|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
1-466 |
0e+00 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 768.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 1 MRETLKTYFGYDNFRPLQEEIIRHILNKQDALVLMPTGGGKSICYQLPALLCEGTAVVVSPLISLMKDQVEALLANGIAA 80
Cdd:COG0514 5 ALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGIRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 81 GALNSSNDETENANLRRACIEGRLKLLYISPEKLLAEK-DYLLRDMNISLFAIDEAHCISQWGHDFRPEYTQMGVLHQQF 159
Cdd:COG0514 85 AFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRfLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGELRERL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 160 PQIPIVALTATADKITREDIVRQLHLNHPRTFISSFDRPNISLTVKRGfQAKEKNKAILEFIHRHGEESGIIYCMSRSKT 239
Cdd:COG0514 165 PNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPK-PPDDKLAQLLDFLKEHPGGSGIVYCLSRKKV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 240 ETVAQMLQKQGIRCGVYHAGLSTQHRDETQNDFINDRIQVVCATIAFGMGIDKSNVRWVIHYNLPKSIESFYQEIGRAGR 319
Cdd:COG0514 244 EELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 320 DGLPSNTVLFYSLGDLILLTKFASESN----QQNINLEKLQRMQQYAEADICRRRILLSYFGETTTEDCGNCDVCKNPPQ 395
Cdd:COG0514 324 DGLPAEALLLYGPEDVAIQRFFIEQSPpdeeRKRVERAKLDAMLAYAETTGCRRQFLLRYFGEELAEPCGNCDNCLGPPE 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495301113 396 RFDGTVIVQKALSAIARTEQQISTGVLIDILRGNYSAEVTGKGYQELKTFGAGRDIPPRDWQDYLLQMLQL 466
Cdd:COG0514 404 TFDGTEAAQKALSCVYRTGQRFGAGHVIDVLRGSKNEKIRQFGHDKLSTYGIGKDLSDKEWRSVIRQLLAQ 474
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
1-598 |
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: 704.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 1 MRETLKTYFGYDNFRPLQEEIIRHILNKQDALVLMPTGGGKSICYQLPALLCEGTAVVVSPLISLMKDQVEALLANGIAA 80
Cdd:TIGR01389 1 AQQVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 81 GALNSSNDETENANLRRACIEGRLKLLYISPEKLlaEKDYLLR---DMNISLFAIDEAHCISQWGHDFRPEYTQMGVLHQ 157
Cdd:TIGR01389 81 AYLNSTLSAKEQQDIEKALVNGELKLLYVAPERL--EQDYFLNmlqRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 158 QFPQIPIVALTATADKITREDIVRQLHLNHPRTFISSFDRPNISLTVKRGFQakeKNKAILEFIHRHGEESGIIYCMSRS 237
Cdd:TIGR01389 159 RFPQVPRIALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKNN---KQKFLLDYLKKHRGQSGIIYASSRK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 238 KTETVAQMLQKQGIRCGVYHAGLSTQHRDETQNDFINDRIQVVCATIAFGMGIDKSNVRWVIHYNLPKSIESFYQEIGRA 317
Cdd:TIGR01389 236 KVEELAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 318 GRDGLPSNTVLFYSLGDLILLTKFASESN----QQNINLEKLQRMQQYAEADICRRRILLSYFGETTTEDCGNCDVCKNP 393
Cdd:TIGR01389 316 GRDGLPAEAILLYSPADIALLKRRIEQSEadddYKQIEREKLRAMIAYCETQTCRRAYILRYFGENEVEPCGNCDNCLDP 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 394 PQRFDGTVIVQKALSAIARTEQQISTGVLIDILRGNYSAEVTGKGYQELKTFGAGRDIPPRDWQDYLLQMLQLGYFEIAY 473
Cdd:TIGR01389 396 PKSYDATVEAQKALSCVYRMGQRFGVGYIIEVLRGSKNDKILQKGHDQLSTYGIGKDYTQKEWRSLIDQLIAEGLLTEND 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 474 NENNHLKITSSGSDVLFGRTQAALvviqheeAVTRKGKKKKVVIAKELpfgaAGGESQDLFEALRGLRKQLADQEALPAY 553
Cdd:TIGR01389 476 EIYIGLQLTEAARKVLKNEVEVLL-------RPFKVVAKEKTRVQKNL----SVGVDNALFEALRELRKEQADEQNVPPY 544
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 495301113 554 IVLSDKVLHLLCISRPTTIEEFGEISGIGEHKKKKYGKDFVNLIR 598
Cdd:TIGR01389 545 VIFSDSTLREMAEKRPATLNALLKIKGVGQNKLDRYGEAFLEVIR 589
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
3-602 |
0e+00 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 617.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 3 ETLKTYFGYDNFRPLQEEIIRHILNKQDALVLMPTGGGKSICYQLPALLCEGTAVVVSPLISLMKDQVEALLANGIAAGA 82
Cdd:PRK11057 15 QVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVAAAC 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 83 LNSSNDETENANLRRACIEGRLKLLYISPEKLLAEkDYL--LRDMNISLFAIDEAHCISQWGHDFRPEYTQMGVLHQQFP 160
Cdd:PRK11057 95 LNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMD-NFLehLAHWNPALLAVDEAHCISQWGHDFRPEYAALGQLRQRFP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 161 QIPIVALTATADKITREDIVRQLHLNHPRTFISSFDRPNISLTVKRGFQAKEKnkaILEFIHRHGEESGIIYCMSRSKTE 240
Cdd:PRK11057 174 TLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLVEKFKPLDQ---LMRYVQEQRGKSGIIYCNSRAKVE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 241 TVAQMLQKQGIRCGVYHAGLSTQHRDETQNDFINDRIQVVCATIAFGMGIDKSNVRWVIHYNLPKSIESFYQEIGRAGRD 320
Cdd:PRK11057 251 DTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRD 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 321 GLPSNTVLFYSLGDLILLTKFASE---SNQQNINLEKLQRMQQYAEADICRRRILLSYFGETTTEDCGNCDVCKNPPQRF 397
Cdd:PRK11057 331 GLPAEAMLFYDPADMAWLRRCLEEkpaGQQQDIERHKLNAMGAFAEAQTCRRLVLLNYFGEGRQEPCGNCDICLDPPKQY 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 398 DGTVIVQKALSAIARTEQQISTGVLIDILRGNYSAEVTGKGYQELKTFGAGRDIPPRDWQDYLLQMLQLGYFEIAYNENN 477
Cdd:PRK11057 411 DGLEDAQKALSCIYRVNQRFGMGYVVEVLRGANNQRIRDYGHDKLKVYGIGRDKSHEHWVSVIRQLIHLGLVTQNIAQHS 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 478 HLKITSSGSDVLFGRTQAALVVIQHEEAVTRKGKKKkvviakelpfgAAGGESQDLFEALRGLRKQLADQEALPAYIVLS 557
Cdd:PRK11057 491 ALQLTEAARPVLRGEVSLQLAVPRIVALKPRAMQKS-----------FGGNYDRKLFAKLRKLRKSIADEENIPPYVVFN 559
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 495301113 558 DKVLHLLCISRPTTIEEFGEISGIGEHKKKKYGKDFVNLIRQFVE 602
Cdd:PRK11057 560 DATLIEMAEQMPITASEMLSVNGVGQRKLERFGKPFMALIRAHVD 604
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
5-450 |
0e+00 |
|
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: 562.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 5 LKTYFGYDNFRPLQEEIIRHILNKQDALVLMPTGGGKSICYQLPALLCEGTAVVVSPLISLMKDQVEALLANGIAAGALN 84
Cdd:TIGR00614 3 LKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATFLN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 85 SSNDETENANLRRACIEGRLKLLYISPEKLLAEKDYLLR---DMNISLFAIDEAHCISQWGHDFRPEYTQMGVLHQQFPQ 161
Cdd:TIGR00614 83 SAQTKEQQLNVLTDLKDGKIKLLYVTPEKISASNRLLQTleeRKGITLIAVDEAHCISQWGHDFRPDYKALGSLKQKFPN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 162 IPIVALTATADKITREDIVRQLHLNHPRTFISSFDRPNISLTVKRgfqaKEKNKA--ILEFIHRHGE-ESGIIYCMSRSK 238
Cdd:TIGR00614 163 VPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRR----KTPKILedLLRFIRKEFEgKSGIIYCPSRKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 239 TETVAQMLQKQGIRCGVYHAGLSTQHRDETQNDFINDRIQVVCATIAFGMGIDKSNVRWVIHYNLPKSIESFYQEIGRAG 318
Cdd:TIGR00614 239 VEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRAG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 319 RDGLPSNTVLFYSLGDLILLTKFASE---SNQQNINLEKLQRMQQYAEADICRRRILLSYFGET----------TTEDCG 385
Cdd:TIGR00614 319 RDGLPSECHLFYAPADMNRLRRLLMEepdGNFRTYKLKLYEMMEYCLNSSTCRRLILLSYFGEKgfnksfcimgTEKCCD 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495301113 386 NCDVCKN------PPQRFDGTVIVQKALSAIARTEQQISTGVLIDILRGNYSAEVTGKGYQELKTFGAGRD 450
Cdd:TIGR00614 399 NCCKRLDyktkdvTDKVYDFGPQAQKALSAVGRLNQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLYGRGKD 469
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
6-590 |
2.53e-122 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 389.64 E-value: 2.53e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 6 KTYFGYDNFRPLQEEIIRHILNKQDALVLMPTGGGKSICYQLPALLCEGTAVVVSPLISLMKDQVEALLANGIAAGALNS 85
Cdd:PLN03137 453 KKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQANIPAASLSA 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 86 SNDETENAN-LRRACIE-GRLKLLYISPEKLlAEKDYLLRDMNI-------SLFAIDEAHCISQWGHDFRPEYTQMGVLH 156
Cdd:PLN03137 533 GMEWAEQLEiLQELSSEySKYKLLYVTPEKV-AKSDSLLRHLENlnsrgllARFVIDEAHCVSQWGHDFRPDYQGLGILK 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 157 QQFPQIPIVALTATADKITREDIVRQLHLNHPRTFISSFDRPNISLTVKrgfqakEKNKAILEFIHR-----HGEESGII 231
Cdd:PLN03137 612 QKFPNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVV------PKTKKCLEDIDKfikenHFDECGII 685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 232 YCMSRSKTETVAQMLQKQGIRCGVYHAGLSTQHRDETQNDFINDRIQVVCATIAFGMGIDKSNVRWVIHYNLPKSIESFY 311
Cdd:PLN03137 686 YCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYH 765
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 312 QEIGRAGRDGLPSNTVLFYSLGDLILL------------------TKFASESNQQNINLEKLQRMQQYAEADI-CRRRIL 372
Cdd:PLN03137 766 QECGRAGRDGQRSSCVLYYSYSDYIRVkhmisqggveqspmamgyNRMASSGRILETNTENLLRMVSYCENEVdCRRFLQ 845
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 373 LSYFGET-TTEDCGN-CDVCKNPPQRF--DGTVIVQKALSAIARTEQQISTGVLIDILRGNYSAEVTGKGYQELKTFGAG 448
Cdd:PLN03137 846 LVHFGEKfDSTNCKKtCDNCSSSKSLIdkDVTEIARQLVELVKLTGERFSSAHILEVYRGSLNQYVKKHRHETLSLHGAG 925
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 449 RDIPPRD---------WQDYLLQMLQLGyfEIAYNENNHLKITSSGSDVLFGRTQAALVVIQHEEAVTRKGK------KK 513
Cdd:PLN03137 926 KHLSKGEasrilhylvTEDILAEDVKKS--DLYGSVSSLLKVNESKAYKLFSGGQTIIMRFPSSVKASKPSKfeatpaKG 1003
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 514 KVVIAKE--LPFGAAGGESQD------LFEALRGLRKQLADQ--EALPAYIVLSDKVLHLLCISRPTTIEEFGEISGIGE 583
Cdd:PLN03137 1004 PLTSGKQstLPMATPAQPPVDlnlsaiLYTALRKLRTALVKEagDGVMAYHIFGNATLQQISKRIPRTKEELLEINGLGK 1083
|
....*..
gi 495301113 584 HKKKKYG 590
Cdd:PLN03137 1084 AKVSKYG 1090
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
2-196 |
7.13e-106 |
|
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: 317.17 E-value: 7.13e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 2 RETLKTYFGYDNFRPLQEEIIRHILNKQDALVLMPTGGGKSICYQLPALLCEGTAVVVSPLISLMKDQVEALLANGIAAG 81
Cdd:cd17920 1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 82 ALNSSNDETENANLRRACIEGRLKLLYISPEKLLAEK-----DYLLRDMNISLFAIDEAHCISQWGHDFRPEYTQMGVLH 156
Cdd:cd17920 81 ALNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDflellQRLPERKRLALIVVDEAHCVSQWGHDFRPDYLRLGRLR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495301113 157 QQFPQIPIVALTATADKITREDIVRQLHLNHPRTFISSFD 196
Cdd:cd17920 161 RALPGVPILALTATATPEVREDILKRLGLRNPVIFRASFD 200
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
2-196 |
1.57e-71 |
|
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: 228.79 E-value: 1.57e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 2 RETLKTYFGYDNFRPLQEEIIRHILNKQDALVLMPTGGGKSICYQLPALLCEGTAVVVSPLISLMKDQVEALLANGIAAG 81
Cdd:cd18015 7 KDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLGISAT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 82 ALNSSNDeTENANLRRACIEGR---LKLLYISPEKLLAEKDYL--LRDMN----ISLFAIDEAHCISQWGHDFRPEYTQM 152
Cdd:cd18015 87 MLNASSS-KEHVKWVHAALTDKnseLKLLYVTPEKIAKSKRFMskLEKAYnagrLARIAIDEVHCCSQWGHDFRPDYKKL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495301113 153 GVLHQQFPQIPIVALTATADKITREDIVRQLHLNHPRTFISSFD 196
Cdd:cd18015 166 GILKRQFPNVPILGLTATATSKVLKDVQKILCIQKCLTFTASFN 209
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
5-196 |
4.37e-68 |
|
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: 219.26 E-value: 4.37e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 5 LKTYFGYDNFRPLQEEIIRHIL-NKQDALVLMPTGGGKSICYQLPALLCEGTAVVVSPLISLMKDQVEALLANGIAAGAL 83
Cdd:cd18017 4 LNEYFGHSSFRPVQWKVIRSVLeERRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPACFL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 84 NSSndetENANLRRACIEGRLKLLYISPEKLLAEKdYLLRDMN--ISLFAIDEAHCISQWGHDFRPEYTQMGVLHQQFPQ 161
Cdd:cd18017 84 GSA----QSQNVLDDIKMGKIRVIYVTPEFVSKGL-ELLQQLRngITLIAIDEAHCVSQWGHDFRSSYRHLGSIRNRLPN 158
|
170 180 190
....*....|....*....|....*....|....*
gi 495301113 162 IPIVALTATADKITREDIVRQLHLNHPRTFISSFD 196
Cdd:cd18017 159 VPIVALTATATPSVRDDIIKNLNLRNPQITCTSFD 193
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
3-183 |
3.58e-64 |
|
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: 209.42 E-value: 3.58e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 3 ETLKTYFGYDNFRPLQEEIIRHILNKQDALVLMPTGGGKSICYQLPALL----CEGTAVVVSPLISLMKDQVEALLAnGI 78
Cdd:cd18018 2 KLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLlrrrGPGLTLVVSPLIALMKDQVDALPR-AI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 79 AAGALNSSNDETENANLRRACIEGRLKLLYISPEKLLAE--KDYLLRDMNISLFAIDEAHCISQWGHDFRPEYTQMGVLH 156
Cdd:cd18018 81 KAAALNSSLTREERRRILEKLRAGEVKILYVSPERLVNEsfRELLRQTPPISLLVVDEAHCISEWSHNFRPDYLRLCRVL 160
|
170 180
....*....|....*....|....*...
gi 495301113 157 QQFPQI-PIVALTATADKITREDIVRQL 183
Cdd:cd18018 161 RELLGApPVLALTATATKRVVEDIASHL 188
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
1-196 |
1.12e-62 |
|
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: 205.83 E-value: 1.12e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 1 MRETLKTYFGYDNFRPLQEEIIRHILNKQDALVLMPTGGGKSICYQLPALLCEGTAVVVSPLISLMKDQVEALLANGIAA 80
Cdd:cd18016 5 MMKIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 81 GALNSSNDETENANLRRACIEGR--LKLLYISPEKLLAEKDYL--LRDMN----ISLFAIDEAHCISQWGHDFRPEYTQM 152
Cdd:cd18016 85 TYLTGDKTDAEATKIYLQLSKKDpiIKLLYVTPEKISASNRLIstLENLYerklLARFVIDEAHCVSQWGHDFRPDYKRL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495301113 153 GVLHQQFPQIPIVALTATADKITREDIVRQLHLNHPRTFISSFD 196
Cdd:cd18016 165 NMLRQKFPSVPMMALTATATPRVQKDILNQLKMLRPQVFTMSFN 208
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
197-330 |
3.62e-62 |
|
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: 201.67 E-value: 3.62e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 197 RPNISLTVKRGFQAKEKNKAILEFIHRHGEESGIIYCMSRSKTETVAQMLQKQGIRCGVYHAGLSTQHRDETQNDFINDR 276
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 495301113 277 IQVVCATIAFGMGIDKSNVRWVIHYNLPKSIESFYQEIGRAGRDGLPSNTVLFY 330
Cdd:cd18794 81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
2-188 |
6.97e-57 |
|
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: 190.38 E-value: 6.97e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 2 RETLKTYFGYDNFR-PLQEEIIRHILNK-QDALVLMPTGGGKSICYQLPALLCEGTAVVVSPLISLMKDQVEALLANGIA 79
Cdd:cd18014 1 RSTLKKVFGHSDFKsPLQEKATMAVVKGnKDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 80 AGALNSSNDETENA----NLRRAciEGRLKLLYISPE--------KLLAEkdyLLRDMNISLFAIDEAHCISQWGHDFRP 147
Cdd:cd18014 81 VDSLNSKLSAQERKriiaDLESE--KPQTKFLYITPEmaatssfqPLLSS---LVSRNLLSYLVVDEAHCVSQWGHDFRP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 495301113 148 EYTQMGVLHQQFPQIPIVALTATADKITREDIVRQLHLNHP 188
Cdd:cd18014 156 DYLRLGALRSRYGHVPWVALTATATPQVQEDIFAQLRLKKP 196
|
|
| DpdF |
NF041063 |
protein DpdF; |
5-335 |
4.70e-52 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 191.28 E-value: 4.70e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 5 LKTYFGYDNFR-PLQEEIIRHILN-KQDA--LVLMPTGGGKSICYQLPALLC---EGTAVVVSPLISLMKDQVEALLANG 77
Cdd:NF041063 131 LAEALGFTHYRsPGQREAVRAALLaPPGStlIVNLPTGSGKSLVAQAPALLAsrqGGLTLVVVPTVALAIDQERRARELL 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 78 IAAG-------ALNSSNDETENANLRRACIEGRLKLLYISPEKL----------LAEKDYLlrdmniSLFAIDEAHCISQ 140
Cdd:NF041063 211 RRAGpdlggplAWHGGLSAEERAAIRQRIRDGTQRILFTSPESLtgslrpalfdAAEAGLL------RYLVVDEAHLVDQ 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 141 WGHDFRPEYTQMGVL-----HQQFPQIPI--VALTATadkITREDI--VRQLhLNHPRTFI---SSFDRPNISLTVKRGF 208
Cdd:NF041063 285 WGDGFRPEFQLLAGLrrsllRLAPSGRPFrtLLLSAT---LTESTLdtLETL-FGPPGPFIvvsAVQLRPEPAYWVAKCD 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 209 QAKEKNKAILEFIhRHGEESGIIYCMSRSKTETVAQMLQKQGI-RCGVYHAGLSTQHRDETQNDFINDRIQVVCATIAFG 287
Cdd:NF041063 361 SEEERRERVLEAL-RHLPRPLILYVTKVEDAEAWLQRLRAAGFrRVALFHGDTPDAERERLIEQWRENELDIVVATSAFG 439
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 495301113 288 MGIDKSNVRWVIHYNLPKSIESFYQEIGRAGRDGLPSNTVLFYSLGDL 335
Cdd:NF041063 440 LGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDL 487
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
393-500 |
1.64e-26 |
|
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: 103.77 E-value: 1.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 393 PPQRFDGTVIVQKALSAIARTEQQISTGVLIDILRGNYSAEVTGKGYQELKTFGAGRDIPPRDWQDYLLQMLQLGYFEIA 472
Cdd:pfam09382 1 PPETVDVTEEAQKILSCVYRTGQRFGAGHLIDVLRGSKNKKIRQLGHDKLSTFGIGKDLSKKEWRRIIRQLIAEGYLEVD 80
|
90 100
....*....|....*....|....*...
gi 495301113 473 YNENNHLKITSSGSDVLFGRTQAALVVI 500
Cdd:pfam09382 81 IEFYSVLKLTPKAREVLKGEEKVMLRVP 108
|
|
| RQC |
smart00956 |
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix ... |
398-489 |
1.60e-25 |
|
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: 100.63 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 398 DGTVIVQKALSAIARTEQQISTGVLIDILRGNYSAEVTGKGYQELKTFGAGRDIPPRDWQDYLLQMLQLGYFEIAYNENN 477
Cdd:smart00956 1 DVTEEAQKLLSCVYRTGQRFGAGHVIDVLRGSKNKKIRQKGHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLREDGGRYP 80
|
90
....*....|..
gi 495301113 478 HLKITSSGSDVL 489
Cdd:smart00956 81 YLKLTEKARPVL 92
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
15-173 |
2.57e-25 |
|
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: 102.32 E-value: 2.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 15 RPLQEEIIRHILNKQDALVLMPTGGGKSICYQLPAL------LCEGTAVVVSPLISLMKDQVEALLANGIAAG-----AL 83
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKLGKGLGlkvasLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 84 NSSNDETENANLRRAciegrlKLLYISPEKLLAEKDYLLRDMNISLFAIDEAHCISQWGhdFRPEYTQMgvLHQQFPQIP 163
Cdd:pfam00270 81 GGDSRKEQLEKLKGP------DILVGTPGRLLDLLQERKLLKNLKLLVLDEAHRLLDMG--FGPDLEEI--LRRLPKKRQ 150
|
170
....*....|
gi 495301113 164 IVALTATADK 173
Cdd:pfam00270 151 ILLLSATLPR 160
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
240-321 |
9.80e-25 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 98.05 E-value: 9.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 240 ETVAQMLQKQGIRCGVYHAGLSTQHRDETQNDFINDRIQVVCATIAFGMGIDKSNVRWVIHYNLPKSIESFYQEIGRAGR 319
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 495301113 320 DG 321
Cdd:smart00490 81 AG 82
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
212-321 |
3.79e-24 |
|
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: 97.28 E-value: 3.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 212 EKNKAILEFIHRHGEESGIIYCMSRSKTETvAQMLQKQGIRCGVYHAGLSTQHRDETQNDFINDRIQVVCATIAFGMGID 291
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 495301113 292 KSNVRWVIHYNLPKSIESFYQEIGRAGRDG 321
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
8-198 |
6.32e-24 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 99.87 E-value: 6.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 8 YFGYDNFRPLQEEIIRHIL-NKQDALVLMPTGGGKSICYQLPALLC-----EGTAVVVSPLISLMKDQVEALLA-----N 76
Cdd:smart00487 3 KFGFEPLRPYQKEAIEALLsGLRDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELKKlgpslG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 77 GIAAGALNSSNDETEnanlRRACIEGRLKLLYISPEKLLAE-KDYLLRDMNISLFAIDEAHCISQWGhdFRPEYtqMGVL 155
Cdd:smart00487 83 LKVVGLYGGDSKREQ----LRKLESGKTDILVTTPGRLLDLlENDKLSLSNVDLVILDEAHRLLDGG--FGDQL--EKLL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495301113 156 HQQFPQIPIVALTATADKITREDIvrQLHLNHPRTFISSFDRP 198
Cdd:smart00487 155 KLLPKNVQLLLLSATPPEEIENLL--ELFLNDPVFIDVGFTPL 195
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
213-319 |
1.06e-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: 85.25 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 213 KNKAILEFIHRHGEESGIIYCMSRSKTETVAQMLQKQGIRCGVYHAGLSTQHRDETQNDFINDRIQVVCATIAFGMGIDK 292
Cdd:cd18787 14 KLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVATDVAARGLDI 93
|
90 100
....*....|....*....|....*..
gi 495301113 293 SNVRWVIHYNLPKSIESFYQEIGRAGR 319
Cdd:cd18787 94 PGVDHVINYDLPRDAEDYVHRIGRTGR 120
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
30-170 |
4.22e-18 |
|
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: 4.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 30 DALVLMPTGGGKSICYQLPALL----CEGTAVVVSPLISLMKDQVEAL---LANGIAAGALNSSndetENANLRRACIEG 102
Cdd:cd00046 3 NVLITAPTGSGKTLAALLAALLlllkKGKKVLVLVPTKALALQTAERLrelFGPGIRVAVLVGG----SSAEEREKNKLG 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 103 RLKLLYISPEKL--LAEKDYLLRDMNISLFAIDEAHCISQWGHDFRPEYTQmgVLHQQFPQIPIVALTAT 170
Cdd:cd00046 79 DADIIIATPDMLlnLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLA--VRKAGLKNAQVILLSAT 146
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
211-371 |
4.44e-18 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 86.74 E-value: 4.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 211 KEKNKAILEFIHRHGEESGIIYCMSRSKTETVAQMLQKQGIRCGVYHAGLSTQHRDETQNDFINDRIQVVCAT-IAfGMG 289
Cdd:COG0513 226 RDKLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATdVA-ARG 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 290 IDKSNVRWVIHYNLPKSIESFYQEIG---RAGRDGLpsnTVLFYSLGDLILLTKFASESNQqninleKLQRMQQYAEADI 366
Cdd:COG0513 305 IDIDDVSHVINYDLPEDPEDYVHRIGrtgRAGAEGT---AISLVTPDERRLLRAIEKLIGQ------KIEEEELPGFEPV 375
|
....*
gi 495301113 367 CRRRI 371
Cdd:COG0513 376 EEKRL 380
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
530-597 |
2.09e-17 |
|
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: 76.81 E-value: 2.09e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495301113 530 SQDLFEALRGLRKQLADQEALPAYIVLSDKVLHLLCISRPTTIEEFGEISGIGEHKKKKYGKDFVNLI 597
Cdd:pfam00570 1 QLALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
332-391 |
5.42e-17 |
|
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: 75.40 E-value: 5.42e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495301113 332 LGDLILLTKFASESN----QQNINLEKLQRMQQYAEADI-CRRRILLSYFGET-TTEDCGNCDVCK 391
Cdd:pfam16124 1 YQDVVRLRFLIEQSEadeeRKEVELQKLQAMVAYCENTTdCRRKQLLRYFGEEfDSEPCGNCDNCL 66
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
9-322 |
7.20e-17 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 83.79 E-value: 7.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 9 FGYDNFRPLQEEIIRHILNKQDALVL-MPTGGGKSICYQLP---ALLCEGTAVVVSPLISL---MKDQVEALLAN----- 76
Cdd:COG1204 18 RGIEELYPPQAEALEAGLLEGKNLVVsAPTASGKTLIAELAilkALLNGGKALYIVPLRALaseKYREFKRDFEElgikv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 77 GIAAGALNSSNDETENANlrraciegrlkLLYISPEKLlaekDYLLRD-----MNISLFAIDEAHCIsqwGHDFRpeytq 151
Cdd:COG1204 98 GVSTGDYDSDDEWLGRYD-----------ILVATPEKL----DSLLRNgpswlRDVDLVVVDEAHLI---DDESR----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 152 mGV--------LHQQFPQIPIVALTATADKItrEDIVRQLhlnhPRTFISSFDRP---------NISLTVKRGfqAKEKN 214
Cdd:COG1204 155 -GPtlevllarLRRLNPEAQIVALSATIGNA--EEIAEWL----DAELVKSDWRPvplnegvlyDGVLRFDDG--SRRSK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 215 KAILEFIHRHGEESG--IIYCMSRSKTETVAQMLQK-----------------------------------QGIRCGV-- 255
Cdd:COG1204 226 DPTLALALDLLEEGGqvLVFVSSRRDAESLAKKLADelkrrltpeereeleelaeellevseethtneklaDCLEKGVaf 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495301113 256 YHAGLSTQHRDETQNDFINDRIQVVCAT--IAFGMGIDKSNVrwVIH-----YNLPKSIESFYQEIGRAGRDGL 322
Cdd:COG1204 306 HHAGLPSELRRLVEDAFREGLIKVLVATptLAAGVNLPARRV--IIRdtkrgGMVPIPVLEFKQMAGRAGRPGY 377
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
10-329 |
3.23e-16 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 82.20 E-value: 3.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 10 GYDNFRPLQEEIIRHILNKQDALVLMPTGGGKSICYQLPaLLCEGTAVVVSPLISLMKDQVEalLANGIAAgALNSSNDE 89
Cdd:PRK11634 25 GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLP-LLHNLDPELKAPQILVLAPTRE--LAVQVAE-AMTDFSKH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 90 TENANL------------RRACIEGRlKLLYISPEKLLaekDYLLR---DM-NISLFAIDEAHcisqwghdfrpEYTQMG 153
Cdd:PRK11634 101 MRGVNVvalyggqrydvqLRALRQGP-QIVVGTPGRLL---DHLKRgtlDLsKLSGLVLDEAD-----------EMLRMG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 154 VLHQQ---FPQIPIVALTATADKITREDIVR--QLHLNHP---RTFISSFDRPNISLTVKRGFQAKeKNKAILEFIHRHG 225
Cdd:PRK11634 166 FIEDVetiMAQIPEGHQTALFSATMPEAIRRitRRFMKEPqevRIQSSVTTRPDISQSYWTVWGMR-KNEALVRFLEAED 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 226 EESGIIYCMSRSKTETVAQMLQKQGIRCGVYHAGLSTQHRDETQNDFINDRIQVVCATIAFGMGIDKSNVRWVIHYNLPK 305
Cdd:PRK11634 245 FDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPM 324
|
330 340
....*....|....*....|....
gi 495301113 306 SIESFYQEIGRAGRDGLPSNTVLF 329
Cdd:PRK11634 325 DSESYVHRIGRTGRAGRAGRALLF 348
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
18-328 |
4.54e-16 |
|
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: 81.81 E-value: 4.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 18 QEEIIRHILNKQDALVLMPTGGGKSICYQLPALLC-----EGTAVVVSPLISLMKDQVEAL------LANGIAAGALNSS 86
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEAlledpGATALYLYPTKALARDQLRRLrelaeaLGLGVRVATYDGD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 87 NDETEnanlRRACIE-GRLklLYISPEKL----LAEKDY---LLRdmNISLFAIDEAHcisqwghdfrpEYTqmGVL--H 156
Cdd:COG1205 141 TPPEE----RRWIREhPDI--VLTNPDMLhyglLPHHTRwarFFR--NLRYVVIDEAH-----------TYR--GVFgsH 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 157 --------QQF-------PQIpiVALTAT-------ADKITREDIV-------RQlhlnHPRTFIssFDRPNISLTVKRG 207
Cdd:COG1205 200 vanvlrrlRRIcrhygsdPQF--ILASATignpaehAERLTGRPVTvvdedgsPR----GERTFV--LWNPPLVDDGIRR 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 208 FQAKEKNKAILEFIHRHGeeSGIIYCMSRSKTETVAQMLQKQ------GIRCGVYHAGLSTQHRDETQNDFINDRIQVVC 281
Cdd:COG1205 272 SALAEAARLLADLVREGL--RTLVFTRSRRGAELLARYARRAlrepdlADRVAAYRAGYLPEERREIERGLRSGELLGVV 349
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 495301113 282 ATIAFGMGIDKSNVRWVIHYNLPKSIESFYQEIGRAGRDGLPSNTVL 328
Cdd:COG1205 350 STNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVL 396
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
10-329 |
1.79e-14 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 76.37 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 10 GYDNFRPLQEEIIRHILNKQDALVLMPTGGGKSICYQLPALL-C------------EGTAVVVSP---LISLMKDQVEaL 73
Cdd:PLN00206 140 GYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISrCctirsghpseqrNPLAMVLTPtreLCVQVEDQAK-V 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 74 LANGIA-AGALNSSNDETENANLRracIEGRLKLLYISPEKL---LAEKDYLLRdmNISLFAIDEAHCISQWGhdFRPEY 149
Cdd:PLN00206 219 LGKGLPfKTALVVGGDAMPQQLYR---IQQGVELIVGTPGRLidlLSKHDIELD--NVSVLVLDEVDCMLERG--FRDQV 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 150 TQmgvLHQQFPQIPIVALTAT--------ADKITREDIVrqLHLNHPRtfissfdRPNISltVKR---GFQAKEKNKAIL 218
Cdd:PLN00206 292 MQ---IFQALSQPQVLLFSATvspevekfASSLAKDIIL--ISIGNPN-------RPNKA--VKQlaiWVETKQKKQKLF 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 219 EFI--HRHGEESGIIYCMSRSKTETVAQMLQK-QGIRCGVYHAGLSTQHRDETQNDFINDRIQVVCATIAFGMGIDKSNV 295
Cdd:PLN00206 358 DILksKQHFKPPAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRV 437
|
330 340 350
....*....|....*....|....*....|....
gi 495301113 296 RWVIHYNLPKSIESFYQEIGRAGRDGLPSNTVLF 329
Cdd:PLN00206 438 RQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVF 471
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
15-334 |
8.00e-14 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 74.29 E-value: 8.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 15 RPLQEEIIRHIL-----NKQDALVLMPTGGGKSI----CYQlpALLCEGTAVVVSPLISLMKDQVEALLANGIAAGALNS 85
Cdd:COG1061 82 RPYQQEALEALLaalerGGGRGLVVAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRRELLEQWAEELRRFLGDPLAGGG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 86 SNDETENanlrraciegrlkLLYISPEKLLAEKDYLLRDMNISLFAIDEAHcisqwgHDFRPEYTQmgVLhQQFPQIPIV 165
Cdd:COG1061 160 KKDSDAP-------------ITVATYQSLARRAHLDELGDRFGLVIIDEAH------HAGAPSYRR--IL-EAFPAAYRL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 166 ALTAT-----------------ADKITREDIVRQLHLNHPRTFI---------SSFDRPNISLTVKRGFQAKEKNKAILE 219
Cdd:COG1061 218 GLTATpfrsdgreillflfdgiVYEYSLKEAIEDGYLAPPEYYGirvdltderAEYDALSERLREALAADAERKDKILRE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 220 FIHRHGEES-GIIYCMSRSKTETVAQMLQKQGIRCGVYHAGLSTQHRDETQNDFINDRIQVVCATIAFGMGIDKSNVRWV 298
Cdd:COG1061 298 LLREHPDDRkTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVA 377
|
330 340 350
....*....|....*....|....*....|....*.
gi 495301113 299 IHYNLPKSIESFYQEIGRAGRDGLPSNTVLFYSLGD 334
Cdd:COG1061 378 ILLRPTGSPREFIQRLGRGLRPAPGKEDALVYDFVG 413
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
531-602 |
4.75e-13 |
|
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: 64.63 E-value: 4.75e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495301113 531 QDLFEALRGLRKQLADQEALPAYIVLSDKVLHLLCISRPTTIEEFGEISGIGEHKKKKYGKDFVNLIRQFVE 602
Cdd:smart00341 5 LRLLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVIQEASD 76
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
215-319 |
3.03e-12 |
|
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: 64.59 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 215 KAILEFIHRHgeESGIIYCMSRSKTETVAQML------QKQGIRCGVYHAGLSTQHRDETQNDFINDRIQVVCATIAFGM 288
Cdd:cd18796 29 AEVIFLLERH--KSTLVFTNTRSQAERLAQRLrelcpdRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLEL 106
|
90 100 110
....*....|....*....|....*....|.
gi 495301113 289 GIDKSNVRWVIHYNLPKSIESFYQEIGRAGR 319
Cdd:cd18796 107 GIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
205-328 |
1.07e-11 |
|
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: 63.04 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 205 KRGFQAKEKNKAILEFIhRHGEESgIIYCMSRSKTETVA----QMLQKQGI---RCGVYHAGLSTQHRDETQNDFINDRI 277
Cdd:cd18797 16 ERGSARREAARLFADLV-RAGVKT-IVFCRSRKLAELLLrylkARLVEEGPlasKVASYRAGYLAEDRREIEAELFNGEL 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 495301113 278 QVVCATIAFGMGIDKSNVRWVIHYNLPKSIESFYQEIGRAGRDGLPSNTVL 328
Cdd:cd18797 94 LGVVATNALELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKDSLVIL 144
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
189-322 |
1.03e-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: 60.26 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 189 RTFISSFDRPNISLTVKRGFQAKEKNKAILEFIHRHGEESGIIYCMSRSKTETVAQMLQkqGIrcGVYHAGLSTQHRDET 268
Cdd:cd18795 6 EEYVLGFNGLGIKLRVDVMNKFDSDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA--GI--AFHHAGLTREDRELV 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495301113 269 QNDFINDRIQVVCATIAFGMGID--------KSNVRWVIHYNLPKSIESFYQEIGRAGRDGL 322
Cdd:cd18795 82 EELFREGLIKVLVATSTLAAGVNlpartviiKGTQRYDGKGYRELSPLEYLQMIGRAGRPGF 143
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
230-348 |
1.03e-10 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 64.08 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 230 IIYCMSRSKTETVAQMLQKQGIRCGVYHAGLSTQHRDETQNDFINDRIQVVCATIAFGMGIDKSNVRWVIHYNLPKSIES 309
Cdd:PTZ00424 271 IIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPEN 350
|
90 100 110
....*....|....*....|....*....|....*....
gi 495301113 310 FYQEIGRAGRDGLPSNTVLFYSLGDLILLTKFASESNQQ 348
Cdd:PTZ00424 351 YIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQ 389
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
18-136 |
3.68e-09 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 56.44 E-value: 3.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 18 QEEIIRHILNKQDALVLMPTGGGKSICYQLPAL--LCE---GTAVVVSPLISLMKDQVEAL------LANGIAAGALNSS 86
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILeaLLRdpgSRALYLYPTKALAQDQLRSLrelleqLGLGIRVATYDGD 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 495301113 87 NDETEnanlRRACIEGRLKLLYISPEKL---LAEKDYLLRD--MNISLFAIDEAH 136
Cdd:cd17923 85 TPREE----RRAIIRNPPRILLTNPDMLhyaLLPHHDRWARflRNLRYVVLDEAH 135
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
14-172 |
7.09e-08 |
|
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: 52.65 E-value: 7.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 14 FRPLQEEIIRHILNKQDALVL-MPTGGGKSICYQLPALLC----EGTAVVVSPLISLMkDQVEALLANGIAAGALNSSN- 87
Cdd:cd17921 2 LNPIQREALRALYLSGDSVLVsAPTSSGKTLIAELAILRAlatsGGKAVYIAPTRALV-NQKEADLRERFGPLGKNVGLl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 88 --DETENANLrraciEGRLKLLYISPEKLLAekdyLLRD------MNISLFAIDEAHCISQwghdfrpeyTQMGV----- 154
Cdd:cd17921 81 tgDPSVNKLL-----LAEADILVATPEKLDL----LLRNggerliQDVRLVVVDEAHLIGD---------GERGVvlell 142
|
170 180
....*....|....*....|.
gi 495301113 155 ---LHQQFPQIPIVALTATAD 172
Cdd:cd17921 143 lsrLLRINKNARFVGLSATLP 163
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
230-319 |
1.46e-07 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 54.51 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 230 IIYCMSRSKTETVAQMLqkqGIRCGVYHAGLSTQHRDETQNDFINDRIQVVCATIAFGMGID--KSNV---------RWV 298
Cdd:COG1202 431 IIFTNSRRRCHEIARAL---GYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDfpASQVifdslamgiEWL 507
|
90 100
....*....|....*....|.
gi 495301113 299 ihynlpkSIESFYQEIGRAGR 319
Cdd:COG1202 508 -------SVQEFHQMLGRAGR 521
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
211-321 |
9.85e-07 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 51.48 E-value: 9.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 211 KEKNKaILEFIHR-----H------------GEESGIIYCMSRSKTETVAQMLQKQGIRCgVYHAGLSTQ-HRDETQNDF 272
Cdd:PRK11192 214 RERKK-IHQWYYRaddleHktallchllkqpEVTRSIVFVRTRERVHELAGWLRKAGINC-CYLEGEMVQaKRNEAIKRL 291
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 495301113 273 INDRIQVVCATIAFGMGIDKSNVRWVIHYNLPKSIESFYQEIGRAGRDG 321
Cdd:PRK11192 292 TDGRVNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAG 340
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
273-321 |
1.02e-06 |
|
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: 46.54 E-value: 1.02e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 495301113 273 INDRIQVVCATIAFGMGIDKSNVRWVIHYNLPKSIESFYQEIGRAGRDG 321
Cdd:cd18785 19 IASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGG 67
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
209-355 |
4.35e-06 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 49.77 E-value: 4.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 209 QAKEKNKAILEFIHRHGEESG--IIYCMSRSKTETVAQMLQKQGIRCGVYHAGLSTQHRDETQNDFINDRIQVVCATIAF 286
Cdd:PTZ00110 358 EEHEKRGKLKMLLQRIMRDGDkiLIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVA 437
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495301113 287 GMGIDKSNVRWVIHYNLPKSIESFYQEIGRAGRDGLPSNTVLFYSLGDLIL---LTKFASESNQQ-NINLEKL 355
Cdd:PTZ00110 438 SRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLardLVKVLREAKQPvPPELEKL 510
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
18-321 |
8.11e-06 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 48.73 E-value: 8.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 18 QEEIIRHILNKQDALVLMPTGGGKS-ICYQ--LPALLCEGTAVVVSPLISLMKDQVEAL-------LANGIAAGALNSSN 87
Cdd:PRK01172 27 QRMAIEQLRKGENVIVSVPTAAGKTlIAYSaiYETFLAGLKSIYIVPLRSLAMEKYEELsrlrslgMRVKISIGDYDDPP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 88 DETENANLRRACIEGRLKLLYISPekllaekdYLLRDmnISLFAIDEAHCISQWGHDFRPEyTQMGVLHQQFPQIPIVAL 167
Cdd:PRK01172 107 DFIKRYDVVILTSEKADSLIHHDP--------YIIND--VGLIVADEIHIIGDEDRGPTLE-TVLSSARYVNPDARILAL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 168 TATADKITreDIVRQLHLNhprTFISSFdRPnisLTVKRGFQAKEK-------------NKAILEFIHRHGEesGIIYCM 234
Cdd:PRK01172 176 SATVSNAN--ELAQWLNAS---LIKSNF-RP---VPLKLGILYRKRlildgyersqvdiNSLIKETVNDGGQ--VLVFVS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 235 SRSKTETVAQMLQK-----------------------QGIRCGV--YHAGLSTQHRDETQNDFINDRIQVVCATIAFGMG 289
Cdd:PRK01172 245 SRKNAEDYAEMLIQhfpefndfkvssennnvyddslnEMLPHGVafHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAG 324
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 495301113 290 ID--------KSNVRWVIHYNLPKSIESFYQEIGRAGRDG 321
Cdd:PRK01172 325 VNlparlvivRDITRYGNGGIRYLSNMEIKQMIGRAGRPG 364
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
215-329 |
1.17e-05 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 48.56 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 215 KAILEFIHRHGeeSGIIYCMSRSKTETVAQMLQKQG------IRCgvYHAGLSTQHRDETQNDFINDRIQVVCATIAFGM 288
Cdd:COG1201 263 PRVLDLIEAHR--TTLVFTNTRSQAERLFQRLNELNpedalpIAA--HHGSLSREQRLEVEEALKAGELRAVVATSSLEL 338
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 495301113 289 GIDKSNVRWVIHYNLPKSIESFYQEIGRAG-RDGLPSNTVLF 329
Cdd:COG1201 339 GIDIGDVDLVIQVGSPKSVARLLQRIGRAGhRVGEVSKGRLV 380
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
212-334 |
1.20e-05 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 47.98 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 212 EKNKAILEFIHRHGEESGIIYCMSRSKTETVAQMLQKQGIRCGVYHAGLSTQHRDETQNDFINDRIQVVCATIAFGMGID 291
Cdd:PRK01297 321 DKYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIH 400
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 495301113 292 KSNVRWVIHYNLPKSIESFYQEIGRAGRDGLPSNTVLFYSLGD 334
Cdd:PRK01297 401 IDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDD 443
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
242-319 |
1.49e-05 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 47.88 E-value: 1.49e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495301113 242 VAQMLQKQGIRCGVYHAGLSTQHRDETQNDFINDRIQVVCATIAFGMGIDKSNVRWVIHYNLPKSIESFYQEIGRAGR 319
Cdd:PRK10590 261 LAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGR 338
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
13-198 |
1.98e-05 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350781 [Multi-domain] Cd Length: 206 Bit Score: 45.81 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 13 NFRPLQEEIIRHILNKQDALVL-MPTGGGKSICYQLP--ALLCEGT--------AVVVSPLISL----MKDQVEALLANG 77
Cdd:cd18023 1 YFNRIQSEVFPDLLYSDKNFVVsAPTGSGKTVLFELAilRLLKERNplpwgnrkVVYIAPIKALcsekYDDWKEKFGPLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 78 IAAGALNSSNDETENANLRRAciegrlKLLYISPEK------LLAEKDYLLRDmnISLFAIDEAHCISQW-GHDFRPEYT 150
Cdd:cd18023 81 LSCAELTGDTEMDDTFEIQDA------DIILTTPEKwdsmtrRWRDNGNLVQL--VALVLIDEVHIIKENrGATLEVVVS 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495301113 151 QMGVLH-------QQFPQIPIVALTATADKItrEDIVRQLHLNHPRTF-ISSFDRP 198
Cdd:cd18023 153 RMKTLSssselrgSTVRPMRFVAVSATIPNI--EDLAEWLGDNPAGCFsFGESFRP 206
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
210-328 |
2.40e-05 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 47.57 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 210 AKEKNKAILEFIHRHGEE--SGIIYCMSRSKTETVAQMLQK--------QGIRCgvYHAGLSTQHRDETQNDFINDRIQV 279
Cdd:PRK13767 266 AEEISEALYETLHELIKEhrTTLIFTNTRSGAERVLYNLRKrfpeeydeDNIGA--HHSSLSREVRLEVEEKLKRGELKV 343
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495301113 280 VCATIAFGMGIDKSNVRWVIHYNLPKSIESFYQEIGRAG---------------RDGLPSNTVL 328
Cdd:PRK13767 344 VVSSTSLELGIDIGYIDLVVLLGSPKSVSRLLQRIGRAGhrlgevskgriivvdRDDLVECAVL 407
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
256-330 |
3.28e-05 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 47.23 E-value: 3.28e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495301113 256 YHAGLSTQHRDETQNDFINDRIQVVCATIAFGMGIDKSNVRWVIHYNLPKSIESFYQEIGRAGRDGLPSNTVLFY 330
Cdd:PRK09751 307 HHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAGHQVGGVSKGLFF 381
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
213-321 |
3.87e-05 |
|
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: 43.62 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 213 KNKAILEFIHRHGEESG--IIYCMSRSKTETVAQMLQKQGIRCGVYHAGLSTQHRDETQNDFINDR--IQVVCATIAFGM 288
Cdd:cd18793 12 KLEALLELLEELREPGEkvLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdiRVFLLSTKAGGV 91
|
90 100 110
....*....|....*....|....*....|....*..
gi 495301113 289 GID--KSNVrwVIHYNLP--KSIESfyQEIGRAGRDG 321
Cdd:cd18793 92 GLNltAANR--VILYDPWwnPAVEE--QAIDRAHRIG 124
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
223-319 |
8.47e-05 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350186 [Multi-domain] Cd Length: 116 Bit Score: 42.16 E-value: 8.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 223 RHGEESGIIYCMSRSKTETVAQMLQKQGIRCGVYHAGLS---TQHRDETQNDFINDRIQVVCATIAFGMGIDKSNVRWVI 299
Cdd:cd18799 3 KYVEIKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSdreRGDEALILLFFGELKPPILVTVDLLTTGVDIPEVDNVV 82
|
90 100
....*....|....*....|...
gi 495301113 300 hynLPKSIES---FYQEIGRAGR 319
Cdd:cd18799 83 ---FLRPTESrtlFLQMLGRGLR 102
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
16-170 |
1.60e-04 |
|
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: 42.71 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 16 PLQEEIIRHILNKQDALVL-MPTGGGKSICYQL---PALLCEGTAVVVSPLISL-------MKDQVEALLANGIAAGALN 84
Cdd:cd18028 4 PPQAEAVRAGLLKGENLLIsIPTASGKTLIAEMamvNTLLEGGKALYLVPLRALasekyeeFKKLEEIGLKVGISTGDYD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 85 SSNDETENANLRRACIEGRLKLLYISPEKLlaekdyllrdMNISLFAIDEAHCISQWGHDFRPEYTQMGVLHqQFPQIPI 164
Cdd:cd18028 84 EDDEWLGDYDIIVATYEKFDSLLRHSPSWL----------RDVGVVVVDEIHLISDEERGPTLESIVARLRR-LNPNTQI 152
|
....*.
gi 495301113 165 VALTAT 170
Cdd:cd18028 153 IGLSAT 158
|
|
| Rnd |
COG0349 |
Ribonuclease D [Translation, ribosomal structure and biogenesis]; |
533-599 |
3.76e-04 |
|
Ribonuclease D [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440118 [Multi-domain] Cd Length: 365 Bit Score: 42.94 E-value: 3.76e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495301113 533 LFEALRGLRKQLADQEALPAYIVLSDKVLHLLCISRPTTIEEFGEISGIGEHKKKKYGKDFVNLIRQ 599
Cdd:COG0349 212 VLRELAAWREREARKRDVPRNRVLKDEALLELARRQPKSLEELARLRGLSPGEIRRHGEELLAAVAE 278
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
181-319 |
1.10e-03 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 42.13 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 181 RQLhLNHPRTFISSFDRpnisLTVKRGfqakeKNKAILEFIHRHGEESG--IIYCMSRSKTETVAQMLQKQGIRCGVYHA 258
Cdd:COG0553 512 RQI-CSHPALLLEEGAE----LSGRSA-----KLEALLELLEELLAEGEkvLVFSQFTDTLDLLEERLEERGIEYAYLHG 581
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495301113 259 GLSTQHRDETQNDFINDR--IQVVCATIAFGMGIDKSNVRWVIHYNL---PKSIEsfyQEIGRAGR 319
Cdd:COG0553 582 GTSAEERDELVDRFQEGPeaPVFLISLKAGGEGLNLTAADHVIHYDLwwnPAVEE---QAIDRAHR 644
|
|
| SF2_C_suv3 |
cd18805 |
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene ... |
231-322 |
1.16e-03 |
|
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: 39.46 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 231 IYCMSRSKTETVAQMLQKQ-GIRCGVYHAGLSTQHRDETQNDFI--NDRIQVVCATIAFGMGIDkSNVRWVIHYNLPK-- 305
Cdd:cd18805 22 VVAFSRKDIFSLKREIEKRtGLKCAVIYGALPPETRRQQARLFNdpESGYDVLVASDAIGMGLN-LNIRRVIFSSLSKfd 100
|
90 100
....*....|....*....|....
gi 495301113 306 -------SIESFYQEIGRAGRDGL 322
Cdd:cd18805 101 gnemrplSPSEVKQIAGRAGRFGS 124
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
1-192 |
1.53e-03 |
|
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350714 [Multi-domain] Cd Length: 231 Bit Score: 40.31 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 1 MRETLKTyFGYDNFRPLQEEIIRHILNKQ---------DALVLMPTGGGKSICYQLP---ALL----CEGTAVVVSP--- 61
Cdd:cd17956 1 LLKNLQN-NGITSAFPVQAAVIPWLLPSSkstppyrpgDLCVSAPTGSGKTLAYVLPivqALSkrvvPRLRALIVVPtke 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 62 LISLMKDQVEALLAN-GIAAGALNSSNDETENANLRRACIEGRLK----LLYISPEKLLaekDYLLRDMNISL-----FA 131
Cdd:cd17956 80 LVQQVYKVFESLCKGtGLKVVSLSGQKSFKKEQKLLLVDTSGRYLsrvdILVATPGRLV---DHLNSTPGFTLkhlrfLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 132 IDEA----------------HCISQWGHDFRPEYTQMGVL-HQQFPQIPIV---ALTATADKITredivrQLHLNHPRTF 191
Cdd:cd17956 157 IDEAdrllnqsfqdwletvmKALGRPTAPDLGSFGDANLLeRSVRPLQKLLfsaTLTRDPEKLS------SLKLHRPRLF 230
|
.
gi 495301113 192 I 192
Cdd:cd17956 231 T 231
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
10-50 |
1.94e-03 |
|
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: 39.73 E-value: 1.94e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 495301113 10 GYDNFRPLQEEIIRHILNKQDALVLMPTGGGKSICYQLPAL 50
Cdd:cd00268 9 GFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPIL 49
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
14-170 |
4.34e-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: 38.06 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 14 FRPLQEEIIRHIL---NKQDALVLMPTGGGKSIC-YQLPALLCEGTAVVVSPLISLMKDQVEALLANGIAA--GALNS-S 86
Cdd:cd17926 1 LRPYQEEALEAWLahkNNRRGILVLPTGSGKTLTaLALIAYLKELRTLIVVPTDALLDQWKERFEDFLGDSsiGLIGGgK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 87 NDETENANLRRACIEgrlkLLYISPEkllAEKDYLLRDMnisLFAIDEAHCIS--QWGHdfrpeytqmgvLHQQFPQIPI 164
Cdd:cd17926 81 KKDFDDANVVVATYQ----SLSNLAE---EEKDLFDQFG---LLIVDEAHHLPakTFSE-----------ILKELNAKYR 139
|
....*.
gi 495301113 165 VALTAT 170
Cdd:cd17926 140 LGLTAT 145
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
256-365 |
6.80e-03 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 39.56 E-value: 6.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 256 YHAGLSTQHRDETQNDFINDRIQVVCATIAFGMGIDKSNVRWVI----HYN-----LPKSIESFYQEIGRAGRDGL-Psn 325
Cdd:PRK02362 309 HHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIrdyrRYDggagmQPIPVLEYHQMAGRAGRPGLdP-- 386
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 495301113 326 tvlfYslGDLILLTKFASEsnqqninLEKLqrMQQYAEAD 365
Cdd:PRK02362 387 ----Y--GEAVLLAKSYDE-------LDEL--FERYIWAD 411
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
13-170 |
8.98e-03 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 37.27 E-value: 8.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 13 NFRPLQEEIIRHILNKQD-----ALVLMPTGGGKSICY-QLPALL----CEGTAVVVSPLISLMKDQVEALLANGIaaga 82
Cdd:pfam04851 3 ELRPYQIEAIENLLESIKngqkrGLIVMATGSGKTLTAaKLIARLfkkgPIKKVLFLVPRKDLLEQALEEFKKFLP---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495301113 83 lNSSNDETENANLRRACIEGRLKLLYISPEKL---LAEKDYLLRDMNISLFAIDEAHcisqwgHDFRPEYTQmgvLHQQF 159
Cdd:pfam04851 79 -NYVEIGEIISGDKKDESVDDNKIVVTTIQSLykaLELASLELLPDFFDVIIIDEAH------RSGASSYRN---ILEYF 148
|
170
....*....|.
gi 495301113 160 PQIPIVALTAT 170
Cdd:pfam04851 149 KPAFLLGLTAT 159
|
|
| |
