|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
3-604 |
0e+00 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 966.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 3 TSTPPSSTLVRKPETVLKQVFGYSEFRDGQKAVIDAAINGQDSLVLLPTGGGKSVCYQIPALVLEGVTIVISPLISLMQD 82
Cdd:PRK11057 1 MAQAEVLNLESLAKQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 83 QVTQLQALGVKAAYVNNSLAREEQQLVYQQLHQGQIKLLYVAPEKVLQHEFLERLSHLNVNLFAIDEAHCVSHWGHDFRP 162
Cdd:PRK11057 81 QVDQLLANGVAAACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 163 HYFRLNELKQRFAHVPMMALTATADKATRFDIVEQLKLQQPYIHTGSFDRPNIRYTIEEKFKPMVQLLRYLKEQKSQSGI 242
Cdd:PRK11057 161 EYAALGQLRQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLVEKFKPLDQLMRYVQEQRGKSGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 243 IYCTSRKRVDDIAEKLADAGLNAAAYHAGMSNEQRQFVQTGFARDDIQIVVATVAFGMGINKPNVRFVLHYDIPKSIESY 322
Cdd:PRK11057 241 IYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 323 YQETGRAGRDGLAAEAIMYFDPADIGRVRRFFEDIDDEQRRRVEEQRFNAMASFAEAQTCRRQILLNYFSEYQREPCGNC 402
Cdd:PRK11057 321 YQETGRAGRDGLPAEAMLFYDPADMAWLRRCLEEKPAGQQQDIERHKLNAMGAFAEAQTCRRLVLLNYFGEGRQEPCGNC 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 403 DICLNPPKSFDGTLVAQQALSCVYRAGQRFGLGYIVELLRGANTSRIRDNNHHELSTYGIGKDKSSEFWLSILRQLIHQG 482
Cdd:PRK11057 401 DICLDPPKQYDGLEDAQKALSCIYRVNQRFGMGYVVEVLRGANNQRIRDYGHDKLKVYGIGRDKSHEHWVSVIRQLIHLG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 483 LLSQDITQGASLRLTEAARVILKGEYALQLAEPRLQ-AKHVYQDKLAQFNYDKKLFARLRALRKELADADDVPPYVVFND 561
Cdd:PRK11057 481 LVTQNIAQHSALQLTEAARPVLRGEVSLQLAVPRIVaLKPRAMQKSFGGNYDRKLFAKLRKLRKSIADEENIPPYVVFND 560
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1822009350 562 KTLAEMAQLMPTNDSEFLKVSGVGFTKLNKYGGEFLTAIRHYL 604
Cdd:PRK11057 561 ATLIEMAEQMPITASEMLSVNGVGQRKLERFGKPFMALIRAHV 603
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
17-603 |
0e+00 |
|
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 residues long. This model represents bacterial proteins with a high degree of similarity in domain architecture and in primary sequence to E. coli RecQ. The model excludes eukaryotic and archaeal proteins with RecQ-like regions, as well as more distantly related bacterial helicases related to RecQ. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273594 [Multi-domain] Cd Length: 591 Bit Score: 813.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 17 TVLKQVFGYSEFRDGQKAVIDAAINGQDSLVLLPTGGGKSVCYQIPALVLEGVTIVISPLISLMQDQVTQLQALGVKAAY 96
Cdd:TIGR01389 3 QVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAAAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 97 VNNSLAREEQQLVYQQLHQGQIKLLYVAPEKVLQHEFLERLSHLNVNLFAIDEAHCVSHWGHDFRPHYFRLNELKQRFAH 176
Cdd:TIGR01389 83 LNSTLSAKEQQDIEKALVNGELKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERFPQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 177 VPMMALTATADKATRFDIVEQLKLQQPYIHTGSFDRPNIRYTIEEKFKPMVQLLRYLKEQKSQSGIIYCTSRKRVDDIAE 256
Cdd:TIGR01389 163 VPRIALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKNNKQKFLLDYLKKHRGQSGIIYASSRKKVEELAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 257 KLADAGLNAAAYHAGMSNEQRQFVQTGFARDDIQIVVATVAFGMGINKPNVRFVLHYDIPKSIESYYQETGRAGRDGLAA 336
Cdd:TIGR01389 243 RLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDGLPA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 337 EAIMYFDPADIGRVRRFFED-IDDEQRRRVEEQRFNAMASFAEAQTCRRQILLNYFSEYQREPCGNCDICLNPPKSFDGT 415
Cdd:TIGR01389 323 EAILLYSPADIALLKRRIEQsEADDDYKQIEREKLRAMIAYCETQTCRRAYILRYFGENEVEPCGNCDNCLDPPKSYDAT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 416 LVAQQALSCVYRAGQRFGLGYIVELLRGANTSRIRDNNHHELSTYGIGKDKSSEFWLSILRQLIHQGLLSQDITQGASLR 495
Cdd:TIGR01389 403 VEAQKALSCVYRMGQRFGVGYIIEVLRGSKNDKILQKGHDQLSTYGIGKDYTQKEWRSLIDQLIAEGLLTENDEIYIGLQ 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 496 LTEAARVILKGEYALQLAEPRLQAK-HVYQDKLAQFNYDKKLFARLRALRKELADADDVPPYVVFNDKTLAEMAQLMPTN 574
Cdd:TIGR01389 483 LTEAARKVLKNEVEVLLRPFKVVAKeKTRVQKNLSVGVDNALFEALRELRKEQADEQNVPPYVIFSDSTLREMAEKRPAT 562
|
570 580
....*....|....*....|....*....
gi 1822009350 575 DSEFLKVSGVGFTKLNKYGGEFLTAIRHY 603
Cdd:TIGR01389 563 LNALLKIKGVGQNKLDRYGEAFLEVIREY 591
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
13-481 |
0e+00 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 793.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 13 RKPETVLKQVFGYSEFRDGQKAVIDAAINGQDSLVLLPTGGGKSVCYQIPALVLEGVTIVISPLISLMQDQVTQLQALGV 92
Cdd:COG0514 3 DDALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 93 KAAYVNNSLAREEQQLVYQQLHQGQIKLLYVAPEKVLQHEFLERLSHLNVNLFAIDEAHCVSHWGHDFRPHYFRLNELKQ 172
Cdd:COG0514 83 RAAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGELRE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 173 RFAHVPMMALTATADKATRFDIVEQLKLQQPYIHTGSFDRPNIRYTIEEKF--KPMVQLLRYLKEQKSQSGIIYCTSRKR 250
Cdd:COG0514 163 RLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKPpdDKLAQLLDFLKEHPGGSGIVYCLSRKK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 251 VDDIAEKLADAGLNAAAYHAGMSNEQRQFVQTGFARDDIQIVVATVAFGMGINKPNVRFVLHYDIPKSIESYYQETGRAG 330
Cdd:COG0514 243 VEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 331 RDGLAAEAIMYFDPADIGRVRRF-FEDIDDEQRRRVEEQRFNAMASFAEAQTCRRQILLNYFSEYQREPCGNCDICLNPP 409
Cdd:COG0514 323 RDGLPAEALLLYGPEDVAIQRFFiEQSPPDEERKRVERAKLDAMLAYAETTGCRRQFLLRYFGEELAEPCGNCDNCLGPP 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1822009350 410 KSFDGTLVAQQALSCVYRAGQRFGLGYIVELLRGANTSRIRDNNHHELSTYGIGKDKSSEFWLSILRQLIHQ 481
Cdd:COG0514 403 ETFDGTEAAQKALSCVYRTGQRFGAGHVIDVLRGSKNEKIRQFGHDKLSTYGIGKDLSDKEWRSVIRQLLAQ 474
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
17-466 |
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: 631.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 17 TVLKQVFGYSEFRDGQKAVIDAAINGQDSLVLLPTGGGKSVCYQIPALVLEGVTIVISPLISLMQDQVTQLQALGVKAAY 96
Cdd:TIGR00614 1 KILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 97 VNNSLAREEQQLVYQQLHQGQIKLLYVAPEKV-LQHEFLERL-SHLNVNLFAIDEAHCVSHWGHDFRPHYFRLNELKQRF 174
Cdd:TIGR00614 81 LNSAQTKEQQLNVLTDLKDGKIKLLYVTPEKIsASNRLLQTLeERKGITLIAVDEAHCISQWGHDFRPDYKALGSLKQKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 175 AHVPMMALTATADKATRFDIVEQLKLQQPYIHTGSFDRPNIRYTIEEKF-KPMVQLLRYL-KEQKSQSGIIYCTSRKRVD 252
Cdd:TIGR00614 161 PNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRRKTpKILEDLLRFIrKEFEGKSGIIYCPSRKKVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 253 DIAEKLADAGLNAAAYHAGMSNEQRQFVQTGFARDDIQIVVATVAFGMGINKPNVRFVLHYDIPKSIESYYQETGRAGRD 332
Cdd:TIGR00614 241 QVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRAGRD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 333 GLAAEAIMYFDPADIGRVRRFFEDIDDEQRRRVEEQRFNAMASFAEAQTCRRQILLNYFSE----------YQREPCGNC 402
Cdd:TIGR00614 321 GLPSECHLFYAPADMNRLRRLLMEEPDGNFRTYKLKLYEMMEYCLNSSTCRRLILLSYFGEkgfnksfcimGTEKCCDNC 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 403 DICLN------PPKSFDGTLVAQQALSCVYRAGQRFGLGYIVELLRGANTSRIRDNNHHELSTYGIGKDK 466
Cdd:TIGR00614 401 CKRLDyktkdvTDKVYDFGPQAQKALSAVGRLNQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLYGRGKDE 470
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
13-607 |
3.14e-134 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 421.61 E-value: 3.14e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 13 RKPETVLKQVFGYSEFRDGQKAVIDAAINGQDSLVLLPTGGGKSVCYQIPALVLEGVTIVISPLISLMQDQVTQLQALGV 92
Cdd:PLN03137 446 KKLEVNNKKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQANI 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 93 KAAYVNNSLAREEQQLVYQQL--HQGQIKLLYVAPEKVLQHEFLER-LSHLN----VNLFAIDEAHCVSHWGHDFRPHYF 165
Cdd:PLN03137 526 PAASLSAGMEWAEQLEILQELssEYSKYKLLYVTPEKVAKSDSLLRhLENLNsrglLARFVIDEAHCVSQWGHDFRPDYQ 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 166 RLNELKQRFAHVPMMALTATADKATRFDIVEQLKLQQPYIHTGSFDRPNIRYTIEEKFKPMVQLL-RYLKEQK-SQSGII 243
Cdd:PLN03137 606 GLGILKQKFPNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPKTKKCLEDIdKFIKENHfDECGII 685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 244 YCTSRKRVDDIAEKLADAGLNAAAYHAGMSNEQRQFVQTGFARDDIQIVVATVAFGMGINKPNVRFVLHYDIPKSIESYY 323
Cdd:PLN03137 686 YCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYH 765
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 324 QETGRAGRDGLAAEAIMYFDPADIGRVRRFFEDIDDEQR-------------RRVEEQRFN--AMASFAEAQT-CRRQIL 387
Cdd:PLN03137 766 QECGRAGRDGQRSSCVLYYSYSDYIRVKHMISQGGVEQSpmamgynrmassgRILETNTENllRMVSYCENEVdCRRFLQ 845
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 388 LNYFSE-YQREPCGN-CDICLNpPKSF---DGTLVAQQALSCVYRAGQRFGLGYIVELLRGANTSRIRDNNHHELSTYGI 462
Cdd:PLN03137 846 LVHFGEkFDSTNCKKtCDNCSS-SKSLidkDVTEIARQLVELVKLTGERFSSAHILEVYRGSLNQYVKKHRHETLSLHGA 924
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 463 GKDKSSEFWLSILRQLIHQGLLSQDI--------------------------TQGASLRLTEAARVILKGEYALQLAEPR 516
Cdd:PLN03137 925 GKHLSKGEASRILHYLVTEDILAEDVkksdlygsvssllkvneskayklfsgGQTIIMRFPSSVKASKPSKFEATPAKGP 1004
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 517 LQAKHVYQDKLAQ-------FNYDKKLFARLRALRKELAD--ADDVPPYVVFNDKTLAEMAQLMPTNDSEFLKVSGVGFT 587
Cdd:PLN03137 1005 LTSGKQSTLPMATpaqppvdLNLSAILYTALRKLRTALVKeaGDGVMAYHIFGNATLQQISKRIPRTKEELLEINGLGKA 1084
|
650 660
....*....|....*....|....
gi 1822009350 588 KLNKYGGEFL----TAIRHYLATN 607
Cdd:PLN03137 1085 KVSKYGDRLLetieSTINEYYKTD 1108
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
16-211 |
4.20e-103 |
|
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: 310.24 E-value: 4.20e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 16 ETVLKQVFGYSEFRDGQKAVIDAAINGQDSLVLLPTGGGKSVCYQIPALVLEGVTIVISPLISLMQDQVTQLQALGVKAA 95
Cdd:cd17920 1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 96 YVNNSLAREEQQLVYQQLHQGQIKLLYVAPEKVLQHEFLERLSHLN----VNLFAIDEAHCVSHWGHDFRPHYFRLNELK 171
Cdd:cd17920 81 ALNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLQRLPerkrLALIVVDEAHCVSQWGHDFRPDYLRLGRLR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1822009350 172 QRFAHVPMMALTATADKATRFDIVEQLKLQQPYIHTGSFD 211
Cdd:cd17920 161 RALPGVPILALTATATPEVREDILKRLGLRNPVIFRASFD 200
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
18-201 |
2.52e-72 |
|
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: 230.99 E-value: 2.52e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 18 VLKQVFGYSEFRDGQKAVIDAAINGQDSLVLLPTGGGKSVCYQIPALVLE----GVTIVISPLISLMQDQVTQLQALgVK 93
Cdd:cd18018 3 LLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRrrgpGLTLVVSPLIALMKDQVDALPRA-IK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 94 AAYVNNSLAREEQQLVYQQLHQGQIKLLYVAPEKVLQHEFLERLSHL-NVNLFAIDEAHCVSHWGHDFRPHYFRLNE-LK 171
Cdd:cd18018 82 AAALNSSLTREERRRILEKLRAGEVKILYVSPERLVNESFRELLRQTpPISLLVVDEAHCISEWSHNFRPDYLRLCRvLR 161
|
170 180 190
....*....|....*....|....*....|
gi 1822009350 172 QRFAHVPMMALTATADKATRFDIVEQLKLQ 201
Cdd:cd18018 162 ELLGAPPVLALTATATKRVVEDIASHLGIP 191
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
18-211 |
1.74e-69 |
|
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: 223.55 E-value: 1.74e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 18 VLKQVFGYSEFRDGQKAVIDAAINGQDSLVLLPTGGGKSVCYQIPALVLEGVTIVISPLISLMQDQVTQLQALGVKAAYV 97
Cdd:cd18016 8 IFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPATYL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 98 NNSLAREEQQLVYQQLHQGQ--IKLLYVAPEKV-LQHEFLERLSHLNVN----LFAIDEAHCVSHWGHDFRPHYFRLNEL 170
Cdd:cd18016 88 TGDKTDAEATKIYLQLSKKDpiIKLLYVTPEKIsASNRLISTLENLYERkllaRFVIDEAHCVSQWGHDFRPDYKRLNML 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1822009350 171 KQRFAHVPMMALTATADKATRFDIVEQLKLQQPYIHTGSFD 211
Cdd:cd18016 168 RQKFPSVPMMALTATATPRVQKDILNQLKMLRPQVFTMSFN 208
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
17-211 |
2.08e-68 |
|
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: 221.09 E-value: 2.08e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 17 TVLKQVFGYSEFRDGQKAVIDAAINGQDSLVLLPTGGGKSVCYQIPALVLEGVTIVISPLISLMQDQVTQLQALGVKAAY 96
Cdd:cd18015 8 DTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLGISATM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 97 VNNSLAREEQQLVYQQLHQG--QIKLLYVAPEKVLQHE-FLERLSHLN----VNLFAIDEAHCVSHWGHDFRPHYFRLNE 169
Cdd:cd18015 88 LNASSSKEHVKWVHAALTDKnsELKLLYVTPEKIAKSKrFMSKLEKAYnagrLARIAIDEVHCCSQWGHDFRPDYKKLGI 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1822009350 170 LKQRFAHVPMMALTATADKATRFDIVEQLKLQQPYIHTGSFD 211
Cdd:cd18015 168 LKRQFPNVPILGLTATATSKVLKDVQKILCIQKCLTFTASFN 209
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
212-342 |
6.78e-63 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350181 [Multi-domain] Cd Length: 134 Bit Score: 203.59 E-value: 6.78e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 212 RPNIRYTIEEKFKP---MVQLLRYLKEQKSQSGIIYCTSRKRVDDIAEKLADAGLNAAAYHAGMSNEQRQFVQTGFARDD 288
Cdd:cd18794 1 RPNLFYSVRPKDKKdekLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1822009350 289 IQIVVATVAFGMGINKPNVRFVLHYDIPKSIESYYQETGRAGRDGLAAEAIMYF 342
Cdd:cd18794 81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
17-203 |
2.14e-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: 202.32 E-value: 2.14e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 17 TVLKQVFGYSEFR-DGQKAVIDAAING-QDSLVLLPTGGGKSVCYQIPALVLEGVTIVISPLISLMQDQVTQLQALGVKA 94
Cdd:cd18014 2 STLKKVFGHSDFKsPLQEKATMAVVKGnKDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 95 AYVNNSLAREEQQLVYQQLHQG--QIKLLYVAPEKVLQHEFLERLSHL----NVNLFAIDEAHCVSHWGHDFRPHYFRLN 168
Cdd:cd18014 82 DSLNSKLSAQERKRIIADLESEkpQTKFLYITPEMAATSSFQPLLSSLvsrnLLSYLVVDEAHCVSQWGHDFRPDYLRLG 161
|
170 180 190
....*....|....*....|....*....|....*
gi 1822009350 169 ELKQRFAHVPMMALTATADKATRFDIVEQLKLQQP 203
Cdd:cd18014 162 ALRSRYGHVPWVALTATATPQVQEDIFAQLRLKKP 196
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
17-211 |
9.67e-59 |
|
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: 194.99 E-value: 9.67e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 17 TVLKQVFGYSEFRDGQKAVIDAAI-NGQDSLVLLPTGGGKSVCYQIPALVLEGVTIVISPLISLMQDQVTQLQALGVKAA 95
Cdd:cd18017 2 NALNEYFGHSSFRPVQWKVIRSVLeERRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPAC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 96 YvnnsLAREEQQLVYQQLHQGQIKLLYVAPEKVLQHEFLERLSHLNVNLFAIDEAHCVSHWGHDFRPHYFRLNELKQRFA 175
Cdd:cd18017 82 F----LGSAQSQNVLDDIKMGKIRVIYVTPEFVSKGLELLQQLRNGITLIAIDEAHCVSQWGHDFRSSYRHLGSIRNRLP 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 1822009350 176 HVPMMALTATADKATRFDIVEQLKLQQPYIHTGSFD 211
Cdd:cd18017 158 NVPIVALTATATPSVRDDIIKNLNLRNPQITCTSFD 193
|
|
| DpdF |
NF041063 |
protein DpdF; |
11-397 |
2.60e-51 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 189.35 E-value: 2.60e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 11 LVRKPETV-----LKQVFGYSEFRD-GQKAVIDAAIN---GQDSLVLLPTGGGKSVCYQIPALVL---EGVTIVISPLIS 78
Cdd:NF041063 118 LRRTLEPVpgdpfLAEALGFTHYRSpGQREAVRAALLappGSTLIVNLPTGSGKSLVAQAPALLAsrqGGLTLVVVPTVA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 79 LMQDQVTQLQALGVKA--------AYVNNsLAREEQQLVYQQLHQGQIKLLYVAPEKV---LQhEFLERLSHLN-VNLFA 146
Cdd:NF041063 198 LAIDQERRARELLRRAgpdlggplAWHGG-LSAEERAAIRQRIRDGTQRILFTSPESLtgsLR-PALFDAAEAGlLRYLV 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 147 IDEAHCVSHWGHDFRPHY----------FRLNELKQRFAHVpmmALTATADKATRFDIVEQLKLQQPYIH-TGSFDRPNI 215
Cdd:NF041063 276 VDEAHLVDQWGDGFRPEFqllaglrrslLRLAPSGRPFRTL---LLSATLTESTLDTLETLFGPPGPFIVvSAVQLRPEP 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 216 RYTI------EEKFKPMVQLLRYLkeqksqsgIIYCTSRKRVDDIAEKLADAGLN-AAAYHAGMSNEQRQFVQTGFARDD 288
Cdd:NF041063 353 AYWVakcdseEERRERVLEALRHLpr----plILYVTKVEDAEAWLQRLRAAGFRrVALFHGDTPDAERERLIEQWRENE 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 289 IQIVVATVAFGMGINKPNVRFVLHYDIPKSIESYYQETGRAGRDGLAAEAIMYFDPADIGRVRRffedIDDEQRRRVEE- 367
Cdd:NF041063 429 LDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLDIAKS----LNRPKLISVEKg 504
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1822009350 368 -QRFNAMasFAEAQTCRRQIL----------LNYFSEYQRE 397
Cdd:NF041063 505 lERWRAM--FDSKQPLGDGRYrvdldtvpphLDRQSDQNRA 543
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
408-515 |
2.11e-41 |
|
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: 145.37 E-value: 2.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 408 PPKSFDGTLVAQQALSCVYRAGQRFGLGYIVELLRGANTSRIRDNNHHELSTYGIGKDKSSEFWLSILRQLIHQGLLSQD 487
Cdd:pfam09382 1 PPETVDVTEEAQKILSCVYRTGQRFGAGHLIDVLRGSKNKKIRQLGHDKLSTFGIGKDLSKKEWRRIIRQLIAEGYLEVD 80
|
90 100
....*....|....*....|....*...
gi 1822009350 488 ITQGASLRLTEAARVILKGEYALQLAEP 515
Cdd:pfam09382 81 IEFYSVLKLTPKAREVLKGEEKVMLRVP 108
|
|
| RQC |
smart00956 |
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix ... |
413-504 |
1.04e-38 |
|
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: 137.22 E-value: 1.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 413 DGTLVAQQALSCVYRAGQRFGLGYIVELLRGANTSRIRDNNHHELSTYGIGKDKSSEFWLSILRQLIHQGLLSQDITQGA 492
Cdd:smart00956 1 DVTEEAQKLLSCVYRTGQRFGAGHVIDVLRGSKNKKIRQKGHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLREDGGRYP 80
|
90
....*....|..
gi 1822009350 493 SLRLTEAARVIL 504
Cdd:smart00956 81 YLKLTEKARPVL 92
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
29-188 |
2.88e-25 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 102.32 E-value: 2.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 29 RDGQKAVIDAAINGQDSLVLLPTGGGKSVCYQIPALVL------EGVTIVISPLISLMQDQVTQLQALGVKAAY-VNNSL 101
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAldkldnGPQALVLAPTRELAEQIYEELKKLGKGLGLkVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 102 AREEQQLVYQQLHQGQIklLYVAPEKVLQHeFLERLSHLNVNLFAIDEAHCVSHWGhdFRPHYFRLneLKQRFAHVPMMA 181
Cdd:pfam00270 81 GGDSRKEQLEKLKGPDI--LVGTPGRLLDL-LQERKLLKNLKLLVLDEAHRLLDMG--FGPDLEEI--LRRLPKKRQILL 153
|
....*..
gi 1822009350 182 LTATADK 188
Cdd:pfam00270 154 LSATLPR 160
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
252-333 |
6.51e-25 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 98.44 E-value: 6.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 252 DDIAEKLADAGLNAAAYHAGMSNEQRQFVQTGFARDDIQIVVATVAFGMGINKPNVRFVLHYDIPKSIESYYQETGRAGR 331
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 1822009350 332 DG 333
Cdd:smart00490 81 AG 82
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
32-369 |
1.09e-24 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 106.77 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 32 QKAVIDAAINGQDSLVLLPTGGGKSVCYQIPAL--VLEGV-----TIVISP---LIslMQ--DQVTQL-QALGVKAAyvn 98
Cdd:COG0513 29 QAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLqrLDPSRprapqALILAPtreLA--LQvaEELRKLaKYLGLRVA--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 99 nslareeqqLVY-QQLHQGQIKLLY------VA-PEKVLQHefLER----LSHLNVnlFAIDEAhcvshwghD------F 160
Cdd:COG0513 104 ---------TVYgGVSIGRQIRALKrgvdivVAtPGRLLDL--IERgaldLSGVET--LVLDEA--------DrmldmgF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 161 RPhyfrlnELKQRFAHVP----MMALTATADKATRfDIVEQLkLQQPY---IHTGSFDRPNIRYTI-----EEKFKpmvQ 228
Cdd:COG0513 163 IE------DIERILKLLPkerqTLLFSATMPPEIR-KLAKRY-LKNPVrieVAPENATAETIEQRYylvdkRDKLE---L 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 229 LLRYLKEQKSQSGIIYCTSRKRVDDIAEKLADAGLNAAAYHAGMSNEQRQFVQTGFARDDIQIVVAT-VAfGMGINKPNV 307
Cdd:COG0513 232 LRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATdVA-ARGIDIDDV 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1822009350 308 RFVLHYDIPKSIESYyq---eTGRAGRDGlaaEAIMYFDPADigrvRRFFEDIDDEQRRRVEEQR 369
Cdd:COG0513 311 SHVINYDLPEDPEDYvhrigrTGRAGAEG---TAISLVTPDE----RRLLRAIEKLIGQKIEEEE 368
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
23-220 |
1.20e-23 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 99.10 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 23 FGYSEFRDGQKAVIDAAING-QDSLVLLPTGGGKSVCYQIPAL-----VLEGVTIVISPLISLMQDQVTQLQALG----V 92
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALealkrGKGGRVLVLVPTRELAEQWAEELKKLGpslgL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 93 KAAYVNNSLAREEQQlvyQQLHQGQIKLLYVAPEKVLQHEFLERLSHLNVNLFAIDEAHCVSHWGhdFRPHYFRLneLKQ 172
Cdd:smart00487 84 KVVGLYGGDSKREQL---RKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGG--FGDQLEKL--LKL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1822009350 173 RFAHVPMMALTATADKATRFDIVEQLKLqqpYIHTGSFDRPNIRYTIE 220
Cdd:smart00487 157 LPKNVQLLLLSATPPEEIENLLELFLND---PVFIDVGFTPLEPIEQF 201
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
229-333 |
4.34e-23 |
|
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: 94.20 E-value: 4.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 229 LLRYLKEQKSQSGIIYCTSRKRVDdiAEKLADA-GLNAAAYHAGMSNEQRQFVQTGFARDDIQIVVATVAFGMGINKPNV 307
Cdd:pfam00271 6 LLELLKKERGGKVLIFSQTKKTLE--AELLLEKeGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDV 83
|
90 100
....*....|....*....|....*.
gi 1822009350 308 RFVLHYDIPKSIESYYQETGRAGRDG 333
Cdd:pfam00271 84 DLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
219-335 |
1.25e-22 |
|
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: 93.73 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 219 IEEKFKPMVQLLRYLKEQKSQSGIIYCTSRKRVDDIAEKLADAGLNAAAYHAGMSNEQRQFVQTGFARDDIQIVVAT-VA 297
Cdd:cd18787 8 VEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVATdVA 87
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1822009350 298 fGMGINKPNVRFVLHYDIPKSIESYYQ---ETGRAGRDGLA 335
Cdd:cd18787 88 -ARGLDIPGVDHVINYDLPRDAEDYVHrigRTGRAGRKGTA 127
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
32-346 |
1.87e-21 |
|
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: 99.14 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 32 QKAVIDAAINGQDSLVLLPTGGGKSVCYQIPAL--VLEG---VTIVISPLISLMQDQVTQLQAL------GVKAAYVNNS 100
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLeaLLEDpgaTALYLYPTKALARDQLRRLRELaealglGVRVATYDGD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 101 LAREEQQLVYQQ----------LHQGqikllyvapekVLQH-----EFLERLSHLnvnlfAIDEAHC---V--SHWGHDF 160
Cdd:COG1205 141 TPPEERRWIREHpdivltnpdmLHYG-----------LLPHhtrwaRFFRNLRYV-----VIDEAHTyrgVfgSHVANVL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 161 RphyfRLNELKQRF-AHVPMMALTAT----ADKATR-----FDIVEQ---------LKLQQPYIHTGSFDRPNIRYTIEe 221
Cdd:COG1205 205 R----RLRRICRHYgSDPQFILASATignpAEHAERltgrpVTVVDEdgsprgertFVLWNPPLVDDGIRRSALAEAAR- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 222 kfkpmvqLLRYLKEQKSQSgIIYCTSRKRVDDIAEKLADA------GLNAAAYHAGMSNEQRQFVQTGFARDDIQIVVAT 295
Cdd:COG1205 280 -------LLADLVREGLRT-LVFTRSRRGAELLARYARRAlrepdlADRVAAYRAGYLPEERREIERGLRSGELLGVVST 351
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1822009350 296 VAFGMGINKPNVRFVLHYDIPKSIESYYQETGRAGRDGlaAEAIMYF----DPAD 346
Cdd:COG1205 352 NALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRG--QDSLVVLvagdDPLD 404
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
533-600 |
4.39e-21 |
|
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: 87.21 E-value: 4.39e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822009350 533 DKKLFARLRALRKELADADDVPPYVVFNDKTLAEMAQLMPTNDSEFLKVSGVGFTKLNKYGGEFLTAI 600
Cdd:pfam00570 1 QLALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
344-406 |
1.58e-19 |
|
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: 82.72 E-value: 1.58e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1822009350 344 PADIGRVRRFFE-DIDDEQRRRVEEQRFNAMASFAEAQT-CRRQILLNYFSE-YQREPCGNCDICL 406
Cdd:pfam16124 1 YQDVVRLRFLIEqSEADEERKEVELQKLQAMVAYCENTTdCRRKQLLRYFGEeFDSEPCGNCDNCL 66
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
531-604 |
8.00e-19 |
|
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: 81.19 E-value: 8.00e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1822009350 531 NYDKKLFARLRALRKELADADDVPPYVVFNDKTLAEMAQLMPTNDSEFLKVSGVGFTKLNKYGGEFLTAIRHYL 604
Cdd:smart00341 2 ERQLRLLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVIQEAS 75
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
27-367 |
5.00e-15 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 78.14 E-value: 5.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 27 EFRDGQKAVIDAAI-----NGQDSLVLLPTGGGKSV----CYQipALVLEGVTIVISPLISLMQDQVTQLQALGVKAAYV 97
Cdd:COG1061 80 ELRPYQQEALEALLaalerGGGRGLVVAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRRELLEQWAEELRRFLGDPLAG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 98 NNSLAREEQQLV--YQQLHQgqikllyvapekvlqHEFLERLSHlNVNLFAIDEAHcvsHWGHDFrphyFRlnELKQRFA 175
Cdd:COG1061 158 GGKKDSDAPITVatYQSLAR---------------RAHLDELGD-RFGLVIIDEAH---HAGAPS----YR--RILEAFP 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 176 HVPMMALTAT--------------ADKATRFDIVEQLK---LQQP--YIHTGSFDRPNIRYTIEEKF---------KPMV 227
Cdd:COG1061 213 AAYRLGLTATpfrsdgreillflfDGIVYEYSLKEAIEdgyLAPPeyYGIRVDLTDERAEYDALSERlrealaadaERKD 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 228 QLLRYLKEQKSQS--GIIYCTSRKRVDDIAEKLADAGLNAAAYHAGMSNEQRQFVQTGFARDDIQIVVATVAFGMGINKP 305
Cdd:COG1061 293 KILRELLREHPDDrkTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVP 372
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1822009350 306 NVRFVLHYDIPKSIESYYQETGRAGRDGLAAEAIMYFD--PADIGRVRRFFEDIDDEQRRRVEE 367
Cdd:COG1061 373 RLDVAILLRPTGSPREFIQRLGRGLRPAPGKEDALVYDfvGNDVPVLEELAKDLRDLAGYRVEF 436
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
242-367 |
8.65e-15 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 76.40 E-value: 8.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 242 IIYCTSRKRVDDIAEKLADAGLNAAAYHAGMSNEQRQFVQTGFARDDIQIVVATVAFGMGINKPNVRFVLHYDIPKSIES 321
Cdd:PTZ00424 271 IIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPEN 350
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1822009350 322 YYQETGRAGRDGLAAEAIMYFDPADIGRVRrffeDIDDEQRRRVEE 367
Cdd:PTZ00424 351 YIHRIGRSGRFGRKGVAINFVTPDDIEQLK----EIERHYNTQIEE 392
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
221-341 |
3.28e-14 |
|
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: 70.27 E-value: 3.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 221 EKFKPMVQLLRYLKEQKSQSG---IIYCTSRKRVDDIAEKLAdaglNAAAYHAGMSNEQRQFVQTGFARDDIQIVVATVA 297
Cdd:cd18795 23 VMNKFDSDIIVLLKIETVSEGkpvLVFCSSRKECEKTAKDLA----GIAFHHAGLTREDRELVEELFREGLIKVLVATST 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1822009350 298 FGMGINKPNVRFVL----HYD----IPKSIESYYQETGRAGRDGL--AAEAIMY 341
Cdd:cd18795 99 LAAGVNLPARTVIIkgtqRYDgkgyRELSPLEYLQMIGRAGRPGFdtRGEAIIM 152
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
23-334 |
1.63e-13 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 73.39 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 23 FGYSEFRDGQKAVIDAAINGQDSLVL-LPTGGGKSVCYQIPAL--VLEGVTIV-ISPLISLmQDQVTQ-----LQALGVK 93
Cdd:COG1204 18 RGIEELYPPQAEALEAGLLEGKNLVVsAPTASGKTLIAELAILkaLLNGGKALyIVPLRAL-ASEKYRefkrdFEELGIK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 94 --AAYVNNSLAREEqqlvyqqLHQGQIkllYVA-PEKVLQ-----HEFLERLShlnvnLFAIDEAHCVshwGHDFR-Phy 164
Cdd:COG1204 97 vgVSTGDYDSDDEW-------LGRYDI---LVAtPEKLDSllrngPSWLRDVD-----LVVVDEAHLI---DDESRgP-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 165 fRLN----ELKQRFAHVPMMALTATADKA-----------TRFDI--VEQlklqqpyiHTGSFDRPNIRYTIEEKF--KP 225
Cdd:COG1204 157 -TLEvllaRLRRLNPEAQIVALSATIGNAeeiaewldaelVKSDWrpVPL--------NEGVLYDGVLRFDDGSRRskDP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 226 MVQLLRYLKEQKSQSgIIYCTSRKRVDDIAEKLADA---------------------------GLN----------AAAY 268
Cdd:COG1204 228 TLALALDLLEEGGQV-LVFVSSRRDAESLAKKLADElkrrltpeereeleelaeellevseetHTNekladclekgVAFH 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1822009350 269 HAGMSNEQRQFVQTGFARDDIQIVVATVAFGMGINKPnVRFVLHYDI------PKSIESYYQETGRAGRDGL 334
Cdd:COG1204 307 HAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLP-ARRVIIRDTkrggmvPIPVLEFKQMAGRAGRPGY 377
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
228-340 |
1.54e-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: 65.36 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 228 QLLRYLKEQKSQSgIIYCTSRKRVD----DIAEKLADAGLNA---AAYHAGMSNEQRQFVQTGFARDDIQIVVATVAFGM 300
Cdd:cd18797 26 RLFADLVRAGVKT-IVFCRSRKLAElllrYLKARLVEEGPLAskvASYRAGYLAEDRREIEAELFNGELLGVVATNALEL 104
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1822009350 301 GINKPNVRFVLHYDIPKSIESYYQETGRAGRDGLAAEAIM 340
Cdd:cd18797 105 GIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKDSLVIL 144
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
24-358 |
3.75e-12 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 69.11 E-value: 3.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 24 GYSEFRDGQKAVIDAAINGQDSLVLLPTGGGKSVCYQIPAL-----VLEGVTI-VISPLISL-------MQDQVTQLQAL 90
Cdd:PRK11634 25 GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLhnldpELKAPQIlVLAPTRELavqvaeaMTDFSKHMRGV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 91 GVKAAYVNNslaREEQQLvyQQLHQGQiKLLYVAPEKVLQHefLER--LSHLNVNLFAIDEAHCVSHWGHdfrphyfrLN 168
Cdd:PRK11634 105 NVVALYGGQ---RYDVQL--RALRQGP-QIVVGTPGRLLDH--LKRgtLDLSKLSGLVLDEADEMLRMGF--------IE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 169 ELKQRFAHVP---MMAL-TATADKATRFDIVEQLK-LQQPYIHTGSFDRPNIR--YTIEEKFKPMVQLLRYLKEQKSQSG 241
Cdd:PRK11634 169 DVETIMAQIPeghQTALfSATMPEAIRRITRRFMKePQEVRIQSSVTTRPDISqsYWTVWGMRKNEALVRFLEAEDFDAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 242 IIYCTSRKRVDDIAEKLADAGLNAAAYHAGMSNEQRQFVQTGFARDDIQIVVATVAFGMGINKPNVRFVLHYDIPKSIES 321
Cdd:PRK11634 249 IIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSES 328
|
330 340 350
....*....|....*....|....*....|....*..
gi 1822009350 322 YYQETGRAGRDGLAAEAIMYFDpadiGRVRRFFEDID 358
Cdd:PRK11634 329 YVHRIGRTGRAGRAGRALLFVE----NRERRLLRNIE 361
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
220-331 |
1.18e-11 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 67.61 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 220 EEKFKPMVQLLRYLKEQKSQSG-----IIYCTSRKRVDDIAEKLadaGLNAAAYHAGMSNEQRQFVQTGFARDDIQIVVA 294
Cdd:COG1202 404 REKIRIINKLVKREFDTKSSKGyrgqtIIFTNSRRRCHEIARAL---GYKAAPYHAGLDYGERKKVERRFADQELAAVVT 480
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1822009350 295 TVAFGMGInkpnvrfvlhyDIPKS----------IE-----SYYQETGRAGR 331
Cdd:COG1202 481 TAALAAGV-----------DFPASqvifdslamgIEwlsvqEFHQMLGRAGR 521
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
32-357 |
1.48e-11 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 67.12 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 32 QKAVIDAAINGQDSLVLLPTGGGKSVCYQIPALV------LEGVT-------IVISP---LISLMQDQVTQL-QALGVKA 94
Cdd:PLN00206 148 QMQAIPAALSGRSLLVSADTGSGKTASFLVPIISrcctirSGHPSeqrnplaMVLTPtreLCVQVEDQAKVLgKGLPFKT 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 95 AYVNNSLAREEQqlVYQqLHQGqIKLLYVAPEKVLqheflERLSHLNVNL-----FAIDEAHCVSHWGhdFRPHYFrlnE 169
Cdd:PLN00206 228 ALVVGGDAMPQQ--LYR-IQQG-VELIVGTPGRLI-----DLLSKHDIELdnvsvLVLDEVDCMLERG--FRDQVM---Q 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 170 LKQRFAHVPMMALTATADKAtrfdiVEQLK---LQQP-YIHTGSFDRPNIRYT-----IEEKFKPMvQLLRYLKEQK--S 238
Cdd:PLN00206 294 IFQALSQPQVLLFSATVSPE-----VEKFAsslAKDIiLISIGNPNRPNKAVKqlaiwVETKQKKQ-KLFDILKSKQhfK 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 239 QSGIIYCTSRKRVDDIAEKLADA-GLNAAAYHAGMSNEQRQFVQTGFARDDIQIVVATVAFGMGINKPNVRFVLHYDIPK 317
Cdd:PLN00206 368 PPAVVFVSSRLGADLLANAITVVtGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPN 447
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1822009350 318 SIESYYQETGRAGRDGLAAEAIMYFDPADigrvRRFFEDI 357
Cdd:PLN00206 448 TIKEYIHQIGRASRMGEKGTAIVFVNEED----RNLFPEL 483
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
196-369 |
2.46e-11 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 66.12 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 196 EQLKLQQPYIHTGSfdrpnirytIEEKFKPMVQLLrylKEQKSQSGIIYCTSRKRVDDIAEKLADAGLNAAAYHAGMSNE 275
Cdd:PRK11192 215 ERKKIHQWYYRADD---------LEHKTALLCHLL---KQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQA 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 276 QRQFVQTGFARDDIQIVVAT-VAfGMGINKPNVRFVLHYDIPKSIESYYQE---TGRAGRDGLAAEAIMYFDPADIGRVR 351
Cdd:PRK11192 283 KRNEAIKRLTDGRVNVLVATdVA-ARGIDIDDVSHVINFDMPRSADTYLHRigrTGRAGRKGTAISLVEAHDHLLLGKIE 361
|
170
....*....|....*...
gi 1822009350 352 RFFEDIDDeqRRRVEEQR 369
Cdd:PRK11192 362 RYIEEPLK--ARVIDELR 377
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
289-341 |
3.39e-11 |
|
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: 59.25 E-value: 3.39e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1822009350 289 IQIVVATVAFGMGINKPNVRFVLHYDIPKSIESYYQETGRAGRDG-LAAEAIMY 341
Cdd:cd18785 23 LEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGkDEGEVILF 76
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
46-185 |
1.24e-10 |
|
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: 59.72 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 46 LVLLPTGGGKSVCYQIPALVL----EGVTIVISPLISLMQDQVTQLQAL---GVKAAYVNNSLAREEQqlvyQQLHQGQI 118
Cdd:cd00046 5 LITAPTGSGKTLAALLAALLLllkkGKKVLVLVPTKALALQTAERLRELfgpGIRVAVLVGGSSAEER----EKNKLGDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822009350 119 KLLYVAPEKVLQ-HEFLERLSHLNVNLFAIDEAHCVSHWGHDFRPHYFRlnELKQRFAHVPMMALTAT 185
Cdd:cd00046 81 DIIIATPDMLLNlLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLA--VRKAGLKNAQVILLSAT 146
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
201-344 |
3.64e-10 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 62.48 E-value: 3.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 201 QQP-YIHTGSFDRP---NIR---YTIEEKFKpMVQLLRYLKEQKSQSG--IIYCTSRKRVDDIAEKLADAGLNAAAYHAG 271
Cdd:PTZ00110 332 EEPvHVNVGSLDLTachNIKqevFVVEEHEK-RGKLKMLLQRIMRDGDkiLIFVETKKGADFLTKELRLDGWPALCIHGD 410
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1822009350 272 MSNEQRQFVQTGFARDDIQIVVATVAFGMGINKPNVRFVLHYDIPKSIESYYQETGRAGRDGLAAEAIMYFDP 344
Cdd:PTZ00110 411 KKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTP 483
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
231-342 |
9.98e-10 |
|
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: 57.27 E-value: 9.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 231 RYLKE-QKSQSGIIYCTSRKRVDDIAEKLADA------GLNAAAYHAGMSNEQRQFVQTGFARDDIQIVVATVAFGMGIN 303
Cdd:cd18796 30 EVIFLlERHKSTLVFTNTRSQAERLAQRLRELcpdrvpPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGID 109
|
90 100 110
....*....|....*....|....*....|....*....
gi 1822009350 304 KPNVRFVLHYDIPKSIESYYQETGRAGRDGLAAEAIMYF 342
Cdd:cd18796 110 IGDVDLVIQIGSPKSVARLLQRLGRSGHRPGAASKGRLV 148
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
215-333 |
4.58e-08 |
|
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: 52.09 E-value: 4.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 215 IRYTIEEKFKPMVQLLRYLKEQKSQSgIIYCTSRKRVDDIAEKLADAGLNAAAYHAGMSNEQRQFVQTGFARDD--IQIV 292
Cdd:cd18793 5 IEEVVSGKLEALLELLEELREPGEKV-LIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdiRVFL 83
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1822009350 293 VATVAFGMGINKPNVRFVLHYDIP--KSIESyyQETGRAGRDG 333
Cdd:cd18793 84 LSTKAGGVGLNLTAANRVILYDPWwnPAVEE--QAIDRAHRIG 124
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
21-333 |
5.02e-08 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 56.04 E-value: 5.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 21 QVFGYSEFR--DGQKAVIDAAINGQDSLVLLPTGGGKSVC--YQIPALVLEGV-TIVISPLISL-MQ--DQVTQLQALGV 92
Cdd:PRK01172 14 NLFTGNDFElyDHQRMAIEQLRKGENVIVSVPTAAGKTLIaySAIYETFLAGLkSIYIVPLRSLaMEkyEELSRLRSLGM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 93 KaayVNNSLAREEQQLVYqqlhqgqIKLLYVApekVLQHEFLERLSH-----LN-VNLFAIDEAHCVshwGHDFRPHYFR 166
Cdd:PRK01172 94 R---VKISIGDYDDPPDF-------IKRYDVV---ILTSEKADSLIHhdpyiINdVGLIVADEIHII---GDEDRGPTLE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 167 LNELKQRFAH--VPMMALTATADKATrfDIVEQLK-------LQQPYIHTGSFDRPniRYTIEEKFKPMVQLLRYLKEQK 237
Cdd:PRK01172 158 TVLSSARYVNpdARILALSATVSNAN--ELAQWLNasliksnFRPVPLKLGILYRK--RLILDGYERSQVDINSLIKETV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 238 SQSG--IIYCTSRKRVDDIAEKLA-------------------DAGLN------AAAYHAGMSNEQRQFVQTGFARDDIQ 290
Cdd:PRK01172 234 NDGGqvLVFVSSRKNAEDYAEMLIqhfpefndfkvssennnvyDDSLNemlphgVAFHHAGLSNEQRRFIEEMFRNRYIK 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1822009350 291 IVVATVAFGMGINKPnVRFVLHYDIPKSIESYY---------QETGRAGRDG 333
Cdd:PRK01172 314 VIVATPTLAAGVNLP-ARLVIVRDITRYGNGGIrylsnmeikQMIGRAGRPG 364
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
253-334 |
1.47e-07 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 54.58 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 253 DIAEKLADAGLNAAAYH-AGMSNEQRQFVQTGFARDDIQIVVATVAFGMGINKPN----VRFVLHYD-----IPKSIESY 322
Cdd:PRK02362 293 ETSKDLADCVAKGAAFHhAGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPArrviIRDYRRYDggagmQPIPVLEY 372
|
90
....*....|..
gi 1822009350 323 YQETGRAGRDGL 334
Cdd:PRK02362 373 HQMAGRAGRPGL 384
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
32-151 |
5.70e-07 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 49.89 E-value: 5.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 32 QKAVIDAAINGQDSLVLLPTGGGKSVCYQIPAL--VLE--GVT-IVISPLISLMQDQVTQLQALGVK-------AAY--- 96
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILeaLLRdpGSRaLYLYPTKALAQDQLRSLRELLEQlglgirvATYdgd 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1822009350 97 ----VNNSLAREEQQLV---YQQLHQGqikllyVAPEKVLQHEFLERLshlnvNLFAIDEAH 151
Cdd:cd17923 85 tpreERRAIIRNPPRILltnPDMLHYA------LLPHHDRWARFLRNL-----RYVVLDEAH 135
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
266-334 |
1.22e-06 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 51.48 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 266 AAYHAGMSNEQRQFVQTGFARDDIQIVVATVAFGMGINKPnVRFVL-----------HYDIpKSIEsYYQETGRAGRDGL 334
Cdd:COG4581 303 AVHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMP-ARTVVftklskfdgerHRPL-TARE-FHQIAGRAGRRGI 379
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
212-341 |
2.07e-06 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 50.72 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 212 RPNIRYTIEEKFKPMvqLLRYLKEQKSQSGIIYCTSRKRVDDIAEKLADAGLNAAAYHAGMSNEQRQFVQTGFARDDIQI 291
Cdd:PRK04537 233 RQRIYFPADEEKQTL--LLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEI 310
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1822009350 292 VVATVAFGMGINKPNVRFVLHYDIPKSIESYYQETGRAGRDGLAAEAIMY 341
Cdd:PRK04537 311 LVATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISF 360
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
221-341 |
2.75e-06 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 50.30 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 221 EKFKPMVQLLRylkEQKSQSGIIYCTSRKRVDDIAEKLADAGLNAAAYHAGMSNEQRQFVQTGFARDDIQIVVATVAFGM 300
Cdd:PRK01297 321 DKYKLLYNLVT---QNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGR 397
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1822009350 301 GINKPNVRFVLHYDIPKSIESYYQETGRAGRDGLAAEAIMY 341
Cdd:PRK01297 398 GIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISF 438
|
|
| Rnd |
COG0349 |
Ribonuclease D [Translation, ribosomal structure and biogenesis]; |
538-606 |
4.38e-06 |
|
Ribonuclease D [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440118 [Multi-domain] Cd Length: 365 Bit Score: 49.10 E-value: 4.38e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1822009350 538 ARLRAL---RKELADADDVPPYVVFNDKTLAEMAQLMPTNDSEFLKVSGVGFTKLNKYGGEFLTAIRHYLAT 606
Cdd:COG0349 211 AVLRELaawREREARKRDVPRNRVLKDEALLELARRQPKSLEELARLRGLSPGEIRRHGEELLAAVAEALAL 282
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
256-331 |
8.88e-06 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 48.66 E-value: 8.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 256 EKLADAGLNAAAYH-AGMSNEQRQFVQTGFARDDIQIVVATVAFGMGINKPNVRFVLH----------YDIPksIESYYQ 324
Cdd:PRK00254 288 EKLKKALRGGVAFHhAGLGRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRdtkrysnfgwEDIP--VLEIQQ 365
|
....*..
gi 1822009350 325 ETGRAGR 331
Cdd:PRK00254 366 MMGRAGR 372
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
181-333 |
2.01e-05 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 47.80 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 181 ALTATADKATRfDIVEQLKLQQpyihtgsfdrpnIRYTIEE------KFKPMVQLL-RYLKEQKSQSGIIYCTSRKRVDD 253
Cdd:COG1111 302 ARSSGGSKASK-RLVSDPRFRK------------AMRLAEEadiehpKLSKLREILkEQLGTNPDSRIIVFTQYRDTAEM 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 254 IAEKLADAGLNAAAY--------HAGMSNEQRQFVQTGFARDDIQIVVATVAFGMGINKPNVRFVLHYD-IPKSIESyYQ 324
Cdd:COG1111 369 IVEFLSEPGIKAGRFvgqaskegDKGLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYEpVPSEIRS-IQ 447
|
....*....
gi 1822009350 325 ETGRAGRDG 333
Cdd:COG1111 448 RKGRTGRKR 456
|
|
| SF2_C_viral |
cd18806 |
C-terminal helicase domain of viral helicase; Viral helicases in this family here are ... |
242-342 |
7.61e-05 |
|
C-terminal helicase domain of viral helicase; Viral helicases in this family here 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: 350193 [Multi-domain] Cd Length: 145 Bit Score: 43.02 E-value: 7.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 242 IIYCTSRKRVDDIAEKLADAGLNAAAYHAGMSNEQRQFVQTGfardDIQIVVATVAFGMGIN-------------KPNV- 307
Cdd:cd18806 28 VWFVHSKKKGNEIAACLSGLGKNVIQLYRKLDDTEYPKIKTI----DWDFVVTTDISEMGANfdadrvidcrtcvKPTIl 103
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1822009350 308 -----RFVLHYDIPKSIESYYQETGRAGRDGLAAEAIMYF 342
Cdd:cd18806 104 fsgdfRVILTGPVPQTAASAAQRRGRTGRNPAQERDIYRF 143
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
254-339 |
8.06e-05 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 45.57 E-value: 8.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 254 IAEKLADAGLNAAAYHAGMSNEQRQFVQTGFARDDIQIVVATVAFGMGINKPNVRFVLHYDIPKSIESYYQETGRAGRDG 333
Cdd:PRK10590 261 LAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGRAA 340
|
....*.
gi 1822009350 334 LAAEAI 339
Cdd:PRK10590 341 ATGEAL 346
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
265-330 |
9.70e-05 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 45.69 E-value: 9.70e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1822009350 265 AAAYHAGMSNEQRQFVQTGFARDDIQIVVATVAFGMGINKPNVRFVLHYDIPKSIESYYQETGRAG 330
Cdd:PRK09751 304 ARSHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
220-339 |
3.48e-04 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 43.42 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 220 EEKFKP-----MVQLLRYLKEQKSQSGIIYCTSRKRVDDIAEKLADAGLNAAAYHAGMSNEQRQFVQTGFARDDIQIVVA 294
Cdd:PRK04837 232 EELFYPsneekMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVA 311
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1822009350 295 TVAFGMGINKPNVRFVLHYDIPKSIESYYQETGRAGRDGLAAEAI 339
Cdd:PRK04837 312 TDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSI 356
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
198-331 |
5.77e-04 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 42.90 E-value: 5.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 198 LKLQQPYIHTGSFDRPNIRYTIEE-KFKpmvQLLRYLKEQKSQSG--IIYCTSRKRVDDIAEKLADAGLNAAAYHAGMSN 274
Cdd:COG0553 509 TRLRQICSHPALLLEEGAELSGRSaKLE---ALLELLEELLAEGEkvLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSA 585
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1822009350 275 EQRQFVQTGFARDD--IQIVVATVAFGMGINKPNVRFVLHYDI---PKSIEsyyQETGRAGR 331
Cdd:COG0553 586 EERDELVDRFQEGPeaPVFLISLKAGGEGLNLTAADHVIHYDLwwnPAVEE---QAIDRAHR 644
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
254-330 |
9.88e-04 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 42.40 E-value: 9.88e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822009350 254 IAEKLADAGLNAAAYHAGMSNEQRQFVQTGFARDDIQIVVATVAFGMGINKPNVRFVLHYDIPKSIESYYQETGRAG 330
Cdd:COG1201 292 LNELNPEDALPIAAHHGSLSREQRLEVEEALKAGELRAVVATSSLELGIDIGDVDLVIQVGSPKSVARLLQRIGRAG 368
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
214-331 |
1.06e-03 |
|
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350185 [Multi-domain] Cd Length: 174 Bit Score: 40.37 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 214 NIRYTIEEKFKPMVQLLRYLKEQKSqSGIIYCTSRK---RVDDIAEKLADAGLNAAAYHAGmsneQRQFVQTgFARDDIQ 290
Cdd:cd18798 1 NIVDVYIEDSDSLEKLLELVKKLGD-GGLIFVSIDYgkeYAEELKEFLERHGIKAELALSS----TEKNLEK-FEEGEID 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1822009350 291 IVVATVAF-GM---GINKPN-VRFVLHYDIPksIESYYQETGRAGR 331
Cdd:cd18798 75 VLIGVASYyGVlvrGIDLPErIKYAIFYGVP--VTTYIQASGRTSR 118
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
221-331 |
3.44e-03 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is 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. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef 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: 350188 [Multi-domain] Cd Length: 143 Bit Score: 38.11 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 221 EKFKP-MVQLLRYLKEQ-------KSQSGIIYCTSRKRVDDIAEKLAD----------AGLNAAAYHAGMSNEQRQFVQT 282
Cdd:cd18801 5 EKIHPkLEKLEEIVKEHfkkkqegSDTRVIIFSEFRDSAEEIVNFLSKirpgiratrfIGQASGKSSKGMSQKEQKEVIE 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1822009350 283 GFARDDIQIVVATVAFGMGINKPNVRFVLHYDIPKSIESYYQETGRAGR 331
Cdd:cd18801 85 QFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
21-150 |
4.85e-03 |
|
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350714 [Multi-domain] Cd Length: 231 Bit Score: 38.77 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 21 QVFGYSEFRDGQKAVIDAAINGQ---------DSLVLLPTGGGKSVCYQIP---ALVLEGVT----IVISPLISLMQdQV 84
Cdd:cd17956 6 QNNGITSAFPVQAAVIPWLLPSSkstppyrpgDLCVSAPTGSGKTLAYVLPivqALSKRVVPrlraLIVVPTKELVQ-QV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 85 TQ-LQA------LGVKAAYVNNSLAREEQQLVYQQLHQGQ--IKLLYVAPEKVLQHefLER-----LSHLnvNLFAIDEA 150
Cdd:cd17956 85 YKvFESlckgtgLKVVSLSGQKSFKKEQKLLLVDTSGRYLsrVDILVATPGRLVDH--LNStpgftLKHL--RFLVIDEA 160
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
249-346 |
5.24e-03 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 38.09 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 249 KRVDDIAEKLAD---AGLNAAAYHAGMSNEQRQFVQTGFARDDIQIVVATVAFGMGINKPNVRFVLHYDIPK-SIESYYQ 324
Cdd:cd18811 45 KAAVAMYEYLKErfrPELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERfGLSQLHQ 124
|
90 100
....*....|....*....|...
gi 1822009350 325 ETGRAGRDGLAAEAI-MYFDPAD 346
Cdd:cd18811 125 LRGRVGRGDHQSYCLlVYKDPLT 147
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
224-333 |
6.65e-03 |
|
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: 37.57 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 224 KPMVQ-LLRYLKEQKSQS----GIIYCTSRKRVDDIAEKLADAGLN----AAAYHAGMSN---------EQRQFVQT--G 283
Cdd:cd18802 6 IPKLQkLIEILREYFPKTpdfrGIIFVERRATAVVLSRLLKEHPSTlafiRCGFLIGRGNssqrkrslmTQRKQKETldK 85
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90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1822009350 284 FARDDIQIVVATVAFGMGINKPNVRFVLHYDIPKSIESYYQETGRAGRDG 333
Cdd:cd18802 86 FRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPN 135
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| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
26-151 |
7.83e-03 |
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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: 38.18 E-value: 7.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 26 SEFRDGQKAVIDAAINGQDSLVLLPTGGGKS-----VC----YQIPALVlEGVTIVISPLISLMQDQVTQLQALGVKAAY 96
Cdd:cd17927 1 FKPRNYQLELAQPALKGKNTIICLPTGSGKTfvavlICehhlKKFPAGR-KGKVVFLANKVPLVEQQKEVFRKHFERPGY 79
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90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1822009350 97 VNNSLAREEQQLVYQQLHQGQIKLLYVAP---EKVLQHEFLERLShlNVNLFAIDEAH 151
Cdd:cd17927 80 KVTGLSGDTSENVSVEQIVESSDVIIVTPqilVNDLKSGTIVSLS--DFSLLVFDECH 135
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| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
28-185 |
7.96e-03 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 37.29 E-value: 7.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 28 FRDGQK-AV--IDAAINGQDSLVLLPTGGGKSVC-YQIPALVLEGVTIVISPLISLMqDQvtqlqalgVKAAYVNNSLAR 103
Cdd:cd17926 1 LRPYQEeALeaWLAHKNNRRGILVLPTGSGKTLTaLALIAYLKELRTLIVVPTDALL-DQ--------WKERFEDFLGDS 71
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822009350 104 EEQQLVYQQLHQGQIKLLYVA-PEKVLQHEFLERLSHLNVNLFAIDEAHcvsHWGHDFrphyfrLNELKQRFAHVPMMAL 182
Cdd:cd17926 72 SIGLIGGGKKKDFDDANVVVAtYQSLSNLAEEEKDLFDQFGLLIVDEAH---HLPAKT------FSEILKELNAKYRLGL 142
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...
gi 1822009350 183 TAT 185
Cdd:cd17926 143 TAT 145
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