|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
25-617 |
0e+00 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 1015.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 25 TALDVLHAVFGYQSFRKGQEEVIDATLMGKDSLVIMATGNGKSLCYQIPALCFEGLTLVISPLISLMKDQVDQLLANGIE 104
Cdd:PRK11057 12 LAKQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 105 ADYLNSSQTFTEQQQVQNKLMSGTLKLLYVSPEKVMTTSFFHLISHCKVSFVAIDEAHCISQWGHDFRPEYTQLGGLKSC 184
Cdd:PRK11057 92 AACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPEYAALGQLRQR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 185 FPHAPIMALTATADHATRQDILRHLNLQSPHVYIGSFDRPNIRYTLVEKFKPMEQLCRFVLGQKGKSGIIYCNSRSKVER 264
Cdd:PRK11057 172 FPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLVEKFKPLDQLMRYVQEQRGKSGIIYCNSRAKVED 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 265 IAESLRNKGVSAQAYHAGLETAQREQVQRAFQRDNVQVVVATIAFGMGINKSNVRFVVHFDLPRSIESYYQETGRAGRDD 344
Cdd:PRK11057 252 TAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 345 LPAEAVLFYEPADYAWLHKILLEKPESPQRQIEALKLQAIGEFAESQTCRRLVLLNYFGEHQQKPCQNCDICLDPPKQYD 424
Cdd:PRK11057 332 LPAEAMLFYDPADMAWLRRCLEEKPAGQQQDIERHKLNAMGAFAEAQTCRRLVLLNYFGEGRQEPCGNCDICLDPPKQYD 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 425 GLIDAQKVMSTIYRIGQRFGVHYVIAVLRGLSSQKIKDNQHEQLSVYGIGKDKSKEHWQSVIRQLIHLGFIKQVFDHfNA 504
Cdd:PRK11057 412 GLEDAQKALSCIYRVNQRFGMGYVVEVLRGANNQRIRDYGHDKLKVYGIGRDKSHEHWVSVIRQLIHLGLVTQNIAQ-HS 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 505 TLQLTENAKPILRGEQPLSLAMPRISSLTSVVAPQRYAmAQYDKDLFARLRFLRKQIADKENIPAYIVFNDATLQEMAQY 584
Cdd:PRK11057 491 ALQLTEAARPVLRGEVSLQLAVPRIVALKPRAMQKSFG-GNYDRKLFAKLRKLRKSIADEENIPPYVVFNDATLIEMAEQ 569
|
570 580 590
....*....|....*....|....*....|...
gi 492027914 585 QPTTKAEMLAINGVGATKFERFAQPFMQIIQQH 617
Cdd:PRK11057 570 MPITASEMLSVNGVGQRKLERFGKPFMALIRAH 602
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
26-617 |
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: 806.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 26 ALDVLHAVFGYQSFRKGQEEVIDATLMGKDSLVIMATGNGKSLCYQIPALCFEGLTLVISPLISLMKDQVDQLLANGIEA 105
Cdd:TIGR01389 1 AQQVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 106 DYLNSSQTFTEQQQVQNKLMSGTLKLLYVSPEKVMTTSFFHLISHCKVSFVAIDEAHCISQWGHDFRPEYTQLGGLKSCF 185
Cdd:TIGR01389 81 AYLNSTLSAKEQQDIEKALVNGELKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 186 PHAPIMALTATADHATRQDILRHLNLQSPHVYIGSFDRPNIRYTLVEKFKPMEQLCRFVLGQKGKSGIIYCNSRSKVERI 265
Cdd:TIGR01389 161 PQVPRIALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKNNKQKFLLDYLKKHRGQSGIIYASSRKKVEEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 266 AESLRNKGVSAQAYHAGLETAQREQVQRAFQRDNVQVVVATIAFGMGINKSNVRFVVHFDLPRSIESYYQETGRAGRDDL 345
Cdd:TIGR01389 241 AERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 346 PAEAVLFYEPADYAWlHKILLEKPESP--QRQIEALKLQAIGEFAESQTCRRLVLLNYFGEHQQKPCQNCDICLDPPKQY 423
Cdd:TIGR01389 321 PAEAILLYSPADIAL-LKRRIEQSEADddYKQIEREKLRAMIAYCETQTCRRAYILRYFGENEVEPCGNCDNCLDPPKSY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 424 DGLIDAQKVMSTIYRIGQRFGVHYVIAVLRGLSSQKIKDNQHEQLSVYGIGKDKSKEHWQSVIRQLIHLGFIKQVfDHFN 503
Cdd:TIGR01389 400 DATVEAQKALSCVYRMGQRFGVGYIIEVLRGSKNDKILQKGHDQLSTYGIGKDYTQKEWRSLIDQLIAEGLLTEN-DEIY 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 504 ATLQLTENAKPILRGEQPLSLAMPRISSLTSvVAPQRYAMAQYDKDLFARLRFLRKQIADKENIPAYIVFNDATLQEMAQ 583
Cdd:TIGR01389 479 IGLQLTEAARKVLKNEVEVLLRPFKVVAKEK-TRVQKNLSVGVDNALFEALRELRKEQADEQNVPPYVIFSDSTLREMAE 557
|
570 580 590
....*....|....*....|....*....|....
gi 492027914 584 YQPTTKAEMLAINGVGATKFERFAQPFMQIIQQH 617
Cdd:TIGR01389 558 KRPATLNALLKIKGVGQNKLDRYGEAFLEVIREY 591
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
22-494 |
0e+00 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 792.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 22 LKQTALDVLHAVFGYQSFRKGQEEVIDATLMGKDSLVIMATGNGKSLCYQIPALCFEGLTLVISPLISLMKDQVDQLLAN 101
Cdd:COG0514 1 LRDDALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 102 GIEADYLNSSQTFTEQQQVQNKLMSGTLKLLYVSPEKVMTTSFFHLISHCKVSFVAIDEAHCISQWGHDFRPEYTQLGGL 181
Cdd:COG0514 81 GIRAAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 182 KSCFPHAPIMALTATADHATRQDILRHLNLQSPHVYIGSFDRPNIRYTLVEKF--KPMEQLCRFVLGQKGKSGIIYCNSR 259
Cdd:COG0514 161 RERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKPpdDKLAQLLDFLKEHPGGSGIVYCLSR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 260 SKVERIAESLRNKGVSAQAYHAGLETAQREQVQRAFQRDNVQVVVATIAFGMGINKSNVRFVVHFDLPRSIESYYQETGR 339
Cdd:COG0514 241 KKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 340 AGRDDLPAEAVLFYEPADYAWLHKILLEKPESP-QRQIEALKLQAIGEFAESQTCRRLVLLNYFGEHQQKPCQNCDICLD 418
Cdd:COG0514 321 AGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEeRKRVERAKLDAMLAYAETTGCRRQFLLRYFGEELAEPCGNCDNCLG 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492027914 419 PPKQYDGLIDAQKVMSTIYRIGQRFGVHYVIAVLRGLSSQKIKDNQHEQLSVYGIGKDKSKEHWQSVIRQLIHLGF 494
Cdd:COG0514 401 PPETFDGTEAAQKALSCVYRTGQRFGAGHVIDVLRGSKNEKIRQFGHDKLSTYGIGKDLSDKEWRSVIRQLLAQLF 476
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
28-477 |
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: 728.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 28 DVLHAVFGYQSFRKGQEEVIDATLMGKDSLVIMATGNGKSLCYQIPALCFEGLTLVISPLISLMKDQVDQLLANGIEADY 107
Cdd:TIGR00614 1 KILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 108 LNSSQTFTEQQQVQNKLMSGTLKLLYVSPEKVMTTSFF--HLISHCKVSFVAIDEAHCISQWGHDFRPEYTQLGGLKSCF 185
Cdd:TIGR00614 81 LNSAQTKEQQLNVLTDLKDGKIKLLYVTPEKISASNRLlqTLEERKGITLIAVDEAHCISQWGHDFRPDYKALGSLKQKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 186 PHAPIMALTATADHATRQDILRHLNLQSPHVYIGSFDRPNIRYTLVEKF-KPMEQLCRFVLG-QKGKSGIIYCNSRSKVE 263
Cdd:TIGR00614 161 PNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRRKTpKILEDLLRFIRKeFEGKSGIIYCPSRKKVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 264 RIAESLRNKGVSAQAYHAGLETAQREQVQRAFQRDNVQVVVATIAFGMGINKSNVRFVVHFDLPRSIESYYQETGRAGRD 343
Cdd:TIGR00614 241 QVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRAGRD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 344 DLPAEAVLFYEPADYAWLHKILLEKPESPQRQIEALKLQAIGEFAESQTCRRLVLLNYFGE----------HQQKPCQNC 413
Cdd:TIGR00614 321 GLPSECHLFYAPADMNRLRRLLMEEPDGNFRTYKLKLYEMMEYCLNSSTCRRLILLSYFGEkgfnksfcimGTEKCCDNC 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 414 DICLD------PPKQYDGLIDAQKVMSTIYRIGQRFGVHYVIAVLRGLSSQKIKDNQHEQLSVYGIGKDK 477
Cdd:TIGR00614 401 CKRLDyktkdvTDKVYDFGPQAQKALSAVGRLNQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLYGRGKDE 470
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
33-615 |
8.43e-128 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 405.43 E-value: 8.43e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 33 VFGYQSFRKGQEEVIDATLMGKDSLVIMATGNGKSLCYQIPALCFEGLTLVISPLISLMKDQVDQLLANGIEADYLNSSQ 112
Cdd:PLN03137 455 VFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQANIPAASLSAGM 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 113 TFTEQQQVQNKLMSGT--LKLLYVSPEKVMTTSFF--HLISHCKVSFVA---IDEAHCISQWGHDFRPEYTQLGGLKSCF 185
Cdd:PLN03137 535 EWAEQLEILQELSSEYskYKLLYVTPEKVAKSDSLlrHLENLNSRGLLArfvIDEAHCVSQWGHDFRPDYQGLGILKQKF 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 186 PHAPIMALTATADHATRQDILRHLNLQSPHVYIGSFDRPNIRYTLVEKFKP-MEQLCRFVLGQK-GKSGIIYCNSRSKVE 263
Cdd:PLN03137 615 PNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPKTKKcLEDIDKFIKENHfDECGIIYCLSRMDCE 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 264 RIAESLRNKGVSAQAYHAGLETAQREQVQRAFQRDNVQVVVATIAFGMGINKSNVRFVVHFDLPRSIESYYQETGRAGRD 343
Cdd:PLN03137 695 KVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGRAGRD 774
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 344 DLPAEAVLFYEPADYAWL-HKILLEKPESPQRQIEALKLQAIGEFAESQT---------------CRRLVLLNYFGE--- 404
Cdd:PLN03137 775 GQRSSCVLYYSYSDYIRVkHMISQGGVEQSPMAMGYNRMASSGRILETNTenllrmvsycenevdCRRFLQLVHFGEkfd 854
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 405 --HQQKPCQNCdicldppKQYDGLID------AQKVMSTIYRIGQRFGVHYVIAVLRGLSSQKIKDNQHEQLSVYGIGKD 476
Cdd:PLN03137 855 stNCKKTCDNC-------SSSKSLIDkdvteiARQLVELVKLTGERFSSAHILEVYRGSLNQYVKKHRHETLSLHGAGKH 927
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 477 KSKEHWQSVIRQLIHLGFIKQ------VFDHFNATLQLTEN-AKPILRGEQPLSL---------------AMPRISSLTS 534
Cdd:PLN03137 928 LSKGEASRILHYLVTEDILAEdvkksdLYGSVSSLLKVNESkAYKLFSGGQTIIMrfpssvkaskpskfeATPAKGPLTS 1007
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 535 --VVAPQRYAMAQYDKD------LFARLRFLRKQIADK--ENIPAYIVFNDATLQEMAQYQPTTKAEMLAINGVGATKFE 604
Cdd:PLN03137 1008 gkQSTLPMATPAQPPVDlnlsaiLYTALRKLRTALVKEagDGVMAYHIFGNATLQQISKRIPRTKEELLEINGLGKAKVS 1087
|
650
....*....|.
gi 492027914 605 RFAQPFMQIIQ 615
Cdd:PLN03137 1088 KYGDRLLETIE 1098
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
27-222 |
9.71e-105 |
|
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: 315.24 E-value: 9.71e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 27 LDVLHAVFGYQSFRKGQEEVIDATLMGKDSLVIMATGNGKSLCYQIPALCFEGLTLVISPLISLMKDQVDQLLANGIEAD 106
Cdd:cd17920 1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 107 YLNSSQTFTEQQQVQNKLMSGTLKLLYVSPEKVMTTSFFHLISHCK----VSFVAIDEAHCISQWGHDFRPEYTQLGGLK 182
Cdd:cd17920 81 ALNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLQRLPerkrLALIVVDEAHCVSQWGHDFRPDYLRLGRLR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 492027914 183 SCFPHAPIMALTATADHATRQDILRHLNLQSPHVYIGSFD 222
Cdd:cd17920 161 RALPGVPILALTATATPEVREDILKRLGLRNPVIFRASFD 200
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
27-213 |
3.51e-71 |
|
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.
Pssm-ID: 350776 [Multi-domain] Cd Length: 201 Bit Score: 228.29 E-value: 3.51e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 27 LDVLHAVFGYQSFRKGQEEVIDATLMGKDSLVIMATGNGKSLCYQIPALCFE----GLTLVISPLISLMKDQVDQLLAnG 102
Cdd:cd18018 1 LKLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRrrgpGLTLVVSPLIALMKDQVDALPR-A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 103 IEADYLNSSQTFTEQQQVQNKLMSGTLKLLYVSPEKVMTTSFFHLISHCK-VSFVAIDEAHCISQWGHDFRPEYTQLGGL 181
Cdd:cd18018 80 IKAAALNSSLTREERRRILEKLRAGEVKILYVSPERLVNESFRELLRQTPpISLLVVDEAHCISEWSHNFRPDYLRLCRV 159
|
170 180 190
....*....|....*....|....*....|...
gi 492027914 182 KSCFPHA-PIMALTATADHATRQDILRHLNLQS 213
Cdd:cd18018 160 LRELLGApPVLALTATATKRVVEDIASHLGIPE 192
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
28-222 |
1.82e-67 |
|
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: 219.16 E-value: 1.82e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 28 DVLHAVFGYQSFRKGQEEVIDATLMGKDSLVIMATGNGKSLCYQIPALCFEGLTLVISPLISLMKDQVDQLLANGIEADY 107
Cdd:cd18015 8 DTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLGISATM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 108 LNSSQTFTEQQQVQNKLMSGT--LKLLYVSPEKVMTTS-FFHLISHC----KVSFVAIDEAHCISQWGHDFRPEYTQLGG 180
Cdd:cd18015 88 LNASSSKEHVKWVHAALTDKNseLKLLYVTPEKIAKSKrFMSKLEKAynagRLARIAIDEVHCCSQWGHDFRPDYKKLGI 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 492027914 181 LKSCFPHAPIMALTATADHATRQDILRHLNLQSPHVYIGSFD 222
Cdd:cd18015 168 LKRQFPNVPILGLTATATSKVLKDVQKILCIQKCLTFTASFN 209
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
27-222 |
5.27e-66 |
|
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: 215.08 E-value: 5.27e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 27 LDVLHAVFGYQSFRKGQEEVIDATLMGKDSLVIMATGNGKSLCYQIPALCFEGLTLVISPLISLMKDQVDQLLANGIEAD 106
Cdd:cd18016 6 MKIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPAT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 107 YLNSSQTFTEQQQVQNKLMSG--TLKLLYVSPEKV-----MTTSFFHLISHCKVSFVAIDEAHCISQWGHDFRPEYTQLG 179
Cdd:cd18016 86 YLTGDKTDAEATKIYLQLSKKdpIIKLLYVTPEKIsasnrLISTLENLYERKLLARFVIDEAHCVSQWGHDFRPDYKRLN 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 492027914 180 GLKSCFPHAPIMALTATADHATRQDILRHLNLQSPHVYIGSFD 222
Cdd:cd18016 166 MLRQKFPSVPMMALTATATPRVQKDILNQLKMLRPQVFTMSFN 208
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
27-222 |
1.17e-62 |
|
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ATP-dependent helicase or WRN) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Werner's syndrome.
Pssm-ID: 350775 [Multi-domain] Cd Length: 193 Bit Score: 205.78 E-value: 1.17e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 27 LDVLHAVFGYQSFRKGQEEVIDATL-MGKDSLVIMATGNGKSLCYQIPALCFEGLTLVISPLISLMKDQVDQLLANGIEA 105
Cdd:cd18017 1 LNALNEYFGHSSFRPVQWKVIRSVLeERRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 106 DYLNSSQtfteQQQVQNKLMSGTLKLLYVSPEkvMTTSFFHLISHCK--VSFVAIDEAHCISQWGHDFRPEYTQLGGLKS 183
Cdd:cd18017 81 CFLGSAQ----SQNVLDDIKMGKIRVIYVTPE--FVSKGLELLQQLRngITLIAIDEAHCVSQWGHDFRSSYRHLGSIRN 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 492027914 184 CFPHAPIMALTATADHATRQDILRHLNLQSPHVYIGSFD 222
Cdd:cd18017 155 RLPNVPIVALTATATPSVRDDIIKNLNLRNPQITCTSFD 193
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
223-353 |
1.33e-62 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350181 [Multi-domain] Cd Length: 134 Bit Score: 203.21 E-value: 1.33e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 223 RPNIRYTLVEKFKPMEQLCRFVLG---QKGKSGIIYCNSRSKVERIAESLRNKGVSAQAYHAGLETAQREQVQRAFQRDN 299
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDLLKRIkveHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 492027914 300 VQVVVATIAFGMGINKSNVRFVVHFDLPRSIESYYQETGRAGRDDLPAEAVLFY 353
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 ... |
27-214 |
1.86e-56 |
|
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: 189.60 E-value: 1.86e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 27 LDVLHAVFGYQSFRKG-QEEVIDATLMGK-DSLVIMATGNGKSLCYQIPALCFEGLTLVISPLISLMKDQVDQLLANGIE 104
Cdd:cd18014 1 RSTLKKVFGHSDFKSPlQEKATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 105 ADYLNSSQTFTEQQQVQNKLMSGT--LKLLYVSPEKVMTTSF----FHLISHCKVSFVAIDEAHCISQWGHDFRPEYTQL 178
Cdd:cd18014 81 VDSLNSKLSAQERKRIIADLESEKpqTKFLYITPEMAATSSFqpllSSLVSRNLLSYLVVDEAHCVSQWGHDFRPDYLRL 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 492027914 179 GGLKSCFPHAPIMALTATADHATRQDILRHLNLQSP 214
Cdd:cd18014 161 GALRSRYGHVPWVALTATATPQVQEDIFAQLRLKKP 196
|
|
| DpdF |
NF041063 |
protein DpdF; |
22-359 |
1.66e-51 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 190.51 E-value: 1.66e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 22 LKQTALD-VLHAVFGYQSFR-KGQEEVIDATL-MGKDS--LVIMATGNGKSLCYQIPALCF---EGLTLVISPLISLMKD 93
Cdd:NF041063 122 LEPVPGDpFLAEALGFTHYRsPGQREAVRAALlAPPGStlIVNLPTGSGKSLVAQAPALLAsrqGGLTLVVVPTVALAID 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 94 QVDQLLANGIEADYLN-------SSQTFTEQQQVQNKLMSGTLKLLYVSPEKVMTTSFFHLISHCK---VSFVAIDEAHC 163
Cdd:NF041063 202 QERRARELLRRAGPDLggplawhGGLSAEERAAIRQRIRDGTQRILFTSPESLTGSLRPALFDAAEaglLRYLVVDEAHL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 164 ISQWGHDFRPEYTQLGGL-----KSCFPHAPI--MALTATADHATRqDILRHLNLQSPHVYI--GSFDRPNIRY------ 228
Cdd:NF041063 282 VDQWGDGFRPEFQLLAGLrrsllRLAPSGRPFrtLLLSATLTESTL-DTLETLFGPPGPFIVvsAVQLRPEPAYwvakcd 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 229 TLVEKF-----------KPMeqlcrfvlgqkgksgIIYCNSRSKVERIAESLRNKGVS-AQAYHAGLETAQREQVQRAFQ 296
Cdd:NF041063 361 SEEERRervlealrhlpRPL---------------ILYVTKVEDAEAWLQRLRAAGFRrVALFHGDTPDAERERLIEQWR 425
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492027914 297 RDNVQVVVATIAFGMGINKSNVRFVVHFDLPRSIESYYQETGRAGRDDLPAEAVLFYEPADYA 359
Cdd:NF041063 426 ENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLD 488
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
419-527 |
8.37e-39 |
|
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: 138.44 E-value: 8.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 419 PPKQYDGLIDAQKVMSTIYRIGQRFGVHYVIAVLRGLSSQKIKDNQHEQLSVYGIGKDKSKEHWQSVIRQLIHLGFIKQV 498
Cdd:pfam09382 1 PPETVDVTEEAQKILSCVYRTGQRFGAGHLIDVLRGSKNKKIRQLGHDKLSTFGIGKDLSKKEWRRIIRQLIAEGYLEVD 80
|
90 100
....*....|....*....|....*....
gi 492027914 499 FDHFNaTLQLTENAKPILRGEQPLSLAMP 527
Cdd:pfam09382 81 IEFYS-VLKLTPKAREVLKGEEKVMLRVP 108
|
|
| RQC |
smart00956 |
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix ... |
424-516 |
9.71e-37 |
|
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: 132.21 E-value: 9.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 424 DGLIDAQKVMSTIYRIGQRFGVHYVIAVLRGLSSQKIKDNQHEQLSVYGIGKDKSKEHWQSVIRQLIHLGFIKQVfDHFN 503
Cdd:smart00956 1 DVTEEAQKLLSCVYRTGQRFGAGHVIDVLRGSKNKKIRQKGHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLRED-GGRY 79
|
90
....*....|...
gi 492027914 504 ATLQLTENAKPIL 516
Cdd:smart00956 80 PYLKLTEKARPVL 92
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
40-198 |
1.54e-26 |
|
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: 106.17 E-value: 1.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 40 RKGQEEVIDATLMGKDSLVIMATGNGKSLCYQIPAL-----CFEGL-TLVISPLISLMKDQVDQLLANGIEADY-LNSSQ 112
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdkLDNGPqALVLAPTRELAEQIYEELKKLGKGLGLkVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 113 TFTEQQQVQNKLmsGTLKLLYVSPEKVMttSFFHLISHCK-VSFVAIDEAHCISQWGhdFRPEYTQLggLKSCFPHAPIM 191
Cdd:pfam00270 81 GGDSRKEQLEKL--KGPDILVGTPGRLL--DLLQERKLLKnLKLLVLDEAHRLLDMG--FGPDLEEI--LRRLPKKRQIL 152
|
....*..
gi 492027914 192 ALTATAD 198
Cdd:pfam00270 153 LLSATLP 159
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
17-364 |
2.87e-25 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 108.70 E-value: 2.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 17 FHEIPLKQTALDVLHAVfGYQSFRKGQEEVIDATLMGKDSLVIMATGNGKSLCYQIPALcfEGL---------TLVISP- 86
Cdd:COG0513 4 FADLGLSPPLLKALAEL-GYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLL--QRLdpsrprapqALILAPt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 87 ----------LISL----------------MKDQVDQLlANGIE---------ADYLNSsqtfteqqqvqnklmsGTLKL 131
Cdd:COG0513 81 relalqvaeeLRKLakylglrvatvyggvsIGRQIRAL-KRGVDivvatpgrlLDLIER----------------GALDL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 132 lyvspekvmttsffhliSHckVSFVAIDEAhcisqwghD------FRPEYTQLggLKSCFPHAPIMALTATADHATRQDI 205
Cdd:COG0513 144 -----------------SG--VETLVLDEA--------DrmldmgFIEDIERI--LKLLPKERQTLLFSATMPPEIRKLA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 206 LRHLNlqSP-HVYI--GSFDRPNI--RYTLVEKFKPMEQLCRFVLGQKGKSGIIYCNSRSKVERIAESLRNKGVSAQAYH 280
Cdd:COG0513 195 KRYLK--NPvRIEVapENATAETIeqRYYLVDKRDKLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALH 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 281 AGLETAQREQVQRAFQRDNVQVVVAT-IAfGMGINKSNVRFVVHFDLPRSIESYyq---eTGRAGRDdlpAEAVLFYEPA 356
Cdd:COG0513 273 GDLSQGQRERALDAFRNGKIRVLVATdVA-ARGIDIDDVSHVINYDLPEDPEDYvhrigrTGRAGAE---GTAISLVTPD 348
|
....*...
gi 492027914 357 DYAWLHKI 364
Cdd:COG0513 349 ERRLLRAI 356
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
263-343 |
2.80e-24 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 96.90 E-value: 2.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 263 ERIAESLRNKGVSAQAYHAGLETAQREQVQRAFQRDNVQVVVATIAFGMGINKSNVRFVVHFDLPRSIESYYQETGRAGR 342
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
.
gi 492027914 343 D 343
Cdd:smart00490 81 A 81
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
237-342 |
1.31e-22 |
|
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: 93.04 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 237 MEQLCRFVLGQKGKSGIIYCNSRSKVErIAESLRNKGVSAQAYHAGLETAQREQVQRAFQRDNVQVVVATIAFGMGINKS 316
Cdd:pfam00271 3 LEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLP 81
|
90 100
....*....|....*....|....*.
gi 492027914 317 NVRFVVHFDLPRSIESYYQETGRAGR 342
Cdd:pfam00271 82 DVDLVINYDLPWNPASYIQRIGRAGR 107
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
34-229 |
3.72e-22 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 94.87 E-value: 3.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 34 FGYQSFRKGQEEVIDATLMG-KDSLVIMATGNGKSLCYQIPALCF-----EGLTLVISPLISLMKDQVDQLLA----NGI 103
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELKKlgpsLGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 104 EADYLNSSQTFTEQQQvqnKLMSGTLKLLYVSPEKVMTTSFFHLISHCKVSFVAIDEAHCISQWGhdFRPEYTQLggLKS 183
Cdd:smart00487 84 KVVGLYGGDSKREQLR---KLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGG--FGDQLEKL--LKL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 492027914 184 CFPHAPIMALTATADHATRQDILRHLNLqspHVYIGSFDRPNIRYT 229
Cdd:smart00487 157 LPKNVQLLLLSATPPEEIENLLELFLND---PVFIDVGFTPLEPIE 199
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
547-614 |
1.80e-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: 88.36 E-value: 1.80e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492027914 547 DKDLFARLRFLRKQIADKENIPAYIVFNDATLQEMAQYQPTTKAEMLAINGVGATKFERFAQPFMQII 614
Cdd:pfam00570 1 QLALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
232-342 |
5.15e-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: 89.10 E-value: 5.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 232 EKFKPMEQLCRFVLGQKGKSGIIYCNSRSKVERIAESLRNKGVSAQAYHAGLETAQREQVQRAFQRDNVQVVVATIAFGM 311
Cdd:cd18787 10 EEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVATDVAAR 89
|
90 100 110
....*....|....*....|....*....|.
gi 492027914 312 GINKSNVRFVVHFDLPRSIESYYQETGRAGR 342
Cdd:cd18787 90 GLDIPGVDHVINYDLPRDAEDYVHRIGRTGR 120
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
546-620 |
1.78e-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: 83.12 E-value: 1.78e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492027914 546 YDKDLFARLRFLRKQIADKENIPAYIVFNDATLQEMAQYQPTTKAEMLAINGVGATKFERFAQPFMQIIQQHKKV 620
Cdd:smart00341 3 RQLRLLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVIQEASDS 77
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
43-351 |
2.40e-17 |
|
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: 86.04 E-value: 2.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 43 QEEVIDATLMGKDSLVIMATGNGKSLCYQIPALcfEGL-------TLVISPLISLMKDQVDQL--LANGIEADYlnSSQT 113
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVL--EALledpgatALYLYPTKALARDQLRRLreLAEALGLGV--RVAT 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 114 FT------EQQQVQNklmsgtlkllyvSPEKVMTT----------------SFFhlishCKVSFVAIDEAHcisqwghdf 171
Cdd:COG1205 137 YDgdtppeERRWIRE------------HPDIVLTNpdmlhygllphhtrwaRFF-----RNLRYVVIDEAH--------- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 172 rpEYT-------------------QLGGlkscfphAP-IMALTAT----ADHATR---QDIL-----------RHLNLQS 213
Cdd:COG1205 191 --TYRgvfgshvanvlrrlrricrHYGS-------DPqFILASATignpAEHAERltgRPVTvvdedgsprgeRTFVLWN 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 214 PHVYIGSFDRPNIRYTlvekfkpMEQLCRFVlgQKGKSGIIYCNSRSKVERIAESLRNK------GVSAQAYHAGLETAQ 287
Cdd:COG1205 262 PPLVDDGIRRSALAEA-------ARLLADLV--REGLRTLVFTRSRRGAELLARYARRAlrepdlADRVAAYRAGYLPEE 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492027914 288 REQVQRAFQRDNVQVVVATIAFGMGINKSNVRFVVHFDLPRSIESYYQETGRAGRDDLPAEAVL 351
Cdd:COG1205 333 RREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVL 396
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
248-352 |
6.30e-15 |
|
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: 72.59 E-value: 6.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 248 KGKSGIIYCNSRSKVERIAESLRnkGVSAqaYHAGLETAQREQVQRAFQRDNVQVVVATIAFGMGIN--------KSNVR 319
Cdd:cd18795 42 EGKPVLVFCSSRKECEKTAKDLA--GIAF--HHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNlpartviiKGTQR 117
|
90 100 110
....*....|....*....|....*....|....*.
gi 492027914 320 FVVHFDLPRSIESYYQETGRAGR---DDLpAEAVLF 352
Cdd:cd18795 118 YDGKGYRELSPLEYLQMIGRAGRpgfDTR-GEAIIM 152
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
35-352 |
6.73e-15 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 77.52 E-value: 6.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 35 GYQSFRKGQEEVIDATLMGKDSLVIMATGNGKSLCYQIP--ALCFE-----------GLTLVISP---LISLMKDQVdQL 98
Cdd:PLN00206 140 GYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPiiSRCCTirsghpseqrnPLAMVLTPtreLCVQVEDQA-KV 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 99 LANG--------IEADYLnSSQTFTEQQQVQnkLMSGTlkllyvsPEKVMTTSFFHLISHCKVSFVAIDEAHCISQWGhd 170
Cdd:PLN00206 219 LGKGlpfktalvVGGDAM-PQQLYRIQQGVE--LIVGT-------PGRLIDLLSKHDIELDNVSVLVLDEVDCMLERG-- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 171 FRPEYTQLgglKSCFPHAPIMALTATADHATRQ---DILRHLNLQSphvyIGSFDRPNirytlvekfKPMEQLCRFVLGQ 247
Cdd:PLN00206 287 FRDQVMQI---FQALSQPQVLLFSATVSPEVEKfasSLAKDIILIS----IGNPNRPN---------KAVKQLAIWVETK 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 248 KGKS---------------GIIYCNSRSKVERIAESLR-NKGVSAQAYHAGLETAQREQVQRAFQRDNVQVVVATIAFGM 311
Cdd:PLN00206 351 QKKQklfdilkskqhfkppAVVFVSSRLGADLLANAITvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGR 430
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 492027914 312 GINKSNVRFVVHFDLPRSIESYYQETGRAGRDDLPAEAVLF 352
Cdd:PLN00206 431 GVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVF 471
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
228-364 |
1.51e-14 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 76.02 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 228 YTLVEKFK-PMEQLCRFVLGQKGKSGIIYCNSRSKVERIAESLRNKGVSAQAYHAGLETAQREQVQRAFQRDNVQVVVAT 306
Cdd:PTZ00424 245 YVAVEKEEwKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITT 324
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 492027914 307 IAFGMGINKSNVRFVVHFDLPRSIESYYQETGRAGRDDLPAEAVLFYEPADYAWLHKI 364
Cdd:PTZ00424 325 DLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEI 382
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
53-196 |
2.21e-14 |
|
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: 70.51 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 53 GKDSLVIMATGNGKSLCYQIPALC----FEGLTLVISPLISLMKDQ---VDQLLANGIEADYLNSSQTFTEQQQVQNklm 125
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLlllkKGKKVLVLVPTKALALQTaerLRELFGPGIRVAVLVGGSSAEEREKNKL--- 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492027914 126 sGTLKLLYVSPEKVMTTSFFHLISHCK-VSFVAIDEAHCISQWGHDFRPEYtqLGGLKSCFPHAPIMALTAT 196
Cdd:cd00046 78 -GDADIIIATPDMLLNLLLREDRLFLKdLKLIIVDEAHALLIDSRGALILD--LAVRKAGLKNAQVILLSAT 146
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
253-351 |
5.73e-14 |
|
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: 69.59 E-value: 5.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 253 IIYCNSRSKVERIAESLRNKGVSA-------QAYHAGLETAQREQVQRAFQRDNVQVVVATIAFGMGINKSNVRFVVHFD 325
Cdd:cd18797 39 IVFCRSRKLAELLLRYLKARLVEEgplaskvASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
|
90 100
....*....|....*....|....*.
gi 492027914 326 LPRSIESYYQETGRAGRDDLPAEAVL 351
Cdd:cd18797 119 YPGSLASLWQQAGRAGRRGKDSLVIL 144
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
355-417 |
6.39e-14 |
|
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: 66.54 E-value: 6.39e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492027914 355 PADYAWLHKILLEKPESP-QRQIEALKLQAIGEFAESQT-CRRLVLLNYFGEH-QQKPCQNCDICL 417
Cdd:pfam16124 1 YQDVVRLRFLIEQSEADEeRKEVELQKLQAMVAYCENTTdCRRKQLLRYFGEEfDSEPCGNCDNCL 66
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
43-354 |
3.39e-13 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 72.36 E-value: 3.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 43 QEEVIDATLM-----GKDSLVIMATGNGKSL----CYQipALCFEGLTLVISPLISLMKDQVDQLlangieADYLNSSQT 113
Cdd:COG1061 85 QQEALEALLAalergGGRGLVVAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRRELLEQWAEEL------RRFLGDPLA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 114 FTEQQQVQNKLMSGTLKLLYVSPEKVMTTSFFHLIshckvsfvAIDEAHcisqwgHDFRPEYTQLggLKScFPHAPIMAL 193
Cdd:COG1061 157 GGGKKDSDAPITVATYQSLARRAHLDELGDRFGLV--------IIDEAH------HAGAPSYRRI--LEA-FPAAYRLGL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 194 TAT----------------------ADHATRQDILRhlnlqsPHVYIG---SFDRPNIRYT-----LVEKFKPMEQLCRF 243
Cdd:COG1061 220 TATpfrsdgreillflfdgivyeysLKEAIEDGYLA------PPEYYGirvDLTDERAEYDalserLREALAADAERKDK 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 244 VLGQ------KGKSGIIYCNSRSKVERIAESLRNKGVSAQAYHAGLETAQREQVQRAFQRDNVQVVVATIAFGMGINKSN 317
Cdd:COG1061 294 ILREllrehpDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPR 373
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 492027914 318 VRFVVHFdlpRSIES---YYQETGRAGRDDLPAEAVLFYE 354
Cdd:COG1061 374 LDVAILL---RPTGSpreFIQRLGRGLRPAPGKEDALVYD 410
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
156-344 |
4.45e-13 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 72.62 E-value: 4.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 156 VAIDEAHCI--SQWGHdfrpeytQLGG----LKSCFPHAPIMALTATADHAtrQDILRHLNLqSPHVYIgsfDRP-NIRY 228
Cdd:COG1202 330 VVIDEVHMLedPERGH-------RLDGliarLKYYCPGAQWIYLSATVGNP--EELAKKLGA-KLVEYE---ERPvPLER 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 229 TLV-----EKFKPMEQLCRFVLGQKGKSG-----IIYCNSRSKVERIAESLrnkGVSAQAYHAGLETAQREQVQRAFQRD 298
Cdd:COG1202 397 HLTfadgrEKIRIINKLVKREFDTKSSKGyrgqtIIFTNSRRRCHEIARAL---GYKAAPYHAGLDYGERKKVERRFADQ 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 492027914 299 NVQVVVATIAFGMGinksnVRF----VVhFD-LPRSIE-----SYYQETGRAGRDD 344
Cdd:COG1202 474 ELAAVVTTAALAAG-----VDFpasqVI-FDsLAMGIEwlsvqEFHQMLGRAGRPD 523
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
253-353 |
3.17e-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: 3.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 253 IIYCNSRSKVERIAESLrnkgvsaqayhagletaqreqvqrafqrdnvQVVVATIAFGMGINKSNVRFVVHFDLPRSIES 332
Cdd:cd18785 7 IVFTNSIEHAEEIASSL-------------------------------EILVATNVLGEGIDVPSLDTVIFFDPPSSAAS 55
|
90 100
....*....|....*....|..
gi 492027914 333 YYQETGRAGRD-DLPAEAVLFY 353
Cdd:cd18785 56 YIQRVGRAGRGgKDEGEVILFV 77
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
17-354 |
1.16e-11 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 67.57 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 17 FHEIPLKQTALDVLHAVfGYQSFRKGQEEVIDATLMGKDSLVIMATGNGKSLCYQIPAL------CFEGLTLVISPLISL 90
Cdd:PRK11634 8 FADLGLKAPILEALNDL-GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLhnldpeLKAPQILVLAPTREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 91 MKdQVDQLLA------NGIEADYLNSSQTFTEQqqvqnklmsgtLKLLYVSPEKVMTTSFfHLISHCK--------VSFV 156
Cdd:PRK11634 87 AV-QVAEAMTdfskhmRGVNVVALYGGQRYDVQ-----------LRALRQGPQIVVGTPG-RLLDHLKrgtldlskLSGL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 157 AIDEAHCISQWG--HDFRPEYTQLgglkscfPHAPIMAL-TATADHATRQDILRHLNlQSPHVYIGS--FDRPNIR--YT 229
Cdd:PRK11634 154 VLDEADEMLRMGfiEDVETIMAQI-------PEGHQTALfSATMPEAIRRITRRFMK-EPQEVRIQSsvTTRPDISqsYW 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 230 LVEKFKPMEQLCRFVLGQKGKSGIIYCNSRSKVERIAESLRNKGVSAQAYHAGLETAQREQVQRAFQRDNVQVVVATIAF 309
Cdd:PRK11634 226 TVWGMRKNEALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVA 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 492027914 310 GMGINKSNVRFVVHFDLPRSIESYYQETGRAGRDDLPAEAVLFYE 354
Cdd:PRK11634 306 ARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVE 350
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
245-342 |
1.57e-11 |
|
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: 62.67 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 245 LGQKGKSGIIYCNSRSKVERIAESLRNK------GVSAQAYHAGLETAQREQVQRAFQRDNVQVVVATIAFGMGINKSNV 318
Cdd:cd18796 34 LLERHKSTLVFTNTRSQAERLAQRLRELcpdrvpPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDV 113
|
90 100
....*....|....*....|....
gi 492027914 319 RFVVHFDLPRSIESYYQETGRAGR 342
Cdd:cd18796 114 DLVIQIGSPKSVARLLQRLGRSGH 137
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
19-342 |
3.07e-10 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 62.99 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 19 EIPLKqTALDVLHAvFGYQSFRKGQEEVIDATLMGKDSLVI-MATGNGKSLCYQIPALC--FEGLT-LVISPLISL---M 91
Cdd:COG1204 5 ELPLE-KVIEFLKE-RGIEELYPPQAEALEAGLLEGKNLVVsAPTASGKTLIAELAILKalLNGGKaLYIVPLRALaseK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 92 KDQVDQLLAN-GIEA-----DYLNSSQTFTEQQqvqnklmsgtlkLLYVSPEKVMttsffHLISH-----CKVSFVAIDE 160
Cdd:COG1204 83 YREFKRDFEElGIKVgvstgDYDSDDEWLGRYD------------ILVATPEKLD-----SLLRNgpswlRDVDLVVVDE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 161 AHCIsqwGHDFRpeytqlGG--------LKSCFPHAPIMALTATADHAtrQDILRHLNlqSPHV---------YIGSFDR 223
Cdd:COG1204 146 AHLI---DDESR------GPtlevllarLRRLNPEAQIVALSATIGNA--EEIAEWLD--AELVksdwrpvplNEGVLYD 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 224 PNIRY--TLVEKFKPMEQLCRFVLGQKGKSgIIYCNSRSKVERIAESLRN------------------------------ 271
Cdd:COG1204 213 GVLRFddGSRRSKDPTLALALDLLEEGGQV-LVFVSSRRDAESLAKKLADelkrrltpeereeleelaeellevseetht 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 272 ---------KGVsaqAYH-AGLETAQREQVQRAFQRDNVQVVVAT--IAfgMGINksnvrfvvhfdLP------RSIES- 332
Cdd:COG1204 292 nekladcleKGV---AFHhAGLPSELRRLVEDAFREGLIKVLVATptLA--AGVN-----------LParrviiRDTKRg 355
|
410
....*....|....*....
gi 492027914 333 ---------YYQETGRAGR 342
Cdd:COG1204 356 gmvpipvleFKQMAGRAGR 374
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
240-380 |
8.48e-10 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 61.11 E-value: 8.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 240 LCRFVLGQKGKSGIIYCNSRSKVERIAESLRNKGVSAqAYHAG-LETAQREQVQRAFQRDNVQVVVATIAFGMGINKSNV 318
Cdd:PRK11192 236 LCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINC-CYLEGeMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDV 314
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492027914 319 RFVVHFDLPRSIESYYQETGRAGRDDLPAEAVLFYEPADYAWLHKI--LLEKPESPqRQIEALK 380
Cdd:PRK11192 315 SHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIerYIEEPLKA-RVIDELR 377
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
51-373 |
2.00e-09 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 60.56 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 51 LMGKDSLVIMATGNGKSLCYQIPALCF----------EG-LTLVISPLISLMKDQVDQLLANGIEADYLNS--------- 110
Cdd:PTZ00110 165 LSGRDMIGIAETGSGKTLAFLLPAIVHinaqpllrygDGpIVLVLAPTRELAEQIREQCNKFGASSKIRNTvayggvpkr 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 111 SQTFTEQQQVQnKLMSGTLKLLYVSPEKVMTTSffhlishcKVSFVAIDEAHCISQWGhdFRPEYTQLggLKSCFPHAPI 190
Cdd:PTZ00110 245 GQIYALRRGVE-ILIACPGRLIDFLESNVTNLR--------RVTYLVLDEADRMLDMG--FEPQIRKI--VSQIRPDRQT 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 191 MALTATADHATrQDILRHLNLQSP-HVYIGSFDRP---NIRYT--LVEKFKPMEQLcRFVLGQKGKSG---IIYCNSRSK 261
Cdd:PTZ00110 312 LMWSATWPKEV-QSLARDLCKEEPvHVNVGSLDLTachNIKQEvfVVEEHEKRGKL-KMLLQRIMRDGdkiLIFVETKKG 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 262 VERIAESLRNKGVSAQAYHAGLETAQREQVQRAFQRDNVQVVVATIAFGMGINKSNVRFVVHFDLPRSIESYYQETGRAG 341
Cdd:PTZ00110 390 ADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTG 469
|
330 340 350
....*....|....*....|....*....|....*..
gi 492027914 342 RDDLPAEAVLFYEPADYAW---LHKILLE--KPESPQ 373
Cdd:PTZ00110 470 RAGAKGASYTFLTPDKYRLardLVKVLREakQPVPPE 506
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
248-352 |
7.19e-08 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 55.34 E-value: 7.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 248 KGKSGIIYCNSRSKVERIAESLRNKGVSAQAYHAGLETAQREQVQRAFQRDNVQVVVATIAFGMGINKSNVRFVVHFDLP 327
Cdd:PRK04537 256 EGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVYNYDLP 335
|
90 100
....*....|....*....|....*
gi 492027914 328 RSIESYYQETGRAGRDDLPAEAVLF 352
Cdd:PRK04537 336 FDAEDYVHRIGRTARLGEEGDAISF 360
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
253-342 |
2.37e-07 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 53.76 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 253 IIYCNSRSKVERIAESLRNKGVSAQAYHAGLETAQREQVQRAFQRDNVQVVVATIAFGMGINKSNVRFVVHFDLPRSIES 332
Cdd:PRK01297 339 MVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDD 418
|
90
....*....|
gi 492027914 333 YYQETGRAGR 342
Cdd:PRK01297 419 YVHRIGRTGR 428
|
|
| Rnd |
COG0349 |
Ribonuclease D [Translation, ribosomal structure and biogenesis]; |
552-628 |
6.62e-07 |
|
Ribonuclease D [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440118 [Multi-domain] Cd Length: 365 Bit Score: 51.80 E-value: 6.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 552 ARLRFL---RKQIADKENIPAYIVFNDATLQEMAQYQPTTKAEMLAINGVGATKFERFAQPFMQIIQQHKKVLTQHEPPL 628
Cdd:COG0349 211 AVLRELaawREREARKRDVPRNRVLKDEALLELARRQPKSLEELARLRGLSPGEIRRHGEELLAAVAEALALPEEELPEP 290
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
226-327 |
7.99e-06 |
|
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: 45.55 E-value: 7.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 226 IRYTLVEKFKPMEQLCRFVLGQKGKSgIIYCNSRSKVERIAESLRNKGVSAQAYHAGLETAQREQVQRAFQRD-NVQVVV 304
Cdd:cd18793 5 IEEVVSGKLEALLELLEELREPGEKV-LIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDpDIRVFL 83
|
90 100
....*....|....*....|....
gi 492027914 305 ATI-AFGMGINKSNVRFVVHFDLP 327
Cdd:cd18793 84 LSTkAGGVGLNLTAANRVILYDPW 107
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
278-342 |
9.98e-06 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 48.78 E-value: 9.98e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492027914 278 AYHAGLETAQREQVQRAFQRDNVQVVVATIAFGMGINKSnVRFVV-----------HFDL-PRsieSYYQETGRAGR 342
Cdd:COG4581 304 VHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMP-ARTVVftklskfdgerHRPLtAR---EFHQIAGRAGR 376
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
264-350 |
3.58e-05 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 46.73 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 264 RIAESLRNKGVSAQAYHAGLETAQREQVQRAFQRDNVQVVVATIAFGMGINKSNVRFVVHFDLPRSIESYYQETGRAGRD 343
Cdd:PRK10590 260 HLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGRA 339
|
....*..
gi 492027914 344 DLPAEAV 350
Cdd:PRK10590 340 AATGEAL 346
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
43-98 |
4.55e-05 |
|
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: 44.50 E-value: 4.55e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492027914 43 QEEVIDATLMGKDSLVIMATGNGKSLCYQIPAlcFEGL-------TLVISPLISLMKDQVDQL 98
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPI--LEALlrdpgsrALYLYPTKALAQDQLRSL 65
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
253-327 |
5.42e-05 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 46.37 E-value: 5.42e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492027914 253 IIYCNSRSKVERIAESLRNKGVSAQAYHAGLETAQREQVQRAFQRDN--VQVVVATIAFGMGINKSNVRFVVHFDLP 327
Cdd:COG0553 553 LVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGGEGLNLTAADHVIHYDLW 629
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
276-353 |
9.51e-05 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 45.69 E-value: 9.51e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492027914 276 AQAYHAGLETAQREQVQRAFQRDNVQVVVATIAFGMGINKSNVRFVVHFDLPRSIESYYQETGRAGRDDLPAEAVLFY 353
Cdd:PRK09751 304 ARSHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAGHQVGGVSKGLFF 381
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
263-370 |
4.35e-04 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 43.27 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 263 ERIAESLRnKGVSAqaYHAGLETAQREQVQRAFQRDNVQVVVATIAFGMGINKSNVRFVVH----------FDLPrsIES 332
Cdd:PRK00254 288 EKLKKALR-GGVAF--HHAGLGRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRdtkrysnfgwEDIP--VLE 362
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 492027914 333 YYQETGRAGRD--DLPAEAVLFY---EPADYawLHKILLEKPE 370
Cdd:PRK00254 363 IQQMMGRAGRPkyDEVGEAIIVAtteEPSKL--MERYIFGKPE 403
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
249-370 |
5.84e-04 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 42.95 E-value: 5.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 249 GKSGIIYCNSRSKVERIAESL-------RNKGVSAQA------------------YHAGLETAQREQVQRAFQRDNVQVV 303
Cdd:PRK01172 236 GGQVLVFVSSRKNAEDYAEMLiqhfpefNDFKVSSENnnvyddslnemlphgvafHHAGLSNEQRRFIEEMFRNRYIKVI 315
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492027914 304 VATIAFGMGINKSnVRFVVHFDLPRSIESYY---------QETGRAGR---DDLPAEAVLFYEPADYAWLHKILLEKPE 370
Cdd:PRK01172 316 VATPTLAAGVNLP-ARLVIVRDITRYGNGGIrylsnmeikQMIGRAGRpgyDQYGIGYIYAASPASYDAAKKYLSGEPE 393
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
38-196 |
6.94e-04 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 40.73 E-value: 6.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 38 SFRKGQEEVIDATLMG-----KDSLVIMATGNGKSLCY-QIPALCFEGL----TLVISPLISLMKDQVDQLLANGIEAD- 106
Cdd:pfam04851 3 ELRPYQIEAIENLLESikngqKRGLIVMATGSGKTLTAaKLIARLFKKGpikkVLFLVPRKDLLEQALEEFKKFLPNYVe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 107 -------------YLNSSQTFTEQQQVQNKLMSGTLKLLYvspekvmttSFFHLIshckvsfvAIDEAHcisqwgHDFRP 173
Cdd:pfam04851 83 igeiisgdkkdesVDDNKIVVTTIQSLYKALELASLELLP---------DFFDVI--------IIDEAH------RSGAS 139
|
170 180
....*....|....*....|...
gi 492027914 174 EYTQlggLKSCFPHAPIMALTAT 196
Cdd:pfam04851 140 SYRN---ILEYFKPAFLLGLTAT 159
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
39-196 |
7.82e-04 |
|
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: 40.37 E-value: 7.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 39 FRKGQEEVIDATLM---GKDSLVIMATGNGKSLC-YQIPALCFEGLTLVISPLISLMKDQVDQLLA-NGIEADYLNSSqt 113
Cdd:cd17926 1 LRPYQEEALEAWLAhknNRRGILVLPTGSGKTLTaLALIAYLKELRTLIVVPTDALLDQWKERFEDfLGDSSIGLIGG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 114 fteqqqvqNKLMSGTLKLLYVS----------PEKVMTTSFFHLIshckvsfvaIDEAHCIS--QWGHdFRPEytqlggl 181
Cdd:cd17926 79 --------GKKKDFDDANVVVAtyqslsnlaeEEKDLFDQFGLLI---------VDEAHHLPakTFSE-ILKE------- 133
|
170
....*....|....*
gi 492027914 182 kscFPHAPIMALTAT 196
Cdd:cd17926 134 ---LNAKYRLGLTAT 145
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
279-351 |
8.45e-04 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 42.64 E-value: 8.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 279 YHAGLETAQREQVQRAFqRDN-VQVVVATIAFGMGINKSNVRFVV----HFD-----LPRSIESYYQETGRAGRDDL-P- 346
Cdd:PRK02362 309 HHAGLSREHRELVEDAF-RDRlIKVISSTPTLAAGLNLPARRVIIrdyrRYDggagmQPIPVLEYHQMAGRAGRPGLdPy 387
|
....*
gi 492027914 347 AEAVL 351
Cdd:PRK02362 388 GEAVL 392
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
53-162 |
1.14e-03 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 40.26 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 53 GKDSLVIMATGNGKSLCYQIPALC------FEGL-TLVISPLISLMKDQVDQL--LANGIEADYLNSSQTFTEQQQVQNK 123
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSsladepEKGVqVLYISPLKALINDQERRLeePLDEIDLEIPVAVRHGDTSQSEKAK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 492027914 124 LMSGTLKLLYVSPE--KVMTTS--FFHLISHCKvsFVAIDEAH 162
Cdd:cd17922 81 QLKNPPGILITTPEslELLLVNkkLRELFAGLR--YVVVDEIH 121
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
229-355 |
1.15e-03 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. 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: 350179 [Multi-domain] Cd Length: 160 Bit Score: 39.94 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 229 TLVEKFKPMEQLCRFVLGQKGKSGIIY--CNsrskveRIAESLRNKGVSAQAYHAGLET----------------AQREQ 290
Cdd:cd18792 4 TYVIPHDDLDLVYEAIERELARGGQVYyvYP------RIEESEKLDLKSIEALAEELKElvpearvallhgkmteDEKEA 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492027914 291 VQRAFQRDNVQVVVATIAFGMGINKSNVRFVVHFDLPR-SIESYYQETGRAGRDDLPAEAVLFYEP 355
Cdd:cd18792 78 VMLEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRfGLSQLHQLRGRVGRGKHQSYCYLLYPD 143
|
|
| DinG |
COG1199 |
Rad3-related DNA helicase DinG [Replication, recombination and repair]; |
30-85 |
2.65e-03 |
|
Rad3-related DNA helicase DinG [Replication, recombination and repair];
Pssm-ID: 440812 [Multi-domain] Cd Length: 629 Bit Score: 40.68 E-value: 2.65e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492027914 30 LHAVFGYQSFRKGQEEVIDA---TLMGKDSLVIMA-TGNGKSLCYQIPALCF---EGLTLVIS 85
Cdd:COG1199 6 LALAFPGFEPRPGQREMAEAvarALAEGRHLLIEAgTGTGKTLAYLVPALLAareTGKKVVIS 68
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
247-354 |
2.79e-03 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 41.02 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 247 QKGKSGIIYCNSRSKVERIAESLRNKGVSA------QAYHAGLETAQREQVQRAFQRDNVQVVVATIAFGMGINKSNVRF 320
Cdd:PRK13767 282 KEHRTTLIFTNTRSGAERVLYNLRKRFPEEydedniGAHHSSLSREVRLEVEEKLKRGELKVVVSSTSLELGIDIGYIDL 361
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 492027914 321 VVHFDLPRSIESYYQETGRAG---------------RDDLPAEAVLFYE 354
Cdd:PRK13767 362 VVLLGSPKSVSRLLQRIGRAGhrlgevskgriivvdRDDLVECAVLLKK 410
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
273-344 |
2.96e-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: 38.34 E-value: 2.96e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492027914 273 GVSAQAYHAGLETAQREQVQRAFQRDNVQVVVATIAFGMGINKSNVRFVVHFDLPRSIESYYQETGRAGRDD 344
Cdd:cd18802 64 GNSSQRKRSLMTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPN 135
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
280-355 |
6.57e-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: 37.71 E-value: 6.57e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492027914 280 HAGLETAQREQVQRAFQRDNVQVVVATIAFGMGINKSNVRFVVHFDLPR-SIESYYQETGRAGRDDLPAEAVLFYEP 355
Cdd:cd18811 68 HGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERfGLSQLHQLRGRVGRGDHQSYCLLVYKD 144
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
249-342 |
7.63e-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: 37.67 E-value: 7.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 249 GKSGIIYCNS---RSKVERIAESLRNKGVSAQAYHAGletaqREQVQRAFQRDNVQVVVA------TIAFGMGINKSnVR 319
Cdd:cd18798 24 GDGGLIFVSIdygKEYAEELKEFLERHGIKAELALSS-----TEKNLEKFEEGEIDVLIGvasyygVLVRGIDLPER-IK 97
|
90 100
....*....|....*....|...
gi 492027914 320 FVVHFDLPrsIESYYQETGRAGR 342
Cdd:cd18798 98 YAIFYGVP--VTTYIQASGRTSR 118
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
253-342 |
8.86e-03 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 38.80 E-value: 8.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492027914 253 IIYCNSRSKVERIAESLrnkgvSAQAYHAGLET---AQ--REQVQRAFQRDNVQVVVATIAFGMGINKSNVRFVVHFDLP 327
Cdd:PRK04837 259 IIFANTKHRCEEIWGHL-----AADGHRVGLLTgdvAQkkRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLP 333
|
90
....*....|....*
gi 492027914 328 RSIESYYQETGRAGR 342
Cdd:PRK04837 334 DDCEDYVHRIGRTGR 348
|
|
| |
