|
Name |
Accession |
Description |
Interval |
E-value |
| DNA_pol_A_theta |
cd08638 |
DNA polymerase theta is a low-fidelity family A enzyme implicated in translesion synthesis and ... |
2093-2588 |
9.33e-174 |
|
DNA polymerase theta is a low-fidelity family A enzyme implicated in translesion synthesis and in somatic hypermutation; DNA polymerase theta is a low-fidelity family A enzyme implicated in translesion synthesis (TLS) and in somatic hypermutation (SHM). DNA-dependent DNA polymerases can be classified in six main groups based upon phylogenetic relationships with E. coli polymerase I (classA), E. coli polymerase II (class B), E.coli polymerase III (class C), euryarchaaeota polymerase II (class D), human polymerase beta (class x), E. coli UmuC/DinB and eukaryotic RAP 30/Xeroderma pigmentosum variant (class Y). Family A polymerase functions primarily to fill DNA gaps that arise during DNA repair, recombination and replication. Pol theta is an exception among family A polymerases and generates processive single base substitutions. Family A polymerase are found primarily in organisms related to prokaryotes and include prokaryotic DNA polymerase I (pol I) ,mitochondrial polymerase delta, and several bacteriphage polymerases including those from odd-numbered phage (T3, T5, and T7). Prokaryotic Pol Is have two functional domains located on the same polypeptide; a 5'-3' polymerase and 5'-3' exonuclease. Pol I uses its 5' nuclease activity to remove the ribonucleotide portion of newly synthesized Okazaki fragments and DNA polymerase activity to fill in the resulting gap. Polymerase theta mostly has amino-terminal helicase domain, a carboxy-terminal polymerase domain and an intervening space region.
Pssm-ID: 176475 Cd Length: 373 Bit Score: 538.35 E-value: 9.33e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2093 GIGFSTAECEGQKHIMQAKLDAIETQAYQlaghsfsftssddiaevlflelklppngemknqgskktlgstrrgndngrk 2172
Cdd:cd08638 1 GIGFDPEELERQRALLQAKLKELEEEAYR--------------------------------------------------- 29
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2173 lrlgrqfSTSKDVLNKLKALHPLPGLILEWRRITNAITKVIFPLQREKRLNPFLGMERIYPV-SQSHTATGRITFTEPNI 2251
Cdd:cd08638 30 -------STSKEVLEQLKRLHPLPKLILEYRKLSKLLTTYVEPLLLLCKLSSSLQMYRIHPTwNQTGTATGRLSSSEPNL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2252 QNVPRDFEIKMPTLvgesppsqaigkgllpmgrgkskkgcslnpgrqaqmeERAADRGMPFSISMRHAFVPFPGGLILAA 2331
Cdd:cd08638 103 QNVPKDFEIKDAPS-------------------------------------PPAGSEGDIPTISLRHAFIPPPGRVLLSA 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2332 DYSQLELRILAHLSHDRRLIQVLNTGADVFRSIAAEWKMIEPESVGDDLRQQAKQICYGIIYGMGAKSLGEQMGIKENDA 2411
Cdd:cd08638 146 DYSQLELRILAHLSGDPALIELLNSGGDVFKMIAAQWLGKPVEEVTDEERQQAKQLVYGILYGMGAKSLAEQLGVSEEEA 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2412 ACYIDSFKSRYTGINQFMRETVKNCKRDGFVQTILGRRRYLPGIKDNNPYHKAHAERQAINTTVQGSAADIVKIATVNIQ 2491
Cdd:cd08638 226 KQFIESFKNAYPGVRRFIRETIERARRNGFVETLTGRRRYLPEINSGNSSERAQAERQAVNTVIQGSAADIMKIAMINIH 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2492 KQLETFHSTfkshghregmlqsdrtagllrkrklqgmfCPVRGGFFILQLHDELLYEVAEEDVVQVAQIVKNEMESAVKL 2571
Cdd:cd08638 306 EKLHSLLPN-----------------------------LPAGRARLVLQIHDELLFEVPESDVDEVARIIKRSMENAAKL 356
|
490
....*....|....*..
gi 1622909152 2572 SVKLKVKVKIGASWGEL 2588
Cdd:cd08638 357 SVPLPVKVSIGKSWGSL 373
|
|
| DNA_pol_A |
pfam00476 |
DNA polymerase family A; |
2110-2587 |
6.77e-134 |
|
DNA polymerase family A;
Pssm-ID: 459825 Cd Length: 368 Bit Score: 424.54 E-value: 6.77e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2110 AKLDAIETQAYQLAGHSFSFTSSDDIAEVLFLELKLPPNgemknqgsKKTlgstrrgndngrklrlGRQFSTSKDVLNKL 2189
Cdd:pfam00476 1 ERLKELEQEIYELAGEEFNINSPKQLGEILFEKLGLPPG--------KKT----------------KTGYSTDAEVLEKL 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2190 KA-LHPLPGLILEWRRITNAITKVIFPLQreKRLNPFLGmeRIYP-VSQSHTATGRITFTEPNIQNVP-RDFEikmptlv 2266
Cdd:pfam00476 57 AAdEHPIPKLILEYRQLAKLKSTYVDALP--KLINPDTG--RIHTsFNQTVTATGRLSSSDPNLQNIPiRTEE------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2267 gesppsqaigkgllpmgrgkskkgcslnpGRQaqmeeraadrgmpfsisMRHAFVPFPGGLILAADYSQLELRILAHLSH 2346
Cdd:pfam00476 126 -----------------------------GRR-----------------IRKAFVAEPGWVLLSADYSQIELRILAHLSG 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2347 DRRLIQVLNTGADVFRSIAAEWKMIEPESVGDDLRQQAKQICYGIIYGMGAKSLGEQMGIKENDAACYIDSFKSRYTGIN 2426
Cdd:pfam00476 160 DENLIEAFRNGEDIHTATASEVFGVPLEEVTPEQRRRAKAINFGIIYGMSAFGLAQQLGISRKEAKEYIDRYFERYPGVK 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2427 QFMRETVKNCKRDGFVQTILGRRRYLPGIKDNNPYHKAHAERQAINTTVQGSAADIVKIATVNIQKQLEtfhstfkshgh 2506
Cdd:pfam00476 240 EYMEETVEEAREKGYVETLLGRRRYLPDINSSNRNLRSFAERAAINAPIQGSAADIIKLAMIRVDEALK----------- 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2507 REGMlqsdrtagllrKRKLqgmfcpvrggffILQLHDELLYEVAEEDVVQVAQIVKNEMES--AVKLSVKLKVKVKIGAS 2584
Cdd:pfam00476 309 EEGL-----------KARL------------LLQVHDELVFEVPEEEVEEVAALVKEEMENenAVKLSVPLKVDVGIGKN 365
|
...
gi 1622909152 2585 WGE 2587
Cdd:pfam00476 366 WGE 368
|
|
| PolA |
COG0749 |
DNA polymerase I, 3'-5' exonuclease and polymerase domains [Replication, recombination and ... |
1902-2589 |
2.62e-125 |
|
DNA polymerase I, 3'-5' exonuclease and polymerase domains [Replication, recombination and repair];
Pssm-ID: 440512 [Multi-domain] Cd Length: 575 Bit Score: 408.29 E-value: 2.62e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 1902 VVGLAVCWGGRDAYYFSLqkeqkhseisASLVPPSLDPSLTLKdriwHLQSCLrkeSDKECSVVIYDFIQSYKILLlSCG 1981
Cdd:COG0749 20 LVGISFAVEPGEAAYIPL----------AHGAPEQLDLDEVLA----ALKPLL---EDPAIPKIGQNLKYDLHVLA-RYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 1982 ISLEQSYEDPKVACWLLDPDSQEPTLHSIVTSFLPHELPLLE---GMETSQ-GIQSLGLNAGSEHSGRyRASVesilIFN 2057
Cdd:COG0749 82 IELAGVAFDTMLASYLLNPGRRRHGLDDLAERYLGHETISYEelaGKGKKQlTFDQVPLEEAAEYAAE-DADI----TLR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2058 SMNQLNSLLQKENLQDVFRKVEMPSQYCLALLELNGIGFSTAECEGQKHIMQAKLDAIETQAYQLAGHSFSFTSSDDIAE 2137
Cdd:COG0749 157 LHEVLKPELEEEGLLKLYEEIELPLVPVLARMERNGILVDRELLAELSAELAKRLAELEQEIYELAGEEFNLNSPKQLGE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2138 VLFLELKLPpngemknqGSKKTlgstrrgndngrKlrlgRQFSTSKDVLNKLKALHPLPGLILEWRRI-------TNAIT 2210
Cdd:COG0749 237 ILFEKLGLP--------VGKKT------------K----TGYSTDAEVLEKLAEDHPIPALILEYRQLsklkstyVDALP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2211 KVIfplqrekrlNPFLGmeRIYPV-SQSHTATGRITFTEPNIQNVPrdfeIKMPTlvgesppsqaigkgllpmgrgkskk 2289
Cdd:COG0749 293 KLI---------NPDTG--RIHTSfNQTVTATGRLSSSDPNLQNIP----IRTEE------------------------- 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2290 gcslnpGRQaqmeeraadrgmpfsisMRHAFVPFPGGLILAADYSQLELRILAHLSHDRRLIQVLNTGADVFRSIAAEwk 2369
Cdd:COG0749 333 ------GRR-----------------IRKAFVAPEGYVLLSADYSQIELRILAHLSGDEGLIEAFREGEDIHAATAAE-- 387
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2370 M--IEPESVGDDLRQQAKQICYGIIYGMGAKSLGEQMGIKENDAACYIDSFKSRYTGINQFMRETVKNCKRDGFVQTILG 2447
Cdd:COG0749 388 VfgVPLEEVTSEQRRRAKAINFGIIYGMSAFGLARQLGISRKEAKEYIDRYFERYPGVKDYMEETVEEAREKGYVETLFG 467
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2448 RRRYLPGIKDNNPYHKAHAERQAINTTVQGSAADIVKIATVNIQKQLetfhstfkshghregmlqsdrtagllRKRKLQG 2527
Cdd:COG0749 468 RRRYLPDINSSNRNRRSFAERAAINAPIQGSAADIIKLAMIRVDRAL--------------------------KEEGLKS 521
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622909152 2528 -MfcpvrggffILQLHDELLYEVAEEDVVQVAQIVKNEMESAVKLSVKLKVKVKIGASWGELK 2589
Cdd:COG0749 522 rM---------LLQVHDELVFEVPEDELEEVKELVKEVMENAVELSVPLVVDVGVGKNWDEAH 575
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
82-667 |
3.91e-122 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 397.34 E-value: 3.91e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 82 LPKAVLEKYHSFGVKKMFEWQAECLLLGqVLEGKNLVYSAPTSAGKTLVAELLILKRVLEmRKKALFILPFVSVAKEKKY 161
Cdd:COG1204 7 PLEKVIEFLKERGIEELYPPQAEALEAG-LLEGKNLVVSAPTASGKTLIAELAILKALLN-GGKALYIVPLRALASEKYR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 162 YLQSLFQEVGIKVDGYMGS-TSPSRHFSSLDIAVCTIERANGLINRliEENKMDLLGMVVVDELHMLGDSHRGYLLELLL 240
Cdd:COG1204 85 EFKRDFEELGIKVGVSTGDyDSDDEWLGRYDILVATPEKLDSLLRN--GPSWLRDVDLVVVDEAHLIDDESRGPTLEVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 241 TKIcyitrksascqadlaSSLSNAVQIVGMSATLPNLELVASWLNAEHYHTDFRPVPLLESVKVGNSIYdssmklvreFE 320
Cdd:COG1204 163 ARL---------------RRLNPEAQIVALSATIGNAEEIAEWLDAELVKSDWRPVPLNEGVLYDGVLR---------FD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 321 PMLQVKGDEdhVVSLCYETIRDNHSVLLFCPSKAWCEKLADIIAREFynlhhqTEGLVKPsecppvnlEQKELLEVMDQL 400
Cdd:COG1204 219 DGSRRSKDP--TLALALDLLEEGGQVLVFVSSRRDAESLAKKLADEL------KRRLTPE--------EREELEELAEEL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 401 RRL--PSGLDSVLQKTVPWGVAFHHAGLTLEERDIIEGAFRQGLIRVLAATSTLSSGVNLPARRVIIRTP-IFGGRPLDI 477
Cdd:COG1204 283 LEVseETHTNEKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDTkRGGMVPIPV 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 478 LTYKQMAGRAGRKGVDTVGESILICKNSEKSKGIA--LLQGSLKPVRSCLqrreGEEVtaSMIRAILEIIVGGVASTSQD 555
Cdd:COG1204 363 LEFKQMAGRAGRPGYDPYGEAILVAKSSDEADELFerYILGEPEPIRSKL----ANES--ALRTHLLALIASGFANSREE 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 556 MHTYAACTFLAasmkegkqgIQRNQESVQlGAIEACVMWLLENEFIQsteasdgTEGKVYHPTHLGSATLSSSLSPaDTL 635
Cdd:COG1204 437 LLDFLENTFYA---------YQYDKGDLE-EVVDDALEFLLENGFIE-------EDGDRLRATKLGKLVSRLYIDP-LTA 498
|
570 580 590
....*....|....*....|....*....|..
gi 1622909152 636 DIFADLQRAMKGFVleNDLHILYLVTpMFEDW 667
Cdd:COG1204 499 AELVDGLRKADEEF--TDLGLLHLIL-ILRDW 527
|
|
| PRK05755 |
PRK05755 |
DNA polymerase I; Provisional |
1902-2589 |
1.66e-117 |
|
DNA polymerase I; Provisional
Pssm-ID: 235591 [Multi-domain] Cd Length: 880 Bit Score: 396.39 E-value: 1.66e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 1902 VVGLAVCWGGRDAYYFSLqkEQKHSEISASLVPPSLDPSlTLKdriwhlqsclrkesdkecsvVIYDFIQSYKILLlSCG 1981
Cdd:PRK05755 334 LVGLSFAVEPGEAAYIPL--DQLDREVLAALKPLLEDPA-IKK--------------------VGQNLKYDLHVLA-RYG 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 1982 ISLEQSYEDPKVACWLLDPDSQEpTLHSIVTSFLPHELPLLEGMETSQ-GIQSLGLNAGSEHSGRyRASVesilIFNSMN 2060
Cdd:PRK05755 390 IELRGIAFDTMLASYLLDPGRRH-GLDSLAERYLGHKTISFEEVAGKQlTFAQVDLEEAAEYAAE-DADV----TLRLHE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2061 QLNS-LLQKENLQDVFRKVEMPSQYCLALLELNGIGFSTAECEGQKHIMQAKLDAIETQAYQLAGHSFSFTSSDDIAEVL 2139
Cdd:PRK05755 464 VLKPkLLEEPGLLELYEEIELPLVPVLARMERNGIKVDREYLKELSAELAQRLAELEQEIYELAGEEFNINSPKQLGEIL 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2140 FLELKLPPngemknqgSKKTlgstRRGndngrklrlgrqFSTSKDVLNKLKALHPLPGLILEWRRI-------TNAITKV 2212
Cdd:PRK05755 544 FEKLGLPV--------GKKT----KTG------------YSTDAEVLEKLADDHPIPDKILEYRQLsklkstyTDALPKL 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2213 IfplqrekrlNPFLGmeRIYP-VSQSHTATGRITFTEPNIQNVPrdfeIKmptlvgesppsqaigkglLPMGRgkskkgc 2291
Cdd:PRK05755 600 I---------NPDTG--RIHTsFNQTVTATGRLSSSDPNLQNIP----IR------------------TEEGR------- 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2292 slnpgrqaqmeeraadrgmpfsiSMRHAFVPFPGGLILAADYSQLELRILAHLSHDRRLIQVLNTGADVFRSIAAEWKMI 2371
Cdd:PRK05755 640 -----------------------RIRKAFVAPEGYKLLSADYSQIELRILAHLSGDEGLIEAFAEGEDIHTATASEVFGV 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2372 EPESVGDDLRQQAKQICYGIIYGMGAKSLGEQMGIKENDAACYIDSFKSRYTGINQFMRETVKNCKRDGFVQTILGRRRY 2451
Cdd:PRK05755 697 PLEEVTSEQRRRAKAINFGIIYGMSAFGLAQQLGISRKEAKEYIDRYFERYPGVKEYMERTVEQAREKGYVETLFGRRRY 776
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2452 LPGIKDNNPYHKAHAERQAINTTVQGSAADIVKIATVNIQKQLEtfhstfkshghrEGMLQSdrtagllrkrKLqgmfcp 2531
Cdd:PRK05755 777 LPDINSRNGNRRAFAERAAINAPIQGSAADIIKLAMIRVDKALK------------EEGLKS----------RM------ 828
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622909152 2532 vrggffILQLHDELLYEVAEEDVVQVAQIVKNEMESAVKLSVKLKVKVKIGASWGELK 2589
Cdd:PRK05755 829 ------LLQVHDELVFEVPEDELEEVKKLVKEVMENAVELSVPLVVDVGVGDNWDEAH 880
|
|
| DNA_pol_A_pol_I_C |
cd08637 |
Polymerase I functions primarily to fill DNA gaps that arise during DNA repair, recombination ... |
2108-2586 |
1.67e-112 |
|
Polymerase I functions primarily to fill DNA gaps that arise during DNA repair, recombination and replication; Family A polymerase (polymerase I) functions primarily to fill DNA gaps that arise during DNA repair, recombination and replication. DNA-dependent DNA polymerases can be classified in six main groups based upon phylogenetic relationships with E. coli polymerase I (classA), E. coli polymerase II (class B), E.coli polymerase III (class C), euryarchaaeota polymerase II (class D), human polymerase beta (class x), E. coli UmuC/DinB and eukaryotic RAP 30/Xeroderma pigmentosum variant (class Y). Family A polymerase are found primarily in organisms related to prokaryotes and include prokaryotic DNA polymerase I (pol I) ,mitochondrial polymerase delta, and several bacteriphage polymerases including those from odd-numbered phage (T3, T5, and T7). Prokaryotic Pol Is have two functional domains located on the same polypeptide; a 5'-3' polymerase and 5'-3' exonuclease. Pol I uses its 5' nuclease activity to remove the ribonucleotide portion of newly synthesized Okazaki fragments and DNA polymerase activity to fill in the resulting gap. A combination of phylogenomic and signature sequence-based (or phonetic) approaches is used to understand the evolutionary relationships among bacteria. DNA polymerase I is one of the conserved proteins that is used to search for protein signatures. The structure of these polymerases resembles in overall morphology a cupped human right hand, with fingers (which bind an incoming nucleotide and interact with the single-stranded template), palm (which harbors the catalytic amino acid residues and also binds an incoming dNTP) and thumb (which binds double-stranded DNA) subdomains.
Pssm-ID: 176474 Cd Length: 377 Bit Score: 363.28 E-value: 1.67e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2108 MQAKLDAIETQAYQLAGHSFSFTSSDDIAEVLFLELKLPPngemknqgSKKTlgstRRGndngrklrlgrqFSTSKDVLN 2187
Cdd:cd08637 12 LEKELAELEEEIYELAGEEFNINSPKQLGEVLFEKLGLPV--------GKKT----KTG------------YSTDAEVLE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2188 KLKALHPLPGLILEWRRITNAITKVIFPLQreKRLNPFLGmeRIYPV-SQSHTATGRITFTEPNIQNVPrdfeIKMPTlv 2266
Cdd:cd08637 68 KLADEHPIVELILEYRELTKLKSTYVDALP--KLINPKTG--RIHTSfNQTVTATGRLSSSDPNLQNIP----IRTEE-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2267 gesppsqaigkgllpmgrgkskkgcslnpGRQaqmeeraadrgmpfsisMRHAFVPFPGGLILAADYSQLELRILAHLSH 2346
Cdd:cd08637 138 -----------------------------GRE-----------------IRKAFVAEEGWVLLSADYSQIELRILAHLSG 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2347 DRRLIQVLNTGADVFRSIAAEWKMIEPESVGDDLRQQAKQICYGIIYGMGAKSLGEQMGIKENDAACYIDSFKSRYTGIN 2426
Cdd:cd08637 172 DEALIEAFKNGEDIHTRTAAEVFGVPPEEVTPEMRRIAKAVNFGIIYGISAFGLSQQLGISRKEAKEYIDRYFARYPGVK 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2427 QFMRETVKNCKRDGFVQTILGRRRYLPGIKDNNPYHKAHAERQAINTTVQGSAADIVKIATVNIQKQLEtfhstfkshgh 2506
Cdd:cd08637 252 EYMEETVEEAREKGYVETLFGRRRYIPEINSKNRNVRAFAERIAINTPIQGTAADIIKLAMIRVHKALK----------- 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2507 regmlqsdrtagllrKRKLQG-MfcpvrggffILQLHDELLYEVAEEDVVQVAQIVKNEMESAVKLSVKLKVKVKIGASW 2585
Cdd:cd08637 321 ---------------EEGLKArM---------LLQVHDELVFEVPEEELEEVAALVKEEMENAVELSVPLKVDVGVGKNW 376
|
.
gi 1622909152 2586 G 2586
Cdd:cd08637 377 G 377
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
82-295 |
6.98e-111 |
|
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in the repair of genomic double-strand breaks (DSBs). POLQ contains an N-terminal type II DEAD box helicase domain which contains the ATP-binding region.
Pssm-ID: 350784 [Multi-domain] Cd Length: 202 Bit Score: 351.13 E-value: 6.98e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 82 LPKAVLEKYHSFGVKKMFEWQAECLLLGQVLEGKNLVYSAPTSAGKTLVAELLILKRVLEMRKKALFILPFVSVAKEKKY 161
Cdd:cd18026 1 LPDAVREAYAKKGIKKLYDWQKECLSLPGLLEGRNLVYSLPTSGGKTLVAEILMLKRLLERRKKALFVLPYVSIVQEKVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 162 YLQSLFQEVGIKVDGYMGS--TSPSRHFSSLDIAVCTIERANGLINRLIEENKMDLLGMVVVDELHMLGDSHRGYLLELL 239
Cdd:cd18026 81 ALSPLFEELGFRVEGYAGNkgRSPPKRRKSLSVAVCTIEKANSLVNSLIEEGRLDELGLVVVDELHMLGDGHRGALLELL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622909152 240 LTKICYITRKSascqadlasslsnaVQIVGMSATLPNLELVASWLNAEHYHTDFRP 295
Cdd:cd18026 161 LTKLLYAAQKN--------------IQIVGMSATLPNLEELASWLRAELYTTNFRP 202
|
|
| pola |
TIGR00593 |
DNA polymerase I; All proteins in this family for which functions are known are DNA ... |
1981-2589 |
2.44e-101 |
|
DNA polymerase I; All proteins in this family for which functions are known are DNA polymerases Many also have an exonuclease motif. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273160 [Multi-domain] Cd Length: 887 Bit Score: 348.95 E-value: 2.44e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 1981 GISLEQSYEDPKVACWLLDPdSQEPTLHSIVTSFLPHELPLLEGMETSQGIQSlglNAGSEHSGRYrASVESILIFNSMN 2060
Cdd:TIGR00593 397 GIELGGVIFDTMLAAYLLDP-AQVSTLDTLARRYLVEELILDEKIGGKLAKFA---FPPLEEATEY-LARRAAATKRLAE 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2061 QLNSLLQKENLQDVFRKVEMPSQYCLALLELNGIGFSTAECEG-QKHIMQaKLDAIETQAYQLAGHSFSFTSSDDIAEVL 2139
Cdd:TIGR00593 472 ELLKELDENKLLSLYREIELPLSKVLAEMEKTGIKVDADYLQElSQEFGE-EIADLEEEIYELAGEEFNINSPKQLGEVL 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2140 FLELKLPPngemknqgskktlgstrrgndnGRKLRLGRqfSTSKDVLNKLKALHPLPGLILEWRRITNAITKVIFPLQre 2219
Cdd:TIGR00593 551 FEKLGLPV----------------------GKKTKTGY--STDADVLEKLREKHPIIALILEYRQLTKLKSTYVDGLP-- 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2220 KRLNPFLGmeRIYPV-SQSHTATGRITFTEPNIQNVPrdfeIKmptlvgesppsqaigkgllpmgrgkskkgcsLNPGRQ 2298
Cdd:TIGR00593 605 ELVNPDTG--RIHTTfNQTGTATGRLSSSNPNLQNIP----IR-------------------------------SEEGRK 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2299 aqmeeraadrgmpfsisMRHAFVPFPGGLILAADYSQLELRILAHLSHDRRLIQVLNTGADVFRSIAAEWKMIEPESVGD 2378
Cdd:TIGR00593 648 -----------------IRKAFVAEKGWLLISADYSQIELRVLAHLSQDENLIEAFQNGEDIHTETASRLFGVEIEDVTP 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2379 DLRQQAKQICYGIIYGMGAKSLGEQMGIKENDAACYIDSFKSRYTGINQFMRETVKNCKRDGFVQTILGRRRYLPGIKDN 2458
Cdd:TIGR00593 711 NMRRIAKTINFGVVYGMSAFGLAQELGISRKEAKEFIERYFARYPGVKDYIENTVEEARKKGYVETLFGRRRYIPDINSR 790
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2459 NPYHKAHAERQAINTTVQGSAADIVKIATVNIQKQletfhstFKSHGHREGMLqsdrtagllrkrklqgmfcpvrggffi 2538
Cdd:TIGR00593 791 NRNVREAAERMAINAPIQGSAADIMKIAMIKLDKR-------LKERKLKARLL--------------------------- 836
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1622909152 2539 LQLHDELLYEVAEEDVVQVAQIVKNEMESAVKLSVKLKVKVKIGASWGELK 2589
Cdd:TIGR00593 837 LQVHDELIFEAPEEEAEEVAALVKEVMEHAYPLAVPLEVEVGTGKNWGEAK 887
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
82-843 |
6.71e-99 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 337.31 E-value: 6.71e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 82 LPKAVLEKYHSFGVKKMFEWQAECLLLGqVLEGKNLVYSAPTSAGKTLVAELLILKRVLEmRKKALFILPFVSVAKEKKY 161
Cdd:PRK02362 8 LPEGVIEFYEAEGIEELYPPQAEAVEAG-LLDGKNLLAAIPTASGKTLIAELAMLKAIAR-GGKALYIVPLRALASEKFE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 162 YLQSlFQEVGIKV----------DGYMGSTspsrhfsslDIAVCTIERANGLInrlieENK---MDLLGMVVVDELHMLG 228
Cdd:PRK02362 86 EFER-FEELGVRVgistgdydsrDEWLGDN---------DIIVATSEKVDSLL-----RNGapwLDDITCVVVDEVHLID 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 229 DSHRGYLLELLLTKIcyitRKsascqadlassLSNAVQIVGMSATLPNLELVASWLNAEHYHTDFRPVPLLESVKVGNSI 308
Cdd:PRK02362 151 SANRGPTLEVTLAKL----RR-----------LNPDLQVVALSATIGNADELADWLDAELVDSEWRPIDLREGVFYGGAI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 309 -YDSSMKLVRefepmlQVKGDEDhvVSLCYETIRDNHSVLLFCPSKAWCE----KLADIIAREFynlhhqteglvkpsec 383
Cdd:PRK02362 216 hFDDSQREVE------VPSKDDT--LNLVLDTLEEGGQCLVFVSSRRNAEgfakRAASALKKTL---------------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 384 ppVNLEQKELLEVMDQLRRL-PSGLDSVLQKTVPWGVAFHHAGLTLEERDIIEGAFRQGLIRVLAATSTLSSGVNLPARR 462
Cdd:PRK02362 272 --TAAERAELAELAEEIREVsDTETSKDLADCVAKGAAFHHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARR 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 463 VIIR-----TPIFGGRPLDILTYKQMAGRAGRKGVDTVGESILICKNSEKSKgiALLQ----GSLKPVRSCLqrreGEEv 533
Cdd:PRK02362 350 VIIRdyrryDGGAGMQPIPVLEYHQMAGRAGRPGLDPYGEAVLLAKSYDELD--ELFEryiwADPEDVRSKL----ATE- 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 534 tASMIRAILEIIVGGVASTSQDMHTYAACTFLAAsmkegKQGIQRNQESVqlgaIEACVMWLLENEFIQSteasdgtEGK 613
Cdd:PRK02362 423 -PALRTHVLSTIASGFARTRDGLLEFLEATFYAT-----QTDDTGRLERV----VDDVLDFLERNGMIEE-------DGE 485
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 614 VYHPTHLGSatLSSSL-----SPADTLDifadlqrAMKGFVLENDLHILYLV--TP-MFE------DWTtidWYRFFC-- 677
Cdd:PRK02362 486 TLEATELGH--LVSRLyidplSAAEIID-------GLEAAKKPTDLGLLHLVcsTPdMYElylrsgDYE---WLNEYLye 553
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 678 ----LWEKLPTSMKRVAelvgvEEGFLaRCVKgkvvtrterqhrqmaihkrffTSLVLLDLISEVPLREINQKYGCNRGQ 753
Cdd:PRK02362 554 hedeLLGDVPSEFEDDE-----FEDFL-SAVK---------------------TALLLEDWIDEVDEERITERYGVGPGD 606
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 754 IQSLQQSAAVYAGMITVFSNRLGWHnMELLLSQFQKRLTFGIQRELCDLVRVSLLNAQRARVLYASGFHTVADLARANIV 833
Cdd:PRK02362 607 IRGKVETAEWLLHAAERLASELDLD-LARAARELEKRVEYGVREELLDLVGLRGVGRVRARRLYNAGIESRADLRAADKS 685
|
810
....*....|
gi 1622909152 834 EVEVILKSAV 843
Cdd:PRK02362 686 VVLAILGEKI 695
|
|
| POLAc |
smart00482 |
DNA polymerase A domain; |
2313-2553 |
8.58e-87 |
|
DNA polymerase A domain;
Pssm-ID: 214687 Cd Length: 207 Bit Score: 282.59 E-value: 8.58e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2313 SISMRHAFVPFPGGLILAADYSQLELRILAHLSHDRRLIQVLNTGADVFRSIAAEWKMIEPESVGDDLRQQAKQICYGII 2392
Cdd:smart00482 1 GREIRRAFIAPPGYVLVSADYSQIELRILAHLSGDENLIEAFNNGGDIHTKTAAQVFGVPEEEVTPELRRAAKAINFGII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2393 YGMGAKSLGEQMGIKENDAACYIDSFKSRYTGINQFMRETVKNCKRDGFVQTILGRRRYLPGIKDNNPYHKAHAERQAIN 2472
Cdd:smart00482 81 YGMGAKGLAEQLGISEAEAKELIKKYFARFPGVRRYIDRTLEEARRKGYVTTLFGRRRYIPDIDSRNPVLRAAAERAAVN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2473 TTVQGSAADIVKIATVNIQKQLETFHStfkshghregmlqsdrtagllrkrklqgmfcpvrGGFFILQLHDELLYEVAEE 2552
Cdd:smart00482 161 TPIQGSAADILKLAMIKMDEALKEFGL----------------------------------RARLLLQVHDELVFEVPEE 206
|
.
gi 1622909152 2553 D 2553
Cdd:smart00482 207 E 207
|
|
| DNA_pol_A |
cd06444 |
Family A polymerase primarily fills DNA gaps that arise during DNA repair, recombination and ... |
2188-2585 |
6.15e-81 |
|
Family A polymerase primarily fills DNA gaps that arise during DNA repair, recombination and replication; DNA polymerase family A, 5'-3' polymerase domain. Family A polymerase functions primarily to fill DNA gaps that arise during DNA repair, recombination and replication. DNA-dependent DNA polymerases can be classified into six main groups based upon phylogenetic relationships with E. coli polymerase I (classA), E. coli polymerase II (class B), E.coli polymerase III (class C), euryarchaeota polymerase II (class D), human polymerase beta (class X), E. coli UmuC/DinB and eukaryotic RAP 30/Xeroderma pigmentosum variant (class Y). Family A polymerases are found primarily in organisms related to prokaryotes and include prokaryotic DNA polymerase I, mitochondrial polymerase gamma, and several bacteriophage polymerases including those from odd-numbered phage (T3, T5, and T7). Prokaryotic polymerase I (pol I) has two functional domains located on the same polypeptide; a 5'-3' polymerase and a 5'-3' exonuclease. Pol I uses its 5' nuclease activity to remove the ribonucleotide portion of newly synthesized Okazaki fragments and the DNA polymerase activity to fill in the resulting gap. The structure of these polymerases resembles in overall morphology a cupped human right hand, with fingers (which bind an incoming nucleotide and interact with the single-stranded template), palm (which harbors the catalytic amino acid residues and also binds an incoming dNTP) and thumb (which binds double-stranded DNA) subdomains.
Pssm-ID: 176473 [Multi-domain] Cd Length: 347 Bit Score: 271.60 E-value: 6.15e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2188 KLKAL-HPLPGLILEWRRITNAITKVIFPLQREKRLnpflgMERIYPVSQSH-TATGRITFTEPNIQNVPRDFeikmptl 2265
Cdd:cd06444 20 ELELLaHPAVPLLLEYKKLAKLWSANGWPWLDQWVR-----DGRFHPEYVPGgTVTGRWASRGGNAQQIPRRD------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2266 vgesppsqaigkgllpmgrgkskkgcslnpgrqaqmeeraadrgmPFSISMRHAFVPFPGGLILAADYSQLELRILAHLS 2345
Cdd:cd06444 88 ---------------------------------------------PLGRDIRQAFVADPGWTLVVADASQLELRVLAALS 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2346 HDRRLIQVLNTGADVFRSIAAEWKMIepeSVGDDLRQQAKQICYGIIYG----MGAKSLGEQMGIKENDAACYIDSFKSR 2421
Cdd:cd06444 123 GDEALAEAFGRGGDLYTATASAMFGV---PVGGGERQHAKIANLGAMYGatsgISARLLAQLRRISTKEAAALIELFFSR 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2422 YTGINQFMRETVKNCKRD---GFVQTILGRRRYLPGIKDN-----------NPYHKAHAERQAINTTVQGSAADIVKIAT 2487
Cdd:cd06444 200 FPAFPKAMEYVEDAARRGergGYVRTLLGRRSPPPDIRWTevvsdpaaasrARRVRRAAGRFARNFVVQGTAADWAKLAM 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2488 VNIQKQLETFHStfkshghregmlqsdrtagllrkrklqgmfcpvrGGFFILQLHDELLYEVAEEDVVQVAQIVKNEMES 2567
Cdd:cd06444 280 VALRRRLEELAL----------------------------------DARLVFFVHDEVVLHCPKEEAEAVAAIVREAAEQ 325
|
410 420
....*....|....*....|.
gi 1622909152 2568 AVKL---SVKLKVKVKIGASW 2585
Cdd:cd06444 326 AVRLlfgSVPVRFPVKIGVVW 346
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
84-835 |
1.32e-77 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 274.39 E-value: 1.32e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 84 KAVLEKYhsfGVKKMFEWQAECLLLGqVLEGKNLVYSAPTSAGKTLVAELLILKRVLEMRKKALFILPFVSVAKEKKYYL 163
Cdd:PRK00254 13 KRVLKER---GIEELYPPQAEALKSG-VLEGKNLVLAIPTASGKTLVAEIVMVNKLLREGGKAVYLVPLKALAEEKYREF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 164 QSlFQEVGIKVDGYMGS-TSPSRHFSSLDIAVCTIERANGLI---NRLIEENKMdllgmVVVDELHMLGDSHRGYLLELL 239
Cdd:PRK00254 89 KD-WEKLGLRVAMTTGDyDSTDEWLGKYDIIIATAEKFDSLLrhgSSWIKDVKL-----VVADEIHLIGSYDRGATLEMI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 240 LTKicyitrksascqadlassLSNAVQIVGMSATLPNLELVASWLNAEHYHTDFRPVPLLESV-KVGNSIYD--SSMKLV 316
Cdd:PRK00254 163 LTH------------------MLGRAQILGLSATVGNAEELAEWLNAELVVSDWRPVKLRKGVfYQGFLFWEdgKIERFP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 317 REFEpmlqvkgdedhvvSLCYETIRDNHSVLLFCPSKAWCEKLADIIAREFYNLhhqtegLVKPsecppvnlEQKELLEV 396
Cdd:PRK00254 225 NSWE-------------SLVYDAVKKGKGALVFVNTRRSAEKEALELAKKIKRF------LTKP--------ELRALKEL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 397 MDQLRRLPSglDSVLQKTVPWGVAFHHAGLTLEERDIIEGAFRQGLIRVLAATSTLSSGVNLPARRVIIRTPI----FGG 472
Cdd:PRK00254 278 ADSLEENPT--NEKLKKALRGGVAFHHAGLGRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRDTKrysnFGW 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 473 RPLDILTYKQMAGRAGRKGVDTVGESILICKNSEKSKGIA-LLQGSLKPVRSCLQRRegeevtaSMIRA-ILEIIVGGVA 550
Cdd:PRK00254 356 EDIPVLEIQQMMGRAGRPKYDEVGEAIIVATTEEPSKLMErYIFGKPEKLFSMLSNE-------SAFRSqVLALITNFGV 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 551 STSQDMHTYAACTFLAAsmkegkqgiQRNQESVQLGAIEACVMWLLENEFIQSTEASDgtegkvYHPTHLGSATLSSSLS 630
Cdd:PRK00254 429 SNFKELVNFLERTFYAH---------QRKDLYSLEEKAKEIVYFLLENEFIDIDLEDR------FIPLPLGIRTSQLYID 493
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 631 PAdTLDIFAD-LQRAMKGfvlENDLHILYLV--TPmfeDWTTIDWYRF-FCLWEKLPTSMK-RVAELVGVEEGFlarcvk 705
Cdd:PRK00254 494 PL-TAKKFKDaFPKIEKN---PNPLGIFQLIasTP---DMTPLNYSRKeMEDLLDEAYEMEdRLYFNIPYWEDY------ 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 706 gkvvtrterqhRQMAIHKRFFTSLVLLDLISEVPLREINQKYGCNRGQIQSLQQSAA--VYAgMITVFsnRLGWHNMELL 783
Cdd:PRK00254 561 -----------KFQKFLRAFKTAKVLLDWINEVPEGEIVETYNIDPGDLYRILELADwlMYS-LIELY--KLFEPKQEVL 626
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 1622909152 784 --LSQFQKRLTFGIQRELCDLVRVSLLNAQRARVLYASGFHTVADLARANIVEV 835
Cdd:PRK00254 627 dyLETLHLRVKHGVREELLELMRLPMIGRKRARALYNAGFRSIEDIVNAKPSEL 680
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
110-838 |
1.32e-70 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 252.50 E-value: 1.32e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 110 QVLEGKNLVYSAPTSAGKTLVAELLILKRVLEmRKKALFILPFVSVAKEKKYYLQSLfQEVGIKVDGYMGSTSPSRHF-S 188
Cdd:PRK01172 33 QLRKGENVIVSVPTAAGKTLIAYSAIYETFLA-GLKSIYIVPLRSLAMEKYEELSRL-RSLGMRVKISIGDYDDPPDFiK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 189 SLDIAVCTIERANGLINRliEENKMDLLGMVVVDELHMLGDSHRGYLLELLLTKICYITRKsascqadlasslsnaVQIV 268
Cdd:PRK01172 111 RYDVVILTSEKADSLIHH--DPYIINDVGLIVADEIHIIGDEDRGPTLETVLSSARYVNPD---------------ARIL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 269 GMSATLPNLELVASWLNAEHYHTDFRPVPLLESVKVGNSIYDSSMKlvrefepmlqvKGDEDhVVSLCYETIRDNHSVLL 348
Cdd:PRK01172 174 ALSATVSNANELAQWLNASLIKSNFRPVPLKLGILYRKRLILDGYE-----------RSQVD-INSLIKETVNDGGQVLV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 349 FCPSKAWCEKLADIIAREFynlhhqteglvkpsecPPVNleqkELLEVMDQlrrlPSGLDSVLQKTVPWGVAFHHAGLTL 428
Cdd:PRK01172 242 FVSSRKNAEDYAEMLIQHF----------------PEFN----DFKVSSEN----NNVYDDSLNEMLPHGVAFHHAGLSN 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 429 EERDIIEGAFRQGLIRVLAATSTLSSGVNLPARRVIIRTPI----FGGRPLDILTYKQMAGRAGRKGVDTVGESIlICKN 504
Cdd:PRK01172 298 EQRRFIEEMFRNRYIKVIVATPTLAAGVNLPARLVIVRDITrygnGGIRYLSNMEIKQMIGRAGRPGYDQYGIGY-IYAA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 505 SEKSKGIA--LLQGSLKPVRSCLQRREgeevtaSMIRAILEIIVGGVASTSQDMHTYAACTFLAAsmkegkqgiqRNQES 582
Cdd:PRK01172 377 SPASYDAAkkYLSGEPEPVISYMGSQR------KVRFNTLAAISMGLASSMEDLILFYNETLMAI----------QNGVD 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 583 VQLGAIEACVMWLLENEFIQsteasdgtEGKVYHPTHLGSATLSSSLSPADTLdifadlqrAMKGFVLEN---DLHILYL 659
Cdd:PRK01172 441 EIDYYIESSLKFLKENGFIK--------GDVTLRATRLGKLTSDLYIDPESAL--------ILKSAFDHDydeDLALYYI 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 660 -VTPMFEDWTTIDWYrffclweklptSMKRVAELVGVEEGFLARCVkgkvvtrterqhrqmaihkrffTSLVLLDLISEV 738
Cdd:PRK01172 505 sLCREIIPANTRDDY-----------YAMEFLEDIGVIDGDISAAK----------------------TAMVLRGWISEA 551
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 739 PLREINQKYGCNRGQIQSLQQSA----AVYAGMITVFSNRlgwhnMELLLSQFQKRLTFGIQRELCDLVRVSLLNAQRAR 814
Cdd:PRK01172 552 SMQKITDTYGIAPGDVQARASSAdwisYSLARLSSIYKPE-----MRRKLEILNIRIKEGIREDLIDLVLIPKVGRVRAR 626
|
730 740
....*....|....*....|....
gi 1622909152 815 VLYASGFHTVADLARANIVEVEVI 838
Cdd:PRK01172 627 RLYDAGFKTVDDIARSSPERIKKI 650
|
|
| DNA_pol_A_plastid_like |
cd08640 |
DNA polymerase A type from plastids of higher plants possibly involve in DNA replication or in ... |
2199-2587 |
4.53e-61 |
|
DNA polymerase A type from plastids of higher plants possibly involve in DNA replication or in the repair of errors occurring during replication; DNA polymerase A type from plastids of higher plants possibly involve in DNA replication or in the repair of errors occurring during replication. Family A polymerase functions primarily to fill DNA gaps that arise during DNA repair, recombination and replication. DNA-dependent DNA polymerases can be classified in six main groups based upon phylogenetic relationships with E. coli polymerase I (classA), E. coli polymerase II (class B), E.coli polymerase III (class C), euryarchaaeota polymerase II (class D), human polymerase beta (class x), E. coli UmuC/DinB and eukaryotic RAP 30/Xeroderma pigmentosum variant (class Y). Family A polymerase are found primarily in organisms related to prokaryotes and include prokaryotic DNA polymerase I ,mitochondrial polymerase delta, and several bacteriphage polymerases including those from odd-numbered phage (T3, T5, and T7). The three-dimensional structure of plastid DNA polymerase has substantial similarity to Pol I. The structure of Pol I resembles in overall morphology a cupped human right hand, with fingers (which bind an incoming nucleotide and interact with the single-stranded template), palm (which harbors the catalytic amino acid residues and also binds an incoming dNTP) and thumb (which binds double-stranded DNA) subdomains.
Pssm-ID: 176477 Cd Length: 371 Bit Score: 214.95 E-value: 4.53e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2199 ILEWRRITNAITKVIFPLQreKRLNPFLGmeRIYPVSQSHTATGRITFTEPNIQNVPRdfeikmptlvgesppsqaigkg 2278
Cdd:cd08640 48 LKEIKSISTLLSTFIIPLQ--ELLNDSTG--RIHCSLNINTETGRLSSRNPNLQNQPA---------------------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2279 llpmgrgkskkgcslnpgrqaqMEEraaDRgmpFSIsmRHAFVPFPGGLILAADYSQLELRILAHLSHDRRLIQVLNTGA 2358
Cdd:cd08640 102 ----------------------LEK---DR---YKI--RKAFIASPGNTLIVADYSQLELRLLAHMTRCKSMIEAFNAGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2359 D------------VFRSIAAEWKMIEPESVGDDL-----------RQQAKQICYGIIYGMGAKSLGEQMGIKENDAACYI 2415
Cdd:cd08640 152 DfhsrtasgmyphVAEAVANGEVLLEWKSEGKPPapllkdkfkseRRKAKVLNFSIAYGKTAHGLAKDWKVKLKEAERTV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2416 DSFKSRYTGINQFMRETVKNCKRDGFVQTILGRRRYLPGIKDNNPYHKAHAERQAINTTVQGSAADIVKIAtvniqkqle 2495
Cdd:cd08640 232 DAWYSDRPEVEQWQKKTKKEARERGYTRTLLGRYRYLPDIKSRNRKKRGHAERAAINTPIQGSAADIAMKA--------- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2496 tfhstfkshghregMLQSDRTAGLlrkrklqgmfcpVRGGF-FILQLHDELLYEVAEEDVVQVAQIVKNEMES--AVKLS 2572
Cdd:cd08640 303 --------------MLRIYRNLRL------------KRLGWkLLLQIHDEVILEGPEEKADEALKIVKDCMENpfFGPLD 356
|
410
....*....|....*
gi 1622909152 2573 VKLKVKVKIGASWGE 2587
Cdd:cd08640 357 VPLEVDGSVGYNWYE 371
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
294-503 |
4.62e-56 |
|
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: 192.00 E-value: 4.62e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 294 RPVPLLESVKVGNSIYDSSMKLVREfepmlqvKGDEDHVVSLCYETIRDNHSVLLFCPSKAWCEKLADIIArefynlhhq 373
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMN-------KFDSDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA--------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 374 teglvkpsecppvnleqkellevmdqlrrlpsgldsvlqktvpwGVAFHHAGLTLEERDIIEGAFRQGLIRVLAATSTLS 453
Cdd:cd18795 65 --------------------------------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLA 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622909152 454 SGVNLPARRVIIR-TPIFGG---RPLDILTYKQMAGRAGRKGVDTVGESILICK 503
Cdd:cd18795 101 AGVNLPARTVIIKgTQRYDGkgyRELSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| PRK14975 |
PRK14975 |
bifunctional 3'-5' exonuclease/DNA polymerase; Provisional |
2060-2589 |
8.66e-54 |
|
bifunctional 3'-5' exonuclease/DNA polymerase; Provisional
Pssm-ID: 237876 [Multi-domain] Cd Length: 553 Bit Score: 199.44 E-value: 8.66e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2060 NQLNSLLQKEN---LQDVFrKVEMPSQYCLALLELNGIGFSTAEcegqkhiMQAKLDAIETQAYQLAGHSFSFTssdDIA 2136
Cdd:PRK14975 142 DQLNRIAAAAHpgrLRLLA-AAESAGALAAAEMELAGLPWDTDV-------HEALLAELLGPRPAAGGRPARLA---ELA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2137 EVLFLELKLPPngemKNQGSKKTLGstrrgndngRKL-RLG-RQFSTSKDVLNKLKalHPLPGLILEWRRITNAITKVIF 2214
Cdd:PRK14975 211 AEIREALGRPR----LNPDSPQQVL---------RALrRAGiELPSTRKWELREID--HPAVEPLLEYRKLSKLLSANGW 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2215 PLQREKRLNpflgmERIYPV-SQSHTATGRITFTEPNIQNVPRDfeikmptlvgesppsqaigkgllpmgrgkskkgcsl 2293
Cdd:PRK14975 276 AWLDYWVRD-----GRFHPEyVPGGVVTGRWASRGPNAQQIPRD------------------------------------ 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2294 npgrqaqmeeraadrgmpfsisMRHAFVPFPGGLILAADYSQLELRILAHLSHDRRLIQVLNTGADVFRSIAAEWKMIEP 2373
Cdd:PRK14975 315 ----------------------IRSAFVADPGWKLVVADASQIELRVLAAYSGDERMIEAFRTGGDLHRLTASVGFGKPE 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2374 ESVGDdlRQQAKQICYGIIYGMGAKSLGEQMGiKENDAACYIDSFKSRYTGINQFMRETVKNCKRDGFVQTILGRRRYLP 2453
Cdd:PRK14975 373 EEKEE--RALAKAANFGAIYGATSKGLQEYAK-NYGEAARLLERLRRAYPRAVGWVERAAREGERGGVVRTLLGRTSPPP 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2454 GIKDNNPYHKAHAERQAINTTVQGSAADIVKIATvniqkqletfhstfkshghregmlqsdrtaGLLRKRKLQGMfcpvr 2533
Cdd:PRK14975 450 GFAWRARRRARSRGRFTRNFPVQGTAADWAKLAL------------------------------ALLRRRLAEGL----- 494
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622909152 2534 GGFFILQLHDELLYEVAEEDVVQVAQIVKNEMESAVKL---SVKLKVKVKIGASWGELK 2589
Cdd:PRK14975 495 DAELVFFVHDEVVVECPEEEAEEVAAAIEEAMEEAGRLlfgPVPFPVEVAVVESYAEAK 553
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
98-291 |
1.91e-50 |
|
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: 177.07 E-value: 1.91e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 98 MFEWQAECLLLGqVLEGKNLVYSAPTSAGKTLVAELLILKRVLEMRKKALFILPFVSVAKEKKYYLQSLFQEVGIKVDGY 177
Cdd:cd17921 2 LNPIQREALRAL-YLSGDSVLVSAPTSSGKTLIAELAILRALATSGGKAVYIAPTRALVNQKEADLRERFGPLGKNVGLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 178 MGSTSPSR-HFSSLDIAVCTIERANGLINRLiEENKMDLLGMVVVDELHMLGDSHRGYLLELLLTKICYITRKsascqad 256
Cdd:cd17921 81 TGDPSVNKlLLAEADILVATPEKLDLLLRNG-GERLIQDVRLVVVDEAHLIGDGERGVVLELLLSRLLRINKN------- 152
|
170 180 190
....*....|....*....|....*....|....*
gi 1622909152 257 lasslsnaVQIVGMSATLPNLELVASWLNAEHYHT 291
Cdd:cd17921 153 --------ARFVGLSATLPNAEDLAEWLGVEDLIR 179
|
|
| DNA_pol_A_Aquificae_like |
cd08639 |
Phylum Aquificae Pol A is different from Escherichia coli Pol A by three signature sequences; ... |
2193-2586 |
2.67e-41 |
|
Phylum Aquificae Pol A is different from Escherichia coli Pol A by three signature sequences; Family A polymerase functions primarily to fill DNA gaps that arise during DNA repair, recombination and replication. DNA-dependent DNA polymerases can be classified in six main groups based upon phylogenetic relationships with E. coli polymerase I (classA), E. coli polymerase II (class B), E.coli polymerase III (class C), euryarchaaeota polymerase II (class D), human polymerase beta (class x), E. coli UmuC/DinB and eukaryotic RAP 30/Xeroderma pigmentosum variant (class Y). Family A polymerase are found primarily in organisms related to prokaryotes and include prokaryotic DNA polymerase I ,mitochondrial polymerase delta, and several bacteriphage polymerases including those from odd-numbered phage (T3, T5, and T7). Prokaryotic Pol Is have two functional domains located on the same polypeptide; a 5'-3' polymerase and 5'-3' exonuclease. Pol I uses its 5' nuclease activity to remove the ribonucleotide portion of newly synthesized Okazaki fragments and DNA polymerase activity to fill in the resulting gap. A combination of phylogenomic and signature sequence-based (or phonetic) approaches is used to understand the evolutionary relationships among bacteria. DNA polymerase I is one of the conserved proteins that is used for phylogenetic anaylsis of bacteria. Species of the phylum Aquificae grow in extreme thermophilic environments. The Aquificae are non-spore-forming, Gram-negative rods and strictly thermophilic. Phylum Aquificae Pol A is different from E. coli Pol I by three signature sequences consisting of a 2 amino acids (aa) insert, a 5-6 aa insert and a 6 aa deletion. These signature sequences may provide a molecular marker for the family Aquificaceae and related species.
Pssm-ID: 176476 Cd Length: 324 Bit Score: 156.29 E-value: 2.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2193 HPLPGLILEWRRITNAITKVIFPLqrEKRLNPFLGmeRIYP-VSQSHTATGRITFTEPNIQNVPRDFEikmptlvgespp 2271
Cdd:cd08639 29 HPAVRLLLEYRKLNKLISTFGEKL--PKHIHPVTG--RIHPsFNQIGAASGRMSCSNPNLQQIPRERE------------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2272 sqaigkgllpmgrgkskkgcslnpgrqaqmeeraadrgmpfsisMRHAFVPFPGGLILAADYSQLELRILAHLSHDRRLI 2351
Cdd:cd08639 93 --------------------------------------------FRRCFVAPEGNKLIIADYSQIELRIAAEISGDERMI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2352 QVLNTGADVFRSIAAEWKMIEPESVGDDLRQQAKQICYGIIYGMGAKSLGEQMGIKEN------DAACYIDSFKSRYTGI 2425
Cdd:cd08639 129 SAYQKGEDLHRLTASLITGKPIEEITKEERQLAKAVNFGLIYGMSAKGLREYARTNYGvemsleEAEKFRESFFFFYKGI 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2426 NQFMRETVKncKRDGFVQTILGRRRylpgIKDNNPYhkahaeRQAINTTVQGSAADIVKIATVniqkqletfhstfkshg 2505
Cdd:cd08639 209 LRWHHRLKA--KGPIEVRTLLGRRR----VFEYFTF------TEALNYPIQGTGADILKLALA----------------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2506 hregmLQSDRTAGLlrkrklqgmfcpvrGGFFILQLHDELLYEVAEEDVVQVAQIVKNEMESAVKL---SVKLKVKVKIG 2582
Cdd:cd08639 260 -----LLVDRLKDL--------------DAKIVLCVHDEIVLEVPEDEAEEAKKILESSMEEAGKRilkKVPVEVEVSIS 320
|
....
gi 1622909152 2583 ASWG 2586
Cdd:cd08639 321 DSWA 324
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
111-499 |
1.49e-40 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 163.19 E-value: 1.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 111 VLEGKNLVYSAPTSAGKTLVAELLILKRVLEMRK-------KALfilpfvsvAKEKKYYLQSLF--QEVGIkvdgyM-GS 180
Cdd:COG4581 37 LEAGRSVLVAAPTGSGKTLVAEFAIFLALARGRRsfytapiKAL--------SNQKFFDLVERFgaENVGL-----LtGD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 181 TSPSRHfssLDIAVCTIERangLINRLIEE-NKMDLLGMVVVDELHMLGDSHRGYLLELLltkICYITRKsascqadlas 259
Cdd:COG4581 104 ASVNPD---APIVVMTTEI---LRNMLYREgADLEDVGVVVMDEFHYLADPDRGWVWEEP---IIHLPAR---------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 260 slsnaVQIVGMSATLPNLELVASWLNAEHYHT-----DFRPVPLLESVKVGNSIYDssmklVREFEPMLQVKGDEDHVVs 334
Cdd:COG4581 165 -----VQLVLLSATVGNAEEFAEWLTRVRGETavvvsEERPVPLEFHYLVTPRLFP-----LFRVNPELLRPPSRHEVI- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 335 lcyETIRDNH--SVLLFCPSKAWCEKLADIIAREfynlhhqteGLVKPSEcppvnleQKELLEVMDQLRRLPSGLD-SVL 411
Cdd:COG4581 234 ---EELDRGGllPAIVFIFSRRGCDEAAQQLLSA---------RLTTKEE-------RAEIREAIDEFAEDFSVLFgKTL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 412 QKTVPWGVAFHHAGLTLEERDIIEGAFRQGLIRVLAATSTLSSGVNLPARRVIIRTPI-FGGRPLDILT---YKQMAGRA 487
Cdd:COG4581 295 SRLLRRGIAVHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFTKLSkFDGERHRPLTareFHQIAGRA 374
|
410
....*....|..
gi 1622909152 488 GRKGVDTVGESI 499
Cdd:COG4581 375 GRRGIDTEGHVV 386
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
97-292 |
3.14e-35 |
|
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: 133.61 E-value: 3.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 97 KMFEWQAECLLLGqVLEGKNLVYSAPTSAGKTLVAELLILKRVLEmRKKALFILPFVSVAKEK-----KYYLQSLfqEVG 171
Cdd:cd18028 1 ELYPPQAEAVRAG-LLKGENLLISIPTASGKTLIAEMAMVNTLLE-GGKALYLVPLRALASEKyeefkKLEEIGL--KVG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 172 IKVDGYmgsTSPSRHFSSLDIAVCTIERANGLINRliEENKMDLLGMVVVDELHMLGDSHRGYLLELLLTKIcyitrksa 251
Cdd:cd18028 77 ISTGDY---DEDDEWLGDYDIIVATYEKFDSLLRH--SPSWLRDVGVVVVDEIHLISDEERGPTLESIVARL-------- 143
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622909152 252 scqadlaSSLSNAVQIVGMSATLPNLELVASWLNAEHYHTD 292
Cdd:cd18028 144 -------RRLNPNTQIIGLSATIGNPDELAEWLNAELVESD 177
|
|
| HTH_61 |
pfam20470 |
Helix-turn-helix domain; This entry represents a presumed helix-turn-helix domain found in DNA ... |
496-602 |
2.13e-32 |
|
Helix-turn-helix domain; This entry represents a presumed helix-turn-helix domain found in DNA polymerase theta.
Pssm-ID: 466619 [Multi-domain] Cd Length: 92 Bit Score: 121.89 E-value: 2.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 496 GESILICKNSEKSKGIALLQGSLKPVRSCLQRRegeevTASMIRAILEIIVGGVASTSQDMHTYAACTFLAASMKEGKQG 575
Cdd:pfam20470 1 GESILICKEKDLEKVAELLRAELPPVYSCLLPE-----KRGIKRALLEIIALGLATSPEDVDEYMSCTLLSVQQKELDVE 75
|
90 100
....*....|....*....|....*..
gi 1622909152 576 IQrnqesvqlgaIEACVMWLLENEFIQ 602
Cdd:pfam20470 76 KS----------IESSLEELVENGLIT 92
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
96-646 |
1.05e-28 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 125.77 E-value: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 96 KKMFEWQAECLLLGQV-------LEGKN-LVYSApTSAGKTLVAELLILKRVLEMRKKALFILPFVSVAKEKkyYLQslF 167
Cdd:COG1202 200 KDLLEGRGEELLPVQSlavenglLEGKDqLVVSA-TATGKTLIGELAGIKNALEGKGKMLFLVPLVALANQK--YED--F 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 168 QE-------VGIKVdgymGST---SPSRHFS-SLDIAVCTIEranGLINRLIEENKMDLLGMVVVDELHMLGDSHRGYLL 236
Cdd:COG1202 275 KDrygdgldVSIRV----GASrirDDGTRFDpNADIIVGTYE---GIDHALRTGRDLGDIGTVVIDEVHMLEDPERGHRL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 237 ELLLTKICYITRKSascqadlasslsnavQIVGMSATLPNLELVASWLNAEHYHTDFRPVPL---------LESVKVGNs 307
Cdd:COG1202 348 DGLIARLKYYCPGA---------------QWIYLSATVGNPEELAKKLGAKLVEYEERPVPLerhltfadgREKIRIIN- 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 308 iydssmKLV-REFepmlqvkgdeDHVVSLCY--ETIrdnhsvlLFCPSKAWCEKLADIIarefynlhhqteglvkpsecp 384
Cdd:COG1202 412 ------KLVkREF----------DTKSSKGYrgQTI-------IFTNSRRRCHEIARAL--------------------- 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 385 pvnleqkellevmdqlrrlpsGLDSvlqktvpwgvAFHHAGLTLEERDIIEGAFRQGLIRVLAATSTLSSGVNLPARRVI 464
Cdd:COG1202 448 ---------------------GYKA----------APYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQVI 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 465 IRTPIFGGRPLDILTYKQMAGRAGRKGVDTVGESILI----------CKNSEKSKGIALLQGSLKPVRSCL-QRREGEEV 533
Cdd:COG1202 497 FDSLAMGIEWLSVQEFHQMLGRAGRPDYHDRGKVYLLvepgksyhrsMEMTEDEVAFKLLKGEMEDVAVEYdEEAAVEET 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 534 TASmiraileIIVGGvaSTSQDMHtyaactflaASMkegkqgiqrnqesvqLGAI--EACVMWLLENEFIqsteasDGTE 611
Cdd:COG1202 577 LAN-------VVVGG--GKAKRLN---------DRM---------------LGEIptKHALGKLLEYGFI------DGLE 617
|
570 580 590
....*....|....*....|....*....|....*
gi 1622909152 612 gkvyhPTHLGSATLSSSLSPADTLDIfADLQRAMK 646
Cdd:COG1202 618 -----PTPLGRAVARHFLGPEEAFLI-LDGVRKGD 646
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
102-280 |
1.87e-21 |
|
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: 93.46 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 102 QAECLLLgqVLEGKNLVYSAPTSAGKTLVAELLILKRVLEMR--KKALFILPFVSVAKEKKYYLQSLFQEVGIKVDGYMG 179
Cdd:pfam00270 4 QAEAIPA--ILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDngPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 180 STSPSRHFSSL---DIAVCTIERangLINRLIEENKMDLLGMVVVDELHMLGDSHRGYLLELLLtkicyitrksascqad 256
Cdd:pfam00270 82 GDSRKEQLEKLkgpDILVGTPGR---LLDLLQERKLLKNLKLLVLDEAHRLLDMGFGPDLEEIL---------------- 142
|
170 180
....*....|....*....|....*
gi 1622909152 257 laSSLSNAVQIVGMSATLP-NLELV 280
Cdd:pfam00270 143 --RRLPKKRQILLLSATLPrNLEDL 165
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
91-291 |
2.57e-20 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 91.40 E-value: 2.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 91 HSFGVKKMFEWQAECLLlgQVLEG-KNLVYSAPTSAGKTLVAELLILKRVLE-MRKKALFILPFVSVAKEKKYYLQSLFQ 168
Cdd:smart00487 2 EKFGFEPLRPYQKEAIE--ALLSGlRDVILAAPTGSGKTLAALLPALEALKRgKGGRVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 169 EVGIKVDGYMGSTSPSRHFSSL-----DIAVCTIERanglINRLIEENKMDL--LGMVVVDELHMLGDSHRGYLLELLLT 241
Cdd:smart00487 80 SLGLKVVGLYGGDSKREQLRKLesgktDILVTTPGR----LLDLLENDKLSLsnVDLVILDEAHRLLDGGFGDQLEKLLK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622909152 242 KicyitrksascqadlassLSNAVQIVGMSATLPNLELVASWLNAEHYHT 291
Cdd:smart00487 156 L------------------LPKNVQLLLLSATPPEEIENLLELFLNDPVF 187
|
|
| phage_DpoZ_1 |
NF038380 |
aminoadenine-incorporating DNA polymerase DpoZ; |
2068-2587 |
3.20e-19 |
|
aminoadenine-incorporating DNA polymerase DpoZ;
Pssm-ID: 468497 [Multi-domain] Cd Length: 604 Bit Score: 94.73 E-value: 3.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2068 KENLQDVFRkVEMPSQYCLALLELNGIGFSTAECEGQKHIMQAKLDAIETQAYQLAGHSFSFTSSDDIAEVLflelKLPP 2147
Cdd:NF038380 173 RQGLQRVVE-LERRLFPVLIDMEWRGIRVDLEAAEAAIPELDKVIDQLQKELNEIAGFEFNVNSSPQIRKLF----KPKK 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2148 NGEMKNQGSKKT-LGSTRRGNDngrklrlgrqfSTSKDVLNKLKalHPLPGLILEWRritnaitKVIfplqreKRLNPFL 2226
Cdd:NF038380 248 ISKGQWVAIDGTpLETTDAGKP-----------SLGADALREIK--HPAAAKILELR-------KLI------KTRDTFL 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2227 G--------MERIYP-VSQS------HTATGRITFTEPNIQNVP-RDFEIKmptlvgesppsqAIgkgllpmgrgkskkg 2290
Cdd:NF038380 302 RghvlghavGGGVHPnINQTkgedggGTGTGRLSYTDPALQQIPsRDKAIA------------AI--------------- 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2291 cslnpgrqaqmeeraadrgmpfsisMRHAFVPFPGGLILAADYSQLELRILAHLSHDRRLIQV--LNTGADvFRSIAAEW 2368
Cdd:NF038380 355 -------------------------VRPIFLPDEGQVWLCSDLAQFEFRIFAHLVNNPSIIAAyaEDPELD-FHQIVADM 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2369 KMIePESVGDDLRQQAKQICYGIIYGMGAKSLGEQMG----IKEND--------------AACYIDSFKSRYTGINQFMR 2430
Cdd:NF038380 409 TGL-PRNATYSGQANAKQINLGMIFNMGNGKLADKMGmpyeWEEFTfgkevrrykkagpeAMAVIENYHRKLPGVKELAD 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2431 ETVKNCKRDGFVQTILGRRRYLPGIKdnnpyhKAHAerqAINTTVQGSAADIVKIATVNIQKQLETfhstfkshghregm 2510
Cdd:NF038380 488 RAKAVAKERGYVRTAMGRRLRFPGGM------KTYK---ASGLLIQATAADLNKENLLEIDEVLGS-------------- 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2511 lqsdrtagllrkrklqgmfcpvRGGFFILQLHDELLYEVAEEDVVQ-VAQIVKNEMESAvklSVKLKVKVKI-----GAS 2584
Cdd:NF038380 545 ----------------------LDGRLLLNTHDEYSMSLPEDDVRKpIKERVKLFIEDS---SPWLRVPIILelsgfGRN 599
|
...
gi 1622909152 2585 WGE 2587
Cdd:NF038380 600 WWE 602
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
115-287 |
6.48e-18 |
|
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: 84.72 E-value: 6.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 115 KNLVYSAPTSAGKTLVAELLILkRVL-------EMRKKALFILPFVSVAKEKKYYLQSLFQEVGIKVDGYMGSTS--PSR 185
Cdd:cd18023 18 KNFVVSAPTGSGKTVLFELAIL-RLLkernplpWGNRKVVYIAPIKALCSEKYDDWKEKFGPLGLSCAELTGDTEmdDTF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 186 HFSSLDIAVCTIERANGLINRLIEENKM-DLLGMVVVDELHMLGDShRGYLLELLLTKICYITRKSASCQADLASslsna 264
Cdd:cd18023 97 EIQDADIILTTPEKWDSMTRRWRDNGNLvQLVALVLIDEVHIIKEN-RGATLEVVVSRMKTLSSSSELRGSTVRP----- 170
|
170 180
....*....|....*....|...
gi 1622909152 265 VQIVGMSATLPNLELVASWLNAE 287
Cdd:cd18023 171 MRFVAVSATIPNIEDLAEWLGDN 193
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
114-273 |
2.11e-17 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 81.30 E-value: 2.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 114 GKNLVYSAPTSAGKTLVAELLILKRVLEMRKKALFILPFVSVAKEKKYYLQSLFQEvGIKVDGYMGSTSPSRHFS----S 189
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLKKGKKVLVLVPTKALALQTAERLRELFGP-GIRVAVLVGGSSAEEREKnklgD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 190 LDIAVCTIERANGLINRLIEENKMDlLGMVVVDELHMLGDSHRGYLLEllltkicyitrksasCQADLASSLSNaVQIVG 269
Cdd:cd00046 80 ADIIIATPDMLLNLLLREDRLFLKD-LKLIIVDEAHALLIDSRGALIL---------------DLAVRKAGLKN-AQVIL 142
|
....
gi 1622909152 270 MSAT 273
Cdd:cd00046 143 LSAT 146
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
418-491 |
1.25e-16 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 76.87 E-value: 1.25e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622909152 418 GVAFHHAGLTLEERDIIEGAFRQGLIRVLAATSTLSSGVNLP-ARRVIIRtpifgGRPLDILTYKQMAGRAGRKG 491
Cdd:smart00490 13 KVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIY-----DLPWSPASYIQRIGRAGRAG 82
|
|
| DNA_pol_A_pol_I_B |
cd08643 |
Polymerase I functions primarily to fill DNA gaps that arise during DNA repair, recombination ... |
2309-2587 |
3.00e-16 |
|
Polymerase I functions primarily to fill DNA gaps that arise during DNA repair, recombination and replication; Family A polymerase functions primarily to fill DNA gaps that arise during DNA repair, recombination and replication. DNA-dependent DNA polymerases can be classified in six main groups based upon phylogenetic relationships with E. coli polymerase I (classA), E. coli polymerase II (class B), E.coli polymerase III (class C), euryarchaaeota polymerase II (class D), human polymerase beta (class x), E. coli UmuC/DinB and eukaryotic RAP 30/Xeroderma pigmentosum variant (class Y). Family A polymerase are found primarily in organisms related to prokaryotes and include prokaryotic DNA polymerase I ,mitochondrial polymerase delta, and several bacteriphage polymerases including those from odd-numbered phage (T3, T5, and T7). Prokaryotic Pol Is have two functional domains located on the same polypeptide; a 5'-3' polymerase and 5'-3' exonuclease. Pol I uses its 5' nuclease activity to remove the ribonucleotide portion of newly synthesized Okazaki fragments and DNA polymerase activity to fill in the resulting gap. A combination of phylogenomic and signature sequence-based (or phonetic) approaches is used to understand the evolutionary relationships among bacteria. DNA polymerase I is one of the conserved proteins that is used to search for protein signatures. The structure of these polymerases resembles in overall morphology a cupped human right hand, with fingers (which bind an incoming nucleotide and interact with the single-stranded template), palm (which harbors the catalytic amino acid residues and also binds an incoming dNTP) and thumb (which binds double-stranded DNA) subdomains.
Pssm-ID: 176480 Cd Length: 429 Bit Score: 84.02 E-value: 3.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2309 GMPFSISMRHAFVPFPGGLILAADYSQLELRILAHLSHDrrliqvLNTGADVFRSIAAEWKMIEPESVGDDLRQQAKQIC 2388
Cdd:cd08643 170 GSPYGKECRELFGVPPGWSLVGADASGLELRCLAHYLAR------YDGGAYTRKVLGGDIHWANAQAMGLLSRDGAKTFI 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2389 YGIIYGMGAKSLGEQMGIKENDA----ACYIDSFKSRYTGINQ----------FMRETV--KNCKRDgfVQTILGRRRYL 2452
Cdd:cd08643 244 YAFLYGAGDEKLGQIVGDDLRTAknlnAEWPQTKKGTIKKIADkakgrvvranFLKGLPalGKLIKK--VKEAAKKRGHL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2453 PGIKDNNPYHK-AHAerqAINTTVQGSAADIVKIATVNIQKQLEtfhstfkshghregmlqsdrTAGLLRKRKLQgmfcp 2531
Cdd:cd08643 322 VGLDGRRIRVRsAHA---ALNTLLQSAGAILMKKWLVLLDDELT--------------------AKGGVWGGDFE----- 373
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622909152 2532 vrggfFILQLHDELLYEVAEEDVVQVAQIVKNEMESAVK---LSVKLKVKVKIGASWGE 2587
Cdd:cd08643 374 -----YCAWVHDEVQIECRKGIAEEVGKIAVEAAEKAGEhfnFRCPLAGEFDIGRNWAE 427
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
114-284 |
4.91e-15 |
|
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: 74.93 E-value: 4.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 114 GKNLVYSAPTSAGKTLVAELLILKRVLEMRKK---ALFILPFVSVAKEKKYYLQSLFQE--VGIKVDGYMGSTSPSRHFS 188
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKgvqVLYISPLKALINDQERRLEEPLDEidLEIPVAVRHGDTSQSEKAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 189 SL----DIAVCTIERANGLINRLIEENKMDLLGMVVVDELHMLGDSHRGYLLELLLTKICYITRKSAscqadlasslsna 264
Cdd:cd17922 81 QLknppGILITTPESLELLLVNKKLRELFAGLRYVVVDEIHALLGSKRGVQLELLLERLRKLTGRPL------------- 147
|
170 180
....*....|....*....|
gi 1622909152 265 vQIVGMSATLPNLELVASWL 284
Cdd:cd17922 148 -RRIGLSATLGNLEEAAAFL 166
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
116-284 |
5.13e-15 |
|
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 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: 350777 [Multi-domain] Cd Length: 214 Bit Score: 76.25 E-value: 5.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 116 NLVYSAPTSAGKTLVAELLILKRVLEMRK----------KALFILPFVSVAKEKKYYLQSLFQEVGIKVDGYMGSTSPSR 185
Cdd:cd18019 35 NLLLCAPTGAGKTNVALLTILREIGKHRNpdgtinldafKIVYIAPMKALVQEMVGNFSKRLAPYGITVAELTGDQQLTK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 186 -HFSSLDIAVCTIERANGLINRLIEENKMDLLGMVVVDELHMLGDShRGYLLELLLTKIcyiTRKSASCQADlasslsna 264
Cdd:cd18019 115 eQISETQIIVTTPEKWDIITRKSGDRTYTQLVRLIIIDEIHLLHDD-RGPVLESIVART---IRQIEQTQEY-------- 182
|
170 180
....*....|....*....|
gi 1622909152 265 VQIVGMSATLPNLELVASWL 284
Cdd:cd18019 183 VRLVGLSATLPNYEDVATFL 202
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
81-491 |
8.02e-15 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 80.65 E-value: 8.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 81 GLPKAVLEKYHSFGVKKMFEWQAECLllGQVLEGKNLVYSAPTSAGKTLVAELLILKRVLEMRK-KALFILPFVSVAKEK 159
Cdd:COG1205 40 WLPPELRAALKKRGIERLYSHQAEAI--EAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPGaTALYLYPTKALARDQ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 160 KYYLQSLFQEVG--IKVDGYMGSTSPS-RH--FSSLDIAVCT-------IERANGLINRLIEEnkmdlLGMVVVDELHM- 226
Cdd:COG1205 118 LRRLRELAEALGlgVRVATYDGDTPPEeRRwiREHPDIVLTNpdmlhygLLPHHTRWARFFRN-----LRYVVIDEAHTy 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 227 ---LGdSHRGYLLELLLtKICyitrksascqADLASSlsnaVQIVGMSATLPN-LELVASWLNAEHYH--TDFRPVP--- 297
Cdd:COG1205 193 rgvFG-SHVANVLRRLR-RIC----------RHYGSD----PQFILASATIGNpAEHAERLTGRPVTVvdEDGSPRGert 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 298 --LLESVKVGNSIYDSSMKLVREfepmlqvkgdedhvvsLCYETIRDNHSVLLFCPSKawceKLADIIAREFynlhhqte 375
Cdd:COG1205 257 fvLWNPPLVDDGIRRSALAEAAR----------------LLADLVREGLRTLVFTRSR----RGAELLARYA-------- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 376 glvkpsecppvnleQKELLEVMDQLRrlpsgldsvlqktvpwgVAFHHAGLTLEERDIIEGAFRQGLIRVLAATSTLSSG 455
Cdd:COG1205 309 --------------RRALREPDLADR-----------------VAAYRAGYLPEERREIERGLRSGELLGVVSTNALELG 357
|
410 420 430
....*....|....*....|....*....|....*....
gi 1622909152 456 VNLP---ArrVIIRtpifgGRPLDILTYKQMAGRAGRKG 491
Cdd:COG1205 358 IDIGgldA--VVLA-----GYPGTRASFWQQAGRAGRRG 389
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
115-285 |
1.11e-14 |
|
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 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: 350780 [Multi-domain] Cd Length: 189 Bit Score: 74.72 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 115 KNLVYSAPTSAGKTLVAELLILkRVLEMR--KKALFILPFVSVAKEK-KYYLQSLFQEVGIKVDGYMGSTSPS-RHFSSL 190
Cdd:cd18022 18 NNVLLGAPTGSGKTIAAELAMF-RAFNKYpgSKVVYIAPLKALVRERvDDWKKRFEEKLGKKVVELTGDVTPDmKALADA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 191 DIAVCTIERANGLINRLIEENKMDLLGMVVVDELHMLGdSHRGYLLELLLTKICYITRKSascqadlasslSNAVQIVGM 270
Cdd:cd18022 97 DIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLG-SDRGPVLEVIVSRMNYISSQT-----------EKPVRLVGL 164
|
170
....*....|....*
gi 1622909152 271 SATLPNLELVASWLN 285
Cdd:cd18022 165 STALANAGDLANWLG 179
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
116-291 |
7.92e-14 |
|
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 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: 350779 [Multi-domain] Cd Length: 191 Bit Score: 72.29 E-value: 7.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 116 NLVYSAPTSAGKTLVAELLILKRVLEMRK-KALFILPFVSVAKEKKYYLQSLFQEV-GIKVDGYMGSTSPS-RHFSSLDI 192
Cdd:cd18021 21 NVFVGAPTGSGKTVCAELALLRHWRQNPKgRAVYIAPMQELVDARYKDWRAKFGPLlGKKVVKLTGETSTDlKLLAKSDV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 193 AVCTIERANGLINRLIEENKMDLLGMVVVDELHMLGDSHrGYLLELLLTKICYItrksascqadlASSLSNAVQIVGMSA 272
Cdd:cd18021 101 ILATPEQWDVLSRRWKQRKNVQSVELFIADELHLIGGEN-GPVYEVVVSRMRYI-----------SSQLEKPIRIVGLSS 168
|
170
....*....|....*....
gi 1622909152 273 TLPNLELVASWLNAEHYHT 291
Cdd:cd18021 169 SLANARDVGEWLGASKSTI 187
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
409-491 |
2.62e-13 |
|
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: 68.39 E-value: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 409 SVLQKTVPWGVAFHHAGLTLEERDIIEGAFRQGLIRVLAATSTLSSGVNLPARRVIIrtpIFGGrPLDILTYKQMAGRAG 488
Cdd:pfam00271 31 ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVI---NYDL-PWNPASYIQRIGRAG 106
|
...
gi 1622909152 489 RKG 491
Cdd:pfam00271 107 RAG 109
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
97-490 |
9.35e-10 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 63.89 E-value: 9.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 97 KMFEWQAECL---LLGQVLEGKNLVYSAPTSAGKTLVAeLLILKRVLEmRKKALFILPFVSVAKekkyylQSL--FQEVG 171
Cdd:COG1061 80 ELRPYQQEALealLAALERGGGRGLVVAPTGTGKTVLA-LALAAELLR-GKRVLVLVPRRELLE------QWAeeLRRFL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 172 IKVDGYMGSTSPSRhfsslDIAVCTIeraNGLINRLIEENKMDLLGMVVVDELHMLG-DSHRGyLLELLltkicyitrks 250
Cdd:COG1061 152 GDPLAGGGKKDSDA-----PITVATY---QSLARRAHLDELGDRFGLVIIDEAHHAGaPSYRR-ILEAF----------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 251 ascqadlasslsNAVQIVGMSAT---LPNLELVASWLNAEHYHTDFR----------------PVPLLESVKVGNSIYDS 311
Cdd:COG1061 212 ------------PAAYRLGLTATpfrSDGREILLFLFDGIVYEYSLKeaiedgylappeyygiRVDLTDERAEYDALSER 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 312 SMKLVREFEPMLqvkgdeDHVVSLCYETIRDNHSVLLFCPSKAWCEKLADIIAREFYNlhhqteglvkpsecppvnleqk 391
Cdd:COG1061 280 LREALAADAERK------DKILRELLREHPDDRKTLVFCSSVDHAEALAELLNEAGIR---------------------- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 392 ellevmdqlrrlpsgldsvlqktvpwgVAFHHAGLTLEERDIIEGAFRQGLIRVLAATSTLSSGVNLP-ARRVIIRTPIf 470
Cdd:COG1061 332 ---------------------------AAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPrLDVAILLRPT- 383
|
410 420
....*....|....*....|
gi 1622909152 471 gGRPldiLTYKQMAGRAGRK 490
Cdd:COG1061 384 -GSP---REFIQRLGRGLRP 399
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
121-490 |
2.75e-09 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 63.02 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 121 APTSAGKTLVAELLILKRVL--------EMRKKA----LFILPF----VSVAKEKKYYLQSLFQE--------VGIKVDG 176
Cdd:PRK09751 3 APTGSGKTLAAFLYALDRLFreggedtrEAHKRKtsriLYISPIkalgTDVQRNLQIPLKGIADErrrrgeteVNLRVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 177 YMGSTsPSRHFSSL-----DIAVCTIEranGLINRLIEENKMDLLGM--VVVDELHMLGDSHRGYLLELLLTKicyitrk 249
Cdd:PRK09751 83 RTGDT-PAQERSKLtrnppDILITTPE---SLYLMLTSRARETLRGVetVIIDEVHAVAGSKRGAHLALSLER------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 250 sascqadLASSLSNAVQIVGMSATLPNLELVASWLNAEhyhtdfRPVPLLESvkvgNSIYDSSMKLVREFEPMLQVK--- 326
Cdd:PRK09751 152 -------LDALLHTSAQRIGLSATVRSASDVAAFLGGD------RPVTVVNP----PAMRHPQIRIVVPVANMDDVSsva 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 327 ---GDED----------HVVSLCYETIRDNHSVLLFCPSKAWCEKLAdiiAR--EFYNLHHQTeglvkpSECPPVNLEQK 391
Cdd:PRK09751 215 sgtGEDShagregsiwpYIETGILDEVLRHRSTIVFTNSRGLAEKLT---ARlnELYAARLQR------SPSIAVDAAHF 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 392 ELLEVMDQLRRlpSGLDSVLQKTvpwgvafHHAGLTLEERDIIEGAFRQGLIRVLAATSTLSSGVNLPARRVIIRTpifg 471
Cdd:PRK09751 286 ESTSGATSNRV--QSSDVFIARS-------HHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQV---- 352
|
410
....*....|....*....
gi 1622909152 472 GRPLDILTYKQMAGRAGRK 490
Cdd:PRK09751 353 ATPLSVASGLQRIGRAGHQ 371
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
115-289 |
5.16e-09 |
|
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 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: 350778 [Multi-domain] Cd Length: 199 Bit Score: 58.60 E-value: 5.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 115 KNLVYSAPTSAGKTLVAELLIL----KRVLEMRK------KALFILPFVSVAKEKKYYLQSLFQEVGIKVDGYMGSTSPS 184
Cdd:cd18020 18 ENMLICAPTGAGKTNIAMLTILheirQHVNQGGVikkddfKIVYIAPMKALAAEMVEKFSKRLAPLGIKVKELTGDMQLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 185 R-HFSSLDIAVCTIERANGLINRLIEENKM-DLLGMVVVDELHMLGDShRGYLLELLLTKIcyiTRKSASCQAdlassls 262
Cdd:cd18020 98 KkEIAETQIIVTTPEKWDVVTRKSSGDVALsQLVRLLIIDEVHLLHDD-RGPVIESLVART---LRQVESTQS------- 166
|
170 180
....*....|....*....|....*..
gi 1622909152 263 nAVQIVGMSATLPNLELVASWLNAEHY 289
Cdd:cd18020 167 -MIRIVGLSATLPNYLDVADFLRVNPY 192
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
219-452 |
2.19e-08 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 59.73 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 219 VVVDELHMLGDSHRGYLLELLLtkicyitrksascqADLASSLSNAVQIVGMSATLPNLELVASWLNAehyHTDFRPVPL 298
Cdd:COG1201 165 VIVDEIHALAGSKRGVHLALSL--------------ERLRALAPRPLQRIGLSATVGPLEEVARFLVG---YEDPRPVTI 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 299 LEsVKVGNSIydsSMKLVREFEPMLQVKGDEDHVVSLCYET----IRDNHSVLLFCPSKAWCEKLadiiareFYNLhhqt 374
Cdd:COG1201 228 VD-AGAGKKP---DLEVLVPVEDLIERFPWAGHLWPHLYPRvldlIEAHRTTLVFTNTRSQAERL-------FQRL---- 292
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622909152 375 eglvkpsecppvnleqkellevmdqLRRLPSGLDSvlqktvpwgVAFHHAGLTLEERDIIEGAFRQGLIRVLAATSTL 452
Cdd:COG1201 293 -------------------------NELNPEDALP---------IAAHHGSLSREQRLEVEEALKAGELRAVVATSSL 336
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
94-285 |
7.03e-08 |
|
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: 55.14 E-value: 7.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 94 GVKKMFEWQAECLLLgqVLEGKNLVYSAPTSAGKTLvAELL-ILKRVLEMRKK------ALFILP----FVSVAKEkkyy 162
Cdd:cd00268 9 GFEKPTPIQAQAIPL--ILSGRDVIGQAQTGSGKTL-AFLLpILEKLLPEPKKkgrgpqALVLAPtrelAMQIAEV---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 163 LQSLFQEVGIKVDGYMGSTSPSRHFSSL----DIAVCTIERanglINRLIEENKMDL--LGMVVVDEL-HMLGDSHRGYL 235
Cdd:cd00268 82 ARKLGKGTGLKVAAIYGGAPIKKQIEALkkgpDIVVGTPGR----LLDLIERGKLDLsnVKYLVLDEAdRMLDMGFEEDV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622909152 236 LELLltkicyitrksascqadlaSSLSNAVQIVGMSATLPN--LELVASWLN 285
Cdd:cd00268 158 EKIL-------------------SALPKDRQTLLFSATLPEevKELAKKFLK 190
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
120-294 |
1.01e-07 |
|
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or SKIV2L2) is a type II DEAD box helicase that plays a role in the processing of structured RNAs, including the maturation of 5.8S ribosomal RNA (rRNA)and is part of the TRAMP complex that is involved in exosome-mediated degradation of aberrant RNAs. Mtr4 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: 350782 [Multi-domain] Cd Length: 205 Bit Score: 54.76 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 120 SAPTSAGKTLVAELLILKrVLEMRKKALFILPFVSVAKEKKYYLQSLFQEVGIKVdgymGSTSPSRHFSSLdiaVCTIER 199
Cdd:cd18024 53 SAHTSAGKTVVAEYAIAQ-SLRDKQRVIYTSPIKALSNQKYRELQEEFGDVGLMT----GDVTINPNASCL---VMTTEI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 200 ANGLINRLIEenKMDLLGMVVVDELHMLGDSHRGYLLE--LLLtkicyitrksascqadlassLSNAVQIVGMSATLPNL 277
Cdd:cd18024 125 LRSMLYRGSE--IMREVAWVIFDEIHYMRDKERGVVWEetIIL--------------------LPDKVRYVFLSATIPNA 182
|
170 180
....*....|....*....|...
gi 1622909152 278 ELVASWLNAEHY------HTDFR 294
Cdd:cd18024 183 RQFAEWICKIHKqpchvvYTDYR 205
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
419-501 |
1.95e-07 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 52.64 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 419 VAFHHAGLTLEERDIIEGAFRQGLIRVLAATSTLSSGVNLPARRVIIRTpifgGRPLDILTYKQMAGRAGRKGVDTVgeS 498
Cdd:cd18797 69 VASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLA----GYPGSLASLWQQAGRAGRRGKDSL--V 142
|
...
gi 1622909152 499 ILI 501
Cdd:cd18797 143 ILV 145
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
111-275 |
2.02e-07 |
|
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: 54.29 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 111 VLEGKNLVYSAPTSAGKTLVAELLILKRVLEMRKK---------ALFILPFVSVAKEKKYYLQSLFQEVGIKVDGYMGST 181
Cdd:cd17948 24 ILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLaegpfnaprGLVITPSRELAEQIGSVAQSLTEGLGLKVKVITGGR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 182 SPSR----HFSSLDIAVCTIeranGLINRLIEEN--KMDLLGMVVVDELH-MLGDShrgyLLELLLtkicYITRKS--AS 252
Cdd:cd17948 104 TKRQirnpHFEEVDILVATP----GALSKLLTSRiySLEQLRHLVLDEADtLLDDS----FNEKLS----HFLRRFplAS 171
|
170 180
....*....|....*....|...
gi 1622909152 253 CQADLASSLSNAVQIVGMSATLP 275
Cdd:cd17948 172 RRSENTDGLDPGTQLVLVSATMP 194
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
102-276 |
4.53e-07 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 52.20 E-value: 4.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 102 QAECLLLgqVLEGKNLVYSAPTSAGKTLVAELLILKRVL-EMRKKALFILPFVSVAKEKKYYLQSLFQEV--GIKVDGYM 178
Cdd:cd17923 5 QAEAIEA--ARAGRSVVVTTGTASGKSLCYQLPILEALLrDPGSRALYLYPTKALAQDQLRSLRELLEQLglGIRVATYD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 179 GSTSPSrhfssldiavctiERANGLIN--RLIEEN-KM-------------DLLGM---VVVDELHM----LGdSHRGYL 235
Cdd:cd17923 83 GDTPRE-------------ERRAIIRNppRILLTNpDMlhyallphhdrwaRFLRNlryVVLDEAHTyrgvFG-SHVALL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622909152 236 LELLLtkicyitrksascqaDLASSLSNAVQIVGMSATLPN 276
Cdd:cd17923 149 LRRLR---------------RLCRRYGADPQFILTSATIGN 174
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
112-275 |
6.56e-06 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350794 [Multi-domain] Cd Length: 204 Bit Score: 49.40 E-value: 6.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 112 LEGKNLVYSAPTSAGKTLVAeLLILKRVLEMRKKA------LFILPFVSVAKEKKYYLQSLFqEVGIKVDGYMGSTSPSR 185
Cdd:cd18036 15 LRGKNTIICAPTGSGKTRVA-VYICRHHLEKRRSAgekgrvVVLVNKVPLVEQQLEKFFKYF-RKGYKVTGLSGDSSHKV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 186 HFSSL----DIAVCTierANGLINRLIEENKMDLL-----GMVVVDELHMLGDSHRGYLLELLLTKicyitrKSASCQAD 256
Cdd:cd18036 93 SFGQIvkasDVIICT---PQILINNLLSGREEERVylsdfSLLIFDECHHTQKEHPYNKIMRMYLD------KKLSSQGP 163
|
170
....*....|....*....
gi 1622909152 257 LAsslsnavQIVGMSATLP 275
Cdd:cd18036 164 LP-------QILGLTASPG 175
|
|
| DNA_polA_I_Bacillus_like_exo |
cd06140 |
inactive DEDDy 3'-5' exonuclease domain of Bacillus stearothermophilus DNA polymerase I and ... |
1902-2087 |
8.01e-06 |
|
inactive DEDDy 3'-5' exonuclease domain of Bacillus stearothermophilus DNA polymerase I and similar family-A DNA polymerases; Bacillus stearothermophilus-like Polymerase I (Pol I), a subgroup of the family-A DNA polymerases, contains an inactive DnaQ-like 3'-5' exonuclease domain in the same polypeptide chain as the polymerase region. The exonuclease-like domain of these proteins possess the same fold as the Klenow fragment (KF) of Escherichia coli Pol I, but does not contain the four critical metal-binding residues necessary for activity. The function of this domain is unknown. It might act as a spacer between the polymerase and the 5'-3' exonuclease domains. Some members of this subgroup, such as those from Bacillus sphaericus and Thermus aquaticus, are thermostable DNA polymerases.
Pssm-ID: 176652 [Multi-domain] Cd Length: 178 Bit Score: 48.80 E-value: 8.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 1902 VVGLAVcWGGRDAYYFSLQKEQKHSEIsaslvppsldpsltLKDriWHlqsclrkeSDKECSVVIYDFIQSYkILLLSCG 1981
Cdd:cd06140 22 IIGLAL-ANGGGAYYIPLELALLDLAA--------------LKE--WL--------EDEKIPKVGHDAKRAY-VALKRHG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 1982 ISLEQSYEDPKVACWLLDPDSQEPTLHSIVTSFLPHELPLLEGmETSQGIQSLGLNAG--SEHSGRyRASVesilIFNSM 2059
Cdd:cd06140 76 IELAGVAFDTMLAAYLLDPTRSSYDLADLAKRYLGRELPSDEE-VYGKGAKFAVPDEEvlAEHLAR-KAAA----IARLA 149
|
170 180
....*....|....*....|....*...
gi 1622909152 2060 NQLNSLLQKENLQDVFRKVEMPSQYCLA 2087
Cdd:cd06140 150 PKLEEELEENEQLELYYEVELPLAEVLA 177
|
|
| SF2_C_suv3 |
cd18805 |
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene ... |
445-491 |
1.73e-05 |
|
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene encodes a DNA and RNA helicase, which is localized in mitochondria and is a subunit of the degradosome complex involved in regulation of RNA surveillance and turnover. SUV3 exhibits DNA and RNA-dependent ATPase, DNA and RNA-binding and DNA and RNA unwinding activities. SUV3 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: 350192 [Multi-domain] Cd Length: 135 Bit Score: 46.78 E-value: 1.73e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1622909152 445 VLAATSTLSSGVNLPARRVIIRTPI-FGGRPLDILT---YKQMAGRAGRKG 491
Cdd:cd18805 73 VLVASDAIGMGLNLNIRRVIFSSLSkFDGNEMRPLSpseVKQIAGRAGRFG 123
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
96-273 |
2.16e-05 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 46.90 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 96 KKMFEWQAECL--LLGQVLEG-KNLVYSAPTSAGKTLVAeLLILKRVLE--MRKKALFILPFVSVAKekkyylQSL--FQ 168
Cdd:pfam04851 2 LELRPYQIEAIenLLESIKNGqKRGLIVMATGSGKTLTA-AKLIARLFKkgPIKKVLFLVPRKDLLE------QALeeFK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 169 EVGIKVDGYMGSTSPSRHFSSLD---IAVCTIERANGLINRLIEENKMDLLGMVVVDElhmlgdSHRGyllellltkicy 245
Cdd:pfam04851 75 KFLPNYVEIGEIISGDKKDESVDdnkIVVTTIQSLYKALELASLELLPDFFDVIIIDE------AHRS------------ 136
|
170 180
....*....|....*....|....*...
gi 1622909152 246 itrkSASCQADLASSLSNAVQIvGMSAT 273
Cdd:pfam04851 137 ----GASSYRNILEYFKPAFLL-GLTAT 159
|
|
| DNA_pol_A_pol_I_A |
cd08642 |
Polymerase I functions primarily to fill DNA gaps that arise during DNA repair, recombination ... |
2311-2448 |
3.08e-05 |
|
Polymerase I functions primarily to fill DNA gaps that arise during DNA repair, recombination and replication; Family A polymerase (polymerase I) functions primarily to fill DNA gaps that arise during DNA repair, recombination and replication. DNA-dependent DNA polymerases can be classified in six main groups based upon phylogenetic relationships with E. coli polymerase I (classA), E. coli polymerase II (class B), E.coli polymerase III (class C), euryarchaaeota polymerase II (class D), human polymerase beta (class x), E. coli UmuC/DinB and eukaryotic RAP 30/Xeroderma pigmentosum variant (class Y). Family A polymerase are found primarily in organisms related to prokaryotes and include prokaryotic DNA polymerase I ,mitochondrial polymerase delta, and several bacteriphage polymerases including those from odd-numbered phage (T3, T5, and T7). Prokaryotic Pol Is have two functional domains located on the same polypeptide; a 5'-3' polymerase and 5'-3' exonuclease. Pol I uses its 5' nuclease activity to remove the ribonucleotide portion of newly synthesized Okazaki fragments and DNA polymerase activity to fill in the resulting gap. A combination of phylogenomic and signature sequence-based (or phonetic) approaches is used to understand the evolutionary relationships among bacteria. DNA polymerase I is one of the conserved proteins that is used to search for protein signatures. The structure of these polymerases resembles in overall morphology a cupped human right hand, with fingers (which bind an incoming nucleotide and interact with the single-stranded template), palm (which harbors the catalytic amino acid residues and also binds an incoming dNTP) and thumb (which binds double-stranded DNA) subdomains.
Pssm-ID: 176479 [Multi-domain] Cd Length: 378 Bit Score: 48.77 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 2311 PFSIS--MRHAFVPFPGGLILAADYSQLELRILAHLSHDRRLIQVLNTGADVFRSIAAewKM----IEPESVGDDLRQQA 2384
Cdd:cd08642 153 PDVLSqlIRTAFIPSEGHRFIVSDFSAIEARVIAWLAGEQWRLDVFATHGKIYEASAS--QMfgvpVEKIGKNSHLRQKG 230
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622909152 2385 K--------QICYGIIYGMGAKslgeQMGIKENDAACYIDSFKSRYTGINQFMRET---VKNCKRDGFVQTILGR 2448
Cdd:cd08642 231 KvaelalgyGGSVGALKAMGAL----EMGLTEDELPGIVDAWRNANPNIVKLWWDVdkaAKKAVKERKTVKLGGK 301
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
419-491 |
3.11e-05 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 49.33 E-value: 3.11e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622909152 419 VAFHHAGLTLEERDIIEGAFRQGLIRVLAATSTLSSGVNLPARRVIIRTPIfggrPLDILTYKQMAGRAGRKG 491
Cdd:PRK11057 263 AAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDI----PRNIESYYQETGRAGRDG 331
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
419-491 |
4.24e-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: 46.10 E-value: 4.24e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622909152 419 VAFHHAGLTLEERDIIEGAFRQGLIRVLAATSTLSSGVNLPA-RRVI-IrtpifgGRPLDILTYKQMAGRAGRKG 491
Cdd:cd18796 71 IALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDvDLVIqI------GSPKSVARLLQRLGRSGHRP 139
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
335-491 |
8.34e-05 |
|
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: 44.51 E-value: 8.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 335 LCYETIRDNH---SVLLFCPSKAWCEKLADiiarefynlhhqteglvkpsecppvnleqkellevmdQLRRLpsGLDSvl 411
Cdd:cd18794 19 DLLKRIKVEHlggSGIIYCLSRKECEQVAA-------------------------------------RLQSK--GISA-- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 412 qktvpwgvAFHHAGLTLEERDIIEGAFRQGLIRVLAATSTLSSGVNLPArrviIRTPIFGGRPLDILTYKQMAGRAGRKG 491
Cdd:cd18794 58 --------AAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPD----VRFVIHYSLPKSMESYYQESGRAGRDG 125
|
|
| DEXHc_RIG-I_DDX58 |
cd18073 |
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ... |
96-274 |
9.13e-05 |
|
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called DEAD box protein 58 (DDX58), is a pathogen-recognition receptor that recognizes viral 5'-triphosphates carrying double-stranded RNA. Upon binding to these microbe-associated molecular patterns (MAMPs), RIG-I forms oligomers and promotes downstream processes that result in type I interferon production and induction of an antiviral state. The optimal ligand for RIG-I has been found to be base-paired or double-stranded RNA (dsRNA) molecules containing a 5' triphosphate (5'-ppp-dsRNA). RIG-I contains two N-terminal caspase activation and recruitment domains (CARDs), which are required for interaction with IPS-1, a superfamily 2 helicase/translocase/ATPase (SF2) domain and a C-terminal regulatory/repressor domain (RD). RIG-I 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: 350831 [Multi-domain] Cd Length: 202 Bit Score: 45.97 E-value: 9.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 96 KKMFEWQAEclLLGQVLEGKNLVYSAPTSAGKTLVAeLLI----LKRVLEMRK-KALFILPFVSVAKEKKYYLQSLFQEV 170
Cdd:cd18073 1 FKPRNYQLE--LALPAMKGKNTIICAPTGCGKTFVS-LLIcehhLKKFPQGQKgKVVFFATKVPVYEQQKSVFSKYFERH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 171 GIKVDGYMGSTSPSRHFSSL----DIAVCTierANGLINRLI--EENKMDLLGMVVVDELHMLGDSHRgylLELLLTKic 244
Cdd:cd18073 78 GYRVTGISGATAENVPVEQIiennDIIILT---PQILVNNLKkgTIPSLSIFTLMIFDECHNTSGNHP---YNMIMFR-- 149
|
170 180 190
....*....|....*....|....*....|
gi 1622909152 245 YITRKsascqadLASSLSNAVQIVGMSATL 274
Cdd:cd18073 150 YLDQK-------LGGSSGPLPQIIGLTASV 172
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
112-225 |
2.57e-04 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 44.73 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 112 LEGKNLVYSAPTSAGKTLVAeLLILKRVLEM-----RKKALFILPFVSVAKEKKYYLQSLFQEVGIKVDGYMGSTSPS-- 184
Cdd:cd17927 15 LKGKNTIICLPTGSGKTFVA-VLICEHHLKKfpagrKGKVVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGDTSENvs 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1622909152 185 --RHFSSLDIAVCTierANGLINRLIEENKMDL--LGMVVVDELH 225
Cdd:cd17927 94 veQIVESSDVIIVT---PQILVNDLKSGTIVSLsdFSLLVFDECH 135
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
112-284 |
3.48e-04 |
|
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also called SKI2 or DHX13) plays a role in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. SKIV2L 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: 350785 [Multi-domain] Cd Length: 179 Bit Score: 43.79 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 112 LEGKNLVY-SAPTSAGKTLVAELLILKRVLEMrKKALFILPFVSVAKEKKYYLQSLFQEVGIKVDGYMGSTSPSRHFSSL 190
Cdd:cd18027 20 LEAGDSVFvAAHTSAGKTVVAEYAIALAQKHM-TRTIYTSPIKALSNQKFRDFKNTFGDVGLITGDVQLNPEASCLIMTT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 191 DIAVCTIERANGLInRLIEenkmdllgMVVVDELHMLGDSHRGYLLELLLTKicyitrksascqadlassLSNAVQIVGM 270
Cdd:cd18027 99 EILRSMLYNGSDVI-RDLE--------WVIFDEVHYINDAERGVVWEEVLIM------------------LPDHVSIILL 151
|
170
....*....|....
gi 1622909152 271 SATLPNLELVASWL 284
Cdd:cd18027 152 SATVPNTVEFADWI 165
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
445-502 |
3.62e-04 |
|
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: 41.15 E-value: 3.62e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622909152 445 VLAATSTLSSGVNLP-ARRVIIRTPIFGGRpldilTYKQMAGRAGRKGvDTVGESILIC 502
Cdd:cd18785 25 ILVATNVLGEGIDVPsLDTVIFFDPPSSAA-----SYIQRVGRAGRGG-KDEGEVILFV 77
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
81-402 |
5.09e-04 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 45.14 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 81 GLPKAVLEKYHSFGVKKMFEWQAECLLLgqVLEGKNLVYSAPTSAGKTLvAELL-ILKRVLEMRKK---ALFILP----F 152
Cdd:COG0513 8 GLSPPLLKALAELGYTTPTPIQAQAIPL--ILAGRDVLGQAQTGTGKTA-AFLLpLLQRLDPSRPRapqALILAPtrelA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 153 VSVAKEkkyyLQSLFQEVGIKVDGYMGSTSPSRHFSSL----DIAVCTIERangLINrLIEENKMDL--LGMVVVDE--- 223
Cdd:COG0513 85 LQVAEE----LRKLAKYLGLRVATVYGGVSIGRQIRALkrgvDIVVATPGR---LLD-LIERGALDLsgVETLVLDEadr 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 224 -LHMlgdshrGYLLEllLTKIcyitrksascqadlASSLSNAVQIVGMSATLPN--LELVASWLNAehyhtdfrpvPLLE 300
Cdd:COG0513 157 mLDM------GFIED--IERI--------------LKLLPKERQTLLFSATMPPeiRKLAKRYLKN----------PVRI 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 301 SVKVGNSIYDSsmklVREFepMLQVkgDEDHVVSLCYETIRDNH--SVLLFCPSKAWCEKLADIIAREFYN---LHhqte 375
Cdd:COG0513 205 EVAPENATAET----IEQR--YYLV--DKRDKLELLRRLLRDEDpeRAIVFCNTKRGADRLAEKLQKRGISaaaLH---- 272
|
330 340
....*....|....*....|....*..
gi 1622909152 376 GlvkpsecppvNLEQKELLEVMDQLRR 402
Cdd:COG0513 273 G----------DLSQGQRERALDAFRN 289
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
115-272 |
7.74e-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: 43.02 E-value: 7.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 115 KNLVYSAPTSAGKTLVAELLIlKRVLEM-------RKKALFILPFVSVAKEKKYYLQSlfqEVGIKVDGYMGSTSPS--- 184
Cdd:cd18034 17 RNTIVVLPTGSGKTLIAVMLI-KEMGELnrkeknpKKRAVFLVPTVPLVAQQAEAIRS---HTDLKVGEYSGEMGVDkwt 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 185 -----RHFSSLDIAVCTierANGLINRLIEEN-KMDLLGMVVVDELHMLGDSH--RgyllelLLTKICYITRKSASCQad 256
Cdd:cd18034 93 kerwkEELEKYDVLVMT---AQILLDALRHGFlSLSDINLLIFDECHHATGDHpyA------RIMKEFYHLEGRTSRP-- 161
|
170
....*....|....*.
gi 1622909152 257 lasslsnavQIVGMSA 272
Cdd:cd18034 162 ---------RILGLTA 168
|
|
| DEXQc_Suv3 |
cd17913 |
DEXQ-box helicase domain of Suv3; Suppressor of var1 3-like protein (Suv3) is a DNA/RNA ... |
122-234 |
1.03e-03 |
|
DEXQ-box helicase domain of Suv3; Suppressor of var1 3-like protein (Suv3) is a DNA/RNA unwinding enzyme belonging to the class of DexH-box helicases. It localizes predominantly in the mitochondria, where it forms an RNA-degrading complex called mitochondrial degradosome (mtEXO) with exonuclease PNP (polynucleotide phosphorylase), that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. Suv3 plays a role in the RNA surveillance system in mitochondria; it regulates the stability of mature mRNAs, the removal of aberrantly formed mRNAs and the rapid degradation of non coding processing intermediates. It also confers salinity and drought stress tolerance by maintaining both photosynthesis and antioxidant machinery, probably via an increase in plant hormone levels such as gibberellic acid (GA3), the cytokinin zeatin (Z), and indole-3-acetic acid (IAA). Suv3 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: 350671 [Multi-domain] Cd Length: 142 Bit Score: 41.77 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 122 PTSAGKTLVAelliLKRvLEMRKKALFILPFVSVAKEkkyyLQSLFQEVGIKVDGYMG----STSPSRHFSsldiavCTI 197
Cdd:cd17913 9 PTNSGKTYHA----LQR-LKSAKSGVYCGPLRLLAWE----VYERLNAEGVPCDLVTGqerrEVEGATHVS------CTV 73
|
90 100 110
....*....|....*....|....*....|....*..
gi 1622909152 198 ERANglINRLIEenkmdllgMVVVDELHMLGDSHRGY 234
Cdd:cd17913 74 EMAS--ISEPYD--------VAVIDEIQMIGDPQRGW 100
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
117-277 |
1.04e-03 |
|
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.
Pssm-ID: 273707 [Multi-domain] Cd Length: 359 Bit Score: 43.98 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 117 LVYSAPTSAGKTLVAeLLILKRVLEMRK--KALFILPFVSVAKEKKYYLQSLFqevGIKVDGYMGSTSPSRHFSSLD--- 191
Cdd:TIGR01587 2 LVIEAPTGYGKTEAA-LLWALHSIKSQKadRVIIALPTRATINAMYRRAKELF---GSELVGLHHSSSFSRIKEMGDsee 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 192 -------------------IAVCTIERANGLINRLIEENKMDLLGM----VVVDELHMLGDSHRGYLLELLltkicyitr 248
Cdd:TIGR01587 78 fehlfplyihsndklfldpITVCTIDQVLKSVFGEFGHYEFTLASIanslLIFDEVHFYDEYTLALILAVL--------- 148
|
170 180
....*....|....*....|....*....
gi 1622909152 249 ksaSCQADlasslsNAVQIVGMSATLPNL 277
Cdd:TIGR01587 149 ---EVLKD------NDVPILLMSATLPKF 168
|
|
| DEXHc_RLR-3 |
cd18075 |
DEXH-box helicase domain of RLR-3; RIG-I-like receptor 3 (RLR-3, also known as laboratory of ... |
112-225 |
1.66e-03 |
|
DEXH-box helicase domain of RLR-3; RIG-I-like receptor 3 (RLR-3, also known as laboratory of genetics and physiology 2 or LGP2 and DHX58) appears to positively and negatively regulate MDA5 and RIG-I signaling, respectively. RLR-3 resembles a chimera combining a MDA5-like helicase domain and RIG-I like CTD supporting both stem and end binding. RNA binding is required for RLR-3-mediated enhancement of MDA5 activation. RLR-3 end-binding may promote nucleation of MDA5 oligomerization on dsRNA. RLR-3 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: 350833 [Multi-domain] Cd Length: 200 Bit Score: 42.15 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 112 LEGKNLVYSAPTSAGKTLVAeLLILKRVLEMRKKALfilpfVSVAKEKKYYL-QSLFQEVGIKVDGYM-----GSTSPSR 185
Cdd:cd18075 15 LRGKNSIIWLPTGAGKTRAA-VYVARRHLETKRGAK-----VAVLVNKVHLVdQHLEKEFHVLLDKYTvtaisGDSSHKC 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1622909152 186 HFSSL----DIAVCTIERANGLINRLIEENKMDL--LGMVVVDELH 225
Cdd:cd18075 89 FFGQLargsDVVICTAQILQNALLSGEEEAHVELtdFSLLVIDECH 134
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
113-286 |
2.52e-03 |
|
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpB 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: 438711 [Multi-domain] Cd Length: 174 Bit Score: 41.16 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 113 EGKNLVYSAPTSAGKTLVAELLILKRVLEMRKKALFILPFVSVAKEKKYYLQSLFQE-----VGIKVDGYMGSTSPSRhf 187
Cdd:cd17990 16 AGGQVVLEAPPGAGKTTRVPLALLAELWIAGGKIIVLEPRRVAARAAARRLATLLGEapgetVGYRVRGESRVGRRTR-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 188 ssldIAVCTieraNG-LINRLIEENKMDLLGMVVVDELHmlgdsHRGYLLELLLtkicyitrksASCqADLASSLSNAVQ 266
Cdd:cd17990 94 ----VEVVT----EGvLLRRLQRDPELSGVGAVILDEFH-----ERSLDADLAL----------ALL-LEVQQLLRDDLR 149
|
170 180
....*....|....*....|
gi 1622909152 267 IVGMSATLPNLELVASWLNA 286
Cdd:cd17990 150 LLAMSATLDGDGLAALLPEA 169
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
419-491 |
2.56e-03 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 42.82 E-value: 2.56e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622909152 419 VAFHHAGLTLEERDIIEGAFRQGLIRVLAATSTLSSGVNLPArrviIRTPIFGGRPLDILTYKQMAGRAGRKG 491
Cdd:COG0514 257 AAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPD----VRFVIHYDLPKSIEAYYQEIGRAGRDG 325
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
118-228 |
4.85e-03 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 39.98 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 118 VYSAPTSAGKTLVAELLILKRvleMRKKALFILPFVSVA---KEKkyylqsLFQEVGIKVDGYMGSTSpSRHFSSLDIAV 194
Cdd:cd17926 22 ILVLPTGSGKTLTALALIAYL---KELRTLIVVPTDALLdqwKER------FEDFLGDSSIGLIGGGK-KKDFDDANVVV 91
|
90 100 110
....*....|....*....|....*....|....*.
gi 1622909152 195 CTIErangLINRLIEENKM--DLLGMVVVDELHMLG 228
Cdd:cd17926 92 ATYQ----SLSNLAEEEKDlfDQFGLLIVDEAHHLP 123
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
423-511 |
5.25e-03 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 41.74 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 423 HAGLTLEERDIIEGAFRQGLIRVLAATSTLSSGVNLPARRVIIRTPIfggrPLDILTYKQMAGRAGRKGVDTVGESILIC 502
Cdd:PTZ00424 298 HGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDL----PASPENYIHRIGRSGRFGRKGVAINFVTP 373
|
....*....
gi 1622909152 503 KNSEKSKGI 511
Cdd:PTZ00424 374 DDIEQLKEI 382
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
92-223 |
8.47e-03 |
|
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: 39.87 E-value: 8.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 92 SFGVKKMFEWQAECLLLgqVLEGKNLVYSAPTSAGKTL-----VAELLiLKRVLEMRKK---ALFILPFVSVAKEKKYYL 163
Cdd:cd17960 7 ELGFTSMTPVQAATIPL--FLSNKDVVVEAVTGSGKTLaflipVLEIL-LKRKANLKKGqvgALIISPTRELATQIYEVL 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622909152 164 QSLFQEVGIKVDG--YMGSTSPSRHFSSL-----DIAVCTIERANGLINRLIEENKMDLLGMVVVDE 223
Cdd:cd17960 84 QSFLEHHLPKLKCqlLIGGTNVEEDVKKFkrngpNILVGTPGRLEELLSRKADKVKVKSLEVLVLDE 150
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
111-227 |
9.04e-03 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 39.83 E-value: 9.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909152 111 VLEGKNLVYSAPTSAGKTLVAEL--LILKRVlemrkkALFILPFVSVAKEKKYYLQSLfqevGIKVDgYMGSTSPSRHFS 188
Cdd:cd17920 24 VLAGRDVLVVMPTGGGKSLCYQLpaLLLDGV------TLVVSPLISLMQDQVDRLQQL----GIRAA-ALNSTLSPEEKR 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1622909152 189 SLDIAV---------CTIERA--NGLINRLIEENKMDLLGMVVVDELHML 227
Cdd:cd17920 93 EVLLRIkngqykllyVTPERLlsPDFLELLQRLPERKRLALIVVDEAHCV 142
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