|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
1-472 |
0e+00 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 746.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 1 MLDQAESLLAHYFGYDSLRAGQKQAIQSVAEERkNTVCIMPTGGGKSICYQIPALLFEGTTIVISPLISLMKDQVDALEE 80
Cdd:COG0514 1 LRDDALEVLKRVFGYDSFRPGQEEIIEAVLAGR-DALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 81 AGIAAAYINSTQTSRDIHERLNGLKEGAYRLFYITPERLTSPEFIHILQNITVPLVAIDEAHCISQWGHDFRPSYRNIEI 160
Cdd:COG0514 80 AGIRAAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 161 LFNELKEPPVIiALTATATPEVHDDICKQLHINKEQTVYTGFARENLTFKVVKG--ENKDRFIEQYLERNKHEAGIIYTA 238
Cdd:COG0514 160 LRERLPNVPVL-ALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKppDDKLAQLLDFLKEHPGGSGIVYCL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 239 TRKETDRLYEKLKRSGINAGRYHGGLADDDRKDQQERFLNDQIQVMVATSAFGMGIDKSNIRFVLHAQIPKDMESYYQEA 318
Cdd:COG0514 239 SRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 319 GRAGRDGLNSECVLLFSAQDIMVQRFLIDQSAAGEEKQKQDLKKLRQMVDYCHTEDCLQRFILKYFGENEAEACGACGNC 398
Cdd:COG0514 319 GRAGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEERKRVERAKLDAMLAYAETTGCRRQFLLRYFGEELAEPCGNCDNC 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 989008095 399 TDTRSAHDVTKEAQMVLSCIIRMNERFGKTMVAQVLSGSKNKKVLENGFSSLSTYGIMKHQTAAEISDFIEFLI 472
Cdd:COG0514 399 LGPPETFDGTEAAQKALSCVYRTGQRFGAGHVIDVLRGSKNEKIRQFGHDKLSTYGIGKDLSDKEWRSVIRQLL 472
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
5-587 |
0e+00 |
|
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 residues long. This model represents bacterial proteins with a high degree of similarity in domain architecture and in primary sequence to E. coli RecQ. The model excludes eukaryotic and archaeal proteins with RecQ-like regions, as well as more distantly related bacterial helicases related to RecQ. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273594 [Multi-domain] Cd Length: 591 Bit Score: 734.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 5 AESLLAHYFGYDSLRAGQKQAIQSVAEERkNTVCIMPTGGGKSICYQIPALLFEGTTIVISPLISLMKDQVDALEEAGIA 84
Cdd:TIGR01389 1 AQQVLKRTFGYDDFRPGQEEIISHVLDGR-DVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 85 AAYINSTQTSRDIHERLNGLKEGAYRLFYITPERLTSPEFIHILQNITVPLVAIDEAHCISQWGHDFRPSYRNIEILFNE 164
Cdd:TIGR01389 80 AAYLNSTLSAKEQQDIEKALVNGELKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 165 LKEPPVIiALTATATPEVHDDICKQLHINKEQTVYTGFARENLTFKVVKGENKDRFIEQYLERNKHEAGIIYTATRKETD 244
Cdd:TIGR01389 160 FPQVPRI-ALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKNNKQKFLLDYLKKHRGQSGIIYASSRKKVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 245 RLYEKLKRSGINAGRYHGGLADDDRKDQQERFLNDQIQVMVATSAFGMGIDKSNIRFVLHAQIPKDMESYYQEAGRAGRD 324
Cdd:TIGR01389 239 ELAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 325 GLNSECVLLFSAQDIMVQRFLIDQSAAGEEKQKQDLKKLRQMVDYCHTEDCLQRFILKYFGENEAEACGACGNCTDTRSA 404
Cdd:TIGR01389 319 GLPAEAILLYSPADIALLKRRIEQSEADDDYKQIEREKLRAMIAYCETQTCRRAYILRYFGENEVEPCGNCDNCLDPPKS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 405 HDVTKEAQMVLSCIIRMNERFGKTMVAQVLSGSKNKKVLENGFSSLSTYGIMKHQTAAEISDFIEFLISDEYIRMAD--- 481
Cdd:TIGR01389 399 YDATVEAQKALSCVYRMGQRFGVGYIIEVLRGSKNDKILQKGHDQLSTYGIGKDYTQKEWRSLIDQLIAEGLLTENDeiy 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 482 ----GTFPTLMVTQKGRDVLLGKSAVARKE--ALQAAAVTENDE-LFEILRRLRKEIAAEQGVPPFVVFSDQTLKEMSAK 554
Cdd:TIGR01389 479 iglqLTEAARKVLKNEVEVLLRPFKVVAKEktRVQKNLSVGVDNaLFEALRELRKEQADEQNVPPYVIFSDSTLREMAEK 558
|
570 580 590
....*....|....*....|....*....|...
gi 989008095 555 LPKTDHDLLSVKGVGEQKRLKYGALFLEEIRNY 587
Cdd:TIGR01389 559 RPATLNALLKIKGVGQNKLDRYGEAFLEVIREY 591
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
4-588 |
0e+00 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 532.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 4 QAESLLAHYFGYDSLRAGQKQAIQSVAEERKNTVcIMPTGGGKSICYQIPALLFEGTTIVISPLISLMKDQVDALEEAGI 83
Cdd:PRK11057 12 LAKQVLQETFGYQQFRPGQQEIIDAVLSGRDCLV-VMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 84 AAAYINSTQTSRDIHERLNGLKEGAYRLFYITPERLTSPEFIHILQNITVPLVAIDEAHCISQWGHDFRPSYRNIEILFN 163
Cdd:PRK11057 91 AAACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPEYAALGQLRQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 164 ELKEPPViIALTATATPEVHDDICKQLHINKEQTVYTGFARENLTFKVVKgenKDRFIEQ---YLERNKHEAGIIYTATR 240
Cdd:PRK11057 171 RFPTLPF-MALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLVE---KFKPLDQlmrYVQEQRGKSGIIYCNSR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 241 KETDRLYEKLKRSGINAGRYHGGLADDDRKDQQERFLNDQIQVMVATSAFGMGIDKSNIRFVLHAQIPKDMESYYQEAGR 320
Cdd:PRK11057 247 AKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 321 AGRDGLNSECVLLFSAQDIMVQRFLIDQSAAGEEKQKQDlKKLRQMVDYCHTEDCLQRFILKYFGENEAEACGACGNCTD 400
Cdd:PRK11057 327 AGRDGLPAEAMLFYDPADMAWLRRCLEEKPAGQQQDIER-HKLNAMGAFAEAQTCRRLVLLNYFGEGRQEPCGNCDICLD 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 401 TRSAHDVTKEAQMVLSCIIRMNERFGKTMVAQVLSGSKNKKVLENGFSSLSTYGIMKHQTAAEISDFIEFLISDEYIRMA 480
Cdd:PRK11057 406 PPKQYDGLEDAQKALSCIYRVNQRFGMGYVVEVLRGANNQRIRDYGHDKLKVYGIGRDKSHEHWVSVIRQLIHLGLVTQN 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 481 DGTFPTLMVTQKGRDVLLGKS----AVARKEALQAAAVTEN------DELFEILRRLRKEIAAEQGVPPFVVFSDQTLKE 550
Cdd:PRK11057 486 IAQHSALQLTEAARPVLRGEVslqlAVPRIVALKPRAMQKSfggnydRKLFAKLRKLRKSIADEENIPPYVVFNDATLIE 565
|
570 580 590
....*....|....*....|....*....|....*...
gi 989008095 551 MSAKLPKTDHDLLSVKGVGEQKRLKYGALFLEEIRNYV 588
Cdd:PRK11057 566 MAEQMPITASEMLSVNGVGQRKLERFGKPFMALIRAHV 603
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
7-459 |
1.74e-159 |
|
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are known are 3'-5' DNA-DNA helicases. These proteins are used for recombination, recombinational repair, and possibly maintenance of chromosome stability. 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: 129701 [Multi-domain] Cd Length: 470 Bit Score: 464.63 E-value: 1.74e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 7 SLLAHYFGYDSLRAGQKQAIQSVAEERKNTVcIMPTGGGKSICYQIPALLFEGTTIVISPLISLMKDQVDALEEAGIAAA 86
Cdd:TIGR00614 1 KILKKYFGLSSFRPVQLEVINAVLLGRDCFV-VMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 87 YINSTQTSRDIHERLNGLKEGAYRLFYITPERL-TSPEFIHILQN-ITVPLVAIDEAHCISQWGHDFRPSYRNIEILFNE 164
Cdd:TIGR00614 80 FLNSAQTKEQQLNVLTDLKDGKIKLLYVTPEKIsASNRLLQTLEErKGITLIAVDEAHCISQWGHDFRPDYKALGSLKQK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 165 LKEPPvIIALTATATPEVHDDICKQLHINKEQTVYTGFARENLTFKVvkGENKDRFIEQYLE----RNKHEAGIIYTATR 240
Cdd:TIGR00614 160 FPNVP-VMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEV--RRKTPKILEDLLRfirkEFEGKSGIIYCPSR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 241 KETDRLYEKLKRSGINAGRYHGGLADDDRKDQQERFLNDQIQVMVATSAFGMGIDKSNIRFVLHAQIPKDMESYYQEAGR 320
Cdd:TIGR00614 237 KKVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 321 AGRDGLNSECVLLFSAQDI-MVQRFLIDQSaagEEKQKQDLKKLRQMVDYC-HTEDCLQRFILKYFGE--NEAEACGA-- 394
Cdd:TIGR00614 317 AGRDGLPSECHLFYAPADMnRLRRLLMEEP---DGNFRTYKLKLYEMMEYClNSSTCRRLILLSYFGEkgFNKSFCIMgt 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 989008095 395 ---CGNCtDTRSAH----------DVTKEAQMVLSCIIRMNERFGKTMVAQVLSGSKNKKVLENGFSSLSTYGIMKHQ 459
Cdd:TIGR00614 394 ekcCDNC-CKRLDYktkdvtdkvyDFGPQAQKALSAVGRLNQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLYGRGKDE 470
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
13-590 |
3.20e-104 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 340.72 E-value: 3.20e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 13 FGYDSLRAGQKQAIQSVAEErKNTVCIMPTGGGKSICYQIPALLFEGTTIVISPLISLMKDQVDALEEAGIAAAYINStq 92
Cdd:PLN03137 456 FGNHSFRPNQREIINATMSG-YDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQANIPAASLSA-- 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 93 tSRDIHERLNGLKE-----GAYRLFYITPERLT-SPEFIHILQNIT----VPLVAIDEAHCISQWGHDFRPSYRNIEILF 162
Cdd:PLN03137 533 -GMEWAEQLEILQElsseySKYKLLYVTPEKVAkSDSLLRHLENLNsrglLARFVIDEAHCVSQWGHDFRPDYQGLGILK 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 163 NELKEPPVIiALTATATPEVHDDICKQLHINKEQTVYTGFARENLTFKVVKGENK-----DRFIEqylERNKHEAGIIYT 237
Cdd:PLN03137 612 QKFPNIPVL-ALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPKTKKclediDKFIK---ENHFDECGIIYC 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 238 ATRKETDRLYEKLKRSGINAGRYHGGLADDDRKDQQERFLNDQIQVMVATSAFGMGIDKSNIRFVLHAQIPKDMESYYQE 317
Cdd:PLN03137 688 LSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQE 767
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 318 AGRAGRDGLNSECVLLFSAQDIMVQRFLIDQSAAGEEKQK--------------QDLKKLRQMVDYCHTE-DCLQRFILK 382
Cdd:PLN03137 768 CGRAGRDGQRSSCVLYYSYSDYIRVKHMISQGGVEQSPMAmgynrmassgrileTNTENLLRMVSYCENEvDCRRFLQLV 847
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 383 YFGEN-EAEACG-ACGNCTDTRS--AHDVTKEAQMVLSCIIRMNERFGKTMVAQVLSGSKNKKVLENGFSSLSTYGIMKH 458
Cdd:PLN03137 848 HFGEKfDSTNCKkTCDNCSSSKSliDKDVTEIARQLVELVKLTGERFSSAHILEVYRGSLNQYVKKHRHETLSLHGAGKH 927
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 459 QTAAEISDFIEFLISD----EYIRMAD--GTFPTLMVTQKGRDVLL---GKSAVAR------------KEALQA------ 511
Cdd:PLN03137 928 LSKGEASRILHYLVTEdilaEDVKKSDlyGSVSSLLKVNESKAYKLfsgGQTIIMRfpssvkaskpskFEATPAkgplts 1007
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 512 ----------AAVTEND-----ELFEILRRLRKEIAAE--QGVPPFVVFSDQTLKEMSAKLPKTDHDLLSVKGVGEQKRL 574
Cdd:PLN03137 1008 gkqstlpmatPAQPPVDlnlsaILYTALRKLRTALVKEagDGVMAYHIFGNATLQQISKRIPRTKEELLEINGLGKAKVS 1087
|
650
....*....|....*.
gi 989008095 575 KYGALFLEEIRNYVRE 590
Cdd:PLN03137 1088 KYGDRLLETIESTINE 1103
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
6-202 |
1.14e-98 |
|
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: 298.68 E-value: 1.14e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 6 ESLLAHYFGYDSLRAGQKQAIQSVaEERKNTVCIMPTGGGKSICYQIPALLFEGTTIVISPLISLMKDQVDALEEAGIAA 85
Cdd:cd17920 1 EQILKEVFGYDEFRPGQLEAINAV-LAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 86 AYINSTQTSRDIHERLNGLKEGAYRLFYITPERLTSPEFIHILQNIT----VPLVAIDEAHCISQWGHDFRPSYRNIEIL 161
Cdd:cd17920 80 AALNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLQRLPerkrLALIVVDEAHCVSQWGHDFRPDYLRLGRL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 989008095 162 FNELKEPPvIIALTATATPEVHDDICKQLHINKEQTVYTGF 202
Cdd:cd17920 160 RRALPGVP-ILALTATATPEVREDILKRLGLRNPVIFRASF 199
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
13-203 |
1.31e-71 |
|
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.
Pssm-ID: 350776 [Multi-domain] Cd Length: 201 Bit Score: 228.68 E-value: 1.31e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 13 FGYDSLRAGQKQAIQSVAEeRKNTVCIMPTGGGKSICYQIPALLFE----GTTIVISPLISLMKDQVDALEeAGIAAAYI 88
Cdd:cd18018 8 FGHPSFRPGQEEAIARLLS-GRSTLVVLPTGAGKSLCYQLPALLLRrrgpGLTLVVSPLIALMKDQVDALP-RAIKAAAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 89 NSTQTSRDIHERLNGLKEGAYRLFYITPERLTSPEFIHILQN-ITVPLVAIDEAHCISQWGHDFRPSYRNIEILFNELKE 167
Cdd:cd18018 86 NSSLTREERRRILEKLRAGEVKILYVSPERLVNESFRELLRQtPPISLLVVDEAHCISEWSHNFRPDYLRLCRVLRELLG 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 989008095 168 PPVIIALTATATPEVHDDICKQLHINKEQTVYTGFA 203
Cdd:cd18018 166 APPVLALTATATKRVVEDIASHLGIPESGVVRGPLY 201
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
204-334 |
2.90e-63 |
|
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: 204.36 E-value: 2.90e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 204 RENLTFKVVKGENKDRFI---EQYLERNKHEAGIIYTATRKETDRLYEKLKRSGINAGRYHGGLADDDRKDQQERFLNDQ 280
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLdllKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 989008095 281 IQVMVATSAFGMGIDKSNIRFVLHAQIPKDMESYYQEAGRAGRDGLNSECVLLF 334
Cdd:cd18794 81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
9-202 |
8.63e-63 |
|
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ATP-dependent helicase or WRN) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Werner's syndrome.
Pssm-ID: 350775 [Multi-domain] Cd Length: 193 Bit Score: 205.39 E-value: 8.63e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 9 LAHYFGYDSLRAGQKQAIQSVAEERKNTVCIMPTGGGKSICYQIPALLFEGTTIVISPLISLMKDQVDALEEAGIAAAYI 88
Cdd:cd18017 4 LNEYFGHSSFRPVQWKVIRSVLEERRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPACFL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 89 NSTQTSRDiherLNGLKEGAYRLFYITPERLTS-PEFIHILQNiTVPLVAIDEAHCISQWGHDFRPSYRNIEILFNELKE 167
Cdd:cd18017 84 GSAQSQNV----LDDIKMGKIRVIYVTPEFVSKgLELLQQLRN-GITLIAIDEAHCVSQWGHDFRSSYRHLGSIRNRLPN 158
|
170 180 190
....*....|....*....|....*....|....*
gi 989008095 168 PPvIIALTATATPEVHDDICKQLHINKEQTVYTGF 202
Cdd:cd18017 159 VP-IVALTATATPSVRDDIIKNLNLRNPQITCTSF 192
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
13-202 |
1.13e-56 |
|
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350773 [Multi-domain] Cd Length: 209 Bit Score: 189.88 E-value: 1.13e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 13 FGYDSLRAGQKQAIqSVAEERKNTVCIMPTGGGKSICYQIPALLFEGTTIVISPLISLMKDQVDALEEAGIAAAYINSTQ 92
Cdd:cd18015 14 FKLEKFRPLQLETI-NATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLGISATMLNASS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 93 TSRDIHERLNGLKEG--AYRLFYITPERLT-SPEFIHILQNI----TVPLVAIDEAHCISQWGHDFRPSYRNIEILFNEL 165
Cdd:cd18015 93 SKEHVKWVHAALTDKnsELKLLYVTPEKIAkSKRFMSKLEKAynagRLARIAIDEVHCCSQWGHDFRPDYKKLGILKRQF 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 989008095 166 KEPPvIIALTATATPEVHDDICKQLHINKEQTVYTGF 202
Cdd:cd18015 173 PNVP-ILGLTATATSKVLKDVQKILCIQKCLTFTASF 208
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
7-194 |
8.29e-52 |
|
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350772 [Multi-domain] Cd Length: 205 Bit Score: 176.51 E-value: 8.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 7 SLLAHYFGYDSLRAG-QKQAIQSVAEERKNTVCIMPTGGGKSICYQIPALLFEGTTIVISPLISLMKDQVDALEEAGIAA 85
Cdd:cd18014 2 STLKKVFGHSDFKSPlQEKATMAVVKGNKDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 86 AYINSTQTSRDIHERLNGLKEGA--YRLFYITPERLTSPEFIHILQNIT----VPLVAIDEAHCISQWGHDFRPSYRNIE 159
Cdd:cd18014 82 DSLNSKLSAQERKRIIADLESEKpqTKFLYITPEMAATSSFQPLLSSLVsrnlLSYLVVDEAHCVSQWGHDFRPDYLRLG 161
|
170 180 190
....*....|....*....|....*....|....*
gi 989008095 160 ILFNELKEPPViIALTATATPEVHDDICKQLHINK 194
Cdd:cd18014 162 ALRSRYGHVPW-VALTATATPQVQEDIFAQLRLKK 195
|
|
| DpdF |
NF041063 |
protein DpdF; |
8-339 |
2.18e-51 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 189.35 E-value: 2.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 8 LLAHYFGYDSLR-AGQKQAIQSV--AEERKNTVCIMPTGGGKSICYQIPALLF---EGTTIVISPLISLMKDQVDALEE- 80
Cdd:NF041063 130 FLAEALGFTHYRsPGQREAVRAAllAPPGSTLIVNLPTGSGKSLVAQAPALLAsrqGGLTLVVVPTVALAIDQERRAREl 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 81 ---AGIAA----AYI--NSTQTSRDIHERLnglKEGAYRLFYITPERLTSPefihiLQnitVPL-----------VAIDE 140
Cdd:NF041063 210 lrrAGPDLggplAWHggLSAEERAAIRQRI---RDGTQRILFTSPESLTGS-----LR---PALfdaaeagllryLVVDE 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 141 AHCISQWGHDFRPSYRNIEILFNEL------KEPPVIIALTATATPEvhddickQLHinkeqTVYTGFARENlTFKVVKG 214
Cdd:NF041063 279 AHLVDQWGDGFRPEFQLLAGLRRSLlrlapsGRPFRTLLLSATLTES-------TLD-----TLETLFGPPG-PFIVVSA 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 215 -----------------ENKDRFIEQ---YLERnkheAGIIYTATRKETDRLYEKLKRSGIN-AGRYHGGLADDDRKDQQ 273
Cdd:NF041063 346 vqlrpepaywvakcdseEERRERVLEalrHLPR----PLILYVTKVEDAEAWLQRLRAAGFRrVALFHGDTPDAERERLI 421
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 989008095 274 ERFLNDQIQVMVATSAFGMGIDKSNIRFVLHAQIPKDMESYYQEAGRAGRDGLNSECVLLFSAQDI 339
Cdd:NF041063 422 EQWRENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDL 487
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
13-202 |
1.97e-49 |
|
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom syndrome protein homolog or BLM) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations in RecQ2 cause Bloom syndrome.
Pssm-ID: 350774 [Multi-domain] Cd Length: 208 Bit Score: 170.39 E-value: 1.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 13 FGYDSLRAGQKQAIQSvAEERKNTVCIMPTGGGKSICYQIPALLFEGTTIVISPLISLMKDQVDALEEAGIAAAYINSTQ 92
Cdd:cd18016 13 FGLHQFRTNQLEAINA-ALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPATYLTGDK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 93 TSRD---IHERLnGLKEGAYRLFYITPERLT-SPEFIHILQNI-TVPLVA---IDEAHCISQWGHDFRPSYRNIeilfNE 164
Cdd:cd18016 92 TDAEatkIYLQL-SKKDPIIKLLYVTPEKISaSNRLISTLENLyERKLLArfvIDEAHCVSQWGHDFRPDYKRL----NM 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 989008095 165 LKE--PPV-IIALTATATPEVHDDICKQLHINKEQTVYTGF 202
Cdd:cd18016 167 LRQkfPSVpMMALTATATPRVQKDILNQLKMLRPQVFTMSF 207
|
|
| RQC |
smart00956 |
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix ... |
406-497 |
2.18e-35 |
|
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix structure; The RQC domain, found only in RecQ family enzymes, is a high affinity G4 DNA binding domain.
Pssm-ID: 214936 [Multi-domain] Cd Length: 92 Bit Score: 127.98 E-value: 2.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 406 DVTKEAQMVLSCIIRMNERFGKTMVAQVLSGSKNKKVLENGFSSLSTYGIMKHQTAAEISDFIEFLISDEYIRMADGTFP 485
Cdd:smart00956 1 DVTEEAQKLLSCVYRTGQRFGAGHVIDVLRGSKNKKIRQKGHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLREDGGRYP 80
|
90
....*....|..
gi 989008095 486 TLMVTQKGRDVL 497
Cdd:smart00956 81 YLKLTEKARPVL 92
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
406-507 |
4.26e-33 |
|
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix structure. The RQC domain, found only in RecQ family enzymes, is a high affinity G4 DNA binding domain.
Pssm-ID: 462780 [Multi-domain] Cd Length: 108 Bit Score: 122.26 E-value: 4.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 406 DVTKEAQMVLSCIIRMNERFGKTMVAQVLSGSKNKKVLENGFSSLSTYGIMKHQTAAEISDFIEFLISDEYIRMADGTFP 485
Cdd:pfam09382 6 DVTEEAQKILSCVYRTGQRFGAGHLIDVLRGSKNKKIRQLGHDKLSTFGIGKDLSKKEWRRIIRQLIAEGYLEVDIEFYS 85
|
90 100
....*....|....*....|..
gi 989008095 486 TLMVTQKGRDVLLGKSAVARKE 507
Cdd:pfam09382 86 VLKLTPKAREVLKGEEKVMLRV 107
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
11-204 |
7.04e-28 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 111.04 E-value: 7.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 11 HYFGYDSLRAGQKQAIQSVAEERKNTVCIMPTGGGKSICYQIPALLF-----EGTTIVISPLISLMKDQVDALEEAGIAA 85
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELKKLGPSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 86 AYINSTQTSRD-IHERLNGLKEGAYRLFYITPERLTSPEFIHILQNITVPLVAIDEAHCISQWGHdfrpsYRNIEILFNE 164
Cdd:smart00487 82 GLKVVGLYGGDsKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGF-----GDQLEKLLKL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 989008095 165 LKEPPVIIALTATATPEVHDDIckQLHINKEQTVYTGFAR 204
Cdd:smart00487 157 LPKNVQLLLLSATPPEEIENLL--ELFLNDPVFIDVGFTP 194
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
19-184 |
2.62e-27 |
|
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: 108.10 E-value: 2.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 19 RAGQKQAIQSVAEERkNTVCIMPTGGGKSICYQIPAL-----LFEGT-TIVISPLISLMKDQVDALEEAGIAAAY-INST 91
Cdd:pfam00270 1 TPIQAEAIPAILEGR-DVLVQAPTGSGKTLAFLLPALealdkLDNGPqALVLAPTRELAEQIYEELKKLGKGLGLkVASL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 92 QTSRDIHERLNGLKEgaYRLFYITPERLTSP-EFIHILQNITvpLVAIDEAHCISQWGhdFRPSYRNIeilFNELKEPPV 170
Cdd:pfam00270 80 LGGDSRKEQLEKLKG--PDILVGTPGRLLDLlQERKLLKNLK--LLVLDEAHRLLDMG--FGPDLEEI---LRRLPKKRQ 150
|
170
....*....|....
gi 989008095 171 IIALTATATPEVHD 184
Cdd:pfam00270 151 ILLLSATLPRNLED 164
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
17-355 |
9.25e-23 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 102.41 E-value: 9.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 17 SLRAGQKQAIQSVAEERKNT----VCIMPTGGGKSI----CYQipALLFEGTTIVISPLISLMKDQVDALEEAgiaaayi 88
Cdd:COG1061 80 ELRPYQQEALEALLAALERGggrgLVVAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRRELLEQWAEELRRF------- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 89 nstqtsRDIHERLNGLKEGAYRLFYITPERLTSPEFIHILQNiTVPLVAIDEAHcisqwgHDFRPSYRNIEILFNelkeP 168
Cdd:COG1061 151 ------LGDPLAGGGKKDSDAPITVATYQSLARRAHLDELGD-RFGLVIIDEAH------HAGAPSYRRILEAFP----A 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 169 PVIIALTATatPE---------------VH---------DDICKQLHI-------NKEQTVYTGFArENLTFKVVKG-EN 216
Cdd:COG1061 214 AYRLGLTAT--PFrsdgreillflfdgiVYeyslkeaieDGYLAPPEYygirvdlTDERAEYDALS-ERLREALAADaER 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 217 KDRFIEQYLERN-KHEAGIIYTATRKETDRLYEKLKRSGINAGRYHGGLADDDRKDQQERFLNDQIQVMVATSAFGMGID 295
Cdd:COG1061 291 KDKILRELLREHpDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVD 370
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 296 KSNIRFVLHAQIPKDMESYYQEAGRAGRDGLNSECVLLFsaqDIMVQRFLIDQSAAGEEK 355
Cdd:COG1061 371 VPRLDVAILLRPTGSPREFIQRLGRGLRPAPGKEDALVY---DFVGNDVPVLEELAKDLR 427
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
244-325 |
6.14e-22 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 89.96 E-value: 6.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 244 DRLYEKLKRSGINAGRYHGGLADDDRKDQQERFLNDQIQVMVATSAFGMGIDKSNIRFVLHAQIPKDMESYYQEAGRAGR 323
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 989008095 324 DG 325
Cdd:smart00490 81 AG 82
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
337-399 |
7.41e-22 |
|
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ.
Pssm-ID: 465031 [Multi-domain] Cd Length: 66 Bit Score: 89.27 E-value: 7.41e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 989008095 337 QDIMVQRFLIDQSAAGEEKQKQDLKKLRQMVDYC-HTEDCLQRFILKYFGEN-EAEACGACGNCT 399
Cdd:pfam16124 2 QDVVRLRFLIEQSEADEERKEVELQKLQAMVAYCeNTTDCRRKQLLRYFGEEfDSEPCGNCDNCL 66
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
519-584 |
9.04e-22 |
|
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic acid binding. Mutations in the HRDC domain cause human disease. It is interesting to note that the RecQ helicase in Deinococcus radiodurans has three tandem HRDC domains.
Pssm-ID: 425755 [Multi-domain] Cd Length: 68 Bit Score: 89.13 E-value: 9.04e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 989008095 519 ELFEILRRLRKEIAAEQGVPPFVVFSDQTLKEMSAKLPKTDHDLLSVKGVGEQKRLKYGALFLEEI 584
Cdd:pfam00570 3 ALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
515-592 |
7.68e-21 |
|
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the HRDC domain cause human disease.
Pssm-ID: 128635 [Multi-domain] Cd Length: 81 Bit Score: 86.97 E-value: 7.68e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 989008095 515 TENDELFEILRRLRKEIAAEQGVPPFVVFSDQTLKEMSAKLPKTDHDLLSVKGVGEQKRLKYGALFLEEIRNYVRETE 592
Cdd:smart00341 2 ERQLRLLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVIQEASDSPS 79
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
216-325 |
9.00e-21 |
|
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: 87.65 E-value: 9.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 216 NKDRFIEQYLERNKHEAGIIYTATRKETDrlYEKL-KRSGINAGRYHGGLADDDRKDQQERFLNDQIQVMVATSAFGMGI 294
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLE--AELLlEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
|
90 100 110
....*....|....*....|....*....|.
gi 989008095 295 DKSNIRFVLHAQIPKDMESYYQEAGRAGRDG 325
Cdd:pfam00271 79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
209-323 |
4.60e-19 |
|
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350174 [Multi-domain] Cd Length: 131 Bit Score: 83.33 E-value: 4.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 209 FKVVKGENK-DRFIEQYLERNKHEAGIIYTATRKETDRLYEKLKRSGINAGRYHGGLADDDRKDQQERFLNDQIQVMVAT 287
Cdd:cd18787 5 YVVVEEEEKkLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVAT 84
|
90 100 110
....*....|....*....|....*....|....*.
gi 989008095 288 SAFGMGIDKSNIRFVLHAQIPKDMESYYQEAGRAGR 323
Cdd:cd18787 85 DVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGR 120
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
169-338 |
6.76e-19 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 89.44 E-value: 6.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 169 PVIIALTATATPevHDDIckqlhinkEQTVYtgfarenltfkVVKGENKDRFIEQYLERNKHEAGIIYTATRKETDRLYE 248
Cdd:COG0513 201 PVRIEVAPENAT--AETI--------EQRYY-----------LVDKRDKLELLRRLLRDEDPERAIVFCNTKRGADRLAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 249 KLKRSGINAGRYHGGLADDDRKDQQERFLNDQIQVMVAT--SAfgMGIDKSNIRFVLHAQIPKDMESYYQEAG---RAGR 323
Cdd:COG0513 260 KLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATdvAA--RGIDIDDVSHVINYDLPEDPEDYVHRIGrtgRAGA 337
|
170
....*....|....*
gi 989008095 324 DGlnsECVLLFSAQD 338
Cdd:COG0513 338 EG---TAISLVTPDE 349
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
22-325 |
5.78e-18 |
|
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: 87.97 E-value: 5.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 22 QKQAIQSvAEERKNTVCIMPTGGGKSICYQIPALL-----FEGTTIVISPLISLMKDQVDALEE------AGI-AAAYIN 89
Cdd:COG1205 61 QAEAIEA-ARAGKNVVIATPTASGKSLAYLLPVLEalledPGATALYLYPTKALARDQLRRLRElaealgLGVrVATYDG 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 90 STqtsrDIHERLNGLKEGAYRLfyitperlTSPEFIHI------------LQNITvpLVAIDEAHcisqwghdfrpSYR- 156
Cdd:COG1205 140 DT----PPEERRWIREHPDIVL--------TNPDMLHYgllphhtrwarfFRNLR--YVVIDEAH-----------TYRg 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 157 ----NIEILFNELKE-------PPVIIALTAT-ATPEVHddiCKQLhINKEQTVYT--GFARENLTFKVVKGENKDRFIE 222
Cdd:COG1205 195 vfgsHVANVLRRLRRicrhygsDPQFILASATiGNPAEH---AERL-TGRPVTVVDedGSPRGERTFVLWNPPLVDDGIR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 223 QYLERnkhEA-------------GIIYTATRKETDRLYEKLKRSGINAGR------YHGGLADDDRKDQQERFLNDQIQV 283
Cdd:COG1205 271 RSALA---EAarlladlvreglrTLVFTRSRRGAELLARYARRALREPDLadrvaaYRAGYLPEERREIERGLRSGELLG 347
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 989008095 284 MVATSAFGMGIDKSNIRFVLHAQIPKDMESYYQEAGRAGRDG 325
Cdd:COG1205 348 VVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRG 389
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
133-325 |
3.20e-15 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 78.42 E-value: 3.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 133 VPLVAIDEAHCISQWGhdFRPSYRNIeILFNELKEPPVIIALTATATPEVHDdICKQLHINK---------------EQT 197
Cdd:PRK01297 238 VEVMVLDEADRMLDMG--FIPQVRQI-IRQTPRKEERQTLLFSATFTDDVMN-LAKQWTTDPaiveiepenvasdtvEQH 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 198 VYtgfarenltfkVVKGENKDRFIEQYLERNKHEAGIIYTATRKETDRLYEKLKRSGINAGRYHGGLADDDRKDQQERFL 277
Cdd:PRK01297 314 VY-----------AVAGSDKYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFR 382
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 989008095 278 NDQIQVMVATSAFGMGIDKSNIRFVLHAQIPKDMESYYQEAGRAGRDG 325
Cdd:PRK01297 383 EGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAG 430
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
234-325 |
1.27e-13 |
|
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: 68.44 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 234 IIYTATRKETDRLY----EKLKRSGINAGR---YHGGLADDDRKDQQERFLNDQIQVMVATSAFGMGIDKSNIRFVLHAQ 306
Cdd:cd18797 39 IVFCRSRKLAELLLrylkARLVEEGPLASKvasYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
|
90
....*....|....*....
gi 989008095 307 IPKDMESYYQEAGRAGRDG 325
Cdd:cd18797 119 YPGSLASLWQQAGRAGRRG 137
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
34-177 |
3.99e-12 |
|
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: 63.96 E-value: 3.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 34 KNTVCIMPTGGGKSICYQIPALL----FEGTTIVISPLISLMKDQVDALEEA---GIAAAYINStqtSRDIHERLNgLKE 106
Cdd:cd00046 2 ENVLITAPTGSGKTLAALLAALLlllkKGKKVLVLVPTKALALQTAERLRELfgpGIRVAVLVG---GSSAEEREK-NKL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 989008095 107 GAYRLFYITPERLTS---PEFIHILQNITVplVAIDEAHCISQWGHDFRPSYrniEILFNELKEPPVIIALTAT 177
Cdd:cd00046 78 GDADIIIATPDMLLNlllREDRLFLKDLKL--IIVDEAHALLIDSRGALILD---LAVRKAGLKNAQVILLSAT 146
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
208-325 |
9.06e-12 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 67.95 E-value: 9.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 208 TFKVVKGENKDRFIEQYLERNKHEAGIIYTATRKETDRLYEKLKRSGINAGRYHGGLADDDRKDQQERFLNDQIQVMVAT 287
Cdd:PRK11634 223 SYWTVWGMRKNEALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIAT 302
|
90 100 110
....*....|....*....|....*....|....*...
gi 989008095 288 SAFGMGIDKSNIRFVLHAQIPKDMESYYQEAGRAGRDG 325
Cdd:PRK11634 303 DVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAG 340
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
17-177 |
3.90e-10 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 58.84 E-value: 3.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 17 SLRAGQKQAIQSVAEERKN---TVCI-MPTGGGKSICY-QIPALLFE----GTTIVISPLISLMKDQVDALEEAGiaaay 87
Cdd:pfam04851 3 ELRPYQIEAIENLLESIKNgqkRGLIvMATGSGKTLTAaKLIARLFKkgpiKKVLFLVPRKDLLEQALEEFKKFL----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 88 INSTQTSRDIHERLNGLKEGAYRLFYITPERLTSPEFIHILQNI--TVPLVAIDEAHcisqwgHDFRPSYRNIEILFNel 165
Cdd:pfam04851 78 PNYVEIGEIISGDKKDESVDDNKIVVTTIQSLYKALELASLELLpdFFDVIIIDEAH------RSGASSYRNILEYFK-- 149
|
170
....*....|..
gi 989008095 166 kePPVIIALTAT 177
Cdd:pfam04851 150 --PAFLLGLTAT 159
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
181-333 |
5.12e-10 |
|
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: 58.33 E-value: 5.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 181 EVHDDICKQLHINKEQTVYTGFARENLTFKVvkgenkdrfIEQYleRNKHEAgIIYTATRKETDRLYEKLkrSGInaGRY 260
Cdd:cd18795 6 EEYVLGFNGLGIKLRVDVMNKFDSDIIVLLK---------IETV--SEGKPV-LVFCSSRKECEKTAKDL--AGI--AFH 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 261 HGGLADDDRKDQQERFLNDQIQVMVATSAFGMGID--------KSNIRFVlhaqiPKDME-----SYYQEAGRAGRDGLN 327
Cdd:cd18795 70 HAGLTREDRELVEELFREGLIKVLVATSTLAAGVNlpartviiKGTQRYD-----GKGYRelsplEYLQMIGRAGRPGFD 144
|
....*...
gi 989008095 328 S--ECVLL 333
Cdd:cd18795 145 TrgEAIIM 152
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
13-329 |
1.44e-09 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 60.68 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 13 FGYDSLRAGQKQAIQSVAEERKNTVCIMPTGGGKSICYQIPAL--LFEGTTIV-ISPLISL----MKDQVDALEEAGiaa 85
Cdd:COG1204 18 RGIEELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILkaLLNGGKALyIVPLRALasekYREFKRDFEELG--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 86 ayINSTQTSRDIHERLNGLKEgaYRLFYITPERLTS-----PEFIhilQNITvpLVAIDEAHCIsqwGHDFR-PsyrNIE 159
Cdd:COG1204 95 --IKVGVSTGDYDSDDEWLGR--YDILVATPEKLDSllrngPSWL---RDVD--LVVVDEAHLI---DDESRgP---TLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 160 ILFNELKE--PPV-IIALTAT------------ATPEVHDD---------ICKQLHINKEQTVYTGFARENLTFKVVKGE 215
Cdd:COG1204 160 VLLARLRRlnPEAqIVALSATignaeeiaewldAELVKSDWrpvplnegvLYDGVLRFDDGSRRSKDPTLALALDLLEEG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 216 -------NKDRFIEQYLER-----------------NKHEAGIIYTATRKETDRLYEKLKRSGInaGRYHGGLADDDRKD 271
Cdd:COG1204 240 gqvlvfvSSRRDAESLAKKladelkrrltpeereelEELAEELLEVSEETHTNEKLADCLEKGV--AFHHAGLPSELRRL 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 989008095 272 QQERFLNDQIQVMVATSAFGMGIdksNI---RFVLH-------AQIPKdMEsYYQEAGRAGRDGLNSE 329
Cdd:COG1204 318 VEDAFREGLIKVLVATPTLAAGV---NLparRVIIRdtkrggmVPIPV-LE-FKQMAGRAGRPGYDPY 380
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
279-333 |
8.58e-09 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 52.32 E-value: 8.58e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 989008095 279 DQIQVMVATSAFGMGIDKSNIRFVLHAQIPKDMESYYQEAGRAGRDG-LNSECVLL 333
Cdd:cd18785 21 SSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGkDEGEVILF 76
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
213-323 |
2.80e-08 |
|
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: 53.04 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 213 KGENKDRFIEQYLERN-KHEAGIIYTATRKETDRLYEKLKR------SGINAGRYHGGLADDDRKDQQERFLNDQIQVMV 285
Cdd:cd18796 20 AGESGADAYAEVIFLLeRHKSTLVFTNTRSQAERLAQRLRElcpdrvPPDFIALHHGSLSRELREEVEAALKRGDLKVVV 99
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 989008095 286 ATSAFGMGIDKSNIRFVLhaQI--PKDMESYYQEAGRAGR 323
Cdd:cd18796 100 ATSSLELGIDIGDVDLVI--QIgsPKSVARLLQRLGRSGH 137
|
|
| RQC_minor_1 |
NF041107 |
RQC-minor-1 family DNA-binding protein; The DNA-binding RQC domain (PF09382) appears primarily ... |
426-493 |
7.59e-08 |
|
RQC-minor-1 family DNA-binding protein; The DNA-binding RQC domain (PF09382) appears primarily in RecQ, a DNA helicase involved in recombination, replication, and repair. However, it appears also in this uncharacterized protein family, to which we give the name "RQC-minor-1 family DNA-binding protein." A majority of members contain an additional C-terminal predicted zinc-ribbon domain. Members appear not to show any conserved gene neighborhood.
Pssm-ID: 469031 [Multi-domain] Cd Length: 173 Bit Score: 52.57 E-value: 7.59e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 989008095 426 GKTMVAQVLSGSKNKKVLENGFSSLSTYGIMKHQTAAEISDFIEFLISDEYIRMA-DGTFPTLMVTQKG 493
Cdd:NF041107 22 GRTMLAKILKGSKDKKVLELGLDQCPAYGYYKSLTLEEITAKIDWMIKHDYLEIEyDGRLPLLVFTERG 90
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
115-325 |
7.92e-08 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 55.18 E-value: 7.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 115 TPERLTSPEFIHILQNITVPLVAIDEAHCISQWGhdFRPSYRNIeilFNELKEPPVIIaLTATATPEVhddickqlhink 194
Cdd:PLN00206 253 TPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERG--FRDQVMQI---FQALSQPQVLL-FSATVSPEV------------ 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 195 eQTVYTGFARENLTFKV----------------VKGENKDRFIEQYLERNKH--EAGIIYTATRKETDRLYEKL-KRSGI 255
Cdd:PLN00206 315 -EKFASSLAKDIILISIgnpnrpnkavkqlaiwVETKQKKQKLFDILKSKQHfkPPAVVFVSSRLGADLLANAItVVTGL 393
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 256 NAGRYHGGLADDDRKDQQERFLNDQIQVMVATSAFGMGIDKSNIRFVLHAQIPKDMESYYQEAGRAGRDG 325
Cdd:PLN00206 394 KALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMG 463
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
234-325 |
4.40e-07 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 52.85 E-value: 4.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 234 IIYTATRKETDRLYEKLKRSGINAGRYHGgladdDRKdQQER------FLNDQIQVMVATSAFGMGIDKSNIRFVLHAQI 307
Cdd:PTZ00110 381 LIFVETKKGADFLTKELRLDGWPALCIHG-----DKK-QEERtwvlneFKTGKSPIMIATDVASRGLDVKDVKYVINFDF 454
|
90
....*....|....*...
gi 989008095 308 PKDMESYYQEAGRAGRDG 325
Cdd:PTZ00110 455 PNQIEDYVHRIGRTGRAG 472
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
234-339 |
5.47e-07 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 52.14 E-value: 5.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 234 IIYTATRKETDRLYEKLKRSGINAGRYHGGLADDDRKDQQERFLNDQIQVMVATSAFGMGIDKSNIRFVLHAQIPKDMES 313
Cdd:PTZ00424 271 IIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPEN 350
|
90 100
....*....|....*....|....*.
gi 989008095 314 YYQEAGRAGRDGLNSECVLLFSAQDI 339
Cdd:PTZ00424 351 YIHRIGRSGRFGRKGVAINFVTPDDI 376
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
18-142 |
7.84e-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: 49.51 E-value: 7.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 18 LRAGQKQAIQSvAEERKNTVCIMPTGGGKSICYQIPAL--LFE---GTTIVISPLISLMKDQVDALEE------AGIAAA 86
Cdd:cd17923 1 LYSHQAEAIEA-ARAGRSVVVTTGTASGKSLCYQLPILeaLLRdpgSRALYLYPTKALAQDQLRSLRElleqlgLGIRVA 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 989008095 87 YINStQTSRDIHERlngLKEGAYRLFyitperLTSPEFIH------------ILQNITvpLVAIDEAH 142
Cdd:cd17923 80 TYDG-DTPREERRA---IIRNPPRIL------LTNPDMLHyallphhdrwarFLRNLR--YVVLDEAH 135
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
22-146 |
1.81e-06 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 48.41 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 22 QKQAIQSVAEERKNTVCIMPTGGGKSIC--YQIPALL--FEGTTIVISPLISLMKDQVDALEEAgIAAAYINSTQTSRDI 97
Cdd:cd17921 6 QREALRALYLSGDSVLVSAPTSSGKTLIaeLAILRALatSGGKAVYIAPTRALVNQKEADLRER-FGPLGKNVGLLTGDP 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 989008095 98 heRLNGLKEGAYRLFYITPERL-----TSPEFihILQNITvpLVAIDEAHCISQ 146
Cdd:cd17921 85 --SVNKLLLAEADILVATPEKLdlllrNGGER--LIQDVR--LVVVDEAHLIGD 132
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
18-177 |
1.85e-06 |
|
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: 47.69 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 18 LRAGQKQAIQSVAEERKNT--VCIMPTGGGKSIC-YQIPALLFEGTTIVISPLISLMKDQVDALEEAGIAAAY------I 88
Cdd:cd17926 1 LRPYQEEALEAWLAHKNNRrgILVLPTGSGKTLTaLALIAYLKELRTLIVVPTDALLDQWKERFEDFLGDSSIgligggK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 89 NSTQTSRDIherLNGLKEGAYRLFYitPERLTSPEFIHILqnitvplvaIDEAHCIS--QWGHdfrpsyrnieiLFNELK 166
Cdd:cd17926 81 KKDFDDANV---VVATYQSLSNLAE--EEKDLFDQFGLLI---------VDEAHHLPakTFSE-----------ILKELN 135
|
170
....*....|.
gi 989008095 167 EPPViIALTAT 177
Cdd:cd17926 136 AKYR-LGLTAT 145
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
221-333 |
2.52e-06 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 50.50 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 221 IEQYLERNKHEAGIIYTATRKETDRLYEKLKRSGINAGRYHG--------GLADDDRKDQQERFLNDQIQVMVATSAFGM 292
Cdd:COG1111 344 LKEQLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGqaskegdkGLTQKEQIEILERFRAGEFNVLVATSVAEE 423
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 989008095 293 GID-------------KSNIRFVlhaqipkdmesyyQEAGRAGRDGLNSECVLL 333
Cdd:COG1111 424 GLDipevdlvifyepvPSEIRSI-------------QRKGRTGRKREGRVVVLI 464
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
15-338 |
3.74e-06 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 49.88 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 15 YDSLRAGQKQAIQSVaEERKNTVCIMPTGGGK------SICYQIPALLFEGT------TIVISPLISLMKDQVDALEE-- 80
Cdd:PRK13767 30 FGTFTPPQRYAIPLI-HEGKNVLISSPTGSGKtlaaflAIIDELFRLGREGEledkvyCLYVSPLRALNNDIHRNLEEpl 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 81 AGIAAAYINSTQTSRDI-----------HERLNGLKEGAYRLFyITPER----LTSPEFIHILQniTVPLVAIDEAHCIS 145
Cdd:PRK13767 109 TEIREIAKERGEELPEIrvairtgdtssYEKQKMLKKPPHILI-TTPESlailLNSPKFREKLR--TVKWVIVDEIHSLA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 146 QwghdfrpSYR------NIEILFNELKEPPVIIALTATATP--EV--------HDDICKQLHInkeqtVYTGFAREnLTF 209
Cdd:PRK13767 186 E-------NKRgvhlslSLERLEELAGGEFVRIGLSATIEPleEVakflvgyeDDGEPRDCEI-----VDARFVKP-FDI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 210 KVV----------KGENKDRFIEQYLER-NKHEAGIIYTATRKETDRLYEKLKR------SGINAGRYHGGLADDDRKDQ 272
Cdd:PRK13767 253 KVIspvddlihtpAEEISEALYETLHELiKEHRTTLIFTNTRSGAERVLYNLRKrfpeeyDEDNIGAHHSSLSREVRLEV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 273 QERFLNDQIQVMVATSAFGMGIDKSNIRFVLHAQIPKDMESYYQEAGRAG---------------RDGLnSEC-VLLFSA 336
Cdd:PRK13767 333 EEKLKRGELKVVVSSTSLELGIDIGYIDLVVLLGSPKSVSRLLQRIGRAGhrlgevskgriivvdRDDL-VECaVLLKKA 411
|
..
gi 989008095 337 QD 338
Cdd:PRK13767 412 RE 413
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
203-323 |
1.36e-05 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 47.88 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 203 ARENLTFKV--VKGENKDRFIEQYLERNKHEAGIIYTATRKETDRLYEKLKRSGINAGRYHGGLADDDRKDQQERFLNDQ 280
Cdd:PRK10590 216 ASEQVTQHVhfVDKKRKRELLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGD 295
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 989008095 281 IQVMVATSAFGMGIDKSNIRFVLHAQIPKDMESYYQEAGRAGR 323
Cdd:PRK10590 296 IRVLVATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGR 338
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
231-341 |
2.25e-05 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 47.24 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 231 EAGIIYTATRKETDRLYEKLKRSGINAGRYHGGLADDDRKDQQERFLNDQIQVMVATSAFGMGIDKSNIRFVLHAQIPKD 310
Cdd:PRK11192 246 TRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRS 325
|
90 100 110
....*....|....*....|....*....|.
gi 989008095 311 MESYYQEAGRAGRDGLNSECVLLFSAQDIMV 341
Cdd:PRK11192 326 ADTYLHRIGRTGRAGRKGTAISLVEAHDHLL 356
|
|
| Rnd |
COG0349 |
Ribonuclease D [Translation, ribosomal structure and biogenesis]; |
523-585 |
1.46e-04 |
|
Ribonuclease D [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440118 [Multi-domain] Cd Length: 365 Bit Score: 44.48 E-value: 1.46e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 989008095 523 ILRRL---RKEIAAEQGVPPFVVFSDQTLKEMSAKLPKTDHDLLSVKGVGEQKRLKYGALFLEEIR 585
Cdd:COG0349 212 VLRELaawREREARKRDVPRNRVLKDEALLELARRQPKSLEELARLRGLSPGEIRRHGEELLAAVA 277
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
219-295 |
1.60e-04 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 41.69 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 219 RFIEQYLERNKHEAG--IIYTATRKETDRLYEKLKRSGINAGRYHGGLADDDRKDQQERFLND-QIQVM-VATSAFGMGI 294
Cdd:cd18793 14 EALLELLEELREPGEkvLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDpDIRVFlLSTKAGGVGL 93
|
.
gi 989008095 295 D 295
Cdd:cd18793 94 N 94
|
|
| DinG |
COG1199 |
Rad3-related DNA helicase DinG [Replication, recombination and repair]; |
4-65 |
1.94e-04 |
|
Rad3-related DNA helicase DinG [Replication, recombination and repair];
Pssm-ID: 440812 [Multi-domain] Cd Length: 629 Bit Score: 44.53 E-value: 1.94e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 989008095 4 QAESLLAHYFGYDSLRAGQKQAIQSVA---EERKNTVCIMPTGGGKSICYQIPALLF---EGTTIVIS 65
Cdd:COG1199 1 ADDGLLALAFPGFEPRPGQREMAEAVAralAEGRHLLIEAGTGTGKTLAYLVPALLAareTGKKVVIS 68
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
210-333 |
3.56e-04 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 41.56 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 210 KVVKGENKD---RFIEQYLERNkHEAGIIYTATrKETDRL--------YEKLK---RSGINAGRYHGGLADDDRKDQQER 275
Cdd:cd18811 5 YLIFHTRLDkvyEFVREEIAKG-RQAYVIYPLI-EESEKLdlkaavamYEYLKerfRPELNVGLLHGRLKSDEKDAVMAE 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 989008095 276 FLNDQIQVMVATSAFGMGIDKSNI---------RFVLhAQIpkdmesyYQEAGRAGRDGLNSECVLL 333
Cdd:cd18811 83 FREGEVDILVSTTVIEVGVDVPNAtvmviedaeRFGL-SQL-------HQLRGRVGRGDHQSYCLLV 141
|
|
| SF2_C_suv3 |
cd18805 |
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene ... |
251-329 |
7.30e-04 |
|
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: 39.85 E-value: 7.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 251 KRSGINAGRYHGGLADDDRKDQQERFlNDQ---IQVMVATSAFGMG--------IDKSNIRFVLHAQIPKDMESYYQEAG 319
Cdd:cd18805 39 KRTGLKCAVIYGALPPETRRQQARLF-NDPesgYDVLVASDAIGMGlnlnirrvIFSSLSKFDGNEMRPLSPSEVKQIAG 117
|
90
....*....|
gi 989008095 320 RAGRDGLNSE 329
Cdd:cd18805 118 RAGRFGSHFP 127
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
257-352 |
1.35e-03 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 41.83 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 257 AGRYHGGLADDDRKDQQERFLNDQIQVMVATSAFGMGIDKSNIRFVLHAQIPKDMESYYQEAGRAGRD--GLNSECVLLF 334
Cdd:PRK09751 304 ARSHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAGHQvgGVSKGLFFPR 383
|
90
....*....|....*...
gi 989008095 335 SAQDIMVQRFLIDQSAAG 352
Cdd:PRK09751 384 TRRDLVDSAVIVECMFAG 401
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
234-294 |
1.85e-03 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 41.36 E-value: 1.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 989008095 234 IIYTATRKETDRLYEKLKRSGINAGRYHGGLADDDRKDQQERFLNDQ--IQVMVATSAFGMGI 294
Cdd:COG0553 553 LVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGGEGL 615
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
221-325 |
1.94e-03 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 41.40 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 221 IEQYLERNKHEAGIIYTATRKETDRLYEKLKRSGINAGRYHG-GLADDDR----KDQQE---RFLNDQIQVMVATSAFGM 292
Cdd:PRK13766 356 VKEQLGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGqASKDGDKgmsqKEQIEildKFRAGEFNVLVSTSVAEE 435
|
90 100 110
....*....|....*....|....*....|....
gi 989008095 293 GIDKSNIRFVL-HAQIPKDMESyYQEAGRAGRDG 325
Cdd:PRK13766 436 GLDIPSVDLVIfYEPVPSEIRS-IQRKGRTGRQE 468
|
|
| dinG |
PRK11747 |
ATP-dependent DNA helicase DinG; Provisional |
19-65 |
4.72e-03 |
|
ATP-dependent DNA helicase DinG; Provisional
Pssm-ID: 236966 [Multi-domain] Cd Length: 697 Bit Score: 39.81 E-value: 4.72e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 989008095 19 RAGQKQAIQSVA------EERKNTVCIM--PTGGGKSICYQIPAL---LFEGTTIVIS 65
Cdd:PRK11747 27 RAGQRQMIAEVAktlageYLKDGRILVIeaGTGVGKTLSYLLAGIpiaRAEKKKLVIS 84
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
22-177 |
5.51e-03 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 38.08 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 22 QKQAIQSVAEERKNTVCIMPTGGGKSICYQ---IPALLFEGTTIVISPLISLMKDQVD---ALEEAGIAAAYinstqTSR 95
Cdd:cd18028 6 QAEAVRAGLLKGENLLISIPTASGKTLIAEmamVNTLLEGGKALYLVPLRALASEKYEefkKLEEIGLKVGI-----STG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 989008095 96 DIHERLNGLKEgaYRLFYITPERLTSpefihILQNIT-----VPLVAIDEAHCISQWGHDFRpsyrnIEILFNELKEP-- 168
Cdd:cd18028 81 DYDEDDEWLGD--YDIIVATYEKFDS-----LLRHSPswlrdVGVVVVDEIHLISDEERGPT-----LESIVARLRRLnp 148
|
170
....*....|
gi 989008095 169 -PVIIALTAT 177
Cdd:cd18028 149 nTQIIGLSAT 158
|
|
| |
