|
Name |
Accession |
Description |
Interval |
E-value |
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
81-543 |
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: 724.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 81 DVLQNVFKLQKFRPLQLETINVTMARKDIFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGISATM 160
Cdd:TIGR00614 1 KILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 161 LNASSSKEHVKWVHAEMvnKNSQLKLIYVTPEKIAKSKMFMSRLEKAYeagRLTGAAVDEVHCCSQWGHDFRPDYKALGI 240
Cdd:TIGR00614 81 LNSAQTKEQQLNVLTDL--KDGKIKLLYVTPEKISASNRLLQTLEERK---GITLIAVDEAHCISQWGHDFRPDYKALGS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 241 LKRQFPNASLMGLTATATNHVLKDVQKILCVGKCLTFTASFNRPNLFYEVRQKPSsaeDFTEDIVKLINGRYKGQSGIIY 320
Cdd:TIGR00614 156 LKQKFPNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRRKTP---KILEDLLRFIRKEFEGKSGIIY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 321 CFSQKDSEQITISLQKLGIHAGTYHANMEPEDKTKVHTQWSANELQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQ 400
Cdd:TIGR00614 233 CPSRKKVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 401 ESGRAGRDDSRADCILYYGFGDIFRISSMVVMENVGQQ-----KLYEMVSYCQNVSKCRRVLIAQHFDEVWNAD-----A 470
Cdd:TIGR00614 313 ESGRAGRDGLPSECHLFYAPADMNRLRRLLMEEPDGNFrtyklKLYEMMEYCLNSSTCRRLILLSYFGEKGFNKsfcimG 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 326368214 471 CNKMCDNCCKDVSFEKKNVTQHCRDLIKILKQAEG----LNEKLTPLKLIDAWMGKGAAKLRVAGVVAPAL-PREDLE 543
Cdd:TIGR00614 393 TEKCCDNCCKRLDYKTKDVTDKVYDFGPQAQKALSavgrLNQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLyGRGKDE 470
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
78-528 |
7.24e-172 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 498.13 E-value: 7.24e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 78 KVKDVLQNVFKLQKFRPLQLETINVTMARKDIFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGIS 157
Cdd:COG0514 4 DALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 158 ATMLNASSSKEHVKWVHAEMvnKNSQLKLIYVTPEKIAKSKmFMSRLEKAyeagRLTGAAVDEVHCCSQWGHDFRPDYKA 237
Cdd:COG0514 84 AAFLNSSLSAEERREVLRAL--RAGELKLLYVAPERLLNPR-FLELLRRL----KISLFAIDEAHCISQWGHDFRPDYRR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 238 LGILKRQFPNASLMGLTATATNHVLKDVQKILCVGKCLTFTASFNRPNLFYEVRQKPSSAEDftEDIVKLINGRyKGQSG 317
Cdd:COG0514 157 LGELRERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKPPDDKL--AQLLDFLKEH-PGGSG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 318 IIYCFSQKDSEQITISLQKLGIHAGTYHANMEPEDKTKVHTQWSANELQVVVATVAFGMGIDKPDVRFVIHHSMSKSMEN 397
Cdd:COG0514 234 IVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 398 YYQESGRAGRDDSRADCILYYGFGDIFRISSMVVMEN-------VGQQKLYEMVSYCQnVSKCRRVLIAQHFDEVwNADA 470
Cdd:COG0514 314 YYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIEQSPpdeerkrVERAKLDAMLAYAE-TTGCRRQFLLRYFGEE-LAEP 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 326368214 471 CNKmCDNCCKDVsfEKKNVTQHCRdliKILKQAEGLNEKLTPLKLIDAWMGKGAAKLR 528
Cdd:COG0514 392 CGN-CDNCLGPP--ETFDGTEAAQ---KALSCVYRTGQRFGAGHVIDVLRGSKNEKIR 443
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
46-597 |
1.33e-150 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 465.52 E-value: 1.33e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 46 IKQYLEDSSAEASSDldtspAAWNKEDFPWFGKVKDVLQNVFKLQKFRPLQLETINVTMARKDIFLVMPTGGGKSLCYQL 125
Cdd:PLN03137 420 VPKFIDVTYTEGSND-----KKWSSRNFPWTKKLEVNNKKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQL 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 126 PALCSDGFTLVICPLISLMEDQLMVLKQLGISATMLNASSSKEHVKWVHAEMVNKNSQLKLIYVTPEKIAKSKMFMSRLE 205
Cdd:PLN03137 495 PALICPGITLVISPLVSLIQDQIMNLLQANIPAASLSAGMEWAEQLEILQELSSEYSKYKLLYVTPEKVAKSDSLLRHLE 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 206 KAYEAGRLTGAAVDEVHCCSQWGHDFRPDYKALGILKRQFPNASLMGLTATATNHVLKDVQKILCVGKCLTFTASFNRPN 285
Cdd:PLN03137 575 NLNSRGLLARFVIDEAHCVSQWGHDFRPDYQGLGILKQKFPNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRPN 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 286 LFYEVRQKPSSAedfTEDIVKLINGRYKGQSGIIYCFSQKDSEQITISLQKLGIHAGTYHANMEPEDKTKVHTQWSANEL 365
Cdd:PLN03137 655 LWYSVVPKTKKC---LEDIDKFIKENHFDECGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEI 731
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 366 QVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESGRAGRDDSRADCILYYGFGDIFRISSMVVMENVGQ-------- 437
Cdd:PLN03137 732 NIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGRAGRDGQRSSCVLYYSYSDYIRVKHMISQGGVEQspmamgyn 811
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 438 -------------QKLYEMVSYCQNVSKCRRVLIAQHFDEVWNADACNKMCDNCCKDVSFEKKNVTQHCRDLIKILKQAe 504
Cdd:PLN03137 812 rmassgriletntENLLRMVSYCENEVDCRRFLQLVHFGEKFDSTNCKKTCDNCSSSKSLIDKDVTEIARQLVELVKLT- 890
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 505 glNEKLTPLKLIDAWMGK----------------GAAKlrvagvvapALPREDLERIVAHALLQQYLKEDYSFT-AYATI 567
Cdd:PLN03137 891 --GERFSSAHILEVYRGSlnqyvkkhrhetlslhGAGK---------HLSKGEASRILHYLVTEDILAEDVKKSdLYGSV 959
|
570 580 590
....*....|....*....|....*....|..
gi 326368214 568 -SYLKVG-PRACLLSNEAHAVTMQVKKSAQSS 597
Cdd:PLN03137 960 sSLLKVNeSKAYKLFSGGQTIIMRFPSSVKAS 991
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
74-282 |
3.60e-150 |
|
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: 432.17 E-value: 3.60e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 74 PWFGKVKDVLQNVFKLQKFRPLQLETINVTMARKDIFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQ 153
Cdd:cd18015 1 PWSGKVKDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 154 LGISATMLNASSSKEHVKWVHAEMVNKNSQLKLIYVTPEKIAKSKMFMSRLEKAYEAGRLTGAAVDEVHCCSQWGHDFRP 233
Cdd:cd18015 81 LGISATMLNASSSKEHVKWVHAALTDKNSELKLLYVTPEKIAKSKRFMSKLEKAYNAGRLARIAIDEVHCCSQWGHDFRP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 326368214 234 DYKALGILKRQFPNASLMGLTATATNHVLKDVQKILCVGKCLTFTASFN 282
Cdd:cd18015 161 DYKKLGILKRQFPNVPILGLTATATSKVLKDVQKILCIQKCLTFTASFN 209
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
80-478 |
4.81e-125 |
|
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: 382.11 E-value: 4.81e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 80 KDVLQNVFKLQKFRPLQLETINVTMARKDIFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGISAT 159
Cdd:TIGR01389 2 QQVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 160 MLNASSSKEHVKwvHAEMVNKNSQLKLIYVTPEKIaKSKMFMSRLEkayeagRLTGA--AVDEVHCCSQWGHDFRPDYKA 237
Cdd:TIGR01389 82 YLNSTLSAKEQQ--DIEKALVNGELKLLYVAPERL-EQDYFLNMLQ------RIPIAlvAVDEAHCVSQWGHDFRPEYQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 238 LGILKRQFPNASLMGLTATATNHVLKDVQKILCVGKCLTFTASFNRPNLFYEVRQKPSSAEDFTEDIVKlingrYKGQSG 317
Cdd:TIGR01389 153 LGSLAERFPQVPRIALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKNNKQKFLLDYLKK-----HRGQSG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 318 IIYCFSQKDSEQITISLQKLGIHAGTYHANMEPEDKTKVHTQWSANELQVVVATVAFGMGIDKPDVRFVIHHSMSKSMEN 397
Cdd:TIGR01389 228 IIYASSRKKVEELAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLES 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 398 YYQESGRAGRDDSRADCILYYGFGDI----FRISSMVVMENVGQ---QKLYEMVSYCQNVsKCRRVLIAQHFDEVWNADA 470
Cdd:TIGR01389 308 YYQEAGRAGRDGLPAEAILLYSPADIallkRRIEQSEADDDYKQierEKLRAMIAYCETQ-TCRRAYILRYFGENEVEPC 386
|
....*...
gi 326368214 471 CNkmCDNC 478
Cdd:TIGR01389 387 GN--CDNC 392
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
80-481 |
1.37e-116 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 360.57 E-value: 1.37e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 80 KDVLQNVFKLQKFRPLQLETINVTMARKDIFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGISAT 159
Cdd:PRK11057 14 KQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVAAA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 160 MLNASSSKEHVKWVHAEMvnKNSQLKLIYVTPEKIAKSKmFMSRLEKAyeagRLTGAAVDEVHCCSQWGHDFRPDYKALG 239
Cdd:PRK11057 94 CLNSTQTREQQLEVMAGC--RTGQIKLLYIAPERLMMDN-FLEHLAHW----NPALLAVDEAHCISQWGHDFRPEYAALG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 240 ILKRQFPNASLMGLTATATNHVLKDVQKILCVGKCLTFTASFNRPNLFYEV--RQKPssaedfTEDIVKLINGRyKGQSG 317
Cdd:PRK11057 167 QLRQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLveKFKP------LDQLMRYVQEQ-RGKSG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 318 IIYCFSQKDSEQITISLQKLGIHAGTYHANMEPEDKTKVHTQWSANELQVVVATVAFGMGIDKPDVRFVIHHSMSKSMEN 397
Cdd:PRK11057 240 IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIES 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 398 YYQESGRAGRDDSRADCILYYGFGDIFRISSMVVMENVGQQ------KLYEMVSYCQnVSKCRRVLIAQHFDEvwnadAC 471
Cdd:PRK11057 320 YYQETGRAGRDGLPAEAMLFYDPADMAWLRRCLEEKPAGQQqdierhKLNAMGAFAE-AQTCRRLVLLNYFGE-----GR 393
|
410
....*....|..
gi 326368214 472 NKMCDNC--CKD 481
Cdd:PRK11057 394 QEPCGNCdiCLD 405
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
80-282 |
2.11e-94 |
|
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: 288.66 E-value: 2.11e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 80 KDVLQNVFKLQKFRPLQLETINVTMARKDIFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGISAT 159
Cdd:cd17920 1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 160 MLNASSSKEHVKWVHAEMvnKNSQLKLIYVTPEKIAkSKMFMSRLEKAYEAGRLTGAAVDEVHCCSQWGHDFRPDYKALG 239
Cdd:cd17920 81 ALNSTLSPEEKREVLLRI--KNGQYKLLYVTPERLL-SPDFLELLQRLPERKRLALIVVDEAHCVSQWGHDFRPDYLRLG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 326368214 240 ILKRQFPNASLMGLTATATNHVLKDVQKILCVGKCLTFTASFN 282
Cdd:cd17920 158 RLRRALPGVPILALTATATPEVREDILKRLGLRNPVIFRASFD 200
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
283-418 |
9.04e-72 |
|
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: 227.48 E-value: 9.04e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 283 RPNLFYEVRQKPSSAEDFteDIVKLINGRYKGQSGIIYCFSQKDSEQITISLQKLGIHAGTYHANMEPEDKTKVHTQWSA 362
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKL--DLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLR 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 326368214 363 NELQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESGRAGRDDSRADCILYY 418
Cdd:cd18794 79 DKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
81-282 |
1.06e-70 |
|
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: 227.40 E-value: 1.06e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 81 DVLQNVFKLQKFRPLQLETINVTMARKDIFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGISATM 160
Cdd:cd18016 7 KIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPATY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 161 LNASSSKEHVKWVHAEMVNKNSQLKLIYVTPEKIAKSKMFMSRLEKAYEAGRLTGAAVDEVHCCSQWGHDFRPDYKALGI 240
Cdd:cd18016 87 LTGDKTDAEATKIYLQLSKKDPIIKLLYVTPEKISASNRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRPDYKRLNM 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 326368214 241 LKRQFPNASLMGLTATATNHVLKDVQKILCVGKCLTFTASFN 282
Cdd:cd18016 167 LRQKFPSVPMMALTATATPRVQKDILNQLKMLRPQVFTMSFN 208
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
81-282 |
9.35e-54 |
|
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: 182.28 E-value: 9.35e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 81 DVLQNVFKLQKFRPLQLETI-NVTMARKDIFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGISAT 159
Cdd:cd18017 2 NALNEYFGHSSFRPVQWKVIrSVLEERRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPAC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 160 MLNASSSKEHVKwvhaemVNKNSQLKLIYVTPEKIAKSKMFMSRLEKayeagRLTGAAVDEVHCCSQWGHDFRPDYKALG 239
Cdd:cd18017 82 FLGSAQSQNVLD------DIKMGKIRVIYVTPEFVSKGLELLQQLRN-----GITLIAIDEAHCVSQWGHDFRSSYRHLG 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 326368214 240 ILKRQFPNASLMGLTATATNHVLKDVQKILCVGKCLTFTASFN 282
Cdd:cd18017 151 SIRNRLPNVPIVALTATATPSVRDDIIKNLNLRNPQITCTSFD 193
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
82-269 |
3.19e-52 |
|
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: 178.22 E-value: 3.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 82 VLQNVFKLQKFRPLQLETINVTMARKDIFLVMPTGGGKSLCYQLPALC----SDGFTLVICPLISLMEDQLMVLKQLgIS 157
Cdd:cd18018 3 LLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLlrrrGPGLTLVVSPLIALMKDQVDALPRA-IK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 158 ATMLNaSSSKEHVKWVHAEMVNKNsQLKLIYVTPEKIAkSKMFMSRLEkayEAGRLTGAAVDEVHCCSQWGHDFRPDYKA 237
Cdd:cd18018 82 AAALN-SSLTREERRRILEKLRAG-EVKILYVSPERLV-NESFRELLR---QTPPISLLVVDEAHCISEWSHNFRPDYLR 155
|
170 180 190
....*....|....*....|....*....|...
gi 326368214 238 LGILKRQFPNA-SLMGLTATATNHVLKDVQKIL 269
Cdd:cd18018 156 LCRVLRELLGApPVLALTATATKRVVEDIASHL 188
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
80-280 |
1.29e-48 |
|
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: 168.80 E-value: 1.29e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 80 KDVLQNVFKLQKFR-PLQLETIN-VTMARKDIFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGIS 157
Cdd:cd18014 1 RSTLKKVFGHSDFKsPLQEKATMaVVKGNKDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 158 ATMLNASSSKEHVKWVHAEMVNKNSQLKLIYVTPEKiAKSKMFMSRLEKAYEAGRLTGAAVDEVHCCSQWGHDFRPDYKA 237
Cdd:cd18014 81 VDSLNSKLSAQERKRIIADLESEKPQTKFLYITPEM-AATSSFQPLLSSLVSRNLLSYLVVDEAHCVSQWGHDFRPDYLR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 326368214 238 LGILKRQFPNASLMGLTATATNHVLKDVQKILCVGK-CLTFTAS 280
Cdd:cd18014 160 LGALRSRYGHVPWVALTATATPQVQEDIFAQLRLKKpVAIFKTP 203
|
|
| DpdF |
NF041063 |
protein DpdF; |
114-423 |
1.61e-42 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 164.31 E-value: 1.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 114 PTGGGKSLCYQLPALCS---DGFTLVICPLISL---MEDQLM-VLKQLGISATMLNA---SSSKEhvkwVHAEMVN--KN 181
Cdd:NF041063 166 PTGSGKSLVAQAPALLAsrqGGLTLVVVPTVALaidQERRAReLLRRAGPDLGGPLAwhgGLSAE----ERAAIRQriRD 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 182 SQLKLIYVTPEKIAKSkmFMSRLEKAYEAGRLTGAAVDEVHCCSQWGHDFRPDYKALGILKRQFPNASLMG-------LT 254
Cdd:NF041063 242 GTQRILFTSPESLTGS--LRPALFDAAEAGLLRYLVVDEAHLVDQWGDGFRPEFQLLAGLRRSLLRLAPSGrpfrtllLS 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 255 ATATNHVLKDVQKILCV-GKCLTFTASFNRPNLFYEVRQKPSsAEDFTEDIVKLIngRYKGQSGIIYCFSQKDSEQITIS 333
Cdd:NF041063 320 ATLTESTLDTLETLFGPpGPFIVVSAVQLRPEPAYWVAKCDS-EEERRERVLEAL--RHLPRPLILYVTKVEDAEAWLQR 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 334 LQKLGIH-AGTYHANMEPEDKTKVHTQWSANELQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESGRAGRDDSRA 412
Cdd:NF041063 397 LRAAGFRrVALFHGDTPDAERERLIEQWRENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKAS 476
|
330
....*....|.
gi 326368214 413 DCILYYGFGDI 423
Cdd:NF041063 477 LSLLIYTPDDL 487
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
107-256 |
2.58e-27 |
|
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: 107.49 E-value: 2.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 107 KDIFLVMPTGGGKSLCYQLPALCSD----GFTLVICPLISLMEDQLMVLKQL---GISATMLNASSSKEHVKwvhaemVN 179
Cdd:cd00046 2 ENVLITAPTGSGKTLAALLAALLLLlkkgKKVLVLVPTKALALQTAERLRELfgpGIRVAVLVGGSSAEERE------KN 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 326368214 180 KNSQLKLIYVTPEKIAKSKMFMSRLEKAyeagRLTGAAVDEVHCCSQWGHDFRPDYkaLGILKRQFPNASLMGLTAT 256
Cdd:cd00046 76 KLGDADIIIATPDMLLNLLLREDRLFLK----DLKLIIVDEAHALLIDSRGALILD--LAVRKAGLKNAQVILLSAT 146
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
93-268 |
4.18e-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: 105.02 E-value: 4.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 93 RPLQLETINVTMARKDIFLVMPTGGGKSLCYQLPAL------CSDGFTLVICPLISLMEDQLMVLKQLGISATMLNASSS 166
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 167 KEHVKWvhaEMVNKNSQLKLIYVTPEKIAKskmfMSRLEKAYEAGRLTgaAVDEVHCCSQWGhdFRPDYKAlgILKRQFP 246
Cdd:pfam00270 81 GGDSRK---EQLEKLKGPDILVGTPGRLLD----LLQERKLLKNLKLL--VLDEAHRLLDMG--FGPDLEE--ILRRLPK 147
|
170 180
....*....|....*....|..
gi 326368214 247 NASLMGLTATATnhvlKDVQKI 268
Cdd:pfam00270 148 KRQILLLSATLP----RNLEDL 165
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
328-408 |
4.87e-22 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 90.35 E-value: 4.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 328 EQITISLQKLGIHAGTYHANMEPEDKTKVHTQWSANELQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESGRAGR 407
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
.
gi 326368214 408 D 408
Cdd:smart00490 81 A 81
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
87-291 |
3.79e-21 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 91.78 E-value: 3.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 87 FKLQKFRPLQLETINVTMAR-KDIFLVMPTGGGKSLCYQLPALC-----SDGFTLVICPLISLMEDQLMVLKQLGISATM 160
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEalkrgKGGRVLVLVPTRELAEQWAEELKKLGPSLGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 161 LNASSSKEHVKWVHAEMVNKNsQLKLIYVTPEKIAksKMFMSRLEKAYEAGRLtgaAVDEVHCCSQWGhdFRPDYKalGI 240
Cdd:smart00487 84 KVVGLYGGDSKREQLRKLESG-KTDILVTTPGRLL--DLLENDKLSLSNVDLV---ILDEAHRLLDGG--FGDQLE--KL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 326368214 241 LKRQFPNASLMGLTATATNHVLKDVQKILcvgKCLTFTASFNRPNLFYEVR 291
Cdd:smart00487 154 LKLLPKNVQLLLLSATPPEEIENLLELFL---NDPVFIDVGFTPLEPIEQF 201
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
302-407 |
3.16e-20 |
|
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: 86.11 E-value: 3.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 302 EDIVKLINGRYKGQSgIIYCFSQKDSEqITISLQKLGIHAGTYHANMEPEDKTKVHTQWSANELQVVVATVAFGMGIDKP 381
Cdd:pfam00271 4 EALLELLKKERGGKV-LIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLP 81
|
90 100
....*....|....*....|....*.
gi 326368214 382 DVRFVIHHSMSKSMENYYQESGRAGR 407
Cdd:pfam00271 82 DVDLVINYDLPWNPASYIQRIGRAGR 107
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
420-479 |
9.30e-17 |
|
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ.
Pssm-ID: 465031 [Multi-domain] Cd Length: 66 Bit Score: 74.63 E-value: 9.30e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 326368214 420 FGDIFRISSMVVMEN-------VGQQKLYEMVSYCQNVSKCRRVLIAQHFDEVWNADACnKMCDNCC 479
Cdd:pfam16124 1 YQDVVRLRFLIEQSEadeerkeVELQKLQAMVAYCENTTDCRRKQLLRYFGEEFDSEPC-GNCDNCL 66
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
362-418 |
1.02e-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: 60.80 E-value: 1.02e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 326368214 362 ANELQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESGRAGRDDSR-ADCILYY 418
Cdd:cd18785 20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDeGEVILFV 77
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
296-407 |
2.40e-11 |
|
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: 61.37 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 296 SAEDFTEDIVKLINGRYKGQSGIIYCFSQKDSEQITISLQKLGIHAGTYHANMEPEDKTKVHTQWSANELQVVVAT-VAf 374
Cdd:cd18787 9 EEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVATdVA- 87
|
90 100 110
....*....|....*....|....*....|...
gi 326368214 375 GMGIDKPDVRFVIHHSMSKSMENYYQESGRAGR 407
Cdd:cd18787 88 ARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGR 120
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
111-407 |
3.00e-11 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 66.20 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 111 LVMPTGGGKSL----CYQlpALCSDGFTLVICPLISLMEdQLM--VLKQLGISATMLNASSSKEHVkwvhaemvnknsql 184
Cdd:COG1061 105 VVAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRRELLE-QWAeeLRRFLGDPLAGGGKKDSDAPI-------------- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 185 klIYVTPEKIAKSKMFmSRLEKAYeagrlTGAAVDEVHccsqwgHDFRPDYKAlgILKRqFPNASLMGLTATATNHVLKD 264
Cdd:COG1061 168 --TVATYQSLARRAHL-DELGDRF-----GLVIIDEAH------HAGAPSYRR--ILEA-FPAAYRLGLTATPFRSDGRE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 265 VQKILCVGKCLTFTAS-------------FNRPNLFYEVRQKPSSAEDFTEDIV------------KLINGRYKGQSGII 319
Cdd:COG1061 231 ILLFLFDGIVYEYSLKeaiedgylappeyYGIRVDLTDERAEYDALSERLREALaadaerkdkilrELLREHPDDRKTLV 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 320 YCFSQKDSEQITISLQKLGIHAGTYHANMEPEDKTKVHTQWSANELQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYY 399
Cdd:COG1061 311 FCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFI 390
|
....*...
gi 326368214 400 QesgRAGR 407
Cdd:COG1061 391 Q---RLGR 395
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
287-407 |
2.73e-09 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 59.78 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 287 FYEVRQKpssaeDFTEDIVKLINgRYKGQSGIIYCFSQKDSEQITISLQKLGIHAGTYHANMEPEDKTKVHTQWSANELQ 366
Cdd:COG0513 220 YYLVDKR-----DKLELLRRLLR-DEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIR 293
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 326368214 367 VVVAT-VAfGMGIDKPDVRFVIHHSMSKSMENYYQESGRAGR 407
Cdd:COG0513 294 VLVATdVA-ARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGR 334
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
312-409 |
4.66e-09 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 59.52 E-value: 4.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 312 YKGQSgIIYCFSQKDSEQITislQKLGIHAGTYHANMEPEDKTKVHTQWSANELQVVVATVAFGMGIDKPDVRfVIHHS- 390
Cdd:COG1202 426 YRGQT-IIFTNSRRRCHEIA---RALGYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQ-VIFDSl 500
|
90 100
....*....|....*....|...
gi 326368214 391 -MSK---SMENYYQESGRAGRDD 409
Cdd:COG1202 501 aMGIewlSVQEFHQMLGRAGRPD 523
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
304-417 |
6.87e-09 |
|
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: 55.25 E-value: 6.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 304 IVKLINGRYKGQSgIIYCFSQKDSEQITISLQKLGIHagtyHANMEPEDKTKVHTQWSANELQVVVATVAFGMGIDKPdV 383
Cdd:cd18795 34 LLKIETVSEGKPV-LVFCSSRKECEKTAKDLAGIAFH----HAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLP-A 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 326368214 384 RFVIHHSMSK---------SMENYYQESGRAGRD--DSRADCILY 417
Cdd:cd18795 108 RTVIIKGTQRydgkgyrelSPLEYLQMIGRAGRPgfDTRGEAIIM 152
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
318-412 |
1.88e-08 |
|
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: 53.80 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 318 IIYCFSQKDSEQITI----SLQKLGIHAGT---YHANMEPEDKTKVHTQWSANELQVVVATVAFGMGIDKPDVRFVIHHS 390
Cdd:cd18797 39 IVFCRSRKLAELLLRylkaRLVEEGPLASKvasYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
|
90 100
....*....|....*....|..
gi 326368214 391 MSKSMENYYQESGRAGRDDSRA 412
Cdd:cd18797 119 YPGSLASLWQQAGRAGRRGKDS 140
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
96-412 |
3.23e-07 |
|
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: 53.69 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 96 QLETINVTMARKDIFLVMPTGGGKSLCYQLPALCS-----DGFTLVICPLISLMEDQLMVLKQL------GISATMLNAS 164
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEAlledpGATALYLYPTKALARDQLRRLRELaealglGVRVATYDGD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 165 SSKEHVKWVHaemvnKNSQlkLIYVTPEKI--------AKSKMFMSRLEkaYeagrltgAAVDEVHCcsqwghdfrpdYK 236
Cdd:COG1205 141 TPPEERRWIR-----EHPD--IVLTNPDMLhygllphhTRWARFFRNLR--Y-------VVIDEAHT-----------YR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 237 -ALG-----ILKR------------QFpnaslMGLTATATN---HVLK----DVQkilCVGKC------LTFtaSFNRPN 285
Cdd:COG1205 194 gVFGshvanVLRRlrricrhygsdpQF-----ILASATIGNpaeHAERltgrPVT---VVDEDgsprgeRTF--VLWNPP 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 286 LFYEVRQKPSSAE--DFTEDIVKlingryKGQSGIIYCFSQKDSEQITISLQK------LGIHAGTYHANMEPEDKTKVH 357
Cdd:COG1205 264 LVDDGIRRSALAEaaRLLADLVR------EGLRTLVFTRSRRGAELLARYARRalrepdLADRVAAYRAGYLPEERREIE 337
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 326368214 358 TQWSANELQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESGRAGRDDSRA 412
Cdd:COG1205 338 RGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDS 392
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
318-407 |
2.36e-06 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 50.21 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 318 IIYCFSQKDSEQITISLQKLGIHAGTYHANMEPEDKTKVHTQWSANELQVVVATVAFGMGIDKPDVRFVIHHSMSKSMEN 397
Cdd:PTZ00424 271 IIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPEN 350
|
90
....*....|
gi 326368214 398 YYQESGRAGR 407
Cdd:PTZ00424 351 YIHRIGRSGR 360
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
96-173 |
1.20e-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: 46.04 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 96 QLETINVTMARKDIFLVMPTGGGKSLCYQLP---ALCSDGFT--LVICPLISLMEDQLMVLKQL------GISATMLNAS 164
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPileALLRDPGSraLYLYPTKALAQDQLRSLRELleqlglGIRVATYDGD 84
|
....*....
gi 326368214 165 SSKEHVKWV 173
Cdd:cd17923 85 TPREERRAI 93
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
484-576 |
2.05e-05 |
|
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: 43.68 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 484 FEKKNVTQHCRDLIKILKQaegLNEKLTPLKLIDAWMGKGAAKLR--------VAGVVAPaLPREDLERIVAHALLQQYL 555
Cdd:pfam09382 2 PETVDVTEEAQKILSCVYR---TGQRFGAGHLIDVLRGSKNKKIRqlghdklsTFGIGKD-LSKKEWRRIIRQLIAEGYL 77
|
90 100
....*....|....*....|.
gi 326368214 556 KEDYSFTayatiSYLKVGPRA 576
Cdd:pfam09382 78 EVDIEFY-----SVLKLTPKA 93
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
263-407 |
2.97e-05 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 47.08 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 263 KDVQKI---LC--------VGKcLTFTASFN-RPNLF-YEVRQKPSSAEDFTEDIVKlingryKGQSGIIYCFSQKDSEQ 329
Cdd:PTZ00110 320 KEVQSLardLCkeepvhvnVGS-LDLTACHNiKQEVFvVEEHEKRGKLKMLLQRIMR------DGDKILIFVETKKGADF 392
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 326368214 330 ITISLQKLGIHAGTYHANMEPEDKTKVHTQWSANELQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESGRAGR 407
Cdd:PTZ00110 393 LTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGR 470
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
345-445 |
3.96e-05 |
|
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: 44.26 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 345 HANMEPEDKTKVHTQWSANELQVVVATVAFGMGIDKPDVR-FVIHHSMSKSMENYYQESGRAGRDDSRADCILYYGfgdi 423
Cdd:cd18811 68 HGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATvMVIEDAERFGLSQLHQLRGRVGRGDHQSYCLLVYK---- 143
|
90 100
....*....|....*....|..
gi 326368214 424 frissmVVMENVGQQKLYEMVS 445
Cdd:cd18811 144 ------DPLTETAKQRLRVMTE 159
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
91-256 |
9.22e-05 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 43.43 E-value: 9.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 91 KFRPLQLETINVTMA-----RKDIFLVMPTGGGKSLCY-QLPALCSDGF----TLVICPLISLMEDQLMVLKQLGISATM 160
Cdd:pfam04851 3 ELRPYQIEAIENLLEsikngQKRGLIVMATGSGKTLTAaKLIARLFKKGpikkVLFLVPRKDLLEQALEEFKKFLPNYVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 161 LNASSSKEhvkwvhaEMVNKNSQLKLIYVTPEKIAKSKMFMSRLEKAYEAGRLTgaaVDEVHccsqwgHDFRPDYKAlgi 240
Cdd:pfam04851 83 IGEIISGD-------KKDESVDDNKIVVTTIQSLYKALELASLELLPDFFDVII---IDEAH------RSGASSYRN--- 143
|
170
....*....|....*.
gi 326368214 241 LKRQFPNASLMGLTAT 256
Cdd:pfam04851 144 ILEYFKPAFLLGLTAT 159
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
345-419 |
7.07e-04 |
|
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: 40.71 E-value: 7.07e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 326368214 345 HANMEPEDKTKVHTQWSANELQVVVATVAFGMGIDKPDVR-FVIHHSMSKSMENYYQESGRAGRDDSRADCILYYG 419
Cdd:cd18792 67 HGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANtMIIEDADRFGLSQLHQLRGRVGRGKHQSYCYLLYP 142
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
338-407 |
1.37e-03 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 41.85 E-value: 1.37e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 326368214 338 GIhaGTYHANMEPEDKTKVHTQWSANELQVVVATVAFGMGIDKPdVRFVIHHSMSK----SMEN-----YYQESGRAGR 407
Cdd:COG4581 301 GI--AVHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMP-ARTVVFTKLSKfdgeRHRPltareFHQIAGRAGR 376
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
92-256 |
2.43e-03 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 38.83 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 92 FRPLQLETINVTMA----RKDIFlVMPTGGGKSLC-YQLPALCSDGFTLVICPLISLMEDQLMVLKQLGISAtMLNASSS 166
Cdd:cd17926 1 LRPYQEEALEAWLAhknnRRGIL-VLPTGSGKTLTaLALIAYLKELRTLIVVPTDALLDQWKERFEDFLGDS-SIGLIGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 167 KEHVKWVHAEMVNKNSQ-LKLIYVTPEKIAKSKMFMsrlekayeagrltgaAVDEVH--CCSQWGHdfrpdykalgILKR 243
Cdd:cd17926 79 GKKKDFDDANVVVATYQsLSNLAEEEKDLFDQFGLL---------------IVDEAHhlPAKTFSE----------ILKE 133
|
170
....*....|...
gi 326368214 244 qFPNASLMGLTAT 256
Cdd:cd17926 134 -LNAKYRLGLTAT 145
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
94-417 |
3.66e-03 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 40.16 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 94 PLQLETINVTMARKDIFLVMPTGGGKSLCYQLP--ALCS-----------DGFTLVICP---LISLMEDQLMVL-KQLGI 156
Cdd:PLN00206 146 PIQMQAIPAALSGRSLLVSADTGSGKTASFLVPiiSRCCtirsghpseqrNPLAMVLTPtreLCVQVEDQAKVLgKGLPF 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 157 SATMLNASSskehvkwVHAEMVNKNSQ-LKLIYVTPEKIAKskmFMSRLEkaYEAGRLTGAAVDEVHCCSQWGhdFRPdy 235
Cdd:PLN00206 226 KTALVVGGD-------AMPQQLYRIQQgVELIVGTPGRLID---LLSKHD--IELDNVSVLVLDEVDCMLERG--FRD-- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 236 KALGILkRQFPNASLMGLTATATNHV-------LKDVQkILCVGKCltftasfNRPN-------LFYEVRQKPS------ 295
Cdd:PLN00206 290 QVMQIF-QALSQPQVLLFSATVSPEVekfasslAKDII-LISIGNP-------NRPNkavkqlaIWVETKQKKQklfdil 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326368214 296 -SAEDFTEDIVKLINGRYKgqsgiiycfSQKDSEQITISLqklGIHAGTYHANMEPEDKTKVHTQWSANELQVVVATVAF 374
Cdd:PLN00206 361 kSKQHFKPPAVVFVSSRLG---------ADLLANAITVVT---GLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVL 428
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 326368214 375 GMGIDKPDVRFVIHHSMSKSMENYYQESGRAGRDDSRADCILY 417
Cdd:PLN00206 429 GRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVF 471
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
79-139 |
5.45e-03 |
|
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1. DDX31 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: 350707 [Multi-domain] Cd Length: 214 Bit Score: 38.72 E-value: 5.45e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 326368214 79 VKDVLQNVFKLQKFRPLQLETINVTMARKDIFLVMPTGGGKSLCYQLPALC-----------SDG-FTLVICP 139
Cdd:cd17949 1 LVSHLKSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQrllsleprvdrSDGtLALVLVP 73
|
|
| |
