|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
213-711 |
3.55e-178 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 528.56 E-value: 3.55e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 213 QEALNALNEFFGHKGFREKQWDVVRNVLGGKDQFVLMSTGYGKSVCYQLPSLLLNSMTVVVSPLISLMNDQVTTLVSKGI 292
Cdd:COG0514 3 DDALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 293 DAVKLdgHSTQ--IEWDQVANNMH--RIRFIYMSPEMVTSQKGLELLTSCRkhISLLAIDEAHCVSQWGHDFRNSYRHLA 368
Cdd:COG0514 83 RAAFL--NSSLsaEERREVLRALRagELKLLYVAPERLLNPRFLELLRRLK--ISLFAIDEAHCISQWGHDFRPDYRRLG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 369 EIRNRsdLCNIPMIALTATATVRVRDDVIANLRLRKPLITTTSFDRKNLYISVH--SSKDMAEDLGLFMKtdevkgRHFG 446
Cdd:COG0514 159 ELRER--LPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVpkPPDDKLAQLLDFLK------EHPG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 447 GPTIIYCQTKQMVDDVNCVLRRIGVRSAHYHAGLTKNQREKAHTDFMRDKITTIVATVAFGMGIDKPDVRNVIHYGCPNN 526
Cdd:COG0514 231 GSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 527 IESYYQEIGRAGRDGSPSICRVFWAPKDLNTIKFKLRNSQQKEEVVENLTMMLRQLELVLTTVGCRRYQLLKHFDPSYAK 606
Cdd:COG0514 311 IEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEERKRVERAKLDAMLAYAETTGCRRQFLLRYFGEELAE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 607 PptmqADCCDRCTEmlngnqdsSSSIVDVTTESKWLFQVINEMyNGKTGIGKPIEFLRGSSKEDWRIKTTSQQKLFGIGK 686
Cdd:COG0514 391 P----CGNCDNCLG--------PPETFDGTEAAQKALSCVYRT-GQRFGAGHVIDVLRGSKNEKIRQFGHDKLSTYGIGK 457
|
490 500
....*....|....*....|....*
gi 32564293 687 HIPDKWWKALAASLrIAGYLGEVRL 711
Cdd:COG0514 458 DLSDKEWRSVIRQL-LAQLFGERKL 481
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
217-686 |
1.10e-146 |
|
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: 446.52 E-value: 1.10e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 217 NALNEFFGHKGFREKQWDVVRNVLGGKDQFVLMSTGYGKSVCYQLPSLLLNSMTVVVSPLISLMNDQVTTLVSKGIDAVK 296
Cdd:TIGR00614 1 KILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 297 LDGHSTQIEWDQVANNMH--RIRFIYMSPEMVTSQKGLELLTSCRKHISLLAIDEAHCVSQWGHDFRNSYRHLAEIRNRs 374
Cdd:TIGR00614 81 LNSAQTKEQQLNVLTDLKdgKIKLLYVTPEKISASNRLLQTLEERKGITLIAVDEAHCISQWGHDFRPDYKALGSLKQK- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 375 dLCNIPMIALTATATVRVRDDVIANLRLRKPLITTTSFDRKNLYISVHSSK-DMAEDLGLFMKtdevkgRHFGGPT-IIY 452
Cdd:TIGR00614 160 -FPNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRRKTpKILEDLLRFIR------KEFEGKSgIIY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 453 CQTKQMVDDVNCVLRRIGVRSAHYHAGLTKNQREKAHTDFMRDKITTIVATVAFGMGIDKPDVRNVIHYGCPNNIESYYQ 532
Cdd:TIGR00614 233 CPSRKKVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 533 EIGRAGRDGSPSICRVFWAPKDLNTIKFKL---RNSQQKEEVVENLTMMlrqlELVLTTVGCRRYQLLKHFDPSYAKPPT 609
Cdd:TIGR00614 313 ESGRAGRDGLPSECHLFYAPADMNRLRRLLmeePDGNFRTYKLKLYEMM----EYCLNSSTCRRLILLSYFGEKGFNKSF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 610 MQA---DCCDRCTEMLNGNQDSSSSivDVTTESKWLFQVI--NEMYNGKTGIGKPIEFLRGSSKEDWRIKTTSQQKLFGI 684
Cdd:TIGR00614 389 CIMgteKCCDNCCKRLDYKTKDVTD--KVYDFGPQAQKALsaVGRLNQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLYGR 466
|
..
gi 32564293 685 GK 686
Cdd:TIGR00614 467 GK 468
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
215-876 |
1.08e-140 |
|
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: 435.27 E-value: 1.08e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 215 ALNALNEFFGHKGFREKQWDVVRNVLGGKDQFVLMSTGYGKSVCYQLPSLLLNSMTVVVSPLISLMNDQVTTLVSKGIDA 294
Cdd:TIGR01389 1 AQQVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 295 VKLDGHSTQIE----WDQVANNmhRIRFIYMSPEMVTSQKGLELLTscRKHISLLAIDEAHCVSQWGHDFRNSYRHLAEI 370
Cdd:TIGR01389 81 AYLNSTLSAKEqqdiEKALVNG--ELKLLYVAPERLEQDYFLNMLQ--RIPIALVAVDEAHCVSQWGHDFRPEYQRLGSL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 371 RNRSDlcNIPMIALTATATVRVRDDVIANLRLRKPLITTTSFDRKNLYISVHSSKDMAEDLglfmkTDEVKgRHFGGPTI 450
Cdd:TIGR01389 157 AERFP--QVPRIALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKNNKQKFL-----LDYLK-KHRGQSGI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 451 IYCQTKQMVDDVNCVLRRIGVRSAHYHAGLTKNQREKAHTDFMRDKITTIVATVAFGMGIDKPDVRNVIHYGCPNNIESY 530
Cdd:TIGR01389 229 IYASSRKKVEELAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESY 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 531 YQEIGRAGRDGSPSICRVFWAPKDLNTIKFKLRNSQQKEEVVENLTMMLRQLELVLTTVGCRRYQLLKHFDPSYAKPptm 610
Cdd:TIGR01389 309 YQEAGRAGRDGLPAEAILLYSPADIALLKRRIEQSEADDDYKQIEREKLRAMIAYCETQTCRRAYILRYFGENEVEP--- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 611 qadcCDRCTEMLngnqdSSSSIVDVTTESKWLFQVINEMyNGKTGIGKPIEFLRGSSKEDWRIKTTSQQKLFGIGKHIPD 690
Cdd:TIGR01389 386 ----CGNCDNCL-----DPPKSYDATVEAQKALSCVYRM-GQRFGVGYIIEVLRGSKNDKILQKGHDQLSTYGIGKDYTQ 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 691 KWWKALAASLRIAGYLGEVrlmqmkfgscitlselgerwlltgkemkiDATPILLQGKKekaapstvpgASRSQSTKsST 770
Cdd:TIGR01389 456 KEWRSLIDQLIAEGLLTEN-----------------------------DEIYIGLQLTE----------AARKVLKN-EV 495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 771 EIptkILGANKIREYEPANENEQLmnlkkqevTGLPEkiDQLRSRLDDIRVGIANMHEVAPFQIVSNTVLDCFANLRPTS 850
Cdd:TIGR01389 496 EV---LLRPFKVVAKEKTRVQKNL--------SVGVD--NALFEALRELRKEQADEQNVPPYVIFSDSTLREMAEKRPAT 562
|
650 660
....*....|....*....|....*.
gi 32564293 851 ASNLEMIDGMSAQQKSRYGKRFVDCV 876
Cdd:TIGR01389 563 LNALLKIKGVGQNKLDRYGEAFLEVI 588
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
216-413 |
5.47e-111 |
|
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: 342.14 E-value: 5.47e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 216 LNALNEFFGHKGFREKQWDVVRNVLG-GKDQFVLMSTGYGKSVCYQLPSLLLNSMTVVVSPLISLMNDQVTTLVSKGIDA 294
Cdd:cd18017 1 LNALNEYFGHSSFRPVQWKVIRSVLEeRRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 295 VKLDGHSTQIEWDqvANNMHRIRFIYMSPEMVtsQKGLELLTSCRKHISLLAIDEAHCVSQWGHDFRNSYRHLAEIRNRs 374
Cdd:cd18017 81 CFLGSAQSQNVLD--DIKMGKIRVIYVTPEFV--SKGLELLQQLRNGITLIAIDEAHCVSQWGHDFRSSYRHLGSIRNR- 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 32564293 375 dLCNIPMIALTATATVRVRDDVIANLRLRKPLITTTSFD 413
Cdd:cd18017 156 -LPNVPIVALTATATPSVRDDIIKNLNLRNPQITCTSFD 193
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
203-874 |
1.33e-109 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 353.63 E-value: 1.33e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 203 MKWASMTSPPQEALNALNEFFGHKGFREKQWDVVRNVLGGKDQFVLMSTGYGKSVCYQLPSLLLNSMTVVVSPLISLMND 282
Cdd:PRK11057 1 MAQAEVLNLESLAKQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 283 QVTTLVSKGIDAVKLDGHSTQIEWDQVANNMH--RIRFIYMSPEMVTSQKGLELLTSCRkhISLLAIDEAHCVSQWGHDF 360
Cdd:PRK11057 81 QVDQLLANGVAAACLNSTQTREQQLEVMAGCRtgQIKLLYIAPERLMMDNFLEHLAHWN--PALLAVDEAHCISQWGHDF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 361 RNSYRHLAEIRNRsdLCNIPMIALTATATVRVRDDVIANLRLRKPLITTTSFDRKNL-YISVHSSKDMaEDLGLFMKTDE 439
Cdd:PRK11057 159 RPEYAALGQLRQR--FPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIrYTLVEKFKPL-DQLMRYVQEQR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 440 vkgrhfGGPTIIYCQTKQMVDDVNCVLRRIGVRSAHYHAGLTKNQREKAHTDFMRDKITTIVATVAFGMGIDKPDVRNVI 519
Cdd:PRK11057 236 ------GKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 520 HYGCPNNIESYYQEIGRAGRDGSPSICRVFWAPKDLNTIKFKLRN---SQQKEEVVENLTMMLRQLElvltTVGCRRYQL 596
Cdd:PRK11057 310 HFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPADMAWLRRCLEEkpaGQQQDIERHKLNAMGAFAE----AQTCRRLVL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 597 LKHFDPSYAKPptmqADCCDRCTE---MLNGNQDSS---SSIVDVtteskwlfqvinemyNGKTGIGKPIEFLRGSSKEd 670
Cdd:PRK11057 386 LNYFGEGRQEP----CGNCDICLDppkQYDGLEDAQkalSCIYRV---------------NQRFGMGYVVEVLRGANNQ- 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 671 wRIKTTSQQKL--FGIGKHIPDKWWKALAASLRIAGYLGEVRLMQmkfgSCITLSElgerwlltgkemkiDATPILlqgK 748
Cdd:PRK11057 446 -RIRDYGHDKLkvYGIGRDKSHEHWVSVIRQLIHLGLVTQNIAQH----SALQLTE--------------AARPVL---R 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 749 KEKAAPSTVPgasRSQSTKSSTEipTKILGANKIReyepaneneqlmnlkkqevtglpekidQLRSRLDDIRVGIANMHE 828
Cdd:PRK11057 504 GEVSLQLAVP---RIVALKPRAM--QKSFGGNYDR---------------------------KLFAKLRKLRKSIADEEN 551
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 32564293 829 VAPFQIVSNTVLDCFANLRPTSASNLEMIDGMSAQQKSRYGKRFVD 874
Cdd:PRK11057 552 IPPYVVFNDATLIEMAEQMPITASEMLSVNGVGQRKLERFGKPFMA 597
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
218-413 |
2.64e-81 |
|
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: 262.86 E-value: 2.64e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 218 ALNEFFGHKGFREKQWDVVRNVLGGKDQFVLMSTGYGKSVCYQLPSLLLNSMTVVVSPLISLMNDQVTTLVSKGIDAVKL 297
Cdd:cd17920 3 ILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAAAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 298 DGHSTQIEWDQVANNMHR--IRFIYMSPEMVTSQKGLELLTSC--RKHISLLAIDEAHCVSQWGHDFRNSYRHLAEIRNR 373
Cdd:cd17920 83 NSTLSPEEKREVLLRIKNgqYKLLYVTPERLLSPDFLELLQRLpeRKRLALIVVDEAHCVSQWGHDFRPDYLRLGRLRRA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 32564293 374 sdLCNIPMIALTATATVRVRDDVIANLRLRKPLITTTSFD 413
Cdd:cd17920 163 --LPGVPILALTATATPEVREDILKRLGLRNPVIFRASFD 200
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
193-876 |
4.38e-81 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 287.95 E-value: 4.38e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 193 NVPQIDEATKMKWASMTSPPQEALNALNE-FFGHKGFREKQWDVVRNVLGGKDQFVLMSTGYGKSVCYQLPSLLLNSMTV 271
Cdd:PLN03137 425 DVTYTEGSNDKKWSSRNFPWTKKLEVNNKkVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITL 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 272 VVSPLISLMNDQVTTLVSKGIDAVKLdghSTQIEWDQ-------VANNMHRIRFIYMSPEMVTSQ----KGLELLTScRK 340
Cdd:PLN03137 505 VISPLVSLIQDQIMNLLQANIPAASL---SAGMEWAEqleilqeLSSEYSKYKLLYVTPEKVAKSdsllRHLENLNS-RG 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 341 HISLLAIDEAHCVSQWGHDFRNSYRHLAEIRNRSDlcNIPMIALTATATVRVRDDVIANLRLRKPLITTTSFDRKNLYIS 420
Cdd:PLN03137 581 LLARFVIDEAHCVSQWGHDFRPDYQGLGILKQKFP--NIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYS 658
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 421 V-HSSKDMAEDLGLFMKTDevkgrHFGGPTIIYCQTKQMVDDVNCVLRRIGVRSAHYHAGLTKNQREKAHTDFMRDKITT 499
Cdd:PLN03137 659 VvPKTKKCLEDIDKFIKEN-----HFDECGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINI 733
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 500 IVATVAFGMGIDKPDVRNVIHYGCPNNIESYYQEIGRAGRDGSPSICRVFWAPKDLNTIKF-----KLRNSQQK------ 568
Cdd:PLN03137 734 ICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGRAGRDGQRSSCVLYYSYSDYIRVKHmisqgGVEQSPMAmgynrm 813
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 569 -------EEVVENLTMMLRQLElvlTTVGCRRYQLLKHFDPSYAkpptmQADC---CDRCTemlngnqdSSSSIV--DVT 636
Cdd:PLN03137 814 assgrilETNTENLLRMVSYCE---NEVDCRRFLQLVHFGEKFD-----STNCkktCDNCS--------SSKSLIdkDVT 877
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 637 TESKWLFQVInEMYNGKTGIGKPIEFLRGSSKEDWRIKTTSQQKLFGIGKHIPDKWWKALAASLRIAGYLGE-VRLMQMk 715
Cdd:PLN03137 878 EIARQLVELV-KLTGERFSSAHILEVYRGSLNQYVKKHRHETLSLHGAGKHLSKGEASRILHYLVTEDILAEdVKKSDL- 955
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 716 FGSCITLSELGER---WLLTGKE---MKIDATPILLQGKKEKAAPSTVPGASRSQSTKssteiptkilgankirEYEPAN 789
Cdd:PLN03137 956 YGSVSSLLKVNESkayKLFSGGQtiiMRFPSSVKASKPSKFEATPAKGPLTSGKQSTL----------------PMATPA 1019
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 790 ENEQLMNLKKQEVTGLpekiDQLRSRLddirVGIANmHEVAPFQIVSNTVLDCFANLRPTSASNLEMIDGMSAQQKSRYG 869
Cdd:PLN03137 1020 QPPVDLNLSAILYTAL----RKLRTAL----VKEAG-DGVMAYHIFGNATLQQISKRIPRTKEELLEINGLGKAKVSKYG 1090
|
....*..
gi 32564293 870 KRFVDCV 876
Cdd:PLN03137 1091 DRLLETI 1097
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
414-550 |
4.91e-68 |
|
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: 223.62 E-value: 4.91e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 414 RKNLYISVHSSKDMAEDLGLFMktdEVKGRHFGGPTIIYCQTKQMVDDVNCVLRRIGVRSAHYHAGLTKNQREKAHTDFM 493
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDLLK---RIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWL 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 32564293 494 RDKITTIVATVAFGMGIDKPDVRNVIHYGCPNNIESYYQEIGRAGRDGSPSICRVFW 550
Cdd:cd18794 78 RDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
216-413 |
1.79e-56 |
|
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: 194.01 E-value: 1.79e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 216 LNALNEFFGHKGFREKQWDVVRNVLGGKDQFVLMSTGYGKSVCYQLPSLLLN----SMTVVVSPLISLMNDQVTTLvSKG 291
Cdd:cd18018 1 LKLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRrrgpGLTLVVSPLIALMKDQVDAL-PRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 292 IDAVKLDGHSTQiewDQVANNMHRIRF-----IYMSPEMVTSQKGLELLTScRKHISLLAIDEAHCVSQWGHDFRNSYRH 366
Cdd:cd18018 80 IKAAALNSSLTR---EERRRILEKLRAgevkiLYVSPERLVNESFRELLRQ-TPPISLLVVDEAHCISEWSHNFRPDYLR 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 32564293 367 LAE-IRNRSDlcNIPMIALTATATVRVRDDVIANLRLRKPLITTTSFD 413
Cdd:cd18018 156 LCRvLRELLG--APPVLALTATATKRVVEDIASHLGIPESGVVRGPLY 201
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
216-405 |
6.17e-52 |
|
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350772 [Multi-domain] Cd Length: 205 Bit Score: 181.13 E-value: 6.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 216 LNALNEFFGHKGFR-EKQWDVVRNVLGGK-DQFVLMSTGYGKSVCYQLPSLLLNSMTVVVSPLISLMNDQVTTLVSKGID 293
Cdd:cd18014 1 RSTLKKVFGHSDFKsPLQEKATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 294 AVKLDGHSTQIEWDQVANNMHR----IRFIYMSPEMVTSQKGLELLTSCRKH--ISLLAIDEAHCVSQWGHDFRNSYRHL 367
Cdd:cd18014 81 VDSLNSKLSAQERKRIIADLESekpqTKFLYITPEMAATSSFQPLLSSLVSRnlLSYLVVDEAHCVSQWGHDFRPDYLRL 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 32564293 368 AEIRNRsdLCNIPMIALTATATVRVRDDVIANLRLRKP 405
Cdd:cd18014 161 GALRSR--YGHVPWVALTATATPQVQEDIFAQLRLKKP 196
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
213-413 |
2.01e-51 |
|
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: 179.87 E-value: 2.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 213 QEALNALNEFFGHKGFREKQWDVVRNVLGGKDQFVLMSTGYGKSVCYQLPSLLLNSMTVVVSPLISLMNDQVTTLVSKGI 292
Cdd:cd18015 4 GKVKDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 293 DAVKLDGHSTQ--IEW--DQVANNMHRIRFIYMSPE-MVTSQKGLELLTSCR--KHISLLAIDEAHCVSQWGHDFRNSYR 365
Cdd:cd18015 84 SATMLNASSSKehVKWvhAALTDKNSELKLLYVTPEkIAKSKRFMSKLEKAYnaGRLARIAIDEVHCCSQWGHDFRPDYK 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 32564293 366 HLAEIrnRSDLCNIPMIALTATATVRVRDDVIANLRLRKPLITTTSFD 413
Cdd:cd18015 164 KLGIL--KRQFPNVPILGLTATATSKVLKDVQKILCIQKCLTFTASFN 209
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
213-413 |
1.42e-50 |
|
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: 177.33 E-value: 1.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 213 QEALNALNEFFGHKGFREKQWDVVRNVLGGKDQFVLMSTGYGKSVCYQLPSLLLNSMTVVVSPLISLMNDQVTTLVSKGI 292
Cdd:cd18016 3 KEMMKIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 293 DAVKLDGHSTQIEWDQVANNMHR----IRFIYMSPEMVTS----QKGLELLTScRKHISLLAIDEAHCVSQWGHDFRNSY 364
Cdd:cd18016 83 PATYLTGDKTDAEATKIYLQLSKkdpiIKLLYVTPEKISAsnrlISTLENLYE-RKLLARFVIDEAHCVSQWGHDFRPDY 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 32564293 365 RHLAEIRNRsdLCNIPMIALTATATVRVRDDVIANLRLRKPLITTTSFD 413
Cdd:cd18016 162 KRLNMLRQK--FPSVPMMALTATATPRVQKDILNQLKMLRPQVFTMSFN 208
|
|
| DpdF |
NF041063 |
protein DpdF; |
251-557 |
6.54e-39 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 156.61 E-value: 6.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 251 TGYGKSVCYQLPSLLL---NSMTVVVSPLISLMNDQ----VTTLVSKGIDAVK-------LDGHSTQIEWDQVANNMHRI 316
Cdd:NF041063 167 TGSGKSLVAQAPALLAsrqGGLTLVVVPTVALAIDQerraRELLRRAGPDLGGplawhggLSAEERAAIRQRIRDGTQRI 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 317 rfIYMSPEMVTSqkGL-ELLTSC--RKHISLLAIDEAHCVSQWGHDFRNSYRHLAEIRnRSDLCNIPM------IALTAT 387
Cdd:NF041063 247 --LFTSPESLTG--SLrPALFDAaeAGLLRYLVVDEAHLVDQWGDGFRPEFQLLAGLR-RSLLRLAPSgrpfrtLLLSAT 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 388 ATVRVRDdVIANLrlrkplitttsFDRKNLYISVHSSK---------DMAEDLGLfmKTDEVKG--RHFGGPTIIYCQTK 456
Cdd:NF041063 322 LTESTLD-TLETL-----------FGPPGPFIVVSAVQlrpepaywvAKCDSEEE--RRERVLEalRHLPRPLILYVTKV 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 457 QMVDDVNCVLRRIGV-RSAHYHAGLTKNQREKAHTDFMRDKITTIVATVAFGMGIDKPDVRNVIHYGCPNNIESYYQEIG 535
Cdd:NF041063 388 EDAEAWLQRLRAAGFrRVALFHGDTPDAERERLIEQWRENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVG 467
|
330 340
....*....|....*....|..
gi 32564293 536 RAGRDGSPSICRVFWAPKDLNT 557
Cdd:NF041063 468 RGGRDGKASLSLLIYTPDDLDI 489
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
443-541 |
2.57e-26 |
|
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: 104.21 E-value: 2.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 443 RHFGGPTIIYCQTKQMVDdVNCVLRRIGVRSAHYHAGLTKNQREKAHTDFMRDKITTIVATVAFGMGIDKPDVRNVIHYG 522
Cdd:pfam00271 12 KERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVINYD 90
|
90
....*....|....*....
gi 32564293 523 CPNNIESYYQEIGRAGRDG 541
Cdd:pfam00271 91 LPWNPASYIQRIGRAGRAG 109
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
460-541 |
2.37e-25 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 100.36 E-value: 2.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 460 DDVNCVLRRIGVRSAHYHAGLTKNQREKAHTDFMRDKITTIVATVAFGMGIDKPDVRNVIHYGCPNNIESYYQEIGRAGR 539
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 32564293 540 DG 541
Cdd:smart00490 81 AG 82
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
232-394 |
1.56e-23 |
|
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: 98.08 E-value: 1.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 232 QWDVVRNVLGGKDQFVLMSTGYGKSVCYQLPSL------LLNSMTVVVSPLISLMNDQVTTLVSKGID-----AVKLDGH 300
Cdd:pfam00270 4 QAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKLGKGlglkvASLLGGD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 301 STQIEWDQVANnmhrIRFIYMSPEMVTSqkgLELLTSCRKHISLLAIDEAHCVSQWGhdFRNSYRHLAeirnRSDLCNIP 380
Cdd:pfam00270 84 SRKEQLEKLKG----PDILVGTPGRLLD---LLQERKLLKNLKLLVLDEAHRLLDMG--FGPDLEEIL----RRLPKKRQ 150
|
170
....*....|....
gi 32564293 381 MIALTATATVRVRD 394
Cdd:pfam00270 151 ILLLSATLPRNLED 164
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
415-539 |
1.48e-21 |
|
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: 91.41 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 415 KNLYISVHSSKDMAEDLGLFMKtdevkgRHFGGPTIIYCQTKQMVDDVNCVLRRIGVRSAHYHAGLTKNQREKAHTDFMR 494
Cdd:cd18787 2 KQLYVVVEEEEKKLLLLLLLLE------KLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRS 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 32564293 495 DKITTIVAT-VAfGMGIDKPDVRNVIHYGCPNNIESYYQEIGRAGR 539
Cdd:cd18787 76 GKVRVLVATdVA-ARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGR 120
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
806-886 |
7.44e-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: 84.66 E-value: 7.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 806 PEKIDQLRSRLDDIRVGIANMHEVAPFQIVSNTVLDCFANLRPTSASNLEMIDGMSAQQKSRYGKRFVDCVVQFSKETGI 885
Cdd:smart00341 1 RERQLRLLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVIQEASDSPSE 80
|
.
gi 32564293 886 A 886
Cdd:smart00341 81 A 81
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
221-412 |
5.08e-18 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 83.70 E-value: 5.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 221 EFFGHKGFREKQWDVVRNVL-GGKDQFVLMSTGYGKSVCYQLPSLLL-----NSMTVVVSPLISLMNDQVTTLV-----S 289
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLsGLRDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELKklgpsL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 290 KGIDAVKLDGHSTQIEWDQVANNMHRIrfIYMSPEMVTSQkgLELLTSCRKHISLLAIDEAHCVSQWGhdFRNSYRHLAE 369
Cdd:smart00487 82 GLKVVGLYGGDSKREQLRKLESGKTDI--LVTTPGRLLDL--LENDKLSLSNVDLVILDEAHRLLDGG--FGDQLEKLLK 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 32564293 370 IRNRsdlcNIPMIALTATATVRVRDdvIANLRLRKPLITTTSF 412
Cdd:smart00487 156 LLPK----NVQLLLLSATPPEEIEN--LLELFLNDPVFIDVGF 192
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
632-738 |
3.18e-16 |
|
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: 75.27 E-value: 3.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 632 IVDVTTESKWLFQVINEMyNGKTGIGKPIEFLRGSSKEDWRIKTTSQQKLFGIGKHIPDKWWKALAASLRIAGYLgEVRL 711
Cdd:pfam09382 4 TVDVTEEAQKILSCVYRT-GQRFGAGHLIDVLRGSKNKKIRQLGHDKLSTFGIGKDLSKKEWRRIIRQLIAEGYL-EVDI 81
|
90 100
....*....|....*....|....*..
gi 32564293 712 MqmkFGSCITLSELGERWLltGKEMKI 738
Cdd:pfam09382 82 E---FYSVLKLTPKAREVL--KGEEKV 103
|
|
| RQC |
smart00956 |
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix ... |
634-730 |
3.11e-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: 72.12 E-value: 3.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 634 DVTTESKWLFQVINEMyNGKTGIGKPIEFLRGSSKEDWRIKTTSQQKLFGIGKHIPDKWWKALAASLRIAGYLGEVrlmq 713
Cdd:smart00956 1 DVTEEAQKLLSCVYRT-GQRFGAGHVIDVLRGSKNKKIRQKGHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLRED---- 75
|
90
....*....|....*..
gi 32564293 714 MKFGSCITLSELGERWL 730
Cdd:smart00956 76 GGRYPYLKLTEKARPVL 92
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
449-541 |
1.03e-13 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 74.41 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 449 TIIYCQTKQMVDDVNCVLRRIGVRSAHYHAGLTKNQREKAHTDFMRDKITTIVAT-VAfGMGIDKPDVRNVIHYGCPNNI 527
Cdd:COG0513 244 AIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATdVA-ARGIDIDDVSHVINYDLPEDP 322
|
90
....*....|....*..
gi 32564293 528 ESYYQEIG---RAGRDG 541
Cdd:COG0513 323 EDYVHRIGrtgRAGAEG 339
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
213-537 |
6.21e-13 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 72.75 E-value: 6.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 213 QEALNALNEFFGHKGFRekqwdvvrnvlggkdqFVL-MSTGYGKSV----CYQlpSLLLNSMTVVVSPLISLMNDQVTTL 287
Cdd:COG1061 86 QEALEALLAALERGGGR----------------GLVvAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRRELLEQWAEEL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 288 vSKGIDAVKLDGHSTQIEWD-QVAnnmhrirfiymSPEMVTSQKGLELLtscRKHISLLAIDEAHcvsqwgHDFRNSYRH 366
Cdd:COG1061 148 -RRFLGDPLAGGGKKDSDAPiTVA-----------TYQSLARRAHLDEL---GDRFGLVIIDEAH------HAGAPSYRR 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 367 LAEirnrsDLCNIPMIALTAT--------ATVRVRDDVIANLRLR--------KPLITTTSFD----RKNLYISVHSSKD 426
Cdd:COG1061 207 ILE-----AFPAAYRLGLTATpfrsdgreILLFLFDGIVYEYSLKeaiedgylAPPEYYGIRVdltdERAEYDALSERLR 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 427 ---MAEDLGLFMKTDEVKGRHFGG-PTIIYCQTKQMVDDVNCVLRRIGVRSAHYHAGLTKNQREKAHTDFMRDKITTIVA 502
Cdd:COG1061 282 ealAADAERKDKILRELLREHPDDrKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVT 361
|
330 340 350
....*....|....*....|....*....|....*...
gi 32564293 503 TVAFGMGIDKPDVRNVIHYGcpnNIES---YYQEIGRA 537
Cdd:COG1061 362 VDVLNEGVDVPRLDVAILLR---PTGSpreFIQRLGRG 396
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
449-544 |
1.00e-12 |
|
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: 66.51 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 449 TIIYCQTKQMVDDVNCVLRRIGV-------RSAHYHAGLTKNQREKAHTDFMRDKITTIVATVAFGMGIDKPDVRNVIHY 521
Cdd:cd18797 38 TIVFCRSRKLAELLLRYLKARLVeegplasKVASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLA 117
|
90 100
....*....|....*....|...
gi 32564293 522 GCPNNIESYYQEIGRAGRDGSPS 544
Cdd:cd18797 118 GYPGSLASLWQQAGRAGRRGKDS 140
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
232-545 |
3.24e-12 |
|
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: 70.63 E-value: 3.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 232 QWDVVRNVLGGKDQFVLMSTGYGKSVCYQLPSL--LL---NSMTVVVSPLISLMNDQVTTLVS------KGIDAVKLDGH 300
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLeaLLedpGATALYLYPTKALARDQLRRLRElaealgLGVRVATYDGD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 301 STQIEWDQVANNMHrirFIYMSPEMV------TSQKGLELLTSCRkhisLLAIDEAHcvsqwghdfrnSYR-----HLAE 369
Cdd:COG1205 141 TPPEERRWIREHPD---IVLTNPDMLhygllpHHTRWARFFRNLR----YVVIDEAH-----------TYRgvfgsHVAN 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 370 -IR--NRsdLC-----NIPMIALTATatvrvrddvIAN-----LRL-----------------RKPLITTTSFDRKNLYI 419
Cdd:COG1205 203 vLRrlRR--ICrhygsDPQFILASAT---------IGNpaehaERLtgrpvtvvdedgsprgeRTFVLWNPPLVDDGIRR 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 420 SVHS-SKDMAEDLglfmktdeVKGRHfggPTIIYCQTKQMVDDVNCVLRR------IGVRSAHYHAGLTKNQREKAHTDF 492
Cdd:COG1205 272 SALAeAARLLADL--------VREGL---RTLVFTRSRRGAELLARYARRalrepdLADRVAAYRAGYLPEERREIERGL 340
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 32564293 493 MRDKITTIVATVAFGMGIDKPDVRNVIHYGCPNNIESYYQEIGRAGRDGSPSI 545
Cdd:COG1205 341 RSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSL 393
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
482-542 |
5.14e-12 |
|
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: 62.34 E-value: 5.14e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32564293 482 KNQREKAHTdfMRDKITTIVATVAFGMGIDKPDVRNVIHYGCPNNIESYYQEIGRAGRDGS 542
Cdd:cd18785 10 TNSIEHAEE--IASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK 68
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
242-387 |
1.34e-11 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 63.58 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 242 GKDQFVLMSTGYGKSVCYQLPSLLLNSM----TVVVSPLISLMNDQ---VTTLVSKGIDAVKLDGhSTQIEwDQVANNMH 314
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLKkgkkVLVLVPTKALALQTaerLRELFGPGIRVAVLVG-GSSAE-EREKNKLG 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32564293 315 RIRFIYMSPEMVTSqKGLELLTSCRKHISLLAIDEAHCVSQWGHDFRNSYRhlaEIRNRSDLcNIPMIALTAT 387
Cdd:cd00046 79 DADIIIATPDMLLN-LLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDL---AVRKAGLK-NAQVILLSAT 146
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
811-876 |
5.09e-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: 59.09 E-value: 5.09e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32564293 811 QLRSRLDDIRVGIANMHEVAPFQIVSNTVLDCFANLRPTSASNLEMIDGMSAQQKSRYGKRFVDCV 876
Cdd:pfam00570 3 ALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
467-549 |
1.39e-09 |
|
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: 57.66 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 467 RRIGVRSAHYHAGLTKNQREKAHTDFMRDKITTIVATVAFGMGIDKPDVRNVIHYGCPNNIESYYQEIGRAGRDGSPSIC 546
Cdd:cd18796 65 RVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGHRPGAASK 144
|
...
gi 32564293 547 RVF 549
Cdd:cd18796 145 GRL 147
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
232-549 |
2.18e-09 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 61.34 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 232 QWDVVRNVLGGKDQFVLMSTGYGKSVCYQLP-------------SLLLNSMTVVVSP---LISLMNDQVTTLvSKGI--- 292
Cdd:PLN00206 148 QMQAIPAALSGRSLLVSADTGSGKTASFLVPiisrcctirsghpSEQRNPLAMVLTPtreLCVQVEDQAKVL-GKGLpfk 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 293 DAVKLDGhstqiewDQVANNMHRIrfiymspemvtsQKGLELL--TSCR------KH------ISLLAIDEAHCVSQWGh 358
Cdd:PLN00206 227 TALVVGG-------DAMPQQLYRI------------QQGVELIvgTPGRlidllsKHdieldnVSVLVLDEVDCMLERG- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 359 dFRNS----YRHLAEirnrsdlcniPMIaLTATATVRVRDDVIANLRLRKPLITTTSFDR------KNLYISVhSSKDMA 428
Cdd:PLN00206 287 -FRDQvmqiFQALSQ----------PQV-LLFSATVSPEVEKFASSLAKDIILISIGNPNrpnkavKQLAIWV-ETKQKK 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 429 EDLGLFMKTDEvkgrHFGGPTIIYCQTKQMVDDV-NCVLRRIGVRSAHYHAGLTKNQREKAHTDFMRDKITTIVATVAFG 507
Cdd:PLN00206 354 QKLFDILKSKQ----HFKPPAVVFVSSRLGADLLaNAITVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLG 429
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 32564293 508 MGIDKPDVRNVIHYGCPNNIESYYQEIGRAGRDGSPSICRVF 549
Cdd:PLN00206 430 RGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVF 471
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
446-567 |
1.48e-08 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 58.63 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 446 GGPTIIYCQTKQMVDDVNCVLRRIGVRSAHYHAGLTKNQREKAHTDFMRDKITTIVATVAFGMGIDKPDVRNVIHYGCPN 525
Cdd:PTZ00110 377 GDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPN 456
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 32564293 526 NIESYYQEIGRAGRDGSPSICRVFWAP------KDLNTIkfkLRNSQQ 567
Cdd:PTZ00110 457 QIEDYVHRIGRTGRAGAKGASYTFLTPdkyrlaRDLVKV---LREAKQ 501
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
425-541 |
1.52e-08 |
|
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: 54.87 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 425 KDMAEDLGLFMKTDEVKGrhfGGPTIIYCQTKQMVddVNCVLRRIGVrsAHYHAGLTKNQREKAHTDFMRDKITTIVATV 504
Cdd:cd18795 25 NKFDSDIIVLLKIETVSE---GKPVLVFCSSRKEC--EKTAKDLAGI--AFHHAGLTREDRELVEELFREGLIKVLVATS 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 32564293 505 AFGMGIDKPdVRNVI-----HYGCPNNIE----SYYQEIGRAGRDG 541
Cdd:cd18795 98 TLAAGVNLP-ARTVIikgtqRYDGKGYRElsplEYLQMIGRAGRPG 142
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
552-619 |
9.95e-08 |
|
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: 49.98 E-value: 9.95e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32564293 552 PKDLNTIKFKLRNSQQKEEVVENLTMMLRQL-ELVLTTVGCRRYQLLKHFDPSYAKPPtmqadC--CDRCT 619
Cdd:pfam16124 1 YQDVVRLRFLIEQSEADEERKEVELQKLQAMvAYCENTTDCRRKQLLRYFGEEFDSEP-----CgnCDNCL 66
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
450-559 |
1.04e-07 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 55.60 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 450 IIYCQTKQMVDDVNCVLRRIGVRSAHYHAGLTKNQREKAHTDFMRDKITTIVATVAFGMGIDKPDVRNVIHYGCPNNIES 529
Cdd:PTZ00424 271 IIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPEN 350
|
90 100 110
....*....|....*....|....*....|
gi 32564293 530 YYQEIGRAGRDGSPSICRVFWAPKDLNTIK 559
Cdd:PTZ00424 351 YIHRIGRSGRFGRKGVAINFVTPDDIEQLK 380
|
|
| HTH_40 |
pfam14493 |
Helix-turn-helix domain; This presumed domain is found at the C-terminus of a large number of ... |
924-1003 |
1.25e-06 |
|
Helix-turn-helix domain; This presumed domain is found at the C-terminus of a large number of helicase proteins.
Pssm-ID: 464189 Cd Length: 89 Bit Score: 47.50 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 924 TAKEVATARGISEGTVYSYLAMAVEKGLPLHLDKLnVSRKNIAMALNAVRvHLGSNvaVLTPWVEAMGVVPDFNQLKLIR 1003
Cdd:pfam14493 14 SIEEIAEERGLKESTIEGHLAELIEAGEPVDIERL-VSEEEQKEILDAIE-KLGSE--SLKPIKEALPEEISYFEIRLVL 89
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
414-541 |
1.55e-06 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 51.87 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 414 RKNLYISVHSSKDMAEDLGL---FMKTDEVKgrhfggPTIIYCQTKQMVDDVNCVLRRIGVRSAHYHAGLTKNQREKAHT 490
Cdd:PRK11192 216 RKKIHQWYYRADDLEHKTALlchLLKQPEVT------RSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIK 289
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 32564293 491 DFMRDKITTIVAT-VAfGMGIDKPDVRNVIHYGCPNNIESYYQEIGRAGRDG 541
Cdd:PRK11192 290 RLTDGRVNVLVATdVA-ARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAG 340
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
450-539 |
4.85e-06 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 50.19 E-value: 4.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 450 IIYCQTKQMVDDVNCVLRRIGVRSAHYHAGLTKNQREKAHTDFMRDKITTIVATVAFGMGIDKPDVRNVIHYGCPNNIES 529
Cdd:PRK10590 249 LVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPED 328
|
90
....*....|
gi 32564293 530 YYQEIGRAGR 539
Cdd:PRK10590 329 YVHRIGRTGR 338
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
449-542 |
6.16e-06 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains 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: 350189 [Multi-domain] Cd Length: 142 Bit Score: 46.82 E-value: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 449 TIIYCQTKQMVDDVNCVLRRIGVRSAHYHAG---------------LTKNQREKAHTDFMRDKITTIVATVAFGMGIDKP 513
Cdd:cd18802 28 GIIFVERRATAVVLSRLLKEHPSTLAFIRCGfligrgnssqrkrslMTQRKQKETLDKFRDGELNLLIATSVLEEGIDVP 107
|
90 100
....*....|....*....|....*....
gi 32564293 514 DVRNVIHYGCPNNIESYYQEIGRAGRDGS 542
Cdd:cd18802 108 ACNLVIRFDLPKTLRSYIQSRGRARAPNS 136
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
467-539 |
6.90e-06 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 50.27 E-value: 6.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 467 RRIGVRSAHYHAGLTKNQREKAHTDFMRDKITTIVATVAFGMGIDKPdVRNVIhygcpnnIES------------YYQEI 534
Cdd:COG1202 445 RALGYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFP-ASQVI-------FDSlamgiewlsvqeFHQML 516
|
....*
gi 32564293 535 GRAGR 539
Cdd:COG1202 517 GRAGR 521
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
406-541 |
3.98e-05 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 47.57 E-value: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 406 LITTTSFDRKNLYISVHSSK---DMAEDLG-LFMKTDEVKgrhfggptIIYCQTKQMVDDVNCVLRRiGVrsAHYHAGLT 481
Cdd:PRK01172 228 LIKETVNDGGQVLVFVSSRKnaeDYAEMLIqHFPEFNDFK--------VSSENNNVYDDSLNEMLPH-GV--AFHHAGLS 296
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32564293 482 KNQREKAHTDFMRDKITTIVATVAFGMGIDKPD----VRNVIHYGCP-----NNIEsYYQEIGRAGRDG 541
Cdd:PRK01172 297 NEQRRFIEEMFRNRYIKVIVATPTLAAGVNLPArlviVRDITRYGNGgirylSNME-IKQMIGRAGRPG 364
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
450-554 |
4.18e-05 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 47.21 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 450 IIYCQTKQMVDDVNCVLRRIGVRSAHYHAGLTKNQREKAHTDFMRDKITTIVATVAFGMGIDKPDVRNVIHYGCPNNIES 529
Cdd:PRK01297 339 MVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDD 418
|
90 100
....*....|....*....|....*
gi 32564293 530 YYQEIGRAGRDGSPSICRVFWAPKD 554
Cdd:PRK01297 419 YVHRIGRTGRAGASGVSISFAGEDD 443
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
216-541 |
9.73e-05 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 46.38 E-value: 9.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 216 LNALNEFfGHKGFREKQWDVVRNVLGGKDQFVLMSTGYGKSVCYQLPslLLNSM--------TVVVSPLISLMNdQVTTL 287
Cdd:PRK11634 18 LEALNDL-GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLP--LLHNLdpelkapqILVLAPTRELAV-QVAEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 288 VS------KGIDAVKLDGHStqiEWDQvannmhRIRFIYMSPEMVTSQKGlELLTSCRK------HISLLAIDEAHCVSQ 355
Cdd:PRK11634 94 MTdfskhmRGVNVVALYGGQ---RYDV------QLRALRQGPQIVVGTPG-RLLDHLKRgtldlsKLSGLVLDEADEMLR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 356 WG--HDFRNSyrhLAEI--RNRSDLCNIPMIALTATATVRVRDDViANLRLRKPLitTTSFDRKNLYISVHSSKDmAEDL 431
Cdd:PRK11634 164 MGfiEDVETI---MAQIpeGHQTALFSATMPEAIRRITRRFMKEP-QEVRIQSSV--TTRPDISQSYWTVWGMRK-NEAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 432 GLFMKTDEVKGrhfggpTIIYCQTKQMVDDVNCVLRRIGVRSAHYHAGLTKNQREKAHTDFMRDKITTIVATVAFGMGID 511
Cdd:PRK11634 237 VRFLEAEDFDA------AIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLD 310
|
330 340 350
....*....|....*....|....*....|
gi 32564293 512 KPDVRNVIHYGCPNNIESYYQEIGRAGRDG 541
Cdd:PRK11634 311 VERISLVVNYDIPMDSESYVHRIGRTGRAG 340
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
443-541 |
1.71e-04 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 45.71 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 443 RHFGGPTIIYCQTKQMVDDVNCVLRRIGVRSAHYHAGLTKNQREKAHTDFMRDKITTIVAT--VAFGMGIDkpDVRNVIH 520
Cdd:PRK04537 254 RSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATdvAARGLHID--GVKYVYN 331
|
90 100
....*....|....*....|.
gi 32564293 521 YGCPNNIESYYQEIGRAGRDG 541
Cdd:PRK04537 332 YDLPFDAEDYVHRIGRTARLG 352
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
450-549 |
2.05e-04 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 42.46 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 450 IIYCQTKQMVDDVNCVLRRIGVRSAHYHAGLTKNQREKAHTDFMRDKITTI--VATVAFGMGIDKPDVRNVIHYGC---P 524
Cdd:cd18793 31 LIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVflLSTKAGGVGLNLTAANRVILYDPwwnP 110
|
90 100
....*....|....*....|....*
gi 32564293 525 NNIEsyyQEIGRAGRDGSPSICRVF 549
Cdd:cd18793 111 AVEE---QAIDRAHRIGQKKPVVVY 132
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
449-539 |
2.89e-04 |
|
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: 41.39 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 449 TIIYCQTKQMVDDVNCVLRRIGVRSAHYHAGLTKNQR--EKAHTDFMRDKITTIVATVA-FGMGIDKPDVRNVIHYgcpN 525
Cdd:cd18799 9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERgdEALILLFFGELKPPILVTVDlLTTGVDIPEVDNVVFL---R 85
|
90
....*....|....*..
gi 32564293 526 NIES---YYQEIGRAGR 539
Cdd:cd18799 86 PTESrtlFLQMLGRGLR 102
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
425-539 |
3.51e-03 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 41.03 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 425 KDMAEDLGLFMKTDEVKGRHFGGPTIIYCQTKQMVDD--VNCVLRRIGVrsaHyHAGLTKNQREkAHTDFMRD-KITTIV 501
Cdd:COG1204 257 KKLADELKRRLTPEEREELEELAEELLEVSEETHTNEklADCLEKGVAF---H-HAGLPSELRR-LVEDAFREgLIKVLV 331
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 32564293 502 ATVAFGMGIDKPdVRNVI------HYGCPNNIESYYQEIGRAGR 539
Cdd:COG1204 332 ATPTLAAGVNLP-ARRVIirdtkrGGMVPIPVLEFKQMAGRAGR 374
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
450-541 |
4.83e-03 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 40.72 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564293 450 IIYCQTKQMVDDVNCVLRRIGVRSAHYHAGLTKNQREKAHTDFMRDKITTIVATVAFGMGIDKPDVRNVIHYGCPNNIES 529
Cdd:PRK04837 259 IIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCED 338
|
90
....*....|..
gi 32564293 530 YYQEIGRAGRDG 541
Cdd:PRK04837 339 YVHRIGRTGRAG 350
|
|
| Sigma70_r4_2 |
pfam08281 |
Sigma-70, region 4; Region 4 of sigma-70 like sigma-factors are involved in binding to the -35 ... |
907-949 |
8.93e-03 |
|
Sigma-70, region 4; Region 4 of sigma-70 like sigma-factors are involved in binding to the -35 promoter element via a helix-turn-helix motif.
Pssm-ID: 400535 [Multi-domain] Cd Length: 54 Bit Score: 35.51 E-value: 8.93e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 32564293 907 LSDAVRRVYTEHLISRSTAKEVATARGISEGTVYSYLAMAVEK 949
Cdd:pfam08281 11 LPPRQREVFLLRYLEGLSYAEIAELLGISEGTVKSRLSRARKK 53
|
|
| |
