|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
122-507 |
8.51e-168 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 485.42 E-value: 8.51e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 122 FNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAGGPDMVKppaftngrrt 201
Cdd:COG0513 4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAPQ---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 202 yypcALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGrENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRY 281
Cdd:COG0513 74 ----ALILAPTRELALQVAEELRKLAKYLGLRVATVYGG-VSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVET 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 282 LVLDEADRMLDMGFEPQIRKIVGQgMPPKtaRTTAMFSATFPKEIQVLAKDFLKdNYIFLAVGRVGSTSENIEQRLLWVN 361
Cdd:COG0513 149 LVLDEADRMLDMGFIEDIERILKL-LPKE--RQTLLFSATMPPEIRKLAKRYLK-NPVRIEVAPENATAETIEQRYYLVD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 362 EMEKRSNLMEILmNEHSENLVLVFVETKRGANELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQCPILVATAVAAR 441
Cdd:COG0513 225 KRDKLELLRRLL-RDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAAR 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17510309 442 GLDIPNVRHVINYDLPGDSDEYVHRIGRTGRCGNLGIATSFFNDKNRGIGRDLKNLIvesNQEVPE 507
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 ... |
122-347 |
5.92e-138 |
|
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: 401.48 E-value: 5.92e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 122 FNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAGGpdmvkPPAFTNGRRT 201
Cdd:cd17967 2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDG-----PPSVGRGRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 202 YYPCALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGREnYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRY 281
Cdd:cd17967 77 AYPSALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGAD-VVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17510309 282 LVLDEADRMLDMGFEPQIRKIV-GQGMPPKTARTTAMFSATFPKEIQVLAKDFLKdNYIFLAVGRVG 347
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 ... |
82-347 |
1.04e-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: 395.10 E-value: 1.04e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 82 PAEySESNLFHRTDSGINFDKYENIPVEVSGDSVPAAIEHFNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLM 161
Cdd:cd18052 6 PPE-DEDEIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 162 SCAQTGSGKTAAFLLPIIQHILAGGpdmVKPPAFTNGRRtyyPCALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGr 241
Cdd:cd18052 85 ACAQTGSGKTAAFLLPVLTGMMKEG---LTASSFSEVQE---PQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGG- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 242 ENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRYLVLDEADRMLDMGFEPQIRKIVGQ-GMPPKTARTTAMFSA 320
Cdd:cd18052 158 VSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEpGMPSKEDRQTLMFSA 237
|
250 260
....*....|....*....|....*..
gi 17510309 321 TFPKEIQVLAKDFLKDNYIFLAVGRVG 347
Cdd:cd18052 238 TFPEEIQRLAAEFLKEDYLFLTVGRVG 264
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
100-348 |
6.82e-133 |
|
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: 389.78 E-value: 6.82e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 100 FDKYENIPVEVSGDSVPAAIEHFNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPII 179
Cdd:cd18051 1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 180 QHILAGGP-DMVKPPAFTNGRRTYYPCALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGrENYRDQVNRLRAGTHIL 258
Cdd:cd18051 81 SQIYEQGPgESLPSESGYYGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGG-ADIGQQMRDLERGCHLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 259 IATPGRLIDIIEQGFIGLAGCRYLVLDEADRMLDMGFEPQIRKIVGQ-GMPPKTARTTAMFSATFPKEIQVLAKDFLkDN 337
Cdd:cd18051 160 VATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQdTMPPTGERQTLMFSATFPKEIQMLARDFL-DN 238
|
250
....*....|.
gi 17510309 338 YIFLAVGRVGS 348
Cdd:cd18051 239 YIFLAVGRVGS 249
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
41-515 |
2.03e-130 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 394.53 E-value: 2.03e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 41 FYNGFANGTPSNNGSS-GYNNFADSGNGFNNNGAESNQWGG--APAEYSESNLF---------HRTDSGINFDKYENIPV 108
Cdd:PTZ00110 34 YGNYQANHQDNYGGFRpGYGNYSGGYGGFGMNSYGSSTLGKrlQPIDWKSINLVpfeknfykeHPEVSALSSKEVDEIRK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 109 E-----VSGDSVPAAIEHFNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHIL 183
Cdd:PTZ00110 114 EkeitiIAGENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHIN 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 184 AggpdmvkPPAFTNGRRtyyPCALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGRENyRDQVNRLRAGTHILIATPG 263
Cdd:PTZ00110 194 A-------QPLLRYGDG---PIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPK-RGQIYALRRGVEILIACPG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 264 RLIDIIEQGFIGLAGCRYLVLDEADRMLDMGFEPQIRKIVGQGMPPktaRTTAMFSATFPKEIQVLAKDFLKDNYIFLAV 343
Cdd:PTZ00110 263 RLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPD---RQTLMWSATWPKEVQSLARDLCKEEPVHVNV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 344 GRVG-STSENIEQRLLWVNEMEKRSNLMEIL---MNEHSEnlVLVFVETKRGANELAYFLNRQQIRSVSIHGDLKQIERE 419
Cdd:PTZ00110 340 GSLDlTACHNIKQEVFVVEEHEKRGKLKMLLqriMRDGDK--ILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERT 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 420 RNLELFRSGQCPILVATAVAARGLDIPNVRHVINYDLPGDSDEYVHRIGRTGRCGNLGIATSFFN-DKNRgIGRDLKNLI 498
Cdd:PTZ00110 418 WVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTpDKYR-LARDLVKVL 496
|
490
....*....|....*..
gi 17510309 499 VESNQEVPEWLHQVAAE 515
Cdd:PTZ00110 497 REAKQPVPPELEKLSNE 513
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
129-486 |
1.19e-102 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 319.82 E-value: 1.19e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 129 PAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHIlaggpdmvkppaftNGRRtYYPCALV 208
Cdd:PRK11776 13 PALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL--------------DVKR-FRVQALV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 209 LSPTRELAIQIHKEATKFS-YKSNIQTAILYGGrENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRYLVLDEA 287
Cdd:PRK11776 78 LCPTRELADQVAKEIRRLArFIPNIKVLTLCGG-VPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 288 DRMLDMGFEPQIRKIVGQgMPPKtaRTTAMFSATFPKEIQVLAKDFLKDNyifLAVgRVGSTSEN--IEQRLLWVNEmEK 365
Cdd:PRK11776 157 DRMLDMGFQDAIDAIIRQ-APAR--RQTLLFSATYPEGIAAISQRFQRDP---VEV-KVESTHDLpaIEQRFYEVSP-DE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 366 RSNLMEILMNEHSENLVLVFVETKRGANELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQCPILVATAVAARGLDI 445
Cdd:PRK11776 229 RLPALQRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDI 308
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 17510309 446 PNVRHVINYDLPGDSDEYVHRIGRTGRCGNLGIATSFFNDK 486
Cdd:PRK11776 309 KALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPE 349
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
122-506 |
2.71e-96 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 303.27 E-value: 2.71e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 122 FNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHilaggpdMVKPPAFTNGRRT 201
Cdd:PRK10590 3 FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQH-------LITRQPHAKGRRP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 202 YYpcALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGrENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRY 281
Cdd:PRK10590 76 VR--ALILTPTRELAAQIGENVRDYSKYLNIRSLVVFGG-VSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 282 LVLDEADRMLDMGFEPQIRKIVGQgMPPKtaRTTAMFSATFPKEIQVLAKDFLkDNYIFLAVGRVGSTSENIEQRLLWVN 361
Cdd:PRK10590 153 LVLDEADRMLDMGFIHDIRRVLAK-LPAK--RQNLLFSATFSDDIKALAEKLL-HNPLEIEVARRNTASEQVTQHVHFVD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 362 EMEKRSnLMEILMNEHSENLVLVFVETKRGANELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQCPILVATAVAAR 441
Cdd:PRK10590 229 KKRKRE-LLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAAR 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17510309 442 GLDIPNVRHVINYDLPGDSDEYVHRIGRTGRCGNLGIATSFFNDKNRGIGRDLKNLIvesNQEVP 506
Cdd:PRK10590 308 GLDIEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLL---KKEIP 369
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
131-336 |
5.93e-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: 5.93e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 131 VMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAGGPDMVKPPAftngrrtyypcALVLS 210
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRGPQ-----------ALVLA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 211 PTRELAIQIHKEATKFSYKSNIQTAILYGGrENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRYLVLDEADRM 290
Cdd:cd00268 70 PTRELAMQIAEVARKLGKGTGLKVAAIYGG-APIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRM 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17510309 291 LDMGFEPQIRKIVGQgMPPKtaRTTAMFSATFPKEIQVLAKDFLKD 336
Cdd:cd00268 149 LDMGFEEDVEKILSA-LPKD--RQTLLFSATLPEEVKELAKKFLKN 191
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
121-482 |
2.17e-90 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 286.87 E-value: 2.17e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 121 HFNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAggpdmvKPPAftNGRR 200
Cdd:PRK04837 9 KFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLS------HPAP--EDRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 201 TYYPCALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGrENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCR 280
Cdd:PRK04837 81 VNQPRALIMAPTRELAVQIHADAEPLAQATGLKLGLAYGG-DGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 281 YLVLDEADRMLDMGFEPQIRKIVgQGMPPKTARTTAMFSATFPKEIQVLAKDFLKD-NYIFLAVGRvgSTSENIEQRLLW 359
Cdd:PRK04837 160 VVVLDEADRMFDLGFIKDIRWLF-RRMPPANQRLNMLFSATLSYRVRELAFEHMNNpEYVEVEPEQ--KTGHRIKEELFY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 360 VNeMEKRSNLMEILMNEHSENLVLVFVETKRGANELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQCPILVATAVA 439
Cdd:PRK04837 237 PS-NEEKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVA 315
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 17510309 440 ARGLDIPNVRHVINYDLPGDSDEYVHRIGRTGRCGNLGIATSF 482
Cdd:PRK04837 316 ARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
104-509 |
4.39e-88 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 283.99 E-value: 4.39e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 104 ENIPVEVSGDSVPAAIEHFNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQH-- 181
Cdd:PLN00206 105 RKLEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRcc 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 182 -ILAGGPDMVKPPaftngrrtyypCALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGRENYRdQVNRLRAGTHILIA 260
Cdd:PLN00206 185 tIRSGHPSEQRNP-----------LAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQ-QLYRIQQGVELIVG 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 261 TPGRLIDIIEQGFIGLAGCRYLVLDEADRMLDMGFEPQIRKIVGQGMPPKTArttaMFSATFPKEIQVLAKDFLKDnYIF 340
Cdd:PLN00206 253 TPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQALSQPQVL----LFSATVSPEVEKFASSLAKD-IIL 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 341 LAVGRVGSTSENIEQRLLWVNEMEKRSNLMEILMN-EHSENLVLVFVETKRGANELAYFLNR-QQIRSVSIHGDLKQIER 418
Cdd:PLN00206 328 ISIGNPNRPNKAVKQLAIWVETKQKKQKLFDILKSkQHFKPPAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKER 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 419 ERNLELFRSGQCPILVATAVAARGLDIPNVRHVINYDLPGDSDEYVHRIGRTGRCGNLGIATSFFNDKNRGIGRDLKNLI 498
Cdd:PLN00206 408 REVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALL 487
|
410
....*....|.
gi 17510309 499 VESNQEVPEWL 509
Cdd:PLN00206 488 KSSGAAIPREL 498
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
122-482 |
6.59e-84 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 270.28 E-value: 6.59e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 122 FNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHIL-----AGGPdmvkppaft 196
Cdd:PRK11192 3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLdfprrKSGP--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 197 ngrrtyyPCALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGReNYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGL 276
Cdd:PRK11192 74 -------PRILILTPTRELAMQVADQARELAKHTHLDIATITGGV-AYMNHAEVFSENQDIVVATPGRLLQYIKEENFDC 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 277 AGCRYLVLDEADRMLDMGFEPQIRKIVGQgmppktAR---TTAMFSATFPKE-IQVLAKDFLKDNyIFLAVGrvGSTSE- 351
Cdd:PRK11192 146 RAVETLILDEADRMLDMGFAQDIETIAAE------TRwrkQTLLFSATLEGDaVQDFAERLLNDP-VEVEAE--PSRREr 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 352 -NIEQRLLWVNEME-KRSNLMEILMNEHSENLVlVFVETKRGANELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQ 429
Cdd:PRK11192 217 kKIHQWYYRADDLEhKTALLCHLLKQPEVTRSI-VFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGR 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 17510309 430 CPILVATAVAARGLDIPNVRHVINYDLPGDSDEYVHRIGRTGRCGNLGIATSF 482
Cdd:PRK11192 296 VNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
122-482 |
1.42e-82 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 267.93 E-value: 1.42e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 122 FNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILaggpdMVKPPAftnGRRT 201
Cdd:PRK01297 89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLL-----QTPPPK---ERYM 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 202 YYPCALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGREnYRDQVNRLRAG-THILIATPGRLIDIIEQGFIGLAGCR 280
Cdd:PRK01297 161 GEPRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMD-FDKQLKQLEARfCDILVATPGRLLDFNQRGEVHLDMVE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 281 YLVLDEADRMLDMGFEPQIRKIVGQgMPPKTARTTAMFSATFPKEIQVLAKDFLKDNYIfLAVGRVGSTSENIEQRLLWV 360
Cdd:PRK01297 240 VMVLDEADRMLDMGFIPQVRQIIRQ-TPRKEERQTLLFSATFTDDVMNLAKQWTTDPAI-VEIEPENVASDTVEQHVYAV 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 361 NEMEKRSNLMEILMNEHSENlVLVFVETKRGANELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQCPILVATAVAA 440
Cdd:PRK01297 318 AGSDKYKLLYNLVTQNPWER-VMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAG 396
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 17510309 441 RGLDIPNVRHVINYDLPGDSDEYVHRIGRTGRCGNLGIATSF 482
Cdd:PRK01297 397 RGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISF 438
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
129-482 |
4.92e-82 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 269.51 E-value: 4.92e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 129 PAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAggpdmvkPPAFTNgRRTYYPCALV 208
Cdd:PRK04537 18 PALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLS-------RPALAD-RKPEDPRALI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 209 LSPTRELAIQIHKEATKFSYKSNIQTAILYGGREnYRDQVNRLRAGTHILIATPGRLIDIIEQ-GFIGLAGCRYLVLDEA 287
Cdd:PRK04537 90 LAPTRELAIQIHKDAVKFGADLGLRFALVYGGVD-YDKQRELLQQGVDVIIATPGRLIDYVKQhKVVSLHACEICVLDEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 288 DRMLDMGFEPQIRKIVGQgMPPKTARTTAMFSATFPKEIQVLAKDFLKDNYIfLAVGRVGSTSENIEQRLLWVNEMEKRS 367
Cdd:PRK04537 169 DRMFDLGFIKDIRFLLRR-MPERGTRQTLLFSATLSHRVLELAYEHMNEPEK-LVVETETITAARVRQRIYFPADEEKQT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 368 NLMEILmnEHSENL-VLVFVETKRGANELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQCPILVATAVAARGLDIP 446
Cdd:PRK04537 247 LLLGLL--SRSEGArTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHID 324
|
330 340 350
....*....|....*....|....*....|....*.
gi 17510309 447 NVRHVINYDLPGDSDEYVHRIGRTGRCGNLGIATSF 482
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 ... |
131-341 |
2.13e-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: 2.13e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 131 VMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAggpdmvKPPAftngRRTYYPCALVLS 210
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINA------QPPL----ERGDGPIVLVLA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 211 PTRELAIQIHKEATKFSYKSNIQTAILYGGRENYrDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRYLVLDEADRM 290
Cdd:cd17966 71 PTRELAQQIQQEANKFGGSSRLRNTCVYGGAPKG-PQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRM 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17510309 291 LDMGFEPQIRKIVGQGMPPktaRTTAMFSATFPKEIQVLAKDFLKDnYIFL 341
Cdd:cd17966 150 LDMGFEPQIRKIVDQIRPD---RQTLMWSATWPKEVRRLAEDFLKD-YIQV 196
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
122-507 |
2.52e-79 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 264.02 E-value: 2.52e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 122 FNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHIlagGPDMVKPPAftngrrt 201
Cdd:PRK11634 8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNL---DPELKAPQI------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 202 yypcaLVLSPTRELAIQIHKEATKFS-YKSNIQTAILYGGrENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCR 280
Cdd:PRK11634 78 -----LVLAPTRELAVQVAEAMTDFSkHMRGVNVVALYGG-QRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 281 YLVLDEADRMLDMGFEPQIRKIVGQgMPPKtaRTTAMFSATFPKEIQVLAKDFLKDNYIFLAVGRVgSTSENIEQRLLWV 360
Cdd:PRK11634 152 GLVLDEADEMLRMGFIEDVETIMAQ-IPEG--HQTALFSATMPEAIRRITRRFMKEPQEVRIQSSV-TTRPDISQSYWTV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 361 NEMEKRSNLMEILMNEHSEnLVLVFVETKRGANELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQCPILVATAVAA 440
Cdd:PRK11634 228 WGMRKNEALVRFLEAEDFD-AAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAA 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17510309 441 RGLDIPNVRHVINYDLPGDSDEYVHRIGRTGRCGNLGIATSFFNDKNRgigRDLKNLIVESNQEVPE 507
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 ... |
131-335 |
1.10e-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: 1.10e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 131 VMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILaggpdmvKPPAFTNGRRTYYPCALVLS 210
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYIS-------RLPPLDEETKDDGPYALILA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 211 PTRELAIQIHKEATKFSYKSNIQTAILYGGReNYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRYLVLDEADRM 290
Cdd:cd17945 74 PTRELAQQIEEETQKFAKPLGIRVVSIVGGH-SIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17510309 291 LDMGFEPQIRKIVGQgMPP------------------KTARTTAMFSATFPKEIQVLAKDFLK 335
Cdd:cd17945 153 IDMGFEPQVTKILDA-MPVsnkkpdteeaeklaasgkHRYRQTMMFTATMPPAVEKIAKGYLR 214
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
131-336 |
4.19e-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: 4.19e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 131 VMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAGgPDMVKPPAftngrrtyyPCALVLS 210
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQ-RELEKGEG---------PIAVIVA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 211 PTRELAIQIHKEATKFSYKSNIQTAILYGGrENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRYLVLDEADRM 290
Cdd:cd17952 71 PTRELAQQIYLEAKKFGKAYNLRVVAVYGG-GSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRM 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17510309 291 LDMGFEPQIRKIVGQGMPPktaRTTAMFSATFPKEIQVLAKDFLKD 336
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) ... |
110-336 |
2.83e-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: 2.83e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 110 VSGDSVPAAIEHFNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAGGPdm 189
Cdd:cd17953 2 VRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRP-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 190 VKPpafTNGrrtyyPCALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGrENYRDQVNRLRAGTHILIATPGRLIDII 269
Cdd:cd17953 80 VKP---GEG-----PIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGG-SGISEQIAELKRGAEIVVCTPGRMIDIL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 270 --EQGFI-GLAGCRYLVLDEADRMLDMGFEPQIRKIVGQGMPPktaRTTAMFSATFPKEIQVLAKDFLKD 336
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, ... |
108-344 |
9.09e-64 |
|
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: 9.09e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 108 VEVSGDSVPAAIEHFNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHIlaggp 187
Cdd:cd18049 12 ITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHI----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 188 dmVKPPAFTNGRRtyyPCALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGRENyRDQVNRLRAGTHILIATPGRLID 267
Cdd:cd18049 87 --NHQPFLERGDG---PICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPK-GPQIRDLERGVEICIATPGRLID 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17510309 268 IIEQGFIGLAGCRYLVLDEADRMLDMGFEPQIRKIVGQGMPPktaRTTAMFSATFPKEIQVLAKDFLKDnYIFLAVG 344
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 ... |
353-483 |
1.74e-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: 1.74e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 353 IEQRLLWVNEMEKRSNLMEILMNEHSENLVLVFVETKRGANELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQCPI 432
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 17510309 433 LVATAVAARGLDIPNVRHVINYDLPGDSDEYVHRIGRTGRCGNLGIATSFF 483
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
118-509 |
7.83e-62 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 210.84 E-value: 7.83e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 118 AIEHFNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHIlagGPDMVKppaftn 197
Cdd:PTZ00424 26 IVDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLI---DYDLNA------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 198 grrtyypC-ALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGrENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGL 276
Cdd:PTZ00424 97 -------CqALILAPTRELAQQIQKVVLALGDYLKVRCHACVGG-TVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 277 AGCRYLVLDEADRMLDMGFEPQIRKIVgQGMPPKTarTTAMFSATFPKEIQVLAKDFLKDNYIFLaVGRVGSTSENIEQR 356
Cdd:PTZ00424 169 DDLKLFILDEADEMLSRGFKGQIYDVF-KKLPPDV--QVALFSATMPNEILELTTKFMRDPKRIL-VKKDELTLEGIRQF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 357 LLWVNEMEKRSNLMEILMNEHSENLVLVFVETKRGANELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQCPILVAT 436
Cdd:PTZ00424 245 YVAVEKEEWKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITT 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17510309 437 AVAARGLDIPNVRHVINYDLPGDSDEYVHRIGRTGRCGNLGIATSFFNDKN----RGIGRDLKNLIVESNQEVPEWL 509
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 ... |
131-336 |
8.05e-61 |
|
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: 201.15 E-value: 8.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 131 VMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAGGPDMVKPPAftngrrtyyPCALVLS 210
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPREQRNG---------PGVLVLT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 211 PTRELAIQIHKEATKFSYKsNIQTAILYGGReNYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRYLVLDEADRM 290
Cdd:cd17958 72 PTRELALQIEAECSKYSYK-GLKSVCVYGGG-NRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRM 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17510309 291 LDMGFEPQIRKIVGQGMPPktaRTTAMFSATFPKEIQVLAKDFLKD 336
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 ... |
131-344 |
7.96e-60 |
|
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: 7.96e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 131 VMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAggpdmvkpPAFTNGRRtyypcALVLS 210
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGK--------PRKKKGLR-----ALILA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 211 PTRELAIQIHKEATKFSYKSNIQTAILYGGRENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRYLVLDEADRM 290
Cdd:cd17957 68 PTRELASQIYRELLKLSKGTGLRIVLLSKSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17510309 291 LDMGFEPQIRKIVGQGMPPKTarTTAMFSATFPKEIQVLAKDFLKDnYIFLAVG 344
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 ... |
108-344 |
1.14e-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: 1.14e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 108 VEVSGDSVPAAIEHFNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHIlaggp 187
Cdd:cd18050 50 ITIRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHI----- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 188 dmVKPPAFTNGRRtyyPCALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGRENyRDQVNRLRAGTHILIATPGRLID 267
Cdd:cd18050 125 --NHQPYLERGDG---PICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPK-GPQIRDLERGVEICIATPGRLID 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17510309 268 IIEQGFIGLAGCRYLVLDEADRMLDMGFEPQIRKIVGQGMPPktaRTTAMFSATFPKEIQVLAKDFLKDnYIFLAVG 344
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 ... |
129-341 |
2.94e-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: 2.94e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 129 PAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSC-AQTGSGKTAAFLLPIIQHILAGgpdmvkPPAFTNGRRTyypcAL 207
Cdd:cd17964 3 PSLLKALTRMGFETMTPVQQKTLKPILSTGDDVLArAKTGTGKTLAFLLPAIQSLLNT------KPAGRRSGVS----AL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 208 VLSPTRELAIQIHKEATKFSYKS---NIQTAIlyGGRENYRDQVNRLRAGTHILIATPGRLIDIIE-QGFIG-LAGCRYL 282
Cdd:cd17964 73 IISPTRELALQIAAEAKKLLQGLrklRVQSAV--GGTSRRAELNRLRRGRPDILVATPGRLIDHLEnPGVAKaFTDLDYL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17510309 283 VLDEADRMLDMGFEPQIRKIVgQGMPPKTA--RTTAMFSATFPKEIQVLAKDFLKDNYIFL 341
Cdd:cd17964 151 VLDEADRLLDMGFRPDLEQIL-RHLPEKNAdpRQTLLFSATVPDEVQQIARLTLKKDYKFI 210
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
139-335 |
8.57e-56 |
|
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: 8.57e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 139 GYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILaggpdmVKPPAFTNGRrtyypcALVLSPTRELAIQ 218
Cdd:cd17947 9 GFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLL------YRPKKKAATR------VLVLVPTRELAMQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 219 IHKEATKFSYKSNIQTAILYGGReNYRDQVNRLRAGTHILIATPGRLIDIIEQGF-IGLAGCRYLVLDEADRMLDMGFEP 297
Cdd:cd17947 77 CFSVLQQLAQFTDITFALAVGGL-SLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGFAD 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 17510309 298 QIRKIVgqGMPPKTaRTTAMFSATFPKEIQVLAKDFLK 335
Cdd:cd17947 156 ELKEIL--RLCPRT-RQTMLFSATMTDEVKDLAKLSLN 190
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
144-327 |
3.03e-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: 3.03e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 144 TPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAGGpdmvkppaftNGRRtyypcALVLSPTRELAIQIHKEA 223
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLD----------NGPQ-----ALVLAPTRELAEQIYEEL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 224 TKFSYKSNIQTAILYGGrENYRDQVNRLRaGTHILIATPGRLIDIIEQGFiGLAGCRYLVLDEADRMLDMGFEPQIRKIV 303
Cdd:pfam00270 66 KKLGKGLGLKVASLLGG-DSRKEQLEKLK-GPDILVGTPGRLLDLLQERK-LLKNLKLLVLDEAHRLLDMGFGPDLEEIL 142
|
170 180
....*....|....*....|....
gi 17510309 304 GQgMPPKtaRTTAMFSATFPKEIQ 327
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 ... |
122-341 |
9.33e-55 |
|
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350713 [Multi-domain] Cd Length: 204 Bit Score: 185.51 E-value: 9.33e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 122 FNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQhILAGGPdmvkppaftngrrt 201
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQ-RLSEDP-------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 202 YYPCALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGRENYRdQVNRLRAGTHILIATPGRLIDIIE---QGFIGLAG 278
Cdd:cd17955 66 YGIFALVLTPTRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVK-QALELSKRPHIVVATPGRLADHLRssdDTTKVLSR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17510309 279 CRYLVLDEADRMLDMGFEPQIRKIVGQgMPPKtaRTTAMFSATFPKEIQVLAKDFLKDNYIFL 341
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) ... |
135-337 |
3.80e-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: 3.80e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 135 VNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAggpdmvKPPAFTngrRTYYPCALVLSPTRE 214
Cdd:cd17949 6 KSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLS------LEPRVD---RSDGTLALVLVPTRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 215 LAIQIHKEATKF-SYKSNIQTAILYGGrENYRDQVNRLRAGTHILIATPGRLIDIIE--QGFiGLAGCRYLVLDEADRML 291
Cdd:cd17949 77 LALQIYEVLEKLlKPFHWIVPGYLIGG-EKRKSEKARLRKGVNILIATPGRLLDHLKntQSF-DVSNLRWLVLDEADRLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17510309 292 DMGFEPQIRKIV----------GQGMPPKTARTTAMFSATFPKEIQVLAKDFLKDN 337
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 ... |
122-336 |
4.31e-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: 4.31e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 122 FNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILaggpdmvkppaftNGRRT 201
Cdd:cd17954 2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALL-------------ENPQR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 202 YYpcALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGReNYRDQVNRLRAGTHILIATPGRLIDIIEQ--GFiGLAGC 279
Cdd:cd17954 69 FF--ALVLAPTRELAQQISEQFEALGSSIGLKSAVLVGGM-DMMAQAIALAKKPHVIVATPGRLVDHLENtkGF-SLKSL 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17510309 280 RYLVLDEADRMLDMGFEPQIRKIVGQgMPpkTARTTAMFSATFPKEIQVLAKDFLKD 336
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 ... |
122-336 |
7.53e-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: 7.53e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 122 FNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHIlaggpdmvKPPAFTNGRRt 201
Cdd:cd17959 3 FQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKL--------KAHSPTVGAR- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 202 yypcALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGrENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRY 281
Cdd:cd17959 74 ----ALILSPTRELALQTLKVTKELGKFTDLRTALLVGG-DSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEY 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17510309 282 LVLDEADRMLDMGFEPQIRKIVGQgMPPktARTTAMFSATFPKEIQVLAKDFLKD 336
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, ... |
131-334 |
1.73e-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: 1.73e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 131 VMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAGGPDMvKPPAFTngrrtyypcALVLS 210
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANL-KKGQVG---------ALIIS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 211 PTRELAIQIHKEATKF--SYKSNIQTAILYGGRENYRDQVNRLRAGTHILIATPGRLIDIIE--QGFIGLAGCRYLVLDE 286
Cdd:cd17960 71 PTRELATQIYEVLQSFleHHLPKLKCQLLIGGTNVEEDVKKFKRNGPNILVGTPGRLEELLSrkADKVKVKSLEVLVLDE 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 17510309 287 ADRMLDMGFEPQIRKIVGQgmPPKTaRTTAMFSATFPKEIQVLAKDFL 334
Cdd:cd17960 151 ADRLLDLGFEADLNRILSK--LPKQ-RRTGLFSATQTDAVEELIKAGL 195
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
135-356 |
1.38e-50 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 174.22 E-value: 1.38e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 135 VNRSGYSKPTPVQKHSIPTLLAN-RDLMSCAQTGSGKTAAFLLPIIQHIlaggpdmvkppaftngRRTYYPCALVLSPTR 213
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAL----------------KRGKGGRVLVLVPTR 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 214 ELAIQIHKEATKFSYKSNIQTAILYGGrENYRDQVNRLRAG-THILIATPGRLIDIIEQGFIGLAGCRYLVLDEADRMLD 292
Cdd:smart00487 65 ELAEQWAEELKKLGPSLGLKVVGLYGG-DSKREQLRKLESGkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLD 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17510309 293 MGFEPQIRKIVGQgMPPKtaRTTAMFSATFPKEIQVLAKDFLKdNYIFLAVGRvgSTSENIEQR 356
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 ... |
122-338 |
1.48e-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: 1.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 122 FNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHIlaggpDMVKppaftngrrt 201
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKI-----DPKK---------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 202 YYPCALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGrENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRY 281
Cdd:cd17940 66 DVIQALILVPTRELALQTSQVCKELGKHMGVKVMVTTGG-TSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKT 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17510309 282 LVLDEADRMLDMGFEPQIRKIVGQgMPPKtaRTTAMFSATFPKEIQVLAKDFLKDNY 338
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 ... |
139-334 |
2.28e-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: 2.28e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 139 GYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAggPDMVKPPAFTNGrrtyyPCALVLSPTRELAIQ 218
Cdd:cd17951 9 GIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALE--QEKKLPFIKGEG-----PYGLIVCPSRELARQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 219 IHKEATKFSYK------SNIQTAILYGGrENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRYLVLDEADRMLD 292
Cdd:cd17951 82 THEVIEYYCKAlqeggyPQLRCLLCIGG-MSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17510309 293 MGFEPQIRKIV----GQgmppktaRTTAMFSATFPKEIQVLAKDFL 334
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 ... |
136-341 |
6.97e-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: 6.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 136 NRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILA---GGPDMVKppaftngrrtyypcALVLSPT 212
Cdd:cd17941 6 KEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRerwTPEDGLG--------------ALIISPT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 213 RELAIQIHKEATKFSYKSNIQTAILYGGReNYRDQVNRLrAGTHILIATPGRLIDIIEQ--GFiGLAGCRYLVLDEADRM 290
Cdd:cd17941 72 RELAMQIFEVLRKVGKYHSFSAGLIIGGK-DVKEEKERI-NRMNILVCTPGRLLQHMDEtpGF-DTSNLQMLVLDEADRI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17510309 291 LDMGFEPQIRKIVGQgMPPKtaRTTAMFSATFPKEIQVLAKDFLKD-NYIFL 341
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 ... |
134-336 |
1.36e-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: 1.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 134 NVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQhilaggpdmvkppaftngRRTYY---PCALVLS 210
Cdd:cd17962 4 NLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVII------------------RCLTEhrnPSALILT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 211 PTRELAIQIHKEATKF-SYKSNIQTAILYGGrENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRYLVLDEADR 289
Cdd:cd17962 66 PTRELAVQIEDQAKELmKGLPPMKTALLVGG-LPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADT 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17510309 290 MLDMGFEPQIRKIVgQGMPPKtaRTTAMFSATFPKEIQVLAKDFLKD 336
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 ... |
122-321 |
1.12e-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: 1.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 122 FNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAggpdmvkppaftngrrt 201
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIVVA----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 202 yypcaLVLSPTRELAIQIHKEATKFSY---KSNIQTAILYGGrENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAG 278
Cdd:cd17938 64 -----LILEPSRELAEQTYNCIENFKKyldNPKLRVALLIGG-VKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSS 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17510309 279 CRYLVLDEADRMLDMGFEPQIRKIVGQgMPPKTAR----TTAMFSAT 321
Cdd:cd17938 138 VRFFVLDEADRLLSQGNLETINRIYNR-IPKITSDgkrlQVIVCSAT 183
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
139-336 |
1.73e-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: 1.73e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 139 GYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHIlaggpdmvkppaftnGRRTYYPCALVLSPTRELAIQ 218
Cdd:cd17939 16 GFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRI---------------DTTVRETQALVLAPTRELAQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 219 IHKEATKFSYKSNIQTAILYGGrENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRYLVLDEADRMLDMGFEPQ 298
Cdd:cd17939 81 IQKVVKALGDYMGVKVHACIGG-TSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQ 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 17510309 299 IRKIVgQGMPPKTarTTAMFSATFPKEIQVLAKDFLKD 336
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 ... |
139-336 |
2.88e-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: 2.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 139 GYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILaggpdMVKppafTNGRRTYYPCALVLSPTRELAIQ 218
Cdd:cd17961 13 GWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIL-----KAK----AESGEEQGTRALILVPTRELAQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 219 IHKEATKFSYKSNIQTAIL-YGGRENYRDQVNRLRAGTHILIATPGRLIDIIEQG-FIGLAGCRYLVLDEADRMLDMGFE 296
Cdd:cd17961 84 VSKVLEQLTAYCRKDVRVVnLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGsLLLLSTLKYLVIDEADLVLSYGYE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17510309 297 PQIRKIVGQGmpPKTARTTAMfSATFPKEIQVLAKDFLKD 336
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 ... |
139-341 |
5.92e-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: 5.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 139 GYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAggpdmVKppaFTNGRRTyypCALVLSPTRELAIQ 218
Cdd:cd17942 9 GFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYK-----LK---FKPRNGT---GVIIISPTRELALQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 219 IH---KEATKFsyksNIQTAILYGGRENYRDQVNRLRAGTHILIATPGRLIDIIE--QGFIgLAGCRYLVLDEADRMLDM 293
Cdd:cd17942 78 IYgvaKELLKY----HSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQntKGFL-YKNLQCLIIDEADRILEI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 17510309 294 GFEPQIRKIVgqGMPPKTaRTTAMFSATFPKEIQVLAKDFLKDNYIFL 341
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 ... |
131-327 |
1.75e-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: 1.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 131 VMENVNRSGYSKPTPVQKHSIPTLLANR-DLMSCAQTGSGKTAAFLLPIIQHILAGGPDMVKPPAFTngrrtyYPCALVL 209
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRDGkDVIGAAETGSGKTLAFGIPILERLLSQKSSNGVGGKQK------PLRALIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 210 SPTRELAIQI--H-KEATKFsykSNIQTAILYGGRENYRdQVNRLRAGTHILIATPGRLIDIIEQG--FIG-LAGCRYLV 283
Cdd:cd17946 75 TPTRELAVQVkdHlKAIAKY---TNIKIASIVGGLAVQK-QERLLKKRPEIVVATPGRLWELIQEGneHLAnLKSLRFLV 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 17510309 284 LDEADRMLDMG-FEP--QIRKIVGQGMP-PKTARTTAMFSATFPKEIQ 327
Cdd:cd17946 151 LDEADRMLEKGhFAEleKILELLNKDRAgKKRKRQTFVFSATLTLDHQ 198
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
364-474 |
6.56e-39 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 138.88 E-value: 6.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 364 EKRSNLMEILmNEHSENLVLVFVETKRGAnELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQCPILVATAVAARGL 443
Cdd:pfam00271 1 EKLEALLELL-KKERGGKVLIFSQTKKTL-EAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
|
90 100 110
....*....|....*....|....*....|.
gi 17510309 444 DIPNVRHVINYDLPGDSDEYVHRIGRTGRCG 474
Cdd:pfam00271 79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
131-331 |
3.91e-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: 3.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 131 VMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAggpDMVKPpaftnGRRTYYPCALVLS 210
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLR---YKLLA-----EGPFNAPRGLVIT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 211 PTRELAIQIHKEATKFSYKSNIQTAILYGGReNYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRYLVLDEADRM 290
Cdd:cd17948 73 PSRELAEQIGSVAQSLTEGLGLKVKVITGGR-TKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17510309 291 LDMGFEPQIRKIVGQ------------GMPPKTARTTAmfSATFPKEI-QVLAK 331
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 ... |
145-339 |
4.53e-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: 4.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 145 PVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAGGPDMvkppaftngRRTYYPCALVLSPTRELAIQIHKEAT 224
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPR---------KRGRAPKVLVLAPTRELANQVTKDFK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 225 KFSYKSNIqtAILYGGrENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRYLVLDEADRMLDMGFEPQIRKI-- 302
Cdd:cd17944 86 DITRKLSV--ACFYGG-TPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEIls 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 17510309 303 VGQGMPPKTARTTAMFSATFPKEIQVLAKDFLKDNYI 339
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 ... |
139-336 |
7.42e-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: 7.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 139 GYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAGGPDmvkppaftngrrtyyPCALVLSPTRELAIQ 218
Cdd:cd18046 18 GFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKA---------------TQALVLAPTRELAQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 219 IHKEATKFSYKSNIQTAILYGGrENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRYLVLDEADRMLDMGFEPQ 298
Cdd:cd18046 83 IQKVVMALGDYMGIKCHACIGG-TSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKDQ 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 17510309 299 IRKIVgQGMPPKTarTTAMFSATFPKEIQVLAKDFLKD 336
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 ... |
122-336 |
8.09e-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: 8.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 122 FNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHIlaggpdmVKPPAFTNgrrt 201
Cdd:cd17950 4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQL-------EPVDGQVS---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 202 yypcALVLSPTRELAIQIHKEATKFS-YKSNIQTAILYGGReNYRDQVNRLRAGT-HILIATPGRLIDIIEQGFIGLAGC 279
Cdd:cd17950 73 ----VLVICHTRELAFQISNEYERFSkYMPNVKTAVFFGGV-PIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHV 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17510309 280 RYLVLDEADRML-DMGFEPQIRKIVgqGMPPKTaRTTAMFSATFPKEIQVLAKDFLKD 336
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 ... |
129-336 |
2.42e-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: 2.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 129 PAVMENVNRSGYSKPTPVQKHSIPTLLAN--RDLMSCAQTGSGKTAAFLLPIIQHIlaggpDMVKPpaftngrrtyYPCA 206
Cdd:cd17963 3 PELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRV-----DPTLK----------SPQA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 207 LVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGRENYRDQvnrlRAGTHILIATPGRLIDIIEQGFIGLAGCRYLVLDE 286
Cdd:cd17963 68 LCLAPTRELARQIGEVVEKMGKFTGVKVALAVPGNDVPRGK----KITAQIVIGTPGTVLDWLKKRQLDLKKIKILVLDE 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17510309 287 ADRMLDM-GFEPQIRKIvgQGMPPKTARTTaMFSATFPKEIQVLAKDFLKD 336
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, ... |
131-324 |
5.19e-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: 5.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 131 VMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAGgpdmvkppaftngRRTyyPCALVLS 210
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLE-------------RRH--PQVLILA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 211 PTRELAIQIHKEATKF-SYKSNIQTAILYGGRENYRDqVNRLRaGTHILIATPGRLIDIIEQGFIGLAGCRYLVLDEADR 289
Cdd:cd17943 66 PTREIAVQIHDVFKKIgKKLEGLKCEVFIGGTPVKED-KKKLK-GCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADK 143
|
170 180 190
....*....|....*....|....*....|....*
gi 17510309 290 MLDMGFEPQIRKIVGQgMPPKtaRTTAMFSATFPK 324
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 ... |
131-296 |
2.45e-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: 2.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 131 VMENVNRSGYSKPTPVQKHSIPTLLAN---------RDLMSCAQTGSGKTAAFLLPIIQhILAGGPDmvkppaftngRRT 201
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQ-ALSKRVV----------PRL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 202 YypcALVLSPTRELAIQIHKEATKFSYKSNIQTAILyGGRENYRDQVNRLRAGTH--------ILIATPGRLIDIIEQ-- 271
Cdd:cd17956 70 R---ALIVVPTKELVQQVYKVFESLCKGTGLKVVSL-SGQKSFKKEQKLLLVDTSgrylsrvdILVATPGRLVDHLNStp 145
|
170 180
....*....|....*....|....*
gi 17510309 272 GFIgLAGCRYLVLDEADRMLDMGFE 296
Cdd:cd17956 146 GFT-LKHLRFLVIDEADRLLNQSFQ 169
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
122-336 |
2.73e-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: 2.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 122 FNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILaggpdmvkppafTNGRRT 201
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLD------------IQVRET 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 202 YypcALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGReNYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRY 281
Cdd:cd18045 69 Q---ALILSPTRELAVQIQKVLLALGDYMNVQCHACIGGT-SVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKM 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17510309 282 LVLDEADRMLDMGFEPQIRKIVgQGMPPKTarTTAMFSATFPKEIQVLAKDFLKD 336
Cdd:cd18045 145 LVLDEADEMLNKGFKEQIYDVY-RYLPPAT--QVVLVSATLPQDILEMTNKFMTD 196
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
394-474 |
2.41e-30 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 113.85 E-value: 2.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 394 ELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQCPILVATAVAARGLDIPNVRHVINYDLPGDSDEYVHRIGRTGRC 473
Cdd:smart00490 2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRA 81
|
.
gi 17510309 474 G 474
Cdd:smart00490 82 G 82
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
133-325 |
3.34e-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: 3.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 133 ENVNRSGYSKPTPVQKHSIPTLLANR----------------DLMSCAQTGSGKTAAFLLPIIQHILAG--GPDMVKPPA 194
Cdd:cd17965 21 GSNKTDEEIKPSPIQTLAIKKLLKTLmrkvtkqtsneepkleVFLLAAETGSGKTLAYLAPLLDYLKRQeqEPFEEAEEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 195 FTNGRRTYYPCALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGR-ENYRDQVNRLRAGTHILIATPGRLIDIIEQGF 273
Cdd:cd17965 101 YESAKDTGRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFgPSYQRLQLAFKGRIDILVTTPGKLASLAKSRP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17510309 274 IGLAGCRYLVLDEADRMLDMGFEPQIRKIVGQGMPPKTArttAMFSATFPKE 325
Cdd:cd17965 181 KILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHL---ILCSATIPKE 229
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
166-469 |
1.94e-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: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 166 TGSGKTAAFLLpIIQHILAGGPdmvkppaftngrrtyypcALVLSPTRELAIQIHKEATKFSYKsniqtAILYGGRENyr 245
Cdd:COG1061 109 TGTGKTVLALA-LAAELLRGKR------------------VLVLVPRRELLEQWAEELRRFLGD-----PLAGGGKKD-- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 246 dqvnrlrAGTHILIATPGRLIDIIEQGFIGlAGCRYLVLDEADRmldmGFEPQIRKIVGQGMPPK----TA---RTTA-- 316
Cdd:COG1061 163 -------SDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHH----AGAPSYRRILEAFPAAYrlglTAtpfRSDGre 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 317 MFSATFPKEI------QVLAKDFLKDnYIFLAV--------GRVGSTSENIEQRLLWVNEMeKRSNLMEILMNEHSENLV 382
Cdd:COG1061 231 ILLFLFDGIVyeyslkEAIEDGYLAP-PEYYGIrvdltderAEYDALSERLREALAADAER-KDKILRELLREHPDDRKT 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 383 LVFVETKRGANELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQCPILVATAVAARGLDIPNVRHVINYDLPGDSDE 462
Cdd:COG1061 309 LVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPRE 388
|
....*..
gi 17510309 463 YVHRIGR 469
Cdd:COG1061 389 FIQRLGR 395
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
118-336 |
2.87e-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: 2.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 118 AIEHFNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLAN--RDLMSCAQTGSGKTAAFLLPIIQHIlaggpdmvkppaf 195
Cdd:cd18048 16 SVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRV------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 196 tNGRRTYYPCaLVLSPTRELAIQIHK---EATKFSykSNIQtaILYGGRENYRDQVNRLRAgtHILIATPGRLID-IIEQ 271
Cdd:cd18048 83 -DALKLYPQC-LCLSPTFELALQTGKvveEMGKFC--VGIQ--VIYAIRGNRPGKGTDIEA--QIVIGTPGTVLDwCFKL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17510309 272 GFIGLAGCRYLVLDEADRMLDM-GFEPQIRKIvgQGMPPKTARTTaMFSATFPKEIQVLAKDFLKD 336
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 ... |
122-336 |
7.93e-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: 7.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 122 FNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLAN--RDLMSCAQTGSGKTAAFLLPIIQHIlaggpdmvkPPAftngr 199
Cdd:cd18047 3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV---------EPA----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 200 rTYYPCALVLSPTRELAIQIHKEATKFSyKSNIQTAILYGGRENYRDQVNRLRagTHILIATPGRLID-IIEQGFIGLAG 278
Cdd:cd18047 69 -NKYPQCLCLSPTYELALQTGKVIEQMG-KFYPELKLAYAVRGNKLERGQKIS--EQIVIGTPGTVLDwCSKLKFIDPKK 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17510309 279 CRYLVLDEADRML-DMGFEPQIRKIvgQGMPPKTARTTaMFSATFPKEIQVLAKDFLKD 336
Cdd:cd18047 145 IKVFVLDEADVMIaTQGHQDQSIRI--QRMLPRNCQML-LFSATFEDSVWKFAQKVVPD 200
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
245-490 |
2.50e-16 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 82.11 E-value: 2.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 245 RDQV-NRLRAG-THILIATPGRL-----IDIIEQGFIGLagcryLVLDEA--------DrmldmgFEP---QIRKIVGQ- 305
Cdd:COG0514 96 RREVlRALRAGeLKLLYVAPERLlnprfLELLRRLKISL-----FAIDEAhcisqwghD------FRPdyrRLGELRERl 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 306 GMPPktartTAMFSATFPKEIQ--VLAKDFLKDNYIFLA-VGRvgstsENIEQRLLWVNEMEKRSNLMEILmNEHSENLV 382
Cdd:COG0514 165 PNVP-----VLALTATATPRVRadIAEQLGLEDPRVFVGsFDR-----PNLRLEVVPKPPDDKLAQLLDFL-KEHPGGSG 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 383 LVFVETKRGANELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQCPILVATaVA-ARGLDIPNVRHVINYDLPGDSD 461
Cdd:COG0514 234 IVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLPKSIE 312
|
250 260
....*....|....*....|....*....
gi 17510309 462 EYVHRIGRTGRCGNLGIATSFFNDKNRGI 490
Cdd:COG0514 313 AYYQEIGRAGRDGLPAEALLLYGPEDVAI 341
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
355-472 |
2.43e-15 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 79.77 E-value: 2.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 355 QRLLW---VNEMEKRSN-----------LMEIL---MNEHSENLVLVFVETKRGANELAYFLNRQQIRSV------SIHG 411
Cdd:COG1111 312 KRLVSdprFRKAMRLAEeadiehpklskLREILkeqLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGrfvgqaSKEG 391
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17510309 412 D--LKQIERERNLELFRSGQCPILVATAVAARGLDIPNVRHVINYDlPGDSD-EYVHRIGRTGR 472
Cdd:COG1111 392 DkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYE-PVPSEiRSIQRKGRTGR 454
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
128-472 |
2.01e-13 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 73.01 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 128 GPAVMENVNRSGYSKPTPVQKHSIP-TLLANRDLMSCAQTGSGKTAAFLLPIIQHILAGGpdmvkppaftngrrtyypCA 206
Cdd:COG1204 8 LEKVIEFLKERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKALLNGG------------------KA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 207 LVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGREnyrdqVNRLRAGTH-ILIATPGRLIDIIEQGFIGLAGCRYLVLD 285
Cdd:COG1204 70 LYIVPLRALASEKYREFKRDFEELGIKVGVSTGDYD-----SDDEWLGRYdILVATPEKLDSLLRNGPSWLRDVDLVVVD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 286 EA----------------DRMLDMGFEPQirkIVGqgmppktarttamFSATF--PKEI-QVLAKDFLKDNY--IFLAVG 344
Cdd:COG1204 145 EAhliddesrgptlevllARLRRLNPEAQ---IVA-------------LSATIgnAEEIaEWLDAELVKSDWrpVPLNEG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 345 RVgstsenIEQRLLWVNEMEKRSNLMEILMNEHSENL--VLVFVETKRGANELA-----------YFLNRQQIRSVSI-- 409
Cdd:COG1204 209 VL------YDGVLRFDDGSRRSKDPTLALALDLLEEGgqVLVFVSSRRDAESLAkkladelkrrlTPEEREELEELAEel 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 410 ------------------------HGDLKQIERERNLELFRSGQCPILVATAVAARGLDIPnVRHVI--NYDLPGDSD-- 461
Cdd:COG1204 283 levseethtnekladclekgvafhHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLP-ARRVIirDTKRGGMVPip 361
|
410
....*....|...
gi 17510309 462 --EYVHRIGRTGR 472
Cdd:COG1204 362 vlEFKQMAGRAGR 374
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
163-321 |
6.92e-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: 6.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 163 CAQTGSGKTAAFLLPIIQHILAGGPDmvkppaftngrrtyypcALVLSPTRELAIQiHKEATKFSYKSNIQTAILYGGRE 242
Cdd:cd00046 7 TAPTGSGKTLAALLAALLLLLKKGKK-----------------VLVLVPTKALALQ-TAERLRELFGPGIRVAVLVGGSS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 243 NYRDQVNRLRAgTHILIATPGRLIDIIEQ-GFIGLAGCRYLVLDEADRMLDMGFEPQIRKIVGQGMPPKTARTTAMfSAT 321
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 ... |
350-483 |
1.08e-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: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 350 SENIEQRLLWVNEMEKRSNLMEILMNEHSENLVLVFVETKRGANELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQ 429
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 17510309 430 CPILVATAVAARGLDIPNVRHVINYDLPGDSDEYVHRIGRTGRCGNLGIATSFF 483
Cdd:cd18794 81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
369-469 |
1.56e-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: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 369 LMEILMNE--HSENLV-LVFVETKRGANELAYFLNRQQIRSVSIHGD---------------LKQIERERNLELFRSGQC 430
Cdd:cd18802 12 LIEILREYfpKTPDFRgIIFVERRATAVVLSRLLKEHPSTLAFIRCGfligrgnssqrkrslMTQRKQKETLDKFRDGEL 91
|
90 100 110
....*....|....*....|....*....|....*....
gi 17510309 431 PILVATAVAARGLDIPNVRHVINYDLPGDSDEYVHRIGR 469
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 ... |
365-472 |
7.48e-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: 7.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 365 KRSNLMEIL------MNEHSENLVLVFVETKRGANELAYFLNRQ-----------QIRSVSIHGdLKQIERERNLELFRS 427
Cdd:cd18801 10 KLEKLEEIVkehfkkKQEGSDTRVIIFSEFRDSAEEIVNFLSKIrpgiratrfigQASGKSSKG-MSQKEQKEVIEQFRK 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 17510309 428 GQCPILVATAVAARGLDIPNVRHVINYDLPGDSDEYVHRIGRTGR 472
Cdd:cd18801 89 GGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
129-479 |
2.22e-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: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 129 PAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAgGPDmvkppaftngrrtyyPCALV 208
Cdd:COG1205 43 PELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLE-DPG---------------ATALY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 209 LSPTRELAiQ-----IHKEATKFSykSNIQTAILYGG-RENYRDQVnrlRAGTHILIATPgrliDIIEQGFIG------- 275
Cdd:COG1205 107 LYPTKALA-RdqlrrLRELAEALG--LGVRVATYDGDtPPEERRWI---REHPDIVLTNP----DMLHYGLLPhhtrwar 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 276 -LAGCRYLVLDEA---------------DRML----DMGFEPQIrkivgqgmppktarttAMFSATF--PKEiqvLAKDF 333
Cdd:COG1205 177 fFRNLRYVVIDEAhtyrgvfgshvanvlRRLRricrHYGSDPQF----------------ILASATIgnPAE---HAERL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 334 LKDNyiFLAVGRVGSTSeNIEQRLLW----VNEMEKRSNLME---ILMNEHSENL-VLVFVETKRGANELAYFLNRQ--- 402
Cdd:COG1205 238 TGRP--VTVVDEDGSPR-GERTFVLWnpplVDDGIRRSALAEaarLLADLVREGLrTLVFTRSRRGAELLARYARRAlre 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 403 QIRSVSI---HGDLKQIEReRNLE-LFRSGQCPILVAT-AVAArGLDIPNVRHVINYDLPGDSDEYVHRIGRTGRCGNLG 477
Cdd:COG1205 315 PDLADRVaayRAGYLPEER-REIErGLRSGELLGVVSTnALEL-GIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDS 392
|
..
gi 17510309 478 IA 479
Cdd:COG1205 393 LV 394
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
432-472 |
6.62e-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: 52.71 E-value: 6.62e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 17510309 432 ILVATAVAARGLDIPNVRHVINYDLPGDSDEYVHRIGRTGR 472
Cdd:cd18785 25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGR 65
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
369-470 |
8.23e-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: 8.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 369 LMEILMNEHSENL-VLVFVETKRGANELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQ-CP-ILVATAVAARGLDI 445
Cdd:COG0553 538 LLELLEELLAEGEkVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeAPvFLISLKAGGEGLNL 617
|
90 100 110
....*....|....*....|....*....|....*.
gi 17510309 446 PNVRHVINYDLPgdsdeY-----------VHRIGRT 470
Cdd:COG0553 618 TAADHVIHYDLW-----WnpaveeqaidrAHRIGQT 648
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
354-483 |
8.68e-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: 8.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 354 EQRLLWVNEMEKRSNLMEILMNEHSENLVLVFVETKRGANELAYFLNRQqirsvSIHGDLKQIERERNLELFRSGQCPIL 433
Cdd:cd18789 24 KRRLLAAMNPNKLRALEELLKRHEQGDKIIVFTDNVEALYRYAKRLLKP-----FITGETPQSEREEILQNFREGEYNTL 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 17510309 434 VATAVAARGLDIP--NVRHVINYdLPGDSDEYVHRIGRTGRCGNLGIATSFF 483
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 ... |
147-287 |
9.98e-09 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 55.28 E-value: 9.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 147 QKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILaggpdmvkppaftngrRTYYPCALVLSPTRELAIQIHKEATKF 226
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALL----------------RDPGSRALYLYPTKALAQDQLRSLREL 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17510309 227 --SYKSNIqTAILYGGRENYRDQVNRLRAGTHILIATPgrliDIIEQGFIG--------LAGCRYLVLDEA 287
Cdd:cd17923 69 leQLGLGI-RVATYDGDTPREERRAIIRNPPRILLTNP----DMLHYALLPhhdrwarfLRNLRYVVLDEA 134
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
140-471 |
1.06e-08 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 58.58 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 140 YSKPTPVQKHSIPTLLANRDLMSCAQTGSGKT-AAFLLPIIQhiLAGGPDMVKPPaftngRRTYypcALVLSPTRELAIQ 218
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAFLPALDE--LARRPRPGELP-----DGLR---VLYISPLKALAND 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 219 IHKeatkfsyksNIQTAILyGGRENYRDQVNRLRAGT------------------HILIATPgrlidiiEQGFI------ 274
Cdd:COG1201 92 IER---------NLRAPLE-EIGEAAGLPLPEIRVGVrtgdtpaserqrqrrrppHILITTP-------ESLALlltspd 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 275 ---GLAGCRYLVLDE----AD--R--MLDMGFEpQIRKIVgqgmpPKTARTTAMfSATF--PKEI-QVLAKDFLKDNYIF 340
Cdd:COG1201 155 areLLRGVRTVIVDEihalAGskRgvHLALSLE-RLRALA-----PRPLQRIGL-SATVgpLEEVaRFLVGYEDPRPVTI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 341 LAVG-------RVGSTSENIEQRLLWVNE----MEKRsnLMEILMNEHSenlVLVFVETKRGANELAYFLNRQ------Q 403
Cdd:COG1201 228 VDAGagkkpdlEVLVPVEDLIERFPWAGHlwphLYPR--VLDLIEAHRT---TLVFTNTRSQAERLFQRLNELnpedalP 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17510309 404 IRSVsiHGDLKQIER---ERNLelfRSGQCPILVATAVAARGLDIPNVRHVINYDLPGDSDEYVHRIGRTG 471
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) ... |
369-468 |
1.15e-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: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 369 LMEILMNEHSENL-VLVFVETKRGANELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQCP--ILVATAVAARGLDI 445
Cdd:cd18793 16 LLELLEELREPGEkVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGVGLNL 95
|
90 100
....*....|....*....|....*....
gi 17510309 446 PNVRHVINYDLPGDS--DEY----VHRIG 468
Cdd:cd18793 96 TAANRVILYDPWWNPavEEQaidrAHRIG 124
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
365-472 |
1.24e-08 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 57.96 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 365 KRSNLMEIL---MNEHSENLVLVFVETKRGANELAYFLNRQQIRSV------SIHGD--LKQIERERNLELFRSGQCPIL 433
Cdd:PRK13766 348 KLEKLREIVkeqLGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVrfvgqaSKDGDkgMSQKEQIEILDKFRAGEFNVL 427
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 17510309 434 VATAVAARGLDIPNVRHVINYDlPGDSD-EYVHRIGRTGR 472
Cdd:PRK13766 428 VSTSVAEEGLDIPSVDLVIFYE-PVPSEiRSIQRKGRTGR 466
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
383-472 |
1.79e-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: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 383 LVFVETKRG---ANELAYFLNRQQIRSVSIHGDlkqieRERNLELFRSGQCPILVATA----VAARGLDIPN-VRHVINY 454
Cdd:cd18798 28 LIFVSIDYGkeyAEELKEFLERHGIKAELALSS-----TEKNLEKFEEGEIDVLIGVAsyygVLVRGIDLPErIKYAIFY 102
|
90
....*....|....*...
gi 17510309 455 DLPGDSdeYVHRIGRTGR 472
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) ... |
382-472 |
3.01e-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: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 382 VLVFVETKRGANELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQCPILVATAVAARGLDIPNVRHV--INYDLPG- 458
Cdd:cd18790 30 VLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVaiLDADKEGf 109
|
90
....*....|....*.
gi 17510309 459 --DSDEYVHRIGRTGR 472
Cdd:cd18790 110 lrSETSLIQTIGRAAR 125
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
383-452 |
8.67e-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: 8.67e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17510309 383 LVFVETKRGANELAYFLNRQQIRSVSIHGDLKQIERERN-LELFRSGQ--CPILVATAVAARGLDIPNVRHVI 452
Cdd:cd18799 10 LIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDEaLILLFFGElkPPILVTVDLLTTGVDIPEVDNVV 82
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
139-474 |
1.20e-06 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 51.64 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 139 GYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIqhILAGgpdmvkppaftngrrtyypCALVLSPTrelaIQ 218
Cdd:PRK11057 22 GYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPAL--VLDG-------------------LTLVVSPL----IS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 219 IHKEATKFSYKSNIQTAILYG--GRENYRDQVNRLRAGT-HILIATPGRLI--DIIEQgfigLAGCR--YLVLDEADRML 291
Cdd:PRK11057 77 LMKDQVDQLLANGVAAACLNStqTREQQLEVMAGCRTGQiKLLYIAPERLMmdNFLEH----LAHWNpaLLAVDEAHCIS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 292 DMG--FEPQIRKIvGQgmppktarttamFSATFPkEIQVLAKDFLKDNyiflavgrvgSTSENIEQRLLWVNEMEK---- 365
Cdd:PRK11057 153 QWGhdFRPEYAAL-GQ------------LRQRFP-TLPFMALTATADD----------TTRQDIVRLLGLNDPLIQissf 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 366 -RSNLMEILMNEHS--ENLVLvFVETKRG------------ANELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQC 430
Cdd:PRK11057 209 dRPNIRYTLVEKFKplDQLMR-YVQEQRGksgiiycnsrakVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDL 287
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 17510309 431 PILVATAVAARGLDIPNVRHVINYDLPGDSDEYVHRIGRTGRCG 474
Cdd:PRK11057 288 QIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDG 331
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
154-287 |
1.46e-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: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 154 LLANRDLMSCAQTGSGKTAAFLLPIIQHILaggpdmvkppafTNGRRTYYpcalvLSPTRELAIQIHKEATKFSYKSNIQ 233
Cdd:cd17921 14 YLSGDSVLVSAPTSSGKTLIAELAILRALA------------TSGGKAVY-----IAPTRALVNQKEADLRERFGPLGKN 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 17510309 234 TAILYGGrenyrDQVNRLR-AGTHILIATP----GRLIDIIEQGFIGLagcRYLVLDEA 287
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 ... |
142-260 |
1.65e-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: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 142 KPTPVQKHSIPTLLAN------RDLMSCAQTGSGKTAAFLLPIIQhilaggpdmvkppAFTNGRRTyypcaLVLSPTREL 215
Cdd:cd17918 15 SLTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAALL-------------AYKNGKQV-----AILVPTEIL 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 17510309 216 AIQIHKEATKfsYKSNIQTAILYGGRENYRDQVNRLRAGTHILIA 260
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 ... |
409-472 |
1.07e-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: 1.07e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17510309 409 IHGDLKQIERERNLELFRSGQCPILVATAVAARGLDIPN--VRHVINYDLPGDSDeyVHRI-GRTGR 472
Cdd:cd18811 67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNatVMVIEDAERFGLSQ--LHQLrGRVGR 131
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
137-286 |
2.05e-05 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 47.96 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 137 RSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKT-AAFlLPIIQHILAGG-----PDMVkppaftngrrtYypcALVLS 210
Cdd:PRK13767 27 KEKFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAF-LAIIDELFRLGregelEDKV-----------Y---CLYVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 211 PTRELAIQIHK-----------EATKFSYK-SNIQTAILYGGRENYRDQvNRLRAGTHILIATPGRL-IDIIEQGFI-GL 276
Cdd:PRK13767 92 PLRALNNDIHRnleeplteireIAKERGEElPEIRVAIRTGDTSSYEKQ-KMLKKPPHILITTPESLaILLNSPKFReKL 170
|
170
....*....|
gi 17510309 277 AGCRYLVLDE 286
Cdd:PRK13767 171 RTVKWVIVDE 180
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
164-445 |
3.02e-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: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 164 AQTGSGKTAAFLLPIIQHILAGGpdmvkppaftnGRRTYYpcALvlsPTRELAIQIHKEATKFsYKSNIQ----TAILYG 239
Cdd:COG1203 154 APTGGGKTEAALLFALRLAAKHG-----------GRRIIY--AL---PFTSIINQTYDRLRDL-FGEDVLlhhsLADLDL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 240 --GRENYRDQVNRLRAGTH-----ILIATPGRLIDIIEQG-------FIGLAGcRYLVLDEADrMLDmgfePQIRKIVGQ 305
Cdd:COG1203 217 leEEEEYESEARWLKLLKElwdapVVVTTIDQLFESLFSNrkgqerrLHNLAN-SVIILDEVQ-AYP----PYMLALLLR 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 306 GMppKTAR---TTAMF-SATFPKEIqvlaKDFLKDNYIFLavgrvgsTSENIEQRLLWVNEMEKR----------SNLME 371
Cdd:COG1203 291 LL--EWLKnlgGSVILmTATLPPLL----REELLEAYELI-------PDEPEELPEYFRAFVRKRvelkegplsdEELAE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 372 ILMNE-HSENLVLVFVETKRGANELAyflnrQQIRSVSIHGDL-----KQIERERN------LELFRSGQCPILVATAVA 439
Cdd:COG1203 358 LILEAlHKGKSVLVIVNTVKDAQELY-----EALKEKLPDEEVyllhsRFCPADRSeiekeiKERLERGKPCILVSTQVV 432
|
....*.
gi 17510309 440 ARGLDI 445
Cdd:COG1203 433 EAGVDI 438
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
348-472 |
3.26e-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: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 348 STSENIEQRLLWVNEMEKR--SNLMEILmnEHSENlVLVFVETKRGANELAYFLNR------QQIRSVSIHGDLKQIERE 419
Cdd:cd18796 8 VILPVAPEIFPWAGESGADayAEVIFLL--ERHKS-TLVFTNTRSQAERLAQRLRElcpdrvPPDFIALHHGSLSRELRE 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 17510309 420 RNLELFRSGQCPILVATAVAARGLDIPNVRHVINYDLPGDSDEYVHRIGRTGR 472
Cdd:cd18796 85 EVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
371-472 |
3.70e-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: 3.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 371 EILMNEHSENL-VLVFVETKRGANELAyflnrQQIRSVSI-HGDLKQIERERNLELFRSGQCPILVATAVAARGLDIPNV 448
Cdd:cd18795 34 LLKIETVSEGKpVLVFCSSRKECEKTA-----KDLAGIAFhHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPAR 108
|
90 100 110
....*....|....*....|....*....|..
gi 17510309 449 RHVINYDLPGDSD--------EYVHRIGRTGR 472
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 ... |
409-472 |
6.59e-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: 6.59e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17510309 409 IHGDLKQIERERNLELFRSGQCPILVATAVAARGLDIPNVRHVI--NYDLPGDSDEYVHRiGRTGR 472
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 ... |
146-262 |
8.51e-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: 8.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 146 VQKHSIPTLL-ANRDLMSCAQTGSGKTAAFLLPIIQHIlaggpdMVKPPAFTNGRRTYYpcalvLSPTRELAIQIHKEAT 224
Cdd:cd18023 5 IQSEVFPDLLySDKNFVVSAPTGSGKTVLFELAILRLL------KERNPLPWGNRKVVY-----IAPIKALCSEKYDDWK 73
|
90 100 110
....*....|....*....|....*....|....*....
gi 17510309 225 -KFSyKSNIQTAILYGGRENYRDqvnRLRAGTHILIATP 262
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 ... |
141-291 |
1.29e-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: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 141 SKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAaFLLpIIQHILAggpdmvkppafTNGRRTYYpcalvLSPTRELAIQIH 220
Cdd:cd17924 16 FPPWGAQRTWAKRLLRGKSFAIIAPTGVGKTT-FGL-ATSLYLA-----------SKGKRSYL-----IFPTKSLVKQAY 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17510309 221 KEATKFSYKSNIQTAIL-YGGRENYRDQ---VNRLRAGT-HILIATPGRLIDIIEQgfigLAGCRY--LVLDEADRML 291
Cdd:cd17924 78 ERLSKYAEKAGVEVKILvYHSRLKKKEKeelLEKIEKGDfDILVTTNQFLSKNFDL----LSNKKFdfVFVDDVDAVL 151
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
157-286 |
1.51e-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: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 157 NRDLMSCAQTGSGKTAAFLLPIIQHILAGGPDMVKppaftngrrtyypcALVLSPTRELAIQIHKEATKFSykSNIQTAI 236
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGVQ--------------VLYISPLKALINDQERRLEEPL--DEIDLEI 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 17510309 237 LYGGRENYRDQVNR---LRAGTHILIATPGRL-IDIIEQGFIG-LAGCRYLVLDE 286
Cdd:cd17922 65 PVAVRHGDTSQSEKakqLKNPPGILITTPESLeLLLVNKKLRElFAGLRYVVVDE 119
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
166-287 |
6.88e-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: 6.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 166 TGSGKT--AAFLLPIIQHILAGGPDmvkppaftNGRRTYYpcalvLSPTRELAIQIHKEATKFSyksNIQTAILYGGREN 243
Cdd:cd18034 25 TGSGKTliAVMLIKEMGELNRKEKN--------PKKRAVF-----LVPTVPLVAQQAEAIRSHT---DLKVGEYSGEMGV 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 17510309 244 Y---RDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRYLVLDEA 287
Cdd:cd18034 89 DkwtKERWKEELEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
403-479 |
1.93e-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: 1.93e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17510309 403 QIRSVSIHGDLKQIERERNLELFRSGQCPILVATAVAARGLDIPNVRHVI--NYDLPGDSDEYVHRiGRTGRCGNLGIA 479
Cdd:cd18810 51 EARIAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIieRADKFGLAQLYQLR-GRVGRSKERAYA 128
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
145-299 |
2.74e-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: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 145 PVQKHSIPT-LLANRDLMSCAQTGSGKTAAFLLPIIQHILAGGPdmvkppaftngrrtyypcALVLSPTRELAIQIHKEA 223
Cdd:cd18028 4 PPQAEAVRAgLLKGENLLISIPTASGKTLIAEMAMVNTLLEGGK------------------ALYLVPLRALASEKYEEF 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510309 224 TKFsYKSNIQTAILYGgreNYRDQVNRLrAGTHILIATPGRLIDIIEQG--FIGLAGCryLVLDE--------------- 286
Cdd:cd18028 66 KKL-EEIGLKVGISTG---DYDEDDEWL-GDYDIIVATYEKFDSLLRHSpsWLRDVGV--VVVDEihlisdeergptles 138
|
170
....*....|....
gi 17510309 287 -ADRMLDMGFEPQI 299
Cdd:cd18028 139 iVARLRRLNPNTQI 152
|
|
| |
