|
Name |
Accession |
Description |
Interval |
E-value |
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
282-768 |
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: 774.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 282 KIFHKKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPATY 361
Cdd:TIGR00614 1 KILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 362 LTGDKTDSEATNIYLQLskKDPIIKLLYVTPEKICASNRLISTLEnlyERKLLARFVIDEAHCVSQWGHDFRQDYKRMNM 441
Cdd:TIGR00614 81 LNSAQTKEQQLNVLTDL--KDGKIKLLYVTPEKISASNRLLQTLE---ERKGITLIAVDEAHCISQWGHDFRPDYKALGS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 442 LRQKFPSVPVMALTATANPRVQKDILTQLKILRPQVFSMSFNRHNLKYYVLPKKPkKVAFDCLEWIRKHHPYDSGIIYCL 521
Cdd:TIGR00614 156 LKQKFPNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRRKTP-KILEDLLRFIRKEFEGKSGIIYCP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 522 SRRECDTMADTLQRDGLAALAYHAGLSDSARDEVQQKWInQDGCQVICATIAFGMGIDKPDVRFVIHASLPKSVEGYYQE 601
Cdd:TIGR00614 235 SRKKVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQ-RDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 602 SGRAGRDGEISHCLLFYTYHDVTRLKRLIMMEKDGNhhtRETHFNNLYSMVHYCENITECRRIQLLAYFGENGFNPDFCK 681
Cdd:TIGR00614 314 SGRAGRDGLPSECHLFYAPADMNRLRRLLMEEPDGN---FRTYKLKLYEMMEYCLNSSTCRRLILLSYFGEKGFNKSFCI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 682 KHPDVSCDNCCKTKDYKTRDVTDDVKSIVRFVQEHSSSQGMRNikhvgpsGRFTMNMLVDIFLGSKSAKIQSGIFGKGSA 761
Cdd:TIGR00614 391 MGTEKCCDNCCKRLDYKTKDVTDKVYDFGPQAQKALSAVGRLN-------QKFGMGYPVDFLRGSNSQKIRDGGFRKHSL 463
|
....*..
gi 564730691 762 YSRHNAE 768
Cdd:TIGR00614 464 YGRGKDE 470
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
279-775 |
0e+00 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 557.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 279 EMMKIFHKKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIP 358
Cdd:COG0514 4 DALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 359 ATYLTGDKTDSEATNIYLQLSKKDpiIKLLYVTPEkicasnRLIS--TLENLYERKLlARFVIDEAHCVSQWGHDFRQDY 436
Cdd:COG0514 84 AAFLNSSLSAEERREVLRALRAGE--LKLLYVAPE------RLLNprFLELLRRLKI-SLFAIDEAHCISQWGHDFRPDY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 437 KRMNMLRQKFPSVPVMALTATANPRVQKDILTQLKILRPQVFSMSFNRHNLKYYVLPKKPKKVAFDCLEWIRKHHPyDSG 516
Cdd:COG0514 155 RRLGELRERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKPPDDKLAQLLDFLKEHPG-GSG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 517 IIYCLSRRECDTMADTLQRDGLAALAYHAGLSDSARDEVQQKWINQDGcQVICATIAFGMGIDKPDVRFVIHASLPKSVE 596
Cdd:COG0514 234 IVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEV-DVIVATIAFGMGIDKPDVRFVIHYDLPKSIE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 597 GYYQESGRAGRDGEISHCLLFYTYHDVTRLKRLIMMEKDGNHHTRETHfNNLYSMVHYCEnITECRRIQLLAYFGENGFN 676
Cdd:COG0514 313 AYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEERKRVER-AKLDAMLAYAE-TTGCRRQFLLRYFGEELAE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 677 PdfCKKhpdvsCDNCCKTKdyKTRDVTDDVKSIVRFVqehsssqgmrniKHVGPsgRFTMNMLVDIFLGSKSAKIQS--- 753
Cdd:COG0514 391 P--CGN-----CDNCLGPP--ETFDGTEAAQKALSCV------------YRTGQ--RFGAGHVIDVLRGSKNEKIRQfgh 447
|
490 500
....*....|....*....|....*
gi 564730691 754 ---GIFGKGSAYSRHNAERLFKKLI 775
Cdd:COG0514 448 dklSTYGIGKDLSDKEWRSVIRQLL 472
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
268-908 |
7.41e-159 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 501.35 E-value: 7.41e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 268 RFQSLSFPHTKEMMKIFHKKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVD 347
Cdd:PLN03137 436 KWSSRNFPWTKKLEVNNKKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQD 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 348 QVQKLTSLDIPATYLTGDKTDSEATNIYLQLSKKDPIIKLLYVTPEKICASNRLISTLENLYERKLLARFVIDEAHCVSQ 427
Cdd:PLN03137 516 QIMNLLQANIPAASLSAGMEWAEQLEILQELSSEYSKYKLLYVTPEKVAKSDSLLRHLENLNSRGLLARFVIDEAHCVSQ 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 428 WGHDFRQDYKRMNMLRQKFPSVPVMALTATANPRVQKDILTQLKILRPQVFSMSFNRHNLKYYVLPKKPKkvafdCLE-- 505
Cdd:PLN03137 596 WGHDFRPDYQGLGILKQKFPNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPKTKK-----CLEdi 670
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 506 --WIRKHHPYDSGIIYCLSRRECDTMADTLQRDGLAALAYHAGLSDSARDEVQQKWiNQDGCQVICATIAFGMGIDKPDV 583
Cdd:PLN03137 671 dkFIKENHFDECGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQW-SKDEINIICATVAFGMGINKPDV 749
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 584 RFVIHASLPKSVEGYYQESGRAGRDGEISHCLLFYTYHDVTRLKRLIM--------MEKDGNHHTR-----ETHFNNLYS 650
Cdd:PLN03137 750 RFVIHHSLPKSIEGYHQECGRAGRDGQRSSCVLYYSYSDYIRVKHMISqggveqspMAMGYNRMASsgrilETNTENLLR 829
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 651 MVHYCENITECRRIQLLAYFGENgFNPDFCKKhpdvSCDNCCKTKDYKTRDVTDDVKSIVRFVqehsssqgmrniKHVGP 730
Cdd:PLN03137 830 MVSYCENEVDCRRFLQLVHFGEK-FDSTNCKK----TCDNCSSSKSLIDKDVTEIARQLVELV------------KLTGE 892
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 731 sgRFTMNMLVDIFLGSKSAKIQS------GIFGKGSAYSRHNAERLFKKLILDKILDEDLYINANDQAIAYVMLGN--KA 802
Cdd:PLN03137 893 --RFSSAHILEVYRGSLNQYVKKhrhetlSLHGAGKHLSKGEASRILHYLVTEDILAEDVKKSDLYGSVSSLLKVNesKA 970
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 803 QTVLNGNLKV--DFMETENSSSVKKQKALVAKVSQRE------EMVKKCLGEL----------------TEVCKSLGKvf 858
Cdd:PLN03137 971 YKLFSGGQTIimRFPSSVKASKPSKFEATPAKGPLTSgkqstlPMATPAQPPVdlnlsailytalrklrTALVKEAGD-- 1048
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 564730691 859 GVHYFNIFNTVTLKKLAESLSSDPEVLLQIDGVTEDKLEKYGAEVISVLQ 908
Cdd:PLN03137 1049 GVMAYHIFGNATLQQISKRIPRTKEELLEINGLGKAKVSKYGDRLLETIE 1098
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
276-483 |
5.38e-152 |
|
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: 449.66 E-value: 5.38e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 276 HTKEMMKIFHKKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSL 355
Cdd:cd18016 1 HSKEMMKIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 356 DIPATYLTGDKTDSEATNIYLQLSKKDPIIKLLYVTPEKICASNRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRQD 435
Cdd:cd18016 81 DIPATYLTGDKTDAEATKIYLQLSKKDPIIKLLYVTPEKISASNRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRPD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 564730691 436 YKRMNMLRQKFPSVPVMALTATANPRVQKDILTQLKILRPQVFSMSFN 483
Cdd:cd18016 161 YKRLNMLRQKFPSVPMMALTATATPRVQKDILNQLKMLRPQVFTMSFN 208
|
|
| BDHCT_assoc |
pfam16204 |
BDHCT-box associated domain on Bloom syndrome protein; This family is found on Bloom ... |
50-272 |
2.50e-140 |
|
BDHCT-box associated domain on Bloom syndrome protein; This family is found on Bloom syndrome-associated DEAD-box helicases in higher eukaryotes. It lies between the BDHCT, and DEAD-box families, pfam08072 and pfam00270.
Pssm-ID: 465065 Cd Length: 223 Bit Score: 419.98 E-value: 2.50e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 50 GSLWRYRPDSLDGPMEGDSCPTGNSMKELNFSHLPSNSVSPGDCLLTTTLGKTGFSATRKNLFERPLFNTHLQKSFVSSN 129
Cdd:pfam16204 1 GSVWRCRPDSLGSPVKGDSCPTGNSVKELNFPHLPSNSLSTGECLLTTTPGKTGFSATTKNLSERPLFSSHLQKSFVSSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 130 WAETPRLGKKNESSYFPGNVLTSTAVKDQNKHTASINDLERETQPSYDIDNFDIDDFDDDDDWEDIMHNLAASKSSTAAY 209
Cdd:pfam16204 81 WAETPRTEKRNESSYFPGNVLTSTAVKDQNKHTASVNDLEREIQASCDIDNFDIDDFDDDDDWENIMHNLAASKSSTAAY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564730691 210 QPIKEGRPIKSVSERLSSAKTDCLPVSSTAQNINFSESIQNYTDKSAQNLASRNLKHERFQSL 272
Cdd:pfam16204 161 QPIKEGGPVKSVSERISSAKTNCLPVASTAQNKNFSESIQNYTDKSAQNLASRNLKHEHFQSL 223
|
|
| DpdF |
NF041063 |
protein DpdF; |
297-634 |
3.68e-50 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 191.28 E-value: 3.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 297 QLEAINAALL---GEDCFILMPTGGGKSLCYQLPACVSP---GVTVVISPLRSLIVDQVQKLTSL-------DIPATYLT 363
Cdd:NF041063 145 QREAVRAALLappGSTLIVNLPTGSGKSLVAQAPALLASrqgGLTLVVVPTVALAIDQERRARELlrragpdLGGPLAWH 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 364 GDKTDSEATNIYLQLskKDPIIKLLYVTPEKICASnrLISTLENLYERKLLARFVIDEAHCVSQWGHDFRQDYKRMNMLR 443
Cdd:NF041063 225 GGLSAEERAAIRQRI--RDGTQRILFTSPESLTGS--LRPALFDAAEAGLLRYLVVDEAHLVDQWGDGFRPEFQLLAGLR 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 444 QKFPSVP-------VMALTATanprvqkdiLTQ-----LKIL-----RPQVFSMSFNRHNLKYYVLPKKPKKVAFDC-LE 505
Cdd:NF041063 301 RSLLRLApsgrpfrTLLLSAT---------LTEstldtLETLfgppgPFIVVSAVQLRPEPAYWVAKCDSEEERRERvLE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 506 WIRkhH---PYdsgIIYCLSRRECDTMADTLQRDGLAALA-YHAGLSDSARDEVQQKWiNQDGCQVICATIAFGMGIDKP 581
Cdd:NF041063 372 ALR--HlprPL---ILYVTKVEDAEAWLQRLRAAGFRRVAlFHGDTPDAERERLIEQW-RENELDIVVATSAFGLGMDKS 445
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 564730691 582 DVRFVIHASLPKSVEGYYQESGRAGRDGEISHCLLFYTYHDVT---RL--KRLIMMEK 634
Cdd:NF041063 446 DVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLDiakSLnrPKLISVEK 503
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
294-466 |
2.93e-30 |
|
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: 117.34 E-value: 2.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 294 RTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPAC------VSPGVTVVISPLRSLIVDQVQKLTSLDIPATY-----L 362
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKLGKGLGLkvaslL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 363 TGDKTDSEATNIylqlsKKdpiIKLLYVTPEKICASNRLISTLENLyerKLLarfVIDEAHCVSQWGhdFRQDYKRmnML 442
Cdd:pfam00270 81 GGDSRKEQLEKL-----KG---PDILVGTPGRLLDLLQERKLLKNL---KLL---VLDEAHRLLDMG--FGPDLEE--IL 142
|
170 180
....*....|....*....|....
gi 564730691 443 RQKFPSVPVMALTATAnPRVQKDI 466
Cdd:pfam00270 143 RRLPKKRQILLLSATL-PRNLEDL 165
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
286-466 |
5.41e-23 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 97.95 E-value: 5.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 286 KKFGLHNFRTNQLEAINAALLGE-DCFILMPTGGGKSLCYQLPA-----CVSPGVTVVISPLRSLIVDQVQKLTSL---- 355
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPAlealkRGKGGRVLVLVPTRELAEQWAEELKKLgpsl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 356 -DIPATYLTGDKTDSEATNIylqlskKDPIIKLLYVTPEKIcasnrLISTLENLYERKLLARFVIDEAHCVSQWGhdFRQ 434
Cdd:smart00487 82 gLKVVGLYGGDSKREQLRKL------ESGKTDILVTTPGRL-----LDLLENDKLSLSNVDLVILDEAHRLLDGG--FGD 148
|
170 180 190
....*....|....*....|....*....|..
gi 564730691 435 DYKRmnMLRQKFPSVPVMALTATANPRVQKDI 466
Cdd:smart00487 149 QLEK--LLKLLPKNVQLLLLSATPPEEIENLL 178
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
838-917 |
4.88e-20 |
|
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: 85.43 E-value: 4.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 838 EMVKKCLGELTEVCKSLGKVFGVHYFNIFNTVTLKKLAESLSSDPEVLLQIDGVTEDKLEKYGAEVISVLQKYSEWTSPA 917
Cdd:smart00341 2 ERQLRLLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVIQEASDSPSEA 81
|
|
| BDHCT |
pfam08072 |
BDHCT (NUC031) domain; This is a C-terminal domain in Bloom's syndrome DEAD helicase subfamily. |
1-37 |
9.52e-19 |
|
BDHCT (NUC031) domain; This is a C-terminal domain in Bloom's syndrome DEAD helicase subfamily.
Pssm-ID: 462356 Cd Length: 41 Bit Score: 80.40 E-value: 9.52e-19
10 20 30
....*....|....*....|....*....|....*..
gi 564730691 1 MEHICKLIDTIPDDKLKLLDCGNELLQQRNIRRKLLT 37
Cdd:pfam08072 5 MEEICKLVDTIPIHELKALSCGNELLQQRDIRRKLLA 41
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
841-907 |
1.60e-11 |
|
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: 60.63 E-value: 1.60e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564730691 841 KKCLGELTEVCKSLGKVFGVHYFNIFNTVTLKKLAESLSSDPEVLLQIDGVTEDKLEKYGAEVISVL 907
Cdd:pfam00570 2 LALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
282-768 |
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: 774.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 282 KIFHKKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPATY 361
Cdd:TIGR00614 1 KILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 362 LTGDKTDSEATNIYLQLskKDPIIKLLYVTPEKICASNRLISTLEnlyERKLLARFVIDEAHCVSQWGHDFRQDYKRMNM 441
Cdd:TIGR00614 81 LNSAQTKEQQLNVLTDL--KDGKIKLLYVTPEKISASNRLLQTLE---ERKGITLIAVDEAHCISQWGHDFRPDYKALGS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 442 LRQKFPSVPVMALTATANPRVQKDILTQLKILRPQVFSMSFNRHNLKYYVLPKKPkKVAFDCLEWIRKHHPYDSGIIYCL 521
Cdd:TIGR00614 156 LKQKFPNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRRKTP-KILEDLLRFIRKEFEGKSGIIYCP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 522 SRRECDTMADTLQRDGLAALAYHAGLSDSARDEVQQKWInQDGCQVICATIAFGMGIDKPDVRFVIHASLPKSVEGYYQE 601
Cdd:TIGR00614 235 SRKKVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQ-RDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 602 SGRAGRDGEISHCLLFYTYHDVTRLKRLIMMEKDGNhhtRETHFNNLYSMVHYCENITECRRIQLLAYFGENGFNPDFCK 681
Cdd:TIGR00614 314 SGRAGRDGLPSECHLFYAPADMNRLRRLLMEEPDGN---FRTYKLKLYEMMEYCLNSSTCRRLILLSYFGEKGFNKSFCI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 682 KHPDVSCDNCCKTKDYKTRDVTDDVKSIVRFVQEHSSSQGMRNikhvgpsGRFTMNMLVDIFLGSKSAKIQSGIFGKGSA 761
Cdd:TIGR00614 391 MGTEKCCDNCCKRLDYKTKDVTDKVYDFGPQAQKALSAVGRLN-------QKFGMGYPVDFLRGSNSQKIRDGGFRKHSL 463
|
....*..
gi 564730691 762 YSRHNAE 768
Cdd:TIGR00614 464 YGRGKDE 470
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
279-775 |
0e+00 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 557.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 279 EMMKIFHKKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIP 358
Cdd:COG0514 4 DALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 359 ATYLTGDKTDSEATNIYLQLSKKDpiIKLLYVTPEkicasnRLIS--TLENLYERKLlARFVIDEAHCVSQWGHDFRQDY 436
Cdd:COG0514 84 AAFLNSSLSAEERREVLRALRAGE--LKLLYVAPE------RLLNprFLELLRRLKI-SLFAIDEAHCISQWGHDFRPDY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 437 KRMNMLRQKFPSVPVMALTATANPRVQKDILTQLKILRPQVFSMSFNRHNLKYYVLPKKPKKVAFDCLEWIRKHHPyDSG 516
Cdd:COG0514 155 RRLGELRERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKPPDDKLAQLLDFLKEHPG-GSG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 517 IIYCLSRRECDTMADTLQRDGLAALAYHAGLSDSARDEVQQKWINQDGcQVICATIAFGMGIDKPDVRFVIHASLPKSVE 596
Cdd:COG0514 234 IVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEV-DVIVATIAFGMGIDKPDVRFVIHYDLPKSIE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 597 GYYQESGRAGRDGEISHCLLFYTYHDVTRLKRLIMMEKDGNHHTRETHfNNLYSMVHYCEnITECRRIQLLAYFGENGFN 676
Cdd:COG0514 313 AYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEERKRVER-AKLDAMLAYAE-TTGCRRQFLLRYFGEELAE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 677 PdfCKKhpdvsCDNCCKTKdyKTRDVTDDVKSIVRFVqehsssqgmrniKHVGPsgRFTMNMLVDIFLGSKSAKIQS--- 753
Cdd:COG0514 391 P--CGN-----CDNCLGPP--ETFDGTEAAQKALSCV------------YRTGQ--RFGAGHVIDVLRGSKNEKIRQfgh 447
|
490 500
....*....|....*....|....*
gi 564730691 754 ---GIFGKGSAYSRHNAERLFKKLI 775
Cdd:COG0514 448 dklSTYGIGKDLSDKEWRSVIRQLL 472
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
268-908 |
7.41e-159 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 501.35 E-value: 7.41e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 268 RFQSLSFPHTKEMMKIFHKKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVD 347
Cdd:PLN03137 436 KWSSRNFPWTKKLEVNNKKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQD 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 348 QVQKLTSLDIPATYLTGDKTDSEATNIYLQLSKKDPIIKLLYVTPEKICASNRLISTLENLYERKLLARFVIDEAHCVSQ 427
Cdd:PLN03137 516 QIMNLLQANIPAASLSAGMEWAEQLEILQELSSEYSKYKLLYVTPEKVAKSDSLLRHLENLNSRGLLARFVIDEAHCVSQ 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 428 WGHDFRQDYKRMNMLRQKFPSVPVMALTATANPRVQKDILTQLKILRPQVFSMSFNRHNLKYYVLPKKPKkvafdCLE-- 505
Cdd:PLN03137 596 WGHDFRPDYQGLGILKQKFPNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPKTKK-----CLEdi 670
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 506 --WIRKHHPYDSGIIYCLSRRECDTMADTLQRDGLAALAYHAGLSDSARDEVQQKWiNQDGCQVICATIAFGMGIDKPDV 583
Cdd:PLN03137 671 dkFIKENHFDECGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQW-SKDEINIICATVAFGMGINKPDV 749
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 584 RFVIHASLPKSVEGYYQESGRAGRDGEISHCLLFYTYHDVTRLKRLIM--------MEKDGNHHTR-----ETHFNNLYS 650
Cdd:PLN03137 750 RFVIHHSLPKSIEGYHQECGRAGRDGQRSSCVLYYSYSDYIRVKHMISqggveqspMAMGYNRMASsgrilETNTENLLR 829
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 651 MVHYCENITECRRIQLLAYFGENgFNPDFCKKhpdvSCDNCCKTKDYKTRDVTDDVKSIVRFVqehsssqgmrniKHVGP 730
Cdd:PLN03137 830 MVSYCENEVDCRRFLQLVHFGEK-FDSTNCKK----TCDNCSSSKSLIDKDVTEIARQLVELV------------KLTGE 892
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 731 sgRFTMNMLVDIFLGSKSAKIQS------GIFGKGSAYSRHNAERLFKKLILDKILDEDLYINANDQAIAYVMLGN--KA 802
Cdd:PLN03137 893 --RFSSAHILEVYRGSLNQYVKKhrhetlSLHGAGKHLSKGEASRILHYLVTEDILAEDVKKSDLYGSVSSLLKVNesKA 970
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 803 QTVLNGNLKV--DFMETENSSSVKKQKALVAKVSQRE------EMVKKCLGEL----------------TEVCKSLGKvf 858
Cdd:PLN03137 971 YKLFSGGQTIimRFPSSVKASKPSKFEATPAKGPLTSgkqstlPMATPAQPPVdlnlsailytalrklrTALVKEAGD-- 1048
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 564730691 859 GVHYFNIFNTVTLKKLAESLSSDPEVLLQIDGVTEDKLEKYGAEVISVLQ 908
Cdd:PLN03137 1049 GVMAYHIFGNATLQQISKRIPRTKEELLEINGLGKAKVSKYGDRLLETIE 1098
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
280-910 |
2.12e-158 |
|
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: 481.11 E-value: 2.12e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 280 MMKIFHKKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPA 359
Cdd:TIGR01389 1 AQQVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 360 TYLTGDKTDSEATNIYLQLSKKDpiIKLLYVTPEKicasnrlistLENLYERKLLAR-----FVIDEAHCVSQWGHDFRQ 434
Cdd:TIGR01389 81 AYLNSTLSAKEQQDIEKALVNGE--LKLLYVAPER----------LEQDYFLNMLQRipialVAVDEAHCVSQWGHDFRP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 435 DYKRMNMLRQKFPSVPVMALTATANPRVQKDILTQLKILRPQVFSMSFNRHNLKYYVLPKKPKKVafDCLEWIRKHHPyD 514
Cdd:TIGR01389 149 EYQRLGSLAERFPQVPRIALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKNNKQK--FLLDYLKKHRG-Q 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 515 SGIIYCLSRRECDTMADTLQRDGLAALAYHAGLSDSARDEVQQKWINQDGcQVICATIAFGMGIDKPDVRFVIHASLPKS 594
Cdd:TIGR01389 226 SGIIYASSRKKVEELAERLESQGISALAYHAGLSNKVRAENQEDFLYDDV-KVMVATNAFGMGIDKPNVRFVIHYDMPGN 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 595 VEGYYQESGRAGRDGEISHCLLFYTYHDVTRLKRLI-MMEKDGNHHTRETHfnNLYSMVHYCENITeCRRIQLLAYFGEN 673
Cdd:TIGR01389 305 LESYYQEAGRAGRDGLPAEAILLYSPADIALLKRRIeQSEADDDYKQIERE--KLRAMIAYCETQT-CRRAYILRYFGEN 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 674 GFNPdfCKKhpdvsCDNCckTKDYKTRDVTDDVKSIvrfvqehsssqgMRNIKHVGpsGRFTMNMLVDIFLGSKSAKI-- 751
Cdd:TIGR01389 382 EVEP--CGN-----CDNC--LDPPKSYDATVEAQKA------------LSCVYRMG--QRFGVGYIIEVLRGSKNDKIlq 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 752 ----QSGIFGKGSAYSRHNAERLFKKLILDKildedlYINANDQAIAYVMLGNKAQTVLNGnlkvdfmETENSSSVKKQK 827
Cdd:TIGR01389 439 kghdQLSTYGIGKDYTQKEWRSLIDQLIAEG------LLTENDEIYIGLQLTEAARKVLKN-------EVEVLLRPFKVV 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 828 ALVAKVSQRE--EMVKKCLGE-LTEVCKSLGKVFGVHYFNIFNTVTLKKLAESLSSDPEVLLQIDGVTEDKLEKYGAEVI 904
Cdd:TIGR01389 506 AKEKTRVQKNlsVGVDNALFEaLRELRKEQADEQNVPPYVIFSDSTLREMAEKRPATLNALLKIKGVGQNKLDRYGEAFL 585
|
....*.
gi 564730691 905 SVLQKY 910
Cdd:TIGR01389 586 EVIREY 591
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
276-483 |
5.38e-152 |
|
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: 449.66 E-value: 5.38e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 276 HTKEMMKIFHKKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSL 355
Cdd:cd18016 1 HSKEMMKIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 356 DIPATYLTGDKTDSEATNIYLQLSKKDPIIKLLYVTPEKICASNRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRQD 435
Cdd:cd18016 81 DIPATYLTGDKTDAEATKIYLQLSKKDPIIKLLYVTPEKISASNRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRPD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 564730691 436 YKRMNMLRQKFPSVPVMALTATANPRVQKDILTQLKILRPQVFSMSFN 483
Cdd:cd18016 161 YKRLNMLRQKFPSVPMMALTATATPRVQKDILNQLKMLRPQVFTMSFN 208
|
|
| BDHCT_assoc |
pfam16204 |
BDHCT-box associated domain on Bloom syndrome protein; This family is found on Bloom ... |
50-272 |
2.50e-140 |
|
BDHCT-box associated domain on Bloom syndrome protein; This family is found on Bloom syndrome-associated DEAD-box helicases in higher eukaryotes. It lies between the BDHCT, and DEAD-box families, pfam08072 and pfam00270.
Pssm-ID: 465065 Cd Length: 223 Bit Score: 419.98 E-value: 2.50e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 50 GSLWRYRPDSLDGPMEGDSCPTGNSMKELNFSHLPSNSVSPGDCLLTTTLGKTGFSATRKNLFERPLFNTHLQKSFVSSN 129
Cdd:pfam16204 1 GSVWRCRPDSLGSPVKGDSCPTGNSVKELNFPHLPSNSLSTGECLLTTTPGKTGFSATTKNLSERPLFSSHLQKSFVSSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 130 WAETPRLGKKNESSYFPGNVLTSTAVKDQNKHTASINDLERETQPSYDIDNFDIDDFDDDDDWEDIMHNLAASKSSTAAY 209
Cdd:pfam16204 81 WAETPRTEKRNESSYFPGNVLTSTAVKDQNKHTASVNDLEREIQASCDIDNFDIDDFDDDDDWENIMHNLAASKSSTAAY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564730691 210 QPIKEGRPIKSVSERLSSAKTDCLPVSSTAQNINFSESIQNYTDKSAQNLASRNLKHERFQSL 272
Cdd:pfam16204 161 QPIKEGGPVKSVSERISSAKTNCLPVASTAQNKNFSESIQNYTDKSAQNLASRNLKHEHFQSL 223
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
281-910 |
4.01e-123 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 389.46 E-value: 4.01e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 281 MKIFHKKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPAT 360
Cdd:PRK11057 14 KQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVAAA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 361 YLTGDKTDSEATNIYLQLSKKDpiIKLLYVTPEKICASNrlisTLENLYERKlLARFVIDEAHCVSQWGHDFRQDYKRMN 440
Cdd:PRK11057 94 CLNSTQTREQQLEVMAGCRTGQ--IKLLYIAPERLMMDN----FLEHLAHWN-PALLAVDEAHCISQWGHDFRPEYAALG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 441 MLRQKFPSVPVMALTATANPRVQKDILTQLKILRPQVFSMSFNRHNLKYYVLPK-KPkkvaFDCLEWIRKHHPYDSGIIY 519
Cdd:PRK11057 167 QLRQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLVEKfKP----LDQLMRYVQEQRGKSGIIY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 520 CLSRRECDTMADTLQRDGLAALAYHAGLSDSARDEVQQKWiNQDGCQVICATIAFGMGIDKPDVRFVIHASLPKSVEGYY 599
Cdd:PRK11057 243 CNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAF-QRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYY 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 600 QESGRAGRDGEISHCLLFYTYHDVTRLKRLIMMEKDGNHHTRETHfnNLYSMVHYCENITeCRRIQLLAYFGENGFNPdf 679
Cdd:PRK11057 322 QETGRAGRDGLPAEAMLFYDPADMAWLRRCLEEKPAGQQQDIERH--KLNAMGAFAEAQT-CRRLVLLNYFGEGRQEP-- 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 680 ckkhpdvsCDNCcktkdyktrDVTDDVKSivRFVQEHSSSQGMRNIKHVGPsgRFTMNMLVDIFLGSKSAKIQS------ 753
Cdd:PRK11057 397 --------CGNC---------DICLDPPK--QYDGLEDAQKALSCIYRVNQ--RFGMGYVVEVLRGANNQRIRDyghdkl 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 754 GIFGKGSAYSRHNAERLFKKLILDKILDEDLYINANDQaiayvmLGNKAQTVLNG--NLKVDFMETENSSSVKKQKalva 831
Cdd:PRK11057 456 KVYGIGRDKSHEHWVSVIRQLIHLGLVTQNIAQHSALQ------LTEAARPVLRGevSLQLAVPRIVALKPRAMQK---- 525
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564730691 832 kvSQREEMVKKCLGELTEVCKSLGKVFGVHYFNIFNTVTLKKLAESLSSDPEVLLQIDGVTEDKLEKYGAEVISVLQKY 910
Cdd:PRK11057 526 --SFGGNYDRKLFAKLRKLRKSIADEENIPPYVVFNDATLIEMAEQMPITASEMLSVNGVGQRKLERFGKPFMALIRAH 602
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
282-483 |
2.67e-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: 308.31 E-value: 2.67e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 282 KIFHKKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPATY 361
Cdd:cd17920 2 QILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 362 LTGDKTDSEATNIYLQLskKDPIIKLLYVTPEKIcASNRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRQDYKRMNM 441
Cdd:cd17920 82 LNSTLSPEEKREVLLRI--KNGQYKLLYVTPERL-LSPDFLELLQRLPERKRLALIVVDEAHCVSQWGHDFRPDYLRLGR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 564730691 442 LRQKFPSVPVMALTATANPRVQKDILTQLKILRPQVFSMSFN 483
Cdd:cd17920 159 LRRALPGVPILALTATATPEVREDILKRLGLRNPVIFRASFD 200
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
275-483 |
5.52e-85 |
|
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: 273.09 E-value: 5.52e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 275 PHTKEMMKIFHKKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTS 354
Cdd:cd18015 1 PWSGKVKDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 355 LDIPATYLTGDKTDSEATNIYLQLSKKDPIIKLLYVTPEKICASNRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRQ 434
Cdd:cd18015 81 LGISATMLNASSSKEHVKWVHAALTDKNSELKLLYVTPEKIAKSKRFMSKLEKAYNAGRLARIAIDEVHCCSQWGHDFRP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 564730691 435 DYKRMNMLRQKFPSVPVMALTATANPRVQKDILTQLKILRPQVFSMSFN 483
Cdd:cd18015 161 DYKKLGILKRQFPNVPILGLTATATSKVLKDVQKILCIQKCLTFTASFN 209
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
484-618 |
3.66e-77 |
|
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: 248.66 E-value: 3.66e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 484 RHNLKYYVLPKKPKKVAFDCLEWIRKHHPYDSGIIYCLSRRECDTMADTLQRDGLAALAYHAGLSDSARDEVQQKWINqD 563
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLR-D 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 564730691 564 GCQVICATIAFGMGIDKPDVRFVIHASLPKSVEGYYQESGRAGRDGEISHCLLFY 618
Cdd:cd18794 80 KIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
281-483 |
5.95e-62 |
|
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: 5.95e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 281 MKIFHKKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPACV----SPGVTVVISPLRSLIVDQVQKLTSLd 356
Cdd:cd18018 1 LKLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLlrrrGPGLTLVVSPLIALMKDQVDALPRA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 357 IPATYLTGDKTDSEATNIYLQLSKKDpiIKLLYVTPEKICASnrliSTLENLYERKLLARFVIDEAHCVSQWGHDFRQDY 436
Cdd:cd18018 80 IKAAALNSSLTREERRRILEKLRAGE--VKILYVSPERLVNE----SFRELLRQTPPISLLVVDEAHCISEWSHNFRPDY 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 564730691 437 KRM-NMLRQKFPSVPVMALTATANPRVQKDILTQLKILRPQVFSMSFN 483
Cdd:cd18018 154 LRLcRVLRELLGAPPVLALTATATKRVVEDIASHLGIPESGVVRGPLY 201
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
282-475 |
1.68e-61 |
|
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: 208.09 E-value: 1.68e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 282 KIFHKKFGLHNFRTN-QLEAINAALLGE-DCFILMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPA 359
Cdd:cd18014 2 STLKKVFGHSDFKSPlQEKATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 360 TYLTGDKTDSEATNIYLQLSKKDPIIKLLYVTPEKiCASNRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRQDYKRM 439
Cdd:cd18014 82 DSLNSKLSAQERKRIIADLESEKPQTKFLYITPEM-AATSSFQPLLSSLVSRNLLSYLVVDEAHCVSQWGHDFRPDYLRL 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 564730691 440 NMLRQKFPSVPVMALTATANPRVQKDILTQLKILRP 475
Cdd:cd18014 161 GALRSRYGHVPWVALTATATPQVQEDIFAQLRLKKP 196
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
288-483 |
3.41e-50 |
|
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: 175.73 E-value: 3.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 288 FGLHNFRTNQLEAINAAL-LGEDCFILMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPATYLTGDK 366
Cdd:cd18017 8 FGHSSFRPVQWKVIRSVLeERRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPACFLGSAQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 367 TDSEATNIylqlskKDPIIKLLYVTPEKICASNRLISTLENlyERKLLArfvIDEAHCVSQWGHDFRQDYKRMNMLRQKF 446
Cdd:cd18017 88 SQNVLDDI------KMGKIRVIYVTPEFVSKGLELLQQLRN--GITLIA---IDEAHCVSQWGHDFRSSYRHLGSIRNRL 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 564730691 447 PSVPVMALTATANPRVQKDILTQLKILRPQVFSMSFN 483
Cdd:cd18017 157 PNVPIVALTATATPSVRDDIIKNLNLRNPQITCTSFD 193
|
|
| DpdF |
NF041063 |
protein DpdF; |
297-634 |
3.68e-50 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 191.28 E-value: 3.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 297 QLEAINAALL---GEDCFILMPTGGGKSLCYQLPACVSP---GVTVVISPLRSLIVDQVQKLTSL-------DIPATYLT 363
Cdd:NF041063 145 QREAVRAALLappGSTLIVNLPTGSGKSLVAQAPALLASrqgGLTLVVVPTVALAIDQERRARELlrragpdLGGPLAWH 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 364 GDKTDSEATNIYLQLskKDPIIKLLYVTPEKICASnrLISTLENLYERKLLARFVIDEAHCVSQWGHDFRQDYKRMNMLR 443
Cdd:NF041063 225 GGLSAEERAAIRQRI--RDGTQRILFTSPESLTGS--LRPALFDAAEAGLLRYLVVDEAHLVDQWGDGFRPEFQLLAGLR 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 444 QKFPSVP-------VMALTATanprvqkdiLTQ-----LKIL-----RPQVFSMSFNRHNLKYYVLPKKPKKVAFDC-LE 505
Cdd:NF041063 301 RSLLRLApsgrpfrTLLLSAT---------LTEstldtLETLfgppgPFIVVSAVQLRPEPAYWVAKCDSEEERRERvLE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 506 WIRkhH---PYdsgIIYCLSRRECDTMADTLQRDGLAALA-YHAGLSDSARDEVQQKWiNQDGCQVICATIAFGMGIDKP 581
Cdd:NF041063 372 ALR--HlprPL---ILYVTKVEDAEAWLQRLRAAGFRRVAlFHGDTPDAERERLIEQW-RENELDIVVATSAFGLGMDKS 445
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 564730691 582 DVRFVIHASLPKSVEGYYQESGRAGRDGEISHCLLFYTYHDVT---RL--KRLIMMEK 634
Cdd:NF041063 446 DVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLDiakSLnrPKLISVEK 503
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
294-466 |
2.93e-30 |
|
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: 117.34 E-value: 2.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 294 RTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPAC------VSPGVTVVISPLRSLIVDQVQKLTSLDIPATY-----L 362
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKLGKGLGLkvaslL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 363 TGDKTDSEATNIylqlsKKdpiIKLLYVTPEKICASNRLISTLENLyerKLLarfVIDEAHCVSQWGhdFRQDYKRmnML 442
Cdd:pfam00270 81 GGDSRKEQLEKL-----KG---PDILVGTPGRLLDLLQERKLLKNL---KLL---VLDEAHRLLDMG--FGPDLEE--IL 142
|
170 180
....*....|....*....|....
gi 564730691 443 RQKFPSVPVMALTATAnPRVQKDI 466
Cdd:pfam00270 143 RRLPKKRQILLLSATL-PRNLEDL 165
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
286-466 |
5.41e-23 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 97.95 E-value: 5.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 286 KKFGLHNFRTNQLEAINAALLGE-DCFILMPTGGGKSLCYQLPA-----CVSPGVTVVISPLRSLIVDQVQKLTSL---- 355
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPAlealkRGKGGRVLVLVPTRELAEQWAEELKKLgpsl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 356 -DIPATYLTGDKTDSEATNIylqlskKDPIIKLLYVTPEKIcasnrLISTLENLYERKLLARFVIDEAHCVSQWGhdFRQ 434
Cdd:smart00487 82 gLKVVGLYGGDSKREQLRKL------ESGKTDILVTTPGRL-----LDLLENDKLSLSNVDLVILDEAHRLLDGG--FGD 148
|
170 180 190
....*....|....*....|....*....|..
gi 564730691 435 DYKRmnMLRQKFPSVPVMALTATANPRVQKDI 466
Cdd:smart00487 149 QLEK--LLKLLPKNVQLLLLSATPPEEIENLL 178
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
620-692 |
6.93e-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: 90.04 E-value: 6.93e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564730691 620 YHDVTRLKRLIMMEkDGNHHTRETHFNNLYSMVHYCENITECRRIQLLAYFGENgFNPDFCKKhpdvsCDNCC 692
Cdd:pfam16124 1 YQDVVRLRFLIEQS-EADEERKEVELQKLQAMVAYCENTTDCRRKQLLRYFGEE-FDSEPCGN-----CDNCL 66
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
527-609 |
3.90e-20 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 85.73 E-value: 3.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 527 DTMADTLQRDGLAALAYHAGLSDSARDEVQQKWiNQDGCQVICATIAFGMGIDKPDVRFVIHASLPKSVEGYYQESGRAG 606
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKF-NNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAG 79
|
...
gi 564730691 607 RDG 609
Cdd:smart00490 80 RAG 82
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
838-917 |
4.88e-20 |
|
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: 85.43 E-value: 4.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 838 EMVKKCLGELTEVCKSLGKVFGVHYFNIFNTVTLKKLAESLSSDPEVLLQIDGVTEDKLEKYGAEVISVLQKYSEWTSPA 917
Cdd:smart00341 2 ERQLRLLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVIQEASDSPSEA 81
|
|
| BDHCT |
pfam08072 |
BDHCT (NUC031) domain; This is a C-terminal domain in Bloom's syndrome DEAD helicase subfamily. |
1-37 |
9.52e-19 |
|
BDHCT (NUC031) domain; This is a C-terminal domain in Bloom's syndrome DEAD helicase subfamily.
Pssm-ID: 462356 Cd Length: 41 Bit Score: 80.40 E-value: 9.52e-19
10 20 30
....*....|....*....|....*....|....*..
gi 564730691 1 MEHICKLIDTIPDDKLKLLDCGNELLQQRNIRRKLLT 37
Cdd:pfam08072 5 MEEICKLVDTIPIHELKALSCGNELLQQRDIRRKLLA 41
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
501-609 |
1.32e-17 |
|
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: 79.18 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 501 FDCLEWIRKHHPYDSGIIYCLSRRECDTMAdTLQRDGLAALAYHAGLSDSARDEVQQKWiNQDGCQVICATIAFGMGIDK 580
Cdd:pfam00271 3 LEALLELLKKERGGKVLIFSQTKKTLEAEL-LLEKEGIKVARLHGDLSQEEREEILEDF-RKGKIDVLVATDVAERGLDL 80
|
90 100
....*....|....*....|....*....
gi 564730691 581 PDVRFVIHASLPKSVEGYYQESGRAGRDG 609
Cdd:pfam00271 81 PDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
307-457 |
1.65e-16 |
|
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: 77.44 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 307 GEDCFILMPTGGGKSLCYQLPA-CVS---PGVTVVISPLRSLIVDQ---VQKLTSLDIPATYLTGDKTDSEATNIYLQLS 379
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAAlLLLlkkGKKVLVLVPTKALALQTaerLRELFGPGIRVAVLVGGSSAEEREKNKLGDA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564730691 380 kkdpiiKLLYVTPEKIcasNRLISTLENLYERKlLARFVIDEAHCVSQWGHDFRQDYKRmnMLRQKFPSVPVMALTAT 457
Cdd:cd00046 81 ------DIIIATPDML---LNLLLREDRLFLKD-LKLIIVDEAHALLIDSRGALILDLA--VRKAGLKNAQVILLSAT 146
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
297-629 |
2.47e-16 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 82.50 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 297 QLEAINAALLGEDCFILMPTGGGKSLCYQLPAC--VSPGV-----TVVISPLRSL---IVDQVQKLTS-LDIPATYLTGd 365
Cdd:COG0513 29 QAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLqrLDPSRprapqALILAPTRELalqVAEELRKLAKyLGLRVATVYG- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 366 ktdseATNIYLQ---LSKKDPIIkllyV-TPekicasNRLIstleNLYERKLLA-----RFVIDEAhcvsqwghD----- 431
Cdd:COG0513 108 -----GVSIGRQiraLKRGVDIV----VaTP------GRLL----DLIERGALDlsgveTLVLDEA--------Drmldm 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 432 -FRQDYKR-MNML---RQkfpsvpVMALTATANPRVQKdiLTQlKILR-PQVfsMSFNRHNLK------YYVLPKKPKKv 499
Cdd:COG0513 161 gFIEDIERiLKLLpkeRQ------TLLFSATMPPEIRK--LAK-RYLKnPVR--IEVAPENATaetieqRYYLVDKRDK- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 500 aFDCLEWIRKHHPYDSGIIYCLSRRECDTMADTLQRDGLAALAYHAGLSDSARDEVQQKWinQDG-CQVICAT-IAfGMG 577
Cdd:COG0513 229 -LELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAF--RNGkIRVLVATdVA-ARG 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 564730691 578 IDKPDVRFVIHASLPKSVEGYYQESG---RAGRDGEishCLLFYTYHDVTRLKRL 629
Cdd:COG0513 305 IDIDDVSHVINYDLPEDPEDYVHRIGrtgRAGAEGT---AISLVTPDERRLLRAI 356
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
287-623 |
3.72e-15 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 79.68 E-value: 3.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 287 KFGLHNFrtnQLEAINAALL----GEDCFIL-MPTGGGKS-----LCYQLPAcvsPGVTVVISPLRSLiVDQ-VQKLTSL 355
Cdd:COG1061 78 SFELRPY---QQEALEALLAalerGGGRGLVvAPTGTGKTvlalaLAAELLR---GKRVLVLVPRREL-LEQwAEELRRF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 356 DiPATYLTGDKTDSEAtniylqlskkdPIIkllyvtpekicasnrlISTLENLYERKLLARF-------VIDEAHcvsqw 428
Cdd:COG1061 151 L-GDPLAGGGKKDSDA-----------PIT----------------VATYQSLARRAHLDELgdrfglvIIDEAH----- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 429 gHDFRQDYKRmnmLRQKFPSVPVMALTATANPRVQKDILTQL----------------KILRPQVF---SMSFNRHNLKY 489
Cdd:COG1061 198 -HAGAPSYRR---ILEAFPAAYRLGLTATPFRSDGREILLFLfdgivyeyslkeaiedGYLAPPEYygiRVDLTDERAEY 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 490 YVL------------PKKPKKVAfdclEWIRKHHPYDSGIIYCLSRRECDTMADTLQRDGLAALAYHAGLSDSARDEVQQ 557
Cdd:COG1061 274 DALserlrealaadaERKDKILR----ELLREHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILE 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564730691 558 kWINQDGCQVICATIAFGMGIDKPDVRFVIHASLPKSVEGYYQESGRAGRDGEISHCLLFYTYHDV 623
Cdd:COG1061 350 -AFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPGKEDALVYDFVGN 414
|
|
| RQC |
smart00956 |
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix ... |
701-806 |
4.27e-15 |
|
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: 71.74 E-value: 4.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 701 DVTDDVKSIVRFVQEHSssqgmrnikhvgpsGRFTMNMLVDIFLGSKSAKI------QSGIFGKGSAYSRHNAERLFKKL 774
Cdd:smart00956 1 DVTEEAQKLLSCVYRTG--------------QRFGAGHVIDVLRGSKNKKIrqkghdRLSTFGIGKDLSKKEWRRLIRQL 66
|
90 100 110
....*....|....*....|....*....|..
gi 564730691 775 ILDKILDEDlyinanDQAIAYVMLGNKAQTVL 806
Cdd:smart00956 67 IAEGYLRED------GGRYPYLKLTEKARPVL 92
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
488-618 |
7.14e-15 |
|
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: 72.15 E-value: 7.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 488 KYYVLPKKPKKVAfdCLEWIRKHHPYDSGIIYCLSRRECDTMADTLQRDGLAALAYHAGLSDSARDEVQQKWINQDgCQV 567
Cdd:cd18787 4 LYVVVEEEEKKLL--LLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGK-VRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 564730691 568 ICATIAFGMGIDKPDVRFVIHASLPKSVEGYYQESGRAGRDGEISHCLLFY 618
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
697-812 |
1.24e-14 |
|
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: 70.64 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 697 YKTRDVTDDVKSIVRFVQEhsssqgMRnikhvgpsGRFTMNMLVDIFLGSKSAKI------QSGIFGKGSAYSRHNAERL 770
Cdd:pfam09382 2 PETVDVTEEAQKILSCVYR------TG--------QRFGAGHLIDVLRGSKNKKIrqlghdKLSTFGIGKDLSKKEWRRI 67
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 564730691 771 FKKLILDKILDEDLyinandQAIAYVMLGNKAQTVLNGNLKV 812
Cdd:pfam09382 68 IRQLIAEGYLEVDI------EFYSVLKLTPKAREVLKGEEKV 103
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
286-612 |
2.67e-14 |
|
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: 77.57 E-value: 2.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 286 KKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPA----CVSPGVTV-VISPLRSLIVDQVQKLTSL----- 355
Cdd:COG1205 50 KKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVlealLEDPGATAlYLYPTKALARDQLRRLRELaealg 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 356 -DI-PATYlTGDkTDSEAtniylqlskKDPIIK---LLYVTPEKICAS-----NRLISTLENLyerkllaRF-VIDEAHC 424
Cdd:COG1205 130 lGVrVATY-DGD-TPPEE---------RRWIREhpdIVLTNPDMLHYGllphhTRWARFFRNL-------RYvVIDEAHT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 425 ---V--SQWGHDFRqdykRMNMLRQKFPSVPVMALT-AT-ANPrvqKDILTQLkILRP-QVFSMSFNRHNLKYYVL---P 493
Cdd:COG1205 192 yrgVfgSHVANVLR----RLRRICRHYGSDPQFILAsATiGNP---AEHAERL-TGRPvTVVDEDGSPRGERTFVLwnpP 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 494 KKPKKVAFDCL--------EWIRKHHpydSGIIYCLSRRECDTMADTLQR------DGLAALAYHAGLSDSARDEVQQKW 559
Cdd:COG1205 264 LVDDGIRRSALaeaarllaDLVREGL---RTLVFTRSRRGAELLARYARRalrepdLADRVAAYRAGYLPEERREIERGL 340
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 564730691 560 inQDG-CQVICATIAFGMGIDKPDVRFVIHASLPKSVEGYYQESGRAGRDGEIS 612
Cdd:COG1205 341 --RSGeLLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDS 392
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
268-607 |
1.50e-13 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 74.55 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 268 RFQSLSFPHTKEMMKifhkKFGLHNFRTNQLEAINAALLGEDCFIL-MPTGGGKSLCYQLPAC--VSPGVTVV-ISPLRS 343
Cdd:COG1204 2 KVAELPLEKVIEFLK----ERGIEELYPPQAEALEAGLLEGKNLVVsAPTASGKTLIAELAILkaLLNGGKALyIVPLRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 344 LIvDQV-----QKLTSLDIPATYLTGDKTDSEAtniylQLSKKDPIIkllyVTPEKicasnrLISTLENlyERKLLARF- 417
Cdd:COG1204 78 LA-SEKyrefkRDFEELGIKVGVSTGDYDSDDE-----WLGRYDILV----ATPEK------LDSLLRN--GPSWLRDVd 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 418 --VIDEAHCVsqwghdfrQDYKR---MNM----LRQKFPSVPVMALTAT-ANPrvqKDIltqLKILRPQVFSMSFNRHNL 487
Cdd:COG1204 140 lvVVDEAHLI--------DDESRgptLEVllarLRRLNPEAQIVALSATiGNA---EEI---AEWLDAELVKSDWRPVPL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 488 KYYVLpkKPKKVAFDC--------LEWIRKHHPYDSG--IIYCLSRRECDTMAD-------------------------- 531
Cdd:COG1204 206 NEGVL--YDGVLRFDDgsrrskdpTLALALDLLEEGGqvLVFVSSRRDAESLAKkladelkrrltpeereeleelaeell 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 532 -----TLQRDGLAAL-----AYH-AGLSDSARDEVQQkWInQDG-CQVICAT--IAfgMGIDKPdVRFVIHASL------ 591
Cdd:COG1204 284 evseeTHTNEKLADClekgvAFHhAGLPSELRRLVED-AF-REGlIKVLVATptLA--AGVNLP-ARRVIIRDTkrggmv 358
|
410
....*....|....*.
gi 564730691 592 PKSVEGYYQESGRAGR 607
Cdd:COG1204 359 PIPVLEFKQMAGRAGR 374
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
297-634 |
8.56e-13 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 72.13 E-value: 8.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 297 QLEAINAALLGEDCFILMPTGGGKSLCYQLP---ACVS----------PGVTVVISPLRSLIVdQVQ---KLTSLDIP-- 358
Cdd:PLN00206 148 QMQAIPAALSGRSLLVSADTGSGKTASFLVPiisRCCTirsghpseqrNPLAMVLTPTRELCV-QVEdqaKVLGKGLPfk 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 359 -ATYLTGDKTDSeatniylQLSKKDPIIKLLYVTPekicasNRLISTL-ENLYERKLLARFVIDEAHCVSQWGhdFRQdy 436
Cdd:PLN00206 227 tALVVGGDAMPQ-------QLYRIQQGVELIVGTP------GRLIDLLsKHDIELDNVSVLVLDEVDCMLERG--FRD-- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 437 kRMNMLRQKFPSVPVMALTATANPRVQKDILTQLKilrpQVFSMSF---NR-----HNLKYYVLPKKPKKVAFDCLEwiR 508
Cdd:PLN00206 290 -QVMQIFQALSQPQVLLFSATVSPEVEKFASSLAK----DIILISIgnpNRpnkavKQLAIWVETKQKKQKLFDILK--S 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 509 KHHPYDSGIIYCLSRRECDTMADTLQR-DGLAALAYHAGLSDSARDEVQQKWINQDgCQVICATIAFGMGIDKPDVRFVI 587
Cdd:PLN00206 363 KQHFKPPAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERREVMKSFLVGE-VPVIVATGVLGRGVDLLRVRQVI 441
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 564730691 588 HASLPKSVEGYYQESGRAGRDGEISHCLLFYTYHDVTRLKRLIMMEK 634
Cdd:PLN00206 442 IFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLK 488
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
841-907 |
1.60e-11 |
|
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: 60.63 E-value: 1.60e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564730691 841 KKCLGELTEVCKSLGKVFGVHYFNIFNTVTLKKLAESLSSDPEVLLQIDGVTEDKLEKYGAEVISVL 907
Cdd:pfam00570 2 LALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
297-423 |
5.89e-10 |
|
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: 59.52 E-value: 5.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 297 QLEAINAALLGEDCFILMPTGGGKSLCYQLP----ACVSPGVT-VVISPLRSLIVDQVQKLTSL------DI-PATYlTG 364
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPileaLLRDPGSRaLYLYPTKALAQDQLRSLRELleqlglGIrVATY-DG 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564730691 365 DKTDSEATNIYLQLSkkdpiiKLLYVTPEKICAS-----NRLISTLENLyerkllaRF-VIDEAH 423
Cdd:cd17923 84 DTPREERRAIIRNPP------RILLTNPDMLHYAllphhDRWARFLRNL-------RYvVLDEAH 135
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
307-423 |
1.14e-09 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 58.36 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 307 GEDCFILMPTGGGKSLCYQLPACVS------PGVTVV-ISPLRSLIVDQVQKLT------SLDIPATYLTGDKTDSEATn 373
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSladepeKGVQVLyISPLKALINDQERRLEepldeiDLEIPVAVRHGDTSQSEKA- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 564730691 374 iylQLSKKDPIIklLYVTPEKICA---SNRLISTLENLyerkllaRFVI-DEAH 423
Cdd:cd17922 80 ---KQLKNPPGI--LITTPESLELllvNKKLRELFAGL-------RYVVvDEIH 121
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
517-610 |
1.72e-09 |
|
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: 57.27 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 517 IIYCLSRRECDTMA----DTLQRDGLAA---LAYHAGLSDSARDEVQQKWINQDGCQVIcATIAFGMGIDKPDVRFVIHA 589
Cdd:cd18797 39 IVFCRSRKLAELLLrylkARLVEEGPLAskvASYRAGYLAEDRREIEAELFNGELLGVV-ATNALELGIDIGGLDAVVLA 117
|
90 100
....*....|....*....|.
gi 564730691 590 SLPKSVEGYYQESGRAGRDGE 610
Cdd:cd18797 118 GYPGSLASLWQQAGRAGRRGK 138
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
517-639 |
3.12e-08 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 57.98 E-value: 3.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 517 IIYCLSRRECDTMADTLqrdGLAALAYHAGLSDSARDEVQQKWINQDgCQVICATIAFGMGIDKPDVRfVIHASLPK--- 593
Cdd:COG1202 431 IIFTNSRRRCHEIARAL---GYKAAPYHAGLDYGERKKVERRFADQE-LAAVVTTAALAAGVDFPASQ-VIFDSLAMgie 505
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 564730691 594 --SVEGYYQESGRAGRDGeishcllfytYHDvtRLKRLIMMEKDGNHH 639
Cdd:COG1202 506 wlSVQEFHQMLGRAGRPD----------YHD--RGKVYLLVEPGKSYH 541
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
513-624 |
6.49e-08 |
|
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: 50.78 E-value: 6.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 513 YDSGIIYCLSRRECDTMADTLQrdglaalayhaglsdsardevqqkwinqdgcqVICATIAFGMGIDKPDVRFVIHASLP 592
Cdd:cd18785 3 VVKIIVFTNSIEHAEEIASSLE--------------------------------ILVATNVLGEGIDVPSLDTVIFFDPP 50
|
90 100 110
....*....|....*....|....*....|..
gi 564730691 593 KSVEGYYQESGRAGRDGEIShcllfYTYHDVT 624
Cdd:cd18785 51 SSAASYIQRVGRAGRGGKDE-----GEVILFV 77
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
297-462 |
6.84e-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: 53.42 E-value: 6.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 297 QLEAINAALLGEDCFIL-MPTGGGKSLCYQLPA----CVSPGVTVVISPLRSLiVDQV-----QKLTSLDIPATYLTGDK 366
Cdd:cd17921 6 QREALRALYLSGDSVLVsAPTSSGKTLIAELAIlralATSGGKAVYIAPTRAL-VNQKeadlrERFGPLGKNVGLLTGDP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 367 TDSeatniYLQLSKKDPIIkllyVTPEKICAsnrLISTLENLYERKLLArFVIDEAHCVSqwghdfrqDYKR-------M 439
Cdd:cd17921 85 SVN-----KLLLAEADILV----ATPEKLDL---LLRNGGERLIQDVRL-VVVDEAHLIG--------DGERgvvlellL 143
|
170 180
....*....|....*....|....
gi 564730691 440 NMLRQKFPSVPVMALTAT-ANPRV 462
Cdd:cd17921 144 SRLLRINKNARFVGLSATlPNAED 167
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
297-628 |
1.16e-07 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 55.55 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 297 QLEAINAALLGEDCFILMPTGGGKSLCYQLPACV--------SPG---VTVVISPLRSLiVDQvqkltsldIPATYLT-G 364
Cdd:PTZ00110 157 QVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVhinaqpllRYGdgpIVLVLAPTREL-AEQ--------IREQCNKfG 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 365 DKTDSEATNIYLQLSKKDPIIKLLYVTPEKICASNRLISTLE-NLYERKLLARFVIDEAHCVSQWGHDFrQDYKRMNMLR 443
Cdd:PTZ00110 228 ASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLEsNVTNLRRVTYLVLDEADRMLDMGFEP-QIRKIVSQIR 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 444 qkfPSVPVMALTATANPRVQK---DILTQLKIlRPQVFSMSFNR-HNLK--YYVLPKKPKKVAFDCLeWIRKHHPYDSGI 517
Cdd:PTZ00110 307 ---PDRQTLMWSATWPKEVQSlarDLCKEEPV-HVNVGSLDLTAcHNIKqeVFVVEEHEKRGKLKML-LQRIMRDGDKIL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 518 IYCLSRRECDTMADTLQRDGLAALAYHAglsDSARDEvqQKWINQD----GCQVICATIAFGMGIDKPDVRFVIHASLPK 593
Cdd:PTZ00110 382 IFVETKKGADFLTKELRLDGWPALCIHG---DKKQEE--RTWVLNEfktgKSPIMIATDVASRGLDVKDVKYVINFDFPN 456
|
330 340 350
....*....|....*....|....*....|....*
gi 564730691 594 SVEGYYQESGRAGRDGEISHCLLFYTyHDVTRLKR 628
Cdd:PTZ00110 457 QIEDYVHRIGRTGRAGAKGASYTFLT-PDKYRLAR 490
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
517-629 |
2.41e-07 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 54.45 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 517 IIYCLSRRECDTMADTLQRDGLAALAYHAGLSDSARDEVQQKWiNQDGCQVICATIAFGMGIDKPDVRFVIHASLPKSVE 596
Cdd:PTZ00424 271 IIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREF-RSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPE 349
|
90 100 110
....*....|....*....|....*....|...
gi 564730691 597 GYYQESGRAGRDGEISHCLLFYTYHDVTRLKRL 629
Cdd:PTZ00424 350 NYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEI 382
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
292-481 |
2.57e-07 |
|
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: 52.36 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 292 NFRTNQLEAINAALLGEDCFIL-MPTGGGKSLCYQL--------PACVSPG--VTVVISPLRSLIVDQV----QKLTSLD 356
Cdd:cd18023 1 YFNRIQSEVFPDLLYSDKNFVVsAPTGSGKTVLFELailrllkeRNPLPWGnrKVVYIAPIKALCSEKYddwkEKFGPLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 357 IPATYLTGDkTDSEATNiylQLSKKDPIIkllyVTPEKICASNRLISTLENLYErkLLARFVIDEAHCVSQW-GHDFRQD 435
Cdd:cd18023 81 LSCAELTGD-TEMDDTF---EIQDADIIL----TTPEKWDSMTRRWRDNGNLVQ--LVALVLIDEVHIIKENrGATLEVV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564730691 436 YKRMNML-------RQKFPSVPVMALTATAnPRVQkDILTQLKILRPQVFSMS 481
Cdd:cd18023 151 VSRMKTLsssselrGSTVRPMRFVAVSATI-PNIE-DLAEWLGDNPAGCFSFG 201
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
498-609 |
7.98e-07 |
|
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: 49.86 E-value: 7.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 498 KVAFDCLEWIRKHHPYdsgIIYCLSRRECDTMADTLQrdGLAalAYHAGLSDSARDEV----QQKWInqdgcQVICATIA 573
Cdd:cd18795 31 IIVLLKIETVSEGKPV---LVFCSSRKECEKTAKDLA--GIA--FHHAGLTREDRELVeelfREGLI-----KVLVATST 98
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 564730691 574 FGMGIDKPdVRFVIHASLPKSVEGYYQE---------SGRAGRDG 609
Cdd:cd18795 99 LAAGVNLP-ARTVIIKGTQRYDGKGYRElspleylqmIGRAGRPG 142
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
503-617 |
8.86e-07 |
|
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: 49.57 E-value: 8.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 503 CLEWIRKHhpyDSGIIYCLSRRECDTMADTL------QRDGLAALAYHAGLSDSARDEVQQKWinQDG-CQVICATIAFG 575
Cdd:cd18796 31 VIFLLERH---KSTLVFTNTRSQAERLAQRLrelcpdRVPPDFIALHHGSLSRELREEVEAAL--KRGdLKVVVATSSLE 105
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 564730691 576 MGIDKPDVRFVIHASLPKSVEGYYQESGRAG-RDGEISHCLLF 617
Cdd:cd18796 106 LGIDIGDVDLVIQIGSPKSVARLLQRLGRSGhRPGAASKGRLV 148
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
293-457 |
2.02e-04 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 43.58 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 293 FRTNQLEAINAALLGEDCFILMPTGGGKS-----LC----YQLPaCVSPGVTVVISPLRSLIVDQVQKL-TSLDIPAtYL 362
Cdd:cd17927 3 PRNYQLELAQPALKGKNTIICLPTGSGKTfvavlICehhlKKFP-AGRKGKVVFLANKVPLVEQQKEVFrKHFERPG-YK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 363 TGDKTDSEATNIYLQLSKKDPiiKLLYVTPEkICASNRLISTLENLYERKLLarfVIDEAHCVSQwGHDFRQDYKRmnML 442
Cdd:cd17927 81 VTGLSGDTSENVSVEQIVESS--DVIIVTPQ-ILVNDLKSGTIVSLSDFSLL---VFDECHNTTK-NHPYNEIMFR--YL 151
|
170
....*....|....*....
gi 564730691 443 RQKFPSV---P-VMALTAT 457
Cdd:cd17927 152 DQKLGSSgplPqILGLTAS 170
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
297-460 |
2.48e-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: 43.09 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 297 QLEAINAALL-GEDCFILMPTGGGKSLCYQL---PACVSPGVTVVISPLRSLIVDQV---QKLTSLDIPATYLTGDkTDS 369
Cdd:cd18028 6 QAEAVRAGLLkGENLLISIPTASGKTLIAEMamvNTLLEGGKALYLVPLRALASEKYeefKKLEEIGLKVGISTGD-YDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 370 EATNiylqLSKKDPIIkllyVTPEKICASNRLISTLENlyerkLLARFVIDEAHCVSqwghdfrqDYKR-------MNML 442
Cdd:cd18028 85 DDEW----LGDYDIIV----ATYEKFDSLLRHSPSWLR-----DVGVVVVDEIHLIS--------DEERgptlesiVARL 143
|
170
....*....|....*....
gi 564730691 443 RQKFPSVPVMALTATA-NP 460
Cdd:cd18028 144 RRLNPNTQIIGLSATIgNP 162
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
513-617 |
7.89e-04 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 43.30 E-value: 7.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 513 YDSGIIYCLSRRECDTMADTLQRDGLAALAYHAGLSDSARDEVQQKWinQDG-CQVICATIAFGMGIDKPDVRFVIHASL 591
Cdd:PRK11634 245 FDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERL--KDGrLDILIATDVAARGLDVERISLVVNYDI 322
|
90 100
....*....|....*....|....*.
gi 564730691 592 PKSVEGYYQESGRAGRDGEISHCLLF 617
Cdd:PRK11634 323 PMDSESYVHRIGRTGRAGRAGRALLF 348
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
297-474 |
1.22e-03 |
|
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of infectious West Nile virus particles. New research suggests that DDX56 relocalizes to the site of virus assembly during WNV infection and that its interaction with WNV capsid in the cytoplasm may occur transiently during virion morphogenesis. DDX56 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350719 [Multi-domain] Cd Length: 206 Bit Score: 41.42 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 297 QLEAINAALLGEDCFILMPTGGGKSLCYQLP-----------ACVSPGVTVVI-SPLRSLiVDQVQK-LTSL------DI 357
Cdd:cd17961 21 QSKAIPLALEGKDILARARTGSGKTAAYALPiiqkilkakaeSGEEQGTRALIlVPTREL-AQQVSKvLEQLtaycrkDV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 358 PATYLTGDKTDSEATNIylqLSKKDPIIkllyV-TPEKI---CASNRLI--STLENLyerkllarfVIDEAHCVSQWGHD 431
Cdd:cd17961 100 RVVNLSASSSDSVQRAL---LAEKPDIV----VsTPARLlshLESGSLLllSTLKYL---------VIDEADLVLSYGYE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 564730691 432 frQDYKRmnmLRQKFPSVPVMALT-ATANPRVQKdiLTQLkILR 474
Cdd:cd17961 164 --EDLKS---LLSYLPKNYQTFLMsATLSEDVEA--LKKL-VLH 199
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
297-464 |
1.81e-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: 40.50 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 297 QLEAINAALLGEDCFILMPTGGGKSLCYQLPACV-----------SPGVtVVISPLRSL---IVDQVQKLTS-LDIPATY 361
Cdd:cd00268 17 QAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEkllpepkkkgrGPQA-LVLAPTRELamqIAEVARKLGKgTGLKVAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 362 LTGdktdseATNIYLQLSKKDPIIKLLYVTPEkicasnRListLENLYERKLLAR----FVIDEAhcvsqwghD------ 431
Cdd:cd00268 96 IYG------GAPIKKQIEALKKGPDIVVGTPG------RL---LDLIERGKLDLSnvkyLVLDEA--------Drmldmg 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 564730691 432 FRQD----YKRMNMLRQkfpsvpVMALTATANPRVQK 464
Cdd:cd00268 153 FEEDvekiLSALPKDRQ------TLLFSATLPEEVKE 183
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
309-461 |
2.09e-03 |
|
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350780 [Multi-domain] Cd Length: 189 Bit Score: 40.43 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 309 DCFILM--PTGGGKSLCYQLPAC----VSPGVTVV-ISPLRSLIVDQVQ----KLT-SLDIPATYLTGDKT-DSEAtniy 375
Cdd:cd18022 17 DNNVLLgaPTGSGKTIAAELAMFrafnKYPGSKVVyIAPLKALVRERVDdwkkRFEeKLGKKVVELTGDVTpDMKA---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 376 lqLSKKDPIIkllyVTPEKICASNRLISTLENLYERKLLarfVIDEAHCV-SQWGHDFRQDYKRMNML-RQKFPSVPVMA 453
Cdd:cd18022 93 --LADADIII----TTPEKWDGISRSWQTREYVQQVSLI---IIDEIHLLgSDRGPVLEVIVSRMNYIsSQTEKPVRLVG 163
|
....*....
gi 564730691 454 L-TATANPR 461
Cdd:cd18022 164 LsTALANAG 172
|
|
| DinG |
COG1199 |
Rad3-related DNA helicase DinG [Replication, recombination and repair]; |
282-364 |
2.46e-03 |
|
Rad3-related DNA helicase DinG [Replication, recombination and repair];
Pssm-ID: 440812 [Multi-domain] Cd Length: 629 Bit Score: 41.83 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 282 KIFHKKFGLHNFRTNQLEAINA---ALL-GEDCFILMPTGGGKSLCYQLPA---CVSPGVTVVIS----PLRSLIVDQ-- 348
Cdd:COG1199 4 GLLALAFPGFEPRPGQREMAEAvarALAeGRHLLIEAGTGTGKTLAYLVPAllaARETGKKVVIStatkALQEQLVEKdl 83
|
90
....*....|....*...
gi 564730691 349 --VQKLTSLDIPATYLTG 364
Cdd:COG1199 84 plLRKALGLPLRVALLKG 101
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
513-617 |
4.57e-03 |
|
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: 37.92 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564730691 513 YDSGIIYCLSRRECDTMADTLQRDGLAALAYHAGLSDSARDE--VQQKWINQDGCQVICATIAFGMGIDKPDVRFVIHAS 590
Cdd:cd18799 6 EIKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDeaLILLFFGELKPPILVTVDLLTTGVDIPEVDNVVFLR 85
|
90 100
....*....|....*....|....*...
gi 564730691 591 LPKSVEGYYQESGRAGR-DGEISHCLLF 617
Cdd:cd18799 86 PTESRTLFLQMLGRGLRlHEGKDFFTIL 113
|
|
| |
