.13e-05 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 47.96 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 156 RSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKT-AAFlLPIIQHILAGG-----PDMVkppaftngrrtYypcALVLS 229
Cdd:PRK13767 27 KEKFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAF-LAIIDELFRLGregelEDKV-----------Y---CLYVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 230 PTRELAIQIHK-----------EATKFSYK-SNIQTAILYGGRENYRDQvNRLRAGTHILIATPGRL-IDIIEQGFI-GL 295
Cdd:PRK13767 92 PLRALNNDIHRnleeplteireIAKERGEElPEIRVAIRTGDTSSYEKQ-KMLKKPPHILITTPESLaILLNSPKFReKL 170
|
170
....*....|
gi 71995514 296 AGCRYLVLDE 305
Cdd:PRK13767 171 RTVKWVIVDE 180
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
183-464 |
3.15e-05 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 47.00 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 183 AQTGSGKTAAFLLPIIQHILAGGpdmvkppaftnGRRTYYpcALvlsPTRELAIQIHKEATKFsYKSNIQ----TAILYG 258
Cdd:COG1203 154 APTGGGKTEAALLFALRLAAKHG-----------GRRIIY--AL---PFTSIINQTYDRLRDL-FGEDVLlhhsLADLDL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 259 --GRENYRDQVNRLRAGTH-----ILIATPGRLIDIIEQG-------FIGLAGcRYLVLDEADrMLDmgfePQIRKIVGQ 324
Cdd:COG1203 217 leEEEEYESEARWLKLLKElwdapVVVTTIDQLFESLFSNrkgqerrLHNLAN-SVIILDEVQ-AYP----PYMLALLLR 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 325 GMppKTAR---TTAMF-SATFPKEIqvlaKDFLKDNYIFLavgrvgsTSENIEQRLLWVNEMEKR----------SNLME 390
Cdd:COG1203 291 LL--EWLKnlgGSVILmTATLPPLL----REELLEAYELI-------PDEPEELPEYFRAFVRKRvelkegplsdEELAE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 391 ILMNE-HSENLVLVFVETKRGANELAyflnrQQIRSVSIHGDL-----KQIERERN------LELFRSGQCPILVATAVA 458
Cdd:COG1203 358 LILEAlHKGKSVLVIVNTVKDAQELY-----EALKEKLPDEEVyllhsRFCPADRSeiekeiKERLERGKPCILVSTQVV 432
|
....*.
gi 71995514 459 ARGLDI 464
Cdd:COG1203 433 EAGVDI 438
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
367-491 |
3.37e-05 |
|
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: 44.18 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 367 STSENIEQRLLWVNEMEKR--SNLMEILmnEHSENlVLVFVETKRGANELAYFLNR------QQIRSVSIHGDLKQIERE 438
Cdd:cd18796 8 VILPVAPEIFPWAGESGADayAEVIFLL--ERHKS-TLVFTNTRSQAERLAQRLRElcpdrvPPDFIALHHGSLSRELRE 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 71995514 439 RNLELFRSGQCPILVATAVAARGLDIPNVRHVINYDLPGDSDEYVHRIGRTGR 491
Cdd:cd18796 85 EVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
390-491 |
4.16e-05 |
|
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: 44.08 E-value: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 390 EILMNEHSENL-VLVFVETKRGANELAyflnrQQIRSVSI-HGDLKQIERERNLELFRSGQCPILVATAVAARGLDIPNV 467
Cdd:cd18795 34 LLKIETVSEGKpVLVFCSSRKECEKTA-----KDLAGIAFhHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPAR 108
|
90 100 110
....*....|....*....|....*....|..
gi 71995514 468 RHVINYDLPGDSD--------EYVHRIGRTGR 491
Cdd:cd18795 109 TVIIKGTQRYDGKgyrelsplEYLQMIGRAGR 140
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
428-491 |
6.69e-05 |
|
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: 43.79 E-value: 6.69e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71995514 428 IHGDLKQIERERNLELFRSGQCPILVATAVAARGLDIPNVRHVI--NYDLPGDSDEYVHRiGRTGR 491
Cdd:cd18792 66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIieDADRFGLSQLHQLR-GRVGR 130
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
165-281 |
8.82e-05 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350781 [Multi-domain] Cd Length: 206 Bit Score: 44.27 E-value: 8.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 165 VQKHSIPTLL-ANRDLMSCAQTGSGKTAAFLLPIIQHIlaggpdMVKPPAFTNGRRTYYpcalvLSPTRELAIQIHKEAT 243
Cdd:cd18023 5 IQSEVFPDLLySDKNFVVSAPTGSGKTVLFELAILRLL------KERNPLPWGNRKVVY-----IAPIKALCSEKYDDWK 73
|
90 100 110
....*....|....*....|....*....|....*....
gi 71995514 244 -KFSyKSNIQTAILYGGRENYRDqvnRLRAGTHILIATP 281
Cdd:cd18023 74 eKFG-PLGLSCAELTGDTEMDDT---FEIQDADIILTTP 108
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
160-310 |
1.34e-04 |
|
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase 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: 350682 [Multi-domain] Cd Length: 189 Bit Score: 43.47 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 160 SKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAaFLLpIIQHILAggpdmvkppafTNGRRTYYpcalvLSPTRELAIQIH 239
Cdd:cd17924 16 FPPWGAQRTWAKRLLRGKSFAIIAPTGVGKTT-FGL-ATSLYLA-----------SKGKRSYL-----IFPTKSLVKQAY 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71995514 240 KEATKFSYKSNIQTAIL-YGGRENYRDQ---VNRLRAGT-HILIATPGRLIDIIEQgfigLAGCRY--LVLDEADRML 310
Cdd:cd17924 78 ERLSKYAEKAGVEVKILvYHSRLKKKEKeelLEKIEKGDfDILVTTNQFLSKNFDL----LSNKKFdfVFVDDVDAVL 151
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
176-305 |
1.56e-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: 42.57 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 176 NRDLMSCAQTGSGKTAAFLLPIIQHILAGGPDMVKppaftngrrtyypcALVLSPTRELAIQIHKEATKFSykSNIQTAI 255
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGVQ--------------VLYISPLKALINDQERRLEEPL--DEIDLEI 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 71995514 256 LYGGRENYRDQVNR---LRAGTHILIATPGRL-IDIIEQGFIG-LAGCRYLVLDE 305
Cdd:cd17922 65 PVAVRHGDTSQSEKakqLKNPPGILITTPESLeLLLVNKKLRElFAGLRYVVVDE 119
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
185-306 |
7.13e-04 |
|
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: 41.48 E-value: 7.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 185 TGSGKT--AAFLLPIIQHILAGGPDmvkppaftNGRRTYYpcalvLSPTRELAIQIHKEATKFSyksNIQTAILYGGREN 262
Cdd:cd18034 25 TGSGKTliAVMLIKEMGELNRKEKN--------PKKRAVF-----LVPTVPLVAQQAEAIRSHT---DLKVGEYSGEMGV 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 71995514 263 Y---RDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRYLVLDEA 306
Cdd:cd18034 89 DkwtKERWKEELEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
422-498 |
1.80e-03 |
|
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350197 [Multi-domain] Cd Length: 151 Bit Score: 39.25 E-value: 1.80e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71995514 422 QIRSVSIHGDLKQIERERNLELFRSGQCPILVATAVAARGLDIPNVRHVI--NYDLPGDSDEYVHRiGRTGRCGNLGIA 498
Cdd:cd18810 51 EARIAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIieRADKFGLAQLYQLR-GRVGRSKERAYA 128
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
164-318 |
2.83e-03 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 39.24 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 164 PVQKHSIPT-LLANRDLMSCAQTGSGKTAAFLLPIIQHILAGGPdmvkppaftngrrtyypcALVLSPTRELAIQIHKEA 242
Cdd:cd18028 4 PPQAEAVRAgLLKGENLLISIPTASGKTLIAEMAMVNTLLEGGK------------------ALYLVPLRALASEKYEEF 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71995514 243 TKFsYKSNIQTAILYGgreNYRDQVNRLrAGTHILIATPGRLIDIIEQG--FIGLAGCryLVLDE--------------- 305
Cdd:cd18028 66 KKL-EEIGLKVGISTG---DYDEDDEWL-GDYDIIVATYEKFDSLLRHSpsWLRDVGV--VVVDEihlisdeergptles 138
|
170
....*....|....
gi 71995514 306 -ADRMLDMGFEPQI 318
Cdd:cd18028 139 iVARLRRLNPNTQI 152
|
|
| |
