|
Name |
Accession |
Description |
Interval |
E-value |
| DEXXQc_DNA2 |
cd18041 |
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ... |
265-468 |
1.67e-123 |
|
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses different enzymatic activities, such as single-stranded DNA (ssDNA)-dependent ATPase, 5-3 helicase, and endonuclease activities, and is involved in DNA replication and DNA repair in the nucleus and mitochondrion. It is involved in Okazaki fragment processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA and becomes a substrate for FEN1. It is also involved in 5-end resection of DNA during double-strand break (DSB) repair; it is recruited by BLM and mediates the cleavage of 5-ssDNA, while the 3-ssDNA cleavage is prevented by the presence of RPA. DNA2 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: 350799 [Multi-domain] Cd Length: 203 Bit Score: 365.79 E-value: 1.67e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 265 GLNKPQRQAMKKVLLSKDYTLIVGMPGTGKTTTICTLVRILYACGFSVLLTSYTHSAVDNILLKLAKFKIGFLRLGQIQK 344
Cdd:cd18041 1 GLNKDQRQAIKKVLNAKDYALILGMPGTGKTTTIAALVRILVALGKSVLLTSYTHSAVDNILLKLKKFGVNFLRLGRLKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 345 VHPAIQQFTEQEIcrSKSIKSLALLEELYNSQLIVATTCMGINHPIFSRKIFDFCIVDEASQISQPICLGPLFFSRRFVL 424
Cdd:cd18041 81 IHPDVQEFTLEAI--LKSCKSVEELESKYESVSVVATTCLGINHPIFRRRTFDYCIVDEASQITLPICLGPLRLAKKFVL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767961922 425 VGDHQQLPPLVLNREARALGMSESLFKRLEQNK-SAVVQLTVQYR 468
Cdd:cd18041 159 VGDHYQLPPLVKSREARELGMDESLFKRLSEAHpDAVVQLTIQYR 203
|
|
| TIGR00376 |
TIGR00376 |
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ... |
111-672 |
3.16e-73 |
|
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of this family have been characterized as binding certain single-stranded G-rich DNA sequences (GGGGT and GGGCT). A number of related proteins are characterized as helicases. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273041 [Multi-domain] Cd Length: 636 Bit Score: 249.35 E-value: 3.16e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 111 EMEKSGSCIGNLirmeHVKIVCD--GQYLHNFQCKHG---AIPVtnlmaGDRVIVSgEERSLFALSRGYVKEINMTTVTC 185
Cdd:TIGR00376 21 QRERRGRAILNL----QGKIRGGllGFLLVRFGRRKAiatEISV-----GDIVLVS-RGNPLQSDLTGVVTRVGKRFITV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 186 LLDrnlSVLPESTL--FRLDQEEKNCDIDTPLGNLSKLMENtfvSKKLRDLIIDFREPQFISYLSSVLPHDakdtvacil 263
Cdd:TIGR00376 91 ALE---ESVPQWSLkrVRIDLYANDVTFKRMKEALRALTEN---HSRLLEFLLGREAPSKASEIHDFQFFD--------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 264 KGLNKPQRQAMKKVLLSKDYTLIVGMPGTGKTTTICTLVRILYACGFSVLLTSYTHSAVDNILLKLAKFKIGFLRLGQIQ 343
Cdd:TIGR00376 156 PNLNESQKEAVLFALSSKDLFLIHGPPGTGKTRTVVELIRQLVKRGLRVLVTAPSNIAVDNLLERLALCDQKIVRLGHPA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 344 KVHPAIQQFT-------------------------------------------EQEICR------------SKSIKSLA- 367
Cdd:TIGR00376 236 RLLKSNKQHSldylienhpkyqivadirekidelieernkktkpspqkrrglsDIKILRkalkkreargieSLKIASMAe 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 368 ----------LLEELYNSQLIVATTCMGINHPIFSRKI--------FDFCIVDEASQISQPICLGPLFFSRRFVLVGDHQ 429
Cdd:TIGR00376 316 wietnksidrLLKLLPESEERIMNEILAESDATNSMAGseilngqyFDVAVIDEASQAMEPSCLIPLLKARKLILAGDHK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 430 QLPPLVLNREARalGMSESLFKRLEQNKSAVVQ-LTVQYRMNSKIMSLSNKLTYEGKLECGSDKVANAVINLrhfkdVKL 508
Cdd:TIGR00376 396 QLPPTILSHDAE--ELSLTLFERLIKEYPERSRtLNVQYRMNQKIMEFPSREFYNGKLTAHESVANILLRDL-----PKV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 509 ELEFYADYSDNPwlmgvfepnNPVCFLNTDKVPAPEQVEKGGVS--NVTEAKLIVFLTSIFVKAGCSPSDIGIIAPYRQQ 586
Cdd:TIGR00376 469 EATESEDDLETG---------IPLLFIDTSGCELFELKEADSTSkyNPGEAELVSEIIQALVKMGVPANDIGVITPYDAQ 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 587 LKIINDLLARSIGMVEVNTVDKYQGRDKSIVLVSFVRSNKDGTVGeLLKDWRRLNVAITRAKHKLILLGCVPSLNCYPPL 666
Cdd:TIGR00376 540 VDLLRQLLEHRHIDIEVSSVDGFQGREKEVIIISFVRSNRKGEVG-FLKDLRRLNVALTRARRKLIVIGDSRTLSNHKFY 618
|
....*.
gi 767961922 667 EKLLNH 672
Cdd:TIGR00376 619 KRLIEW 624
|
|
| AAA_12 |
pfam13087 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
445-657 |
3.20e-71 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.
Pssm-ID: 463780 [Multi-domain] Cd Length: 196 Bit Score: 229.74 E-value: 3.20e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 445 MSESLFKRL-EQNKSAVVQLTVQYRMNSKIMSLSNKLTYEGKLECGSDkvanaVINLRhfkdvklelefyadysdNPWLM 523
Cdd:pfam13087 1 LDRSLFERLqELGPSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPS-----VAERP-----------------LPDDF 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 524 GVFEPNNPVCFLNTDKVPAPEQVEKGGVSNVTEAKLIVFLTSIFVKAGCSP-SDIGIIAPYRQQLKIINDLLARS---IG 599
Cdd:pfam13087 59 HLPDPLGPLVFIDVDGSEEEESDGGTSYSNEAEAELVVQLVEKLIKSGPEEpSDIGVITPYRAQVRLIRKLLKRKlggKL 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767961922 600 MVEVNTVDKYQGRDKSIVLVSFVRSNKDGTVGeLLKDWRRLNVAITRAKHKLILLGCV 657
Cdd:pfam13087 139 EIEVNTVDGFQGREKDVIIFSCVRSNEKGGIG-FLSDPRRLNVALTRAKRGLIIVGNA 195
|
|
| DNA2 |
COG1112 |
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair]; |
344-676 |
4.27e-67 |
|
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
Pssm-ID: 440729 [Multi-domain] Cd Length: 819 Bit Score: 236.18 E-value: 4.27e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 344 KVHPAIQQFTEQEICRSKSIKSLALlEELYNSQLIVATTCMGI-NHPIFSRKIFDFCIVDEASQISQPICLGPLFFSRRF 422
Cdd:COG1112 504 REAARLRRALRRELKKRRELRKLLW-DALLELAPVVGMTPASVaRLLPLGEGSFDLVIIDEASQATLAEALGALARAKRV 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 423 VLVGDHQQLPPLVLNREA---RALGMSESLFKRL-EQNKSAVVQLTVQYRMNSKIMSLSNKLTYEGKLecgsdkvanavI 498
Cdd:COG1112 583 VLVGDPKQLPPVVFGEEAeevAEEGLDESLLDRLlARLPERGVMLREHYRMHPEIIAFSNRLFYDGKL-----------V 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 499 NLRHFKDVKLElefyadysdnpwlmgvfEPNNPVCFLNTDKVPAPEQvekGGVSNVTEAKLIVFLTSIFVKAGCSPSDIG 578
Cdd:COG1112 652 PLPSPKARRLA-----------------DPDSPLVFIDVDGVYERRG---GSRTNPEEAEAVVELVRELLEDGPDGESIG 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 579 IIAPYRQQLKIINDLLARSIGM----VEVNTVDKYQGRDKSIVLVSFVRSNKDGTVGE---LLKDWRRLNVAITRAKHKL 651
Cdd:COG1112 712 VITPYRAQVALIRELLREALGDglepVFVGTVDRFQGDERDVIIFSLVYSNDEDVPRNfgfLNGGPRRLNVAVSRARRKL 791
|
330 340
....*....|....*....|....*...
gi 767961922 652 ILLGCVP---SLNCYPPLEKLLNHLNSE 676
Cdd:COG1112 792 IVVGSRElldSDPSTPALKRLLEYLERA 819
|
|
| SF1_C_Upf1 |
cd18808 |
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ... |
469-673 |
1.63e-54 |
|
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), and similar proteins. They are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 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: 350195 [Multi-domain] Cd Length: 184 Bit Score: 184.75 E-value: 1.63e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 469 MNSKIMSLSNKLTYEGKLECGSDKvanavinlrhfkdvklelefyadySDNPWLMGVFEPNNPVCFLNTDKvpaPEQVEK 548
Cdd:cd18808 1 MHPEISEFPSKLFYEGKLKAGVSV------------------------AARLNPPPLPGPSKPLVFVDVSG---GEEREE 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 549 GGVS--NVTEAKLIVFLTSIFVKAGCSPSDIGIIAPYRQQLKIINDLLARSIGM---VEVNTVDKYQGRDKSIVLVSFVR 623
Cdd:cd18808 54 SGTSksNEAEAELVVELVKYLLKSGVKPSSIGVITPYRAQVALIRELLRKRGGLledVEVGTVDNFQGREKDVIILSLVR 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767961922 624 SNKDGTVGELLKDWRRLNVAITRAKHKLILLGCVPSLNCYPPLEKLLNHL 673
Cdd:cd18808 134 SNESGGSIGFLSDPRRLNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEYL 183
|
|
| AAA_11 |
pfam13086 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
269-438 |
8.11e-27 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.
Pssm-ID: 404072 [Multi-domain] Cd Length: 248 Bit Score: 109.74 E-value: 8.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 269 PQRQAMKKVLLSKDYTLIVGMPGTGKTTTICTLVRILYACGFS-------VLLTSYTHSAVDNILLKLA----KFKIGFL 337
Cdd:pfam13086 1 SQREAIRSALSSSHFTLIQGPPGTGKTTTIVELIRQLLSYPATsaaagprILVCAPSNAAVDNILERLLrkgqKYGPKIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 338 RLGQIQKVHPAIQQFTEQEICRSKS-------------------IKSLALLEELYNSQL--------------------- 377
Cdd:pfam13086 81 RIGHPAAISEAVLPVSLDYLVESKLnneedaqivkdiskeleklAKALRAFEKEIIVEKllksrnkdkskleqerrklrs 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 378 -------------------------IVATTCMGINHPIFSR-KIFDFCIVDEASQISQPICLGPLFF-SRRFVLVGDHQQ 430
Cdd:pfam13086 161 erkelrkelrrreqslereildeaqIVCSTLSGAGSRLLSSlANFDVVIIDEAAQALEPSTLIPLLRgPKKVVLVGDPKQ 240
|
....*...
gi 767961922 431 LPPLVLNR 438
Cdd:pfam13086 241 LPPTVISK 248
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
266-480 |
1.28e-11 |
|
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];
Pssm-ID: 440273 [Multi-domain] Cd Length: 514 Bit Score: 67.69 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 266 LNKPQRQAMKKVLLSKDYTLIVGMPGTGKTTTICTLVRILYACGFSVLLTSYTHSAVDNIllklakfkigflrlgqiqkv 345
Cdd:COG0507 125 LSDEQREAVALALTTRRVSVLTGGAGTGKTTTLRALLAALEALGLRVALAAPTGKAAKRL-------------------- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 346 hpaiqqftEQEICR-SKSIKSlaLLEELYNSQLIVAttcmGINHPIFSRKIFdfcIVDEASQISQPIclgplfFSR---- 420
Cdd:COG0507 185 --------SESTGIeARTIHR--LLGLRPDSGRFRH----NRDNPLTPADLL---VVDEASMVDTRL------MAAllea 241
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767961922 421 ------RFVLVGDHQQLPPlVlnrEA-RALGMseslfkRLEQNKSAVVQLTVQYRM--NSKIMSLSNKL 480
Cdd:COG0507 242 lpragaRLILVGDPDQLPS-V---GAgAVLRD------LIESGTVPVVELTEVYRQadDSRIIELAHAI 300
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
266-404 |
7.31e-04 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 41.32 E-value: 7.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 266 LNKPQRQAMKKVLLSKDYTLIVGMPGTGKTTTICT--LVRILYACGFSVLLTSYTHSAVDNILLKLAKFkigflrlgqiq 343
Cdd:smart00487 9 LRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLpaLEALKRGKGGRVLVLVPTRELAEQWAEELKKL----------- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767961922 344 kvhpaIQQFTEQEICRSKSIKSLALLEELYNS--QLIVATTCMGINHPI---FSRKIFDFCIVDEA 404
Cdd:smart00487 78 -----GPSLGLKVVGLYGGDSKREQLRKLESGktDILVTTPGRLLDLLEndkLSLSNVDLVILDEA 138
|
|
| ftsY |
TIGR00064 |
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ... |
223-314 |
4.88e-03 |
|
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and SRP54; both are GTPases. In E.coli, ftsY is an essential gene located in an operon with cell division genes ftsE and ftsX, but its apparent function is as the signal recognition particle docking protein. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 272883 [Multi-domain] Cd Length: 277 Bit Score: 39.55 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 223 ENTFVSKKLRDLIIDfrepqfiSYLSSVLPHDAKDTVACILKGLNKPQrqamkkVLLskdytlIVGMPGTGKTTTICTLV 302
Cdd:TIGR00064 38 KKVKDAEKLKEILKE-------YLKEILKEDLLKNTDLELIVEENKPN------VIL------FVGVNGVGKTTTIAKLA 98
|
90
....*....|..
gi 767961922 303 RILYACGFSVLL 314
Cdd:TIGR00064 99 NKLKKQGKSVLL 110
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DEXXQc_DNA2 |
cd18041 |
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ... |
265-468 |
1.67e-123 |
|
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses different enzymatic activities, such as single-stranded DNA (ssDNA)-dependent ATPase, 5-3 helicase, and endonuclease activities, and is involved in DNA replication and DNA repair in the nucleus and mitochondrion. It is involved in Okazaki fragment processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA and becomes a substrate for FEN1. It is also involved in 5-end resection of DNA during double-strand break (DSB) repair; it is recruited by BLM and mediates the cleavage of 5-ssDNA, while the 3-ssDNA cleavage is prevented by the presence of RPA. DNA2 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: 350799 [Multi-domain] Cd Length: 203 Bit Score: 365.79 E-value: 1.67e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 265 GLNKPQRQAMKKVLLSKDYTLIVGMPGTGKTTTICTLVRILYACGFSVLLTSYTHSAVDNILLKLAKFKIGFLRLGQIQK 344
Cdd:cd18041 1 GLNKDQRQAIKKVLNAKDYALILGMPGTGKTTTIAALVRILVALGKSVLLTSYTHSAVDNILLKLKKFGVNFLRLGRLKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 345 VHPAIQQFTEQEIcrSKSIKSLALLEELYNSQLIVATTCMGINHPIFSRKIFDFCIVDEASQISQPICLGPLFFSRRFVL 424
Cdd:cd18041 81 IHPDVQEFTLEAI--LKSCKSVEELESKYESVSVVATTCLGINHPIFRRRTFDYCIVDEASQITLPICLGPLRLAKKFVL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767961922 425 VGDHQQLPPLVLNREARALGMSESLFKRLEQNK-SAVVQLTVQYR 468
Cdd:cd18041 159 VGDHYQLPPLVKSREARELGMDESLFKRLSEAHpDAVVQLTIQYR 203
|
|
| TIGR00376 |
TIGR00376 |
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ... |
111-672 |
3.16e-73 |
|
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of this family have been characterized as binding certain single-stranded G-rich DNA sequences (GGGGT and GGGCT). A number of related proteins are characterized as helicases. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273041 [Multi-domain] Cd Length: 636 Bit Score: 249.35 E-value: 3.16e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 111 EMEKSGSCIGNLirmeHVKIVCD--GQYLHNFQCKHG---AIPVtnlmaGDRVIVSgEERSLFALSRGYVKEINMTTVTC 185
Cdd:TIGR00376 21 QRERRGRAILNL----QGKIRGGllGFLLVRFGRRKAiatEISV-----GDIVLVS-RGNPLQSDLTGVVTRVGKRFITV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 186 LLDrnlSVLPESTL--FRLDQEEKNCDIDTPLGNLSKLMENtfvSKKLRDLIIDFREPQFISYLSSVLPHDakdtvacil 263
Cdd:TIGR00376 91 ALE---ESVPQWSLkrVRIDLYANDVTFKRMKEALRALTEN---HSRLLEFLLGREAPSKASEIHDFQFFD--------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 264 KGLNKPQRQAMKKVLLSKDYTLIVGMPGTGKTTTICTLVRILYACGFSVLLTSYTHSAVDNILLKLAKFKIGFLRLGQIQ 343
Cdd:TIGR00376 156 PNLNESQKEAVLFALSSKDLFLIHGPPGTGKTRTVVELIRQLVKRGLRVLVTAPSNIAVDNLLERLALCDQKIVRLGHPA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 344 KVHPAIQQFT-------------------------------------------EQEICR------------SKSIKSLA- 367
Cdd:TIGR00376 236 RLLKSNKQHSldylienhpkyqivadirekidelieernkktkpspqkrrglsDIKILRkalkkreargieSLKIASMAe 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 368 ----------LLEELYNSQLIVATTCMGINHPIFSRKI--------FDFCIVDEASQISQPICLGPLFFSRRFVLVGDHQ 429
Cdd:TIGR00376 316 wietnksidrLLKLLPESEERIMNEILAESDATNSMAGseilngqyFDVAVIDEASQAMEPSCLIPLLKARKLILAGDHK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 430 QLPPLVLNREARalGMSESLFKRLEQNKSAVVQ-LTVQYRMNSKIMSLSNKLTYEGKLECGSDKVANAVINLrhfkdVKL 508
Cdd:TIGR00376 396 QLPPTILSHDAE--ELSLTLFERLIKEYPERSRtLNVQYRMNQKIMEFPSREFYNGKLTAHESVANILLRDL-----PKV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 509 ELEFYADYSDNPwlmgvfepnNPVCFLNTDKVPAPEQVEKGGVS--NVTEAKLIVFLTSIFVKAGCSPSDIGIIAPYRQQ 586
Cdd:TIGR00376 469 EATESEDDLETG---------IPLLFIDTSGCELFELKEADSTSkyNPGEAELVSEIIQALVKMGVPANDIGVITPYDAQ 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 587 LKIINDLLARSIGMVEVNTVDKYQGRDKSIVLVSFVRSNKDGTVGeLLKDWRRLNVAITRAKHKLILLGCVPSLNCYPPL 666
Cdd:TIGR00376 540 VDLLRQLLEHRHIDIEVSSVDGFQGREKEVIIISFVRSNRKGEVG-FLKDLRRLNVALTRARRKLIVIGDSRTLSNHKFY 618
|
....*.
gi 767961922 667 EKLLNH 672
Cdd:TIGR00376 619 KRLIEW 624
|
|
| AAA_12 |
pfam13087 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
445-657 |
3.20e-71 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.
Pssm-ID: 463780 [Multi-domain] Cd Length: 196 Bit Score: 229.74 E-value: 3.20e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 445 MSESLFKRL-EQNKSAVVQLTVQYRMNSKIMSLSNKLTYEGKLECGSDkvanaVINLRhfkdvklelefyadysdNPWLM 523
Cdd:pfam13087 1 LDRSLFERLqELGPSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPS-----VAERP-----------------LPDDF 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 524 GVFEPNNPVCFLNTDKVPAPEQVEKGGVSNVTEAKLIVFLTSIFVKAGCSP-SDIGIIAPYRQQLKIINDLLARS---IG 599
Cdd:pfam13087 59 HLPDPLGPLVFIDVDGSEEEESDGGTSYSNEAEAELVVQLVEKLIKSGPEEpSDIGVITPYRAQVRLIRKLLKRKlggKL 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767961922 600 MVEVNTVDKYQGRDKSIVLVSFVRSNKDGTVGeLLKDWRRLNVAITRAKHKLILLGCV 657
Cdd:pfam13087 139 EIEVNTVDGFQGREKDVIIFSCVRSNEKGGIG-FLSDPRRLNVALTRAKRGLIIVGNA 195
|
|
| DNA2 |
COG1112 |
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair]; |
344-676 |
4.27e-67 |
|
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
Pssm-ID: 440729 [Multi-domain] Cd Length: 819 Bit Score: 236.18 E-value: 4.27e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 344 KVHPAIQQFTEQEICRSKSIKSLALlEELYNSQLIVATTCMGI-NHPIFSRKIFDFCIVDEASQISQPICLGPLFFSRRF 422
Cdd:COG1112 504 REAARLRRALRRELKKRRELRKLLW-DALLELAPVVGMTPASVaRLLPLGEGSFDLVIIDEASQATLAEALGALARAKRV 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 423 VLVGDHQQLPPLVLNREA---RALGMSESLFKRL-EQNKSAVVQLTVQYRMNSKIMSLSNKLTYEGKLecgsdkvanavI 498
Cdd:COG1112 583 VLVGDPKQLPPVVFGEEAeevAEEGLDESLLDRLlARLPERGVMLREHYRMHPEIIAFSNRLFYDGKL-----------V 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 499 NLRHFKDVKLElefyadysdnpwlmgvfEPNNPVCFLNTDKVPAPEQvekGGVSNVTEAKLIVFLTSIFVKAGCSPSDIG 578
Cdd:COG1112 652 PLPSPKARRLA-----------------DPDSPLVFIDVDGVYERRG---GSRTNPEEAEAVVELVRELLEDGPDGESIG 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 579 IIAPYRQQLKIINDLLARSIGM----VEVNTVDKYQGRDKSIVLVSFVRSNKDGTVGE---LLKDWRRLNVAITRAKHKL 651
Cdd:COG1112 712 VITPYRAQVALIRELLREALGDglepVFVGTVDRFQGDERDVIIFSLVYSNDEDVPRNfgfLNGGPRRLNVAVSRARRKL 791
|
330 340
....*....|....*....|....*...
gi 767961922 652 ILLGCVP---SLNCYPPLEKLLNHLNSE 676
Cdd:COG1112 792 IVVGSRElldSDPSTPALKRLLEYLERA 819
|
|
| SF1_C_Upf1 |
cd18808 |
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ... |
469-673 |
1.63e-54 |
|
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), and similar proteins. They are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 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: 350195 [Multi-domain] Cd Length: 184 Bit Score: 184.75 E-value: 1.63e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 469 MNSKIMSLSNKLTYEGKLECGSDKvanavinlrhfkdvklelefyadySDNPWLMGVFEPNNPVCFLNTDKvpaPEQVEK 548
Cdd:cd18808 1 MHPEISEFPSKLFYEGKLKAGVSV------------------------AARLNPPPLPGPSKPLVFVDVSG---GEEREE 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 549 GGVS--NVTEAKLIVFLTSIFVKAGCSPSDIGIIAPYRQQLKIINDLLARSIGM---VEVNTVDKYQGRDKSIVLVSFVR 623
Cdd:cd18808 54 SGTSksNEAEAELVVELVKYLLKSGVKPSSIGVITPYRAQVALIRELLRKRGGLledVEVGTVDNFQGREKDVIILSLVR 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767961922 624 SNKDGTVGELLKDWRRLNVAITRAKHKLILLGCVPSLNCYPPLEKLLNHL 673
Cdd:cd18808 134 SNESGGSIGFLSDPRRLNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEYL 183
|
|
| DEXXQc_SMUBP2 |
cd18044 |
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ... |
266-468 |
1.24e-44 |
|
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, or IGHMBP2) is a 5' to 3' helicase that unwinds RNA and DNA duplexes in an ATP-dependent reaction. It is a DNA-binding protein specific to 5'-phosphorylated single-stranded guanine-rich sequence (5'-GGGCT-3') related to the immunoglobulin mu chain switch region. The IGHMBP2 gene is responsible for Charcot-Marie-Tooth disease (CMT) type 2S and spinal muscular atrophy with respiratory distress type 1 (SMARD1). It is also thought to play a role in frontotemporal dementia (FTD) with amyotrophic lateral sclerosis (ALS) and major depressive disorder (MDD). SMUBP2 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: 350802 [Multi-domain] Cd Length: 191 Bit Score: 158.16 E-value: 1.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 266 LNKPQRQAMKKVLLSKDYTLIVGMPGTGKTTTICTLVRILYACGFSVLLTSYTHSAVDNILLKLAKFKIGFLRLGQIQKV 345
Cdd:cd18044 2 LNDSQKEAVKFALSQKDVALIHGPPGTGKTTTVVEIILQAVKRGEKVLACAPSNIAVDNLVERLVALKVKVVRIGHPARL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 346 HPAIQQFTeqeicrsksikslalLEELYNSQlIVATTCMGINHPIFSRKI-FDFCIVDEASQISQPICLGPLFFSRRFVL 424
Cdd:cd18044 82 LESVLDHS---------------LDALVAAQ-VVLATNTGAGSRQLLPNElFDVVVIDEAAQALEASCWIPLLKARRCIL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767961922 425 VGDHQQLPPLVLNREARALGMSESLFKRLEQ--NKSAVVQLTVQYR 468
Cdd:cd18044 146 AGDHKQLPPTILSDKAARGGLGVTLFERLVNlyGESVVRMLTVQYR 191
|
|
| DEXXQc_SETX |
cd18042 |
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ... |
266-468 |
2.95e-35 |
|
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in transcription, neurogenesis, and antiviral response. SEXT is an R-loop-associated protein that is thought to function as an RNA/DNA helicase. R-loops consist of RNA/DNA hybrids, formed during transcription when nascent RNA hybridizes to the DNA template strand, displacing the non-template DNA strand. Mutations in SETX are linked to two neurodegenerative disorders: ataxia with oculomotor apraxia type 2 (AOA2) and amyotrophic lateral sclerosis type 4 (ALS4). S. cerevisiae homolog splicing endonuclease 1 (Sen1) is an exclusively nuclear protein, important for nucleolar organization. S. cerevisiae Sen1 and its ortholog, the Schizosaccharomyces pombe Sen1, share conserved domains and belong to the family I class of helicases. Both proteins translocate 5' to 3' and unwind both DNA and RNA duplexes and also RNA/DNA hybrids in vitro. SETX 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: 438712 [Multi-domain] Cd Length: 218 Bit Score: 133.11 E-value: 2.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 266 LNKPQRQAMKKVLL-SKDYTLIVGMPGTGKTTTICTLVRILYA-------------------------CGFSVLLTSYTH 319
Cdd:cd18042 1 LNESQLEAIASALQnSPGITLIQGPPGTGKTKTIVGILSVLLAgkyrkyyekvkkklrklqrnlnnkkKKNRILVCAPSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 320 SAVDNILLKLAKfkiGFLRLGQIQKVHPAIQQFTEQEICRSksikslalleeLYNSQLIVATTCMGINHPIFSRKI--FD 397
Cdd:cd18042 81 AAVDEIVLRLLS---EGFLDGDGRSYKPNVVRVGRQELRAS-----------ILNEADIVCTTLSSSGSDLLESLPrgFD 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767961922 398 FCIVDEASQISQPICLGPL-FFSRRFVLVGDHQQLPPLVLNREARALGMSESLFKRLEQNKSAVVQLTVQYR 468
Cdd:cd18042 147 TVIIDEAAQAVELSTLIPLrLGCKRLILVGDPKQLPATVFSKVAQKLGYDRSLFERLQLAGYPVLMLTTQYR 218
|
|
| DEXXQc_Upf1-like |
cd17934 |
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ... |
283-468 |
1.21e-34 |
|
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), coronavirus Nsp13, and similar proteins. They belong to 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: 438708 [Multi-domain] Cd Length: 121 Bit Score: 127.74 E-value: 1.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 283 YTLIVGMPGTGKTTTICTLVRIL--YACGFSVLLTSYTHSAVDNIllklakfkigflrlgqiqkvhpaiqqfteqeicrs 360
Cdd:cd17934 1 ISLIQGPPGTGKTTTIAAIVLQLlkGLRGKRVLVTAQSNVAVDNV----------------------------------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 361 ksikslalleelynsqlivattcmginhpifsrkifDFCIVDEASQISQPICLGPLFFSRRFVLVGDHQQLPPLVLNREA 440
Cdd:cd17934 46 ------------------------------------DVVIIDEASQITEPELLIALIRAKKVVLVGDPKQLPPVVQEDHA 89
|
170 180 190
....*....|....*....|....*....|..
gi 767961922 441 RALG----MSESLFKRLEQNKSAVVQLTVQYR 468
Cdd:cd17934 90 ALLGlsfiLSLLLLFRLLLPGSPKVMLDTQYR 121
|
|
| DEXXQc_UPF1 |
cd18039 |
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ... |
266-468 |
2.80e-33 |
|
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of Nonsense Transcripts, or ATP-Dependent Helicase RENT1) is an RNA-dependent helicase and ATPase required for nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. It is recruited to mRNAs upon translation termination and undergoes a cycle of phosphorylation and dephosphorylation; its phosphorylation appears to be a key step in NMD. It is recruited by release factors to stalled ribosomes together with the SMG1C protein kinase complex to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) located downstream from the termination codon through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD. Diseases associated with UPF1 include juvenile amyotrophic lateral sclerosis and epidermolysis bullosa, junctional, non-Herlitz type. UPF1 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: 350797 [Multi-domain] Cd Length: 234 Bit Score: 127.75 E-value: 2.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 266 LNKPQRQAMKKVLlSKDYTLIVGMPGTGKTTTICTLV-RILYACGFSVLLTSYTHSAVDNILLKLAKFKIGFLRL----- 339
Cdd:cd18039 2 LNHSQVDAVKTAL-QRPLSLIQGPPGTGKTVTSATIVyHLVKQGNGPVLVCAPSNVAVDQLTEKIHQTGLKVVRLcaksr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 340 -------------------GQIQKVHPAIQQFTEQ-EICRSKSIKSLALLE----ELYNSQLIVATTCMGINHPIFSRKI 395
Cdd:cd18039 81 eavespvsflalhnqvrnlDSAEKLELLKLLKLETgELSSADEKRYRKLKRkaerELLRNADVICCTCVGAGDPRLSKMK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767961922 396 FDFCIVDEASQISQPICLGPLFF-SRRFVLVGDHQQLPPLVLNREARALGMSESLFKRLEQNKSAVVQLTVQYR 468
Cdd:cd18039 161 FRTVLIDEATQATEPECLIPLVHgAKQVILVGDHCQLGPVVMCKKAAKAGLSQSLFERLVQLGIRPIRLQVQYR 234
|
|
| AAA_11 |
pfam13086 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
269-438 |
8.11e-27 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.
Pssm-ID: 404072 [Multi-domain] Cd Length: 248 Bit Score: 109.74 E-value: 8.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 269 PQRQAMKKVLLSKDYTLIVGMPGTGKTTTICTLVRILYACGFS-------VLLTSYTHSAVDNILLKLA----KFKIGFL 337
Cdd:pfam13086 1 SQREAIRSALSSSHFTLIQGPPGTGKTTTIVELIRQLLSYPATsaaagprILVCAPSNAAVDNILERLLrkgqKYGPKIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 338 RLGQIQKVHPAIQQFTEQEICRSKS-------------------IKSLALLEELYNSQL--------------------- 377
Cdd:pfam13086 81 RIGHPAAISEAVLPVSLDYLVESKLnneedaqivkdiskeleklAKALRAFEKEIIVEKllksrnkdkskleqerrklrs 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 378 -------------------------IVATTCMGINHPIFSR-KIFDFCIVDEASQISQPICLGPLFF-SRRFVLVGDHQQ 430
Cdd:pfam13086 161 erkelrkelrrreqslereildeaqIVCSTLSGAGSRLLSSlANFDVVIIDEAAQALEPSTLIPLLRgPKKVVLVGDPKQ 240
|
....*...
gi 767961922 431 LPPLVLNR 438
Cdd:pfam13086 241 LPPTVISK 248
|
|
| DEXXQc_Helz-like |
cd18038 |
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ... |
266-468 |
1.73e-24 |
|
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and similar proteins. Helicase with zinc finger (HELZ) acts as a helicase that plays a role in RNA metabolism during development. Moloney leukemia virus 10-like protein 1 (Mov10L1) binds Piwi-interacting RNA (piRNA) precursors to initiate piRNA processing. All are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350796 [Multi-domain] Cd Length: 229 Bit Score: 102.31 E-value: 1.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 266 LNKPQRQAMKKVLLSKD----YtLIVGMPGTGKTTTI--CTL-VRILYaCGFSVLLTSYTHSAVDNILLKLAKFKIG--- 335
Cdd:cd18038 2 LNDEQKLAVRNIVTGTSrpppY-IIFGPPGTGKTVTLveAILqVLRQP-PEARILVCAPSNSAADLLAERLLNALVTkre 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 336 FLRLG----QIQKVHPAIQQFTeqeICRSKSIKSLALLEELYNSQlIVATTCMGINHPI---FSRKIFDFCIVDEASQIS 408
Cdd:cd18038 80 ILRLNapsrDRASVPPELLPYC---NSKAEGTFRLPSLEELKKYR-IVVCTLMTAGRLVqagVPNGHFTHIFIDEAGQAT 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767961922 409 QPICLGPLFFSR----RFVLVGDHQQLPPLVLNREARALGMSESLFKRL----------EQNKSAVVQLTVQYR 468
Cdd:cd18038 156 EPEALIPLSELAskntQIVLAGDPKQLGPVVRSPLARKYGLGKSLLERLmerplyykdgEYNPSYITKLLKNYR 229
|
|
| DEXXQc_Mov10L1 |
cd18078 |
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ... |
266-456 |
1.63e-18 |
|
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds Piwi-interacting RNA (piRNA) precursors to initiate piRNA processing. Mov10L1 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: 350836 [Multi-domain] Cd Length: 230 Bit Score: 85.11 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 266 LNKPQRQAMKKVLLSKDYTL---IVGMPGTGKTTTIC-TLVRILYACGFS-VLLTSYTHSAVDNILLKLAKFKIgfLRLG 340
Cdd:cd18078 2 LNELQKEAVKRILGGECRPLpyiLFGPPGTGKTVTIIeAILQVVYNLPRSrILVCAPSNSAADLVTSRLHESKV--LKPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 341 QIQKVhPAIQQFTEQEI------CRSKSIKSLALLEElynsqlIVATTC--MGINHPI-FSRKIFDFCIVDEASQISQPI 411
Cdd:cd18078 80 DMVRL-NAVNRFESTVIdarklyCRLGEDLSKASRHR------IVISTCstAGLLYQMgLPVGHFTHVFVDEAGQATEPE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767961922 412 CLGPL-FFSRR---FVLVGDHQQLPPLVLNREARALGMSESLFKRLEQN 456
Cdd:cd18078 153 SLIPLgLISSRdgqIILAGDPMQLGPVIKSRLASAYGLGVSFLERLMNR 201
|
|
| EEXXQc_AQR |
cd17935 |
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ... |
284-478 |
2.04e-17 |
|
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds precursor-mRNA introns at a defined position and is part of a pentameric intron-binding complex (IBC). It 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: 350693 [Multi-domain] Cd Length: 207 Bit Score: 81.32 E-value: 2.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 284 TLIVGMPGTGKTTTICTLVRILYACGFS--VLLTSYTHSAVDNILLKLAKFKIG---FLRLGQIQKvhpaiqqfteqeic 358
Cdd:cd17935 23 TMVVGPPGTGKTDVAVQIISNLYHNFPNqrTLIVTHSNQALNQLFEKIMALDIDerhLLRLGHGAK-------------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 359 rsksikslalleelynsqlIVATTCmgiNHPIFSRKIF---DFC----IVDEASQISQPICLGPLFFSR---------RF 422
Cdd:cd17935 89 -------------------IIAMTC---THAALKRGELvelGFKydniLMEEAAQILEIETFIPLLLQNpedgpnrlkRL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767961922 423 VLVGDHQQLPPLVLNREARALG-MSESLFKRLEQNKSAVVQLTVQYRMNSKIMSLSN 478
Cdd:cd17935 147 IMIGDHHQLPPVIKNMAFQKYSnMEQSLFTRLVRLGVPTVDLDAQGRARASISSLYN 203
|
|
| DEXXQc_SF1 |
cd18043 |
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ... |
267-439 |
1.80e-15 |
|
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are nucleic acid motor proteins that couple ATP hydrolysis to translocation along with the concomitant unwinding of DNA or RNA. This is central to many aspects of cellular DNA and RNA metabolism and accordingly, they are implicated in a wide range of nucleic acid processing events including DNA replication, recombination, and repair as well as many aspects of RNA metabolism. Superfamily 1 helicases are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350801 [Multi-domain] Cd Length: 127 Bit Score: 73.39 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 267 NKPQRQAMKKVLLSKDyTLIVGMPGTGKTTTICTLVRILYACGFSVLLTSYTHSAVDNILLklakfkigflrlgqiqkvh 346
Cdd:cd18043 1 DSSQEAAIISARNGKN-VVIQGPPGTGKSQTIANIIANALARGKRVLFVSEKKAALDVVRF------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 347 PAIqqfteqeicrsksIKSLALLEELYNsqlivattcmginhpiFSRKIFDFCIVDEASQISQPICLGPLFFSRRFVLVG 426
Cdd:cd18043 61 PCW-------------IMSPLSVSQYLP----------------LNRNLFDLVIFDEASQIPIEEALPALFRGKQVVVVG 111
|
170
....*....|...
gi 767961922 427 DHQQLPPLVLNRE 439
Cdd:cd18043 112 DDKQLPPSILLRE 124
|
|
| EEXXEc_NFX1 |
cd17936 |
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ... |
265-467 |
2.13e-15 |
|
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that represses class II MHC (major histocompatibility complex) gene expression. NFX1 binds a conserved cis-acting element, termed the X-box, in promoters of human class II MHC genes. The Cys-rich region contains several NFX1-type zinc finger domains. Frequently, a R3H domain is present in the C-terminus, and a RING finger domain and a PAM2 motif are present in the N-terminus. The lack of R3H and PAM2 motifs in the plant proteins indicates functional differences. Plant NFX1-like proteins are proposed to modulate growth and survival by coordinating reactive oxygen species, salicylic acid, further biotic stress and abscisic acid responses. A common feature of all members may be E3 ubiquitin ligase, due to the presence of a RING finger domain, as well as DNA binding. NFX1 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: 350694 [Multi-domain] Cd Length: 178 Bit Score: 74.50 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 265 GLNKPQRQAMKKVLlSKDYTLIVGMPGTGKTTTICTLVRILY-----ACGFSVLLTSYTHSAVDNILLKLAKFKIG-FLR 338
Cdd:cd17936 1 TLDPSQLEALKHAL-TSELALIQGPPGTGKTFLGVKLVRALLqnqdlSITGPILVVCYTNHALDQFLEGLLDFGPTkIVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 339 LGqiqkvhpaiqqfteqeicrsKSIkslalleelynsqLIVATTCMGINHPIFSRKIFDFCIVDEASQI--SQPI-CLGP 415
Cdd:cd17936 80 LG--------------------ARV-------------IGMTTTGAAKYRELLQALGPKVVIVEEAAEVleAHILaALTP 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767961922 416 LFfsRRFVLVGDHQQLPPLVLNRE--ARALGMSESLFKRLEQNKSAVVQLTVQY 467
Cdd:cd17936 127 ST--EHLILIGDHKQLRPKVNVYEltAKKYNLDVSLFERLVKNGLPFVTLNVQR 178
|
|
| DEXXc_HELZ2-C |
cd18040 |
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ... |
265-468 |
6.60e-15 |
|
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known as PPAR-alpha-interacting complex protein 285 or PRIC285 and PPAR-gamma DBD-interacting protein 1 or PDIP1) acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB and RXRA. It belongs to 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: 350798 [Multi-domain] Cd Length: 271 Bit Score: 75.64 E-value: 6.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 265 GLNKPQRQAMKKVLlSKDYTLIVGMPGTGKTTTICTLV--------RILYACGFS-----VLLTSYTHSAVD---NILLK 328
Cdd:cd18040 1 KLNPSQNHAVRTAL-TKPFTLIQGPPGTGKTVTGVHIAywfakqnrEIQSVSGEGdggpcVLYCGPSNKSVDvvaELLLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 329 LAKFKIgfLRL--GQIQK------------------------------VHPAIQQ----------------------FTE 354
Cdd:cd18040 80 VPGLKI--LRVysEQIETteypipneprhpnkksereskpnselssitLHHRIRQpsnphsqqikafearfertqekITE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 355 QEICRSKSIKSLALLEELYNSQLIVATtCMGINHPIFSRKI-FDFCIVDEASQISQPICLGPL---FFSRRFVLVGDHQQ 430
Cdd:cd18040 158 EDIKTYKILIWEARFEELETVDVILCT-CSEAASQKMRTHAnVKQCIVDECGMCTEPESLIPIvsaPRAEQVVLIGDHKQ 236
|
250 260 270
....*....|....*....|....*....|....*...
gi 767961922 431 LPPLVLNREARALGMSESLFKRLEQnksAVVQLTVQYR 468
Cdd:cd18040 237 LRPVVQNKEAQKLGLGRSLFERYAE---KACMLDTQYR 271
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
270-433 |
1.48e-12 |
|
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD 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: 350691 [Multi-domain] Cd Length: 155 Bit Score: 65.65 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 270 QRQAMKKVLLSKdYTLIVGMPGTGKTTTICTLVRILYACGFSVLLTSYTHSAvdnillklAKfkigflRLGQIQKVHpai 349
Cdd:cd17933 2 QKAAVRLVLRNR-VSVLTGGAGTGKTTTLKALLAALEAEGKRVVLAAPTGKA--------AK------RLSESTGIE--- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 350 qqfteqeicrSKSIKSlaLLEELYNSQLivattcMGINHP-IFSRKIFdfcIVDEASQISQPIclgplfFSR-------- 420
Cdd:cd17933 64 ----------ASTIHR--LLGINPGGGG------FYYNEEnPLDADLL---IVDEASMVDTRL------MAAllsaipag 116
|
170
....*....|....
gi 767961922 421 -RFVLVGDHQQLPP 433
Cdd:cd17933 117 aRLILVGDPDQLPS 130
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
266-480 |
1.28e-11 |
|
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];
Pssm-ID: 440273 [Multi-domain] Cd Length: 514 Bit Score: 67.69 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 266 LNKPQRQAMKKVLLSKDYTLIVGMPGTGKTTTICTLVRILYACGFSVLLTSYTHSAVDNIllklakfkigflrlgqiqkv 345
Cdd:COG0507 125 LSDEQREAVALALTTRRVSVLTGGAGTGKTTTLRALLAALEALGLRVALAAPTGKAAKRL-------------------- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 346 hpaiqqftEQEICR-SKSIKSlaLLEELYNSQLIVAttcmGINHPIFSRKIFdfcIVDEASQISQPIclgplfFSR---- 420
Cdd:COG0507 185 --------SESTGIeARTIHR--LLGLRPDSGRFRH----NRDNPLTPADLL---VVDEASMVDTRL------MAAllea 241
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767961922 421 ------RFVLVGDHQQLPPlVlnrEA-RALGMseslfkRLEQNKSAVVQLTVQYRM--NSKIMSLSNKL 480
Cdd:COG0507 242 lpragaRLILVGDPDQLPS-V---GAgAVLRD------LIESGTVPVVELTEVYRQadDSRIIELAHAI 300
|
|
| DEXXQc_HELZ |
cd18077 |
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ... |
266-453 |
1.63e-11 |
|
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that plays a role in RNA metabolism during development. HELZ is a member of the family I class of RNA helicases 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: 350835 [Multi-domain] Cd Length: 226 Bit Score: 64.43 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 266 LNKPQRQAMKKVLLSKDYT----LIVGMPGTGKTTTICTLVR-ILYACGFSVLLTSYTHSAVD-----------NILLKL 329
Cdd:cd18077 2 LNAKQKEAVLAITTPLSIQlppvLLIGPFGTGKTFTLAQAVKhILQQPETRILICTHSNSAADlyikeylhpyvETGNPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 330 AKFKIGFLRLGQIQKVHPAIQQFTeqeICRSKSIKSLALLEELYNSQLIVAT--TCMGINHPIFSRKIFDFCIVDEASQI 407
Cdd:cd18077 82 ARPLRVYYRNRWVKTVHPVVQKYC---LIDEHGTFRMPTREDVMRHRVVVVTlsTSQYLCQLDLEPGFFTHILLDEAAQA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767961922 408 SQPICLGPLFF---SRRFVLVGDHQQLPPLVLNREARALGMSESLFKRL 453
Cdd:cd18077 159 MECEAIMPLALatkSTRIVLAGDHMQLSPEVYSEFARERNLHISLLERL 207
|
|
| SF1_C |
cd18786 |
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ... |
576-655 |
7.38e-11 |
|
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Similar to SF2 helicases, they do not form toroidal, predominantly hexameric structures like SF3-6. SF1 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: 350173 [Multi-domain] Cd Length: 89 Bit Score: 58.99 E-value: 7.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 576 DIGIIAPYRQQLKIINDLLARS------IGMVEVNTVDKYQGRDKSIVLVSFVRSNKDgtvgellkDWRRLNVAITRAKH 649
Cdd:cd18786 12 KGVVLTPYHRDRAYLNQYLQGLsldefdLQLVGAITIDSSQGLTFDVVTLYLPTANSL--------TPRRLYVALTRARK 83
|
....*.
gi 767961922 650 KLILLG 655
Cdd:cd18786 84 RLVIYD 89
|
|
| AAA_30 |
pfam13604 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
265-433 |
6.11e-08 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. There is a Walker A and Walker B.
Pssm-ID: 433343 [Multi-domain] Cd Length: 191 Bit Score: 53.34 E-value: 6.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 265 GLNKPQRQAMKKVLLSKD-YTLIVGMPGTGKTTTICTLVRILYACGFSVLLTSYTHSAVDnillKLAKfkigflRLGqiq 343
Cdd:pfam13604 1 TLNAEQAAAVRALLTSGDrVAVLVGPAGTGKTTALKALREAWEAAGYRVIGLAPTGRAAK----VLGE------ELG--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 344 kvHPA--IQQFTeqeicrsksiKSLALLEELYNSQLIvattcmginhpifsrkifdfcIVDEASQISQPICLGplFFSR- 420
Cdd:pfam13604 68 --IPAdtIAKLL----------HRLGGRAGLDPGTLL---------------------IVDEAGMVGTRQMAR--LLKLa 112
|
170
....*....|....*...
gi 767961922 421 -----RFVLVGDHQQLPP 433
Cdd:pfam13604 113 edagaRVILVGDPRQLPS 130
|
|
| AAA_19 |
pfam13245 |
AAA domain; |
270-433 |
3.08e-07 |
|
AAA domain;
Pssm-ID: 433059 [Multi-domain] Cd Length: 136 Bit Score: 49.91 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 270 QRQAMKKVLLSKdYTLIVGMPGTGKTTTICTLVRILYACG---FSVLLTSYTHSAVDNillkLAKfkigflRLGQ-IQKV 345
Cdd:pfam13245 1 QREAVRTALPSK-VVLLTGGPGTGKTTTIRHIVALLVALGgvsFPILLAAPTGRAAKR----LSE------RTGLpASTI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 346 HpAIQQFteqeicrsKSIKSLALL--EELYNSQLIVattcmginhpifsrkifdfcIVDEASQISQPIC---LGPLFFSR 420
Cdd:pfam13245 70 H-RLLGF--------DDLEAGGFLrdEEEPLDGDLL--------------------IVDEFSMVDLPLAyrlLKALPDGA 120
|
170
....*....|...
gi 767961922 421 RFVLVGDHQQLPP 433
Cdd:pfam13245 121 QLLLVGDPDQLPS 133
|
|
| DExxQc_SF1-N |
cd17914 |
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ... |
284-467 |
1.02e-06 |
|
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Like SF2, they do not form toroidal, predominantly hexameric structures like SF3-6. 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. SF1 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: 438706 [Multi-domain] Cd Length: 121 Bit Score: 48.25 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 284 TLIVGMPGTGKTTTICTLVRILYACG----FSVLLTSYTHSAVDNillklakfkigflrlgqiqkvhpaiqqfteqeicr 359
Cdd:cd17914 2 SLIQGPPGTGKTRVLVKIVAALMQNKngepGRILLVTPTNKAAAQ----------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 360 sksikslalleelynsqlivattcmginhpifsrkiFDFCIVDEASQISQPICLGP-LFFSR--RFVLVGDHQQLPPLVL 436
Cdd:cd17914 47 ------------------------------------LDNILVDEAAQILEPETSRLiDLALDqgRVILVGDHDQLGPVWR 90
|
170 180 190
....*....|....*....|....*....|.
gi 767961922 437 NREARALGMSESLFKRLEQNKSAVVQLTVQY 467
Cdd:cd17914 91 GAVLAKICNEQSLFTRLVRLGVSLIRLQVQY 121
|
|
| betaCoV_Nsp13-helicase |
cd21722 |
helicase domain of betacoronavirus non-structural protein 13; This model represents the ... |
270-659 |
7.80e-05 |
|
helicase domain of betacoronavirus non-structural protein 13; This model represents the helicase domain of non-structural protein 13 (Nsp13) from betacoronavirus, including pathogenic human viruses such as Severe acute respiratory syndrome coronavirus (SARS-CoV), SARS-CoV2 (also called 2019 novel CoV or 2019-nCoV), and Middle East respiratory syndrome-related (MERS) CoV. Helicases catalyze NTP-dependent unwinding of nucleic acid duplexes into single strands and are classified based on the arrangement of conserved motifs into six superfamilies. CoV Nsp13 is a member of the helicase superfamily 1 (SF1); SF1 and SF2 helicases do not form toroidal structures, while SF3-6 helicases do. Nsp13 is a component of the viral RNA synthesis replication and transcription complex (RTC). It is a multidomain protein containing a Cys/His rich zinc-binding domain (CH/ZBD), a stalk domain, a 1B domain involved in nucleic acid substrate binding, and a SF1 helicase core.
Pssm-ID: 409655 [Multi-domain] Cd Length: 340 Bit Score: 45.56 E-value: 7.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 270 QRQAMKKvllskdYTLIVGMPGTGKTTTICTLVriLYACGFSVLLTSYTHSAVDNILLKLAKfkigFLRLGQIQKVHPA- 348
Cdd:cd21722 20 QKIGMKR------YCTVQGPPGTGKSHLAIGLA--VYYPTARVVYTACSHAAVDALCEKAFK----FLNINKCSRIIPAk 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 349 -----IQQFTEQEICRSKSIKSLALLEELYNSQLIVATTCMGINhpifsrkiFDFCIVDeaSQISqpiclgplffSRRFV 423
Cdd:cd21722 88 arvecYDKFKVNDTSRQYVFSTINALPETVTDILVVDEVSMCTN--------YDLSVIN--ARVR----------AKHIV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 424 LVGDHQQLP-PLVLNREARALGMSESLFKRLEQNKSAVVQLTVQYRMNSKIMSLSNKLTYEGKLECGSDKVANavinlrh 502
Cdd:cd21722 148 YIGDPAQLPaPRTLLTKGTLEPEYFNSVTRLMCCLGPDIFLGTCYRCPKEIVDTVSALVYDNKLKAKKDNSGQ------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 503 fkdvklelefyadysdnpwlmgvfepnnpvCFlntdKVPAPEQVEKGGVSNVTEAKLivFLTSIFVKAGCSPSDIGIIAP 582
Cdd:cd21722 221 ------------------------------CF----KVYYKGSVTHDSSSAINRPQI--YLVKKFLKANPAWSKAVFISP 264
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767961922 583 YRQQlkiinDLLARSIGMVEVNTVDKYQGRDKSIVLVSFVRSNKDGTvgellkDWRRLNVAITRAKhKLILlgCVPS 659
Cdd:cd21722 265 YNSQ-----NAVARRVLGLQTQTVDSSQGSEYDYVIYCQTAETAHSV------NVNRFNVAITRAK-KGIL--CVMS 327
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
266-404 |
7.31e-04 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 41.32 E-value: 7.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 266 LNKPQRQAMKKVLLSKDYTLIVGMPGTGKTTTICT--LVRILYACGFSVLLTSYTHSAVDNILLKLAKFkigflrlgqiq 343
Cdd:smart00487 9 LRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLpaLEALKRGKGGRVLVLVPTRELAEQWAEELKKL----------- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767961922 344 kvhpaIQQFTEQEICRSKSIKSLALLEELYNS--QLIVATTCMGINHPI---FSRKIFDFCIVDEA 404
Cdd:smart00487 78 -----GPSLGLKVVGLYGGDSKREQLRKLESGktDILVTTPGRLLDLLEndkLSLSNVDLVILDEA 138
|
|
| DEXXQc_HELZ2-N |
cd18076 |
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ... |
285-453 |
7.90e-04 |
|
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known as PPAR-alpha-interacting complex protein 285 or PRIC285 and PPAR-gamma DBD-interacting protein 1 or PDIP1) acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB, and RXRA. It belongs to 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: 350834 [Multi-domain] Cd Length: 230 Bit Score: 41.80 E-value: 7.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 285 LIVGMPGTGKTTTICTLVR-ILYACGFSVLLTSYTHSA------------VDNILLKLAKFKIGFLRLGqIQKVHPAIQQ 351
Cdd:cd18076 27 LIYGPFGTGKTFTLAMAALeVIREPGTKVLICTHTNSAadiyireyfhpyVDKGHPEARPLRIKATDRP-NAITDPDTIT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 352 FTeqeiCRSKSIKSLAL--LEELYNSQLIVATTCMGINHPIFSrKIFDFCIVDEASQISQPICLGPLF---FSRRFVLVG 426
Cdd:cd18076 106 YC----CLTKDRQCFRLptRDELDFHNIVITTTAMAFNLHVLS-GFFTHIFIDEAAQMLECEALIPLSyagPKTRVVLAG 180
|
170 180
....*....|....*....|....*..
gi 767961922 427 DHQQLPPLVLNrEARALGMSESLFKRL 453
Cdd:cd18076 181 DHMQMTPKLFS-VADYNRANHTLLNRL 206
|
|
| SF1_C_UvrD |
cd18807 |
C-terminal helicase domain of UvrD family helicases; UvrD is a highly conserved helicase ... |
531-655 |
2.52e-03 |
|
C-terminal helicase domain of UvrD family helicases; UvrD is a highly conserved helicase involved in mismatch repair, nucleotide excision repair, and recombinational repair. It plays a critical role in maintaining genomic stability and facilitating DNA lesion repair in many prokaryotic species including Helicobacter pylori and Escherichia coli. This family also includes ATP-dependent helicase/nuclease AddA and helicase/nuclease RecBCD subunit RecB, among others. UvrD family helicases are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 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: 350194 [Multi-domain] Cd Length: 150 Bit Score: 39.14 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 531 PVCFLNTDKVPAPEQVEKGGVSnvtEAKLIVF-LTSIFVKAGCSPSDIGIIAPYRQQLKIINDLLarsigMVEVNTVDKY 609
Cdd:cd18807 23 PLKAGNKSGGPVELLLAKDEAD---EAKAIADeIKRLIESGPVQYSDIAILVRTNRQARVIEEAL-----RVTLMTIHAS 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 767961922 610 QGRDKSIVLVSFVR---------SNKDGTVGELLKDWRRL-NVAITRAKHKLILLG 655
Cdd:cd18807 95 KGLEFPVVFIVGLGegfipsdasYHAAKEDEERLEEERRLlYVALTRAKKELYLVG 150
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
284-316 |
3.29e-03 |
|
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases.
Pssm-ID: 410871 [Multi-domain] Cd Length: 144 Bit Score: 38.35 E-value: 3.29e-03
10 20 30
....*....|....*....|....*....|...
gi 767961922 284 TLIVGMPGTGKTTTICTLVRILYACGFSVLLTS 316
Cdd:cd01127 2 TLVLGTTGSGKTTSIVIPLLDQAARGGSVIITD 34
|
|
| ftsY |
TIGR00064 |
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ... |
223-314 |
4.88e-03 |
|
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and SRP54; both are GTPases. In E.coli, ftsY is an essential gene located in an operon with cell division genes ftsE and ftsX, but its apparent function is as the signal recognition particle docking protein. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 272883 [Multi-domain] Cd Length: 277 Bit Score: 39.55 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961922 223 ENTFVSKKLRDLIIDfrepqfiSYLSSVLPHDAKDTVACILKGLNKPQrqamkkVLLskdytlIVGMPGTGKTTTICTLV 302
Cdd:TIGR00064 38 KKVKDAEKLKEILKE-------YLKEILKEDLLKNTDLELIVEENKPN------VIL------FVGVNGVGKTTTIAKLA 98
|
90
....*....|..
gi 767961922 303 RILYACGFSVLL 314
Cdd:TIGR00064 99 NKLKKQGKSVLL 110
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
285-349 |
7.96e-03 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 37.51 E-value: 7.96e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767961922 285 LIVGMPGTGKTTTICTLVRILYACGFSVLLTSYTHSAVDNILLKLAKFKIGFLRLGQIQKVHPAI 349
Cdd:cd00009 23 LLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELAEKAKPGV 87
|
|
| |
