|
Name |
Accession |
Description |
Interval |
E-value |
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
82-543 |
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: 704.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 82 VLRDVFKLQKFRPLQLETVNATMARKDIFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLQQLGISATML 161
Cdd:TIGR00614 2 ILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 162 NSSSSKEHVKCVHTEMmnKNSHLKLIYVTPEKIAKSKMFMSRLEKAYeagRLTGVAVDEVHCCSQWGHDFRPDYKALGIL 241
Cdd:TIGR00614 82 NSAQTKEQQLNVLTDL--KDGKIKLLYVTPEKISASNRLLQTLEERK---GITLIAVDEAHCISQWGHDFRPDYKALGSL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 242 KRQFPNISLIGLTATATNHVLKDAQKILCVEKCLTFTASFNRPNLYYEVRQKPSsaeDFIENIANLINGRYKGKSGIIYC 321
Cdd:TIGR00614 157 KQKFPNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRRKTP---KILEDLLRFIRKEFEGKSGIIYC 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 322 FSQKDSEQVTISLQKLGVRAGTYHANMEPEDRTKVHTQWSANELQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQE 401
Cdd:TIGR00614 234 PSRKKVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 402 SGRAGRDDWRADCILYYGFGDIFRISSMVVMENVGQQ-----KLYEMVSYCQNISKCRRALIAQHFDEVWNAD-----AC 471
Cdd:TIGR00614 314 SGRAGRDGLPSECHLFYAPADMNRLRRLLMEEPDGNFrtyklKLYEMMEYCLNSSTCRRLILLSYFGEKGFNKsfcimGT 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958769850 472 NKMCDNCCKDDSFEKKNITEHCQALIKILKQAEG----LNEKLTPLKLIDAWMGKGAAKFRVAGVAVPAL-PREDLE 543
Cdd:TIGR00614 394 EKCCDNCCKRLDYKTKDVTDKVYDFGPQAQKALSavgrLNQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLyGRGKDE 470
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
78-528 |
2.65e-176 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 508.91 E-value: 2.65e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 78 KVKHVLRDVFKLQKFRPLQLETVNATMARKDIFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLQQLGIS 157
Cdd:COG0514 4 DALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 158 ATMLNSSSSKEHVKCVHTEMMNKnsHLKLIYVTPEKIAKSKmFMSRLEKAyeagRLTGVAVDEVHCCSQWGHDFRPDYKA 237
Cdd:COG0514 84 AAFLNSSLSAEERREVLRALRAG--ELKLLYVAPERLLNPR-FLELLRRL----KISLFAIDEAHCISQWGHDFRPDYRR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 238 LGILKRQFPNISLIGLTATATNHVLKDAQKILCVEKCLTFTASFNRPNLYYEVRQKPssAEDFIENIANLINGRyKGKSG 317
Cdd:COG0514 157 LGELRERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKP--PDDKLAQLLDFLKEH-PGGSG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 318 IIYCFSQKDSEQVTISLQKLGVRAGTYHANMEPEDRTKVHTQWSANELQVVVATVAFGMGIDKPDVRFVIHHSMSKSMEN 397
Cdd:COG0514 234 IVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 398 YYQESGRAGRDDWRADCILYYGFGDIFRISSMVVMEN-------VGQQKLYEMVSYCQnISKCRRALIAQHFDEVwNADA 470
Cdd:COG0514 314 YYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIEQSPpdeerkrVERAKLDAMLAYAE-TTGCRRQFLLRYFGEE-LAEP 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958769850 471 CNKmCDNCckDDSFEKKNITEHCQaliKILKQAEGLNEKLTPLKLIDAWMGKGAAKFR 528
Cdd:COG0514 392 CGN-CDNC--LGPPETFDGTEAAQ---KALSCVYRTGQRFGAGHVIDVLRGSKNEKIR 443
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
68-610 |
6.04e-151 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 465.91 E-value: 6.04e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 68 WSKEDFPWSGKVKHVLRDVFKLQKFRPLQLETVNATMARKDIFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQ 147
Cdd:PLN03137 437 WSSRNFPWTKKLEVNNKKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQ 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 148 LMVLQQLGISATMLNSSSSKEHVKCVHTEMMNKNSHLKLIYVTPEKIAKSKMFMSRLEKAYEAGRLTGVAVDEVHCCSQW 227
Cdd:PLN03137 517 IMNLLQANIPAASLSAGMEWAEQLEILQELSSEYSKYKLLYVTPEKVAKSDSLLRHLENLNSRGLLARFVIDEAHCVSQW 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 228 GHDFRPDYKALGILKRQFPNISLIGLTATATNHVLKDAQKILCVEKCLTFTASFNRPNLYYEVRQKPSSAedfIENIANL 307
Cdd:PLN03137 597 GHDFRPDYQGLGILKQKFPNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVPKTKKC---LEDIDKF 673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 308 INGRYKGKSGIIYCFSQKDSEQVTISLQKLGVRAGTYHANMEPEDRTKVHTQWSANELQVVVATVAFGMGIDKPDVRFVI 387
Cdd:PLN03137 674 IKENHFDECGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVI 753
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 388 HHSMSKSMENYYQESGRAGRDDWRADCILYYGFGDIFRISSMVVMENVGQ---------------------QKLYEMVSY 446
Cdd:PLN03137 754 HHSLPKSIEGYHQECGRAGRDGQRSSCVLYYSYSDYIRVKHMISQGGVEQspmamgynrmassgriletntENLLRMVSY 833
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 447 CQNISKCRRALIAQHFDEVWNADACNKMCDNCCKDDSFEKKNITEHCQALIKILKQAeglNEKLTPLKLIDAWMG---KG 523
Cdd:PLN03137 834 CENEVDCRRFLQLVHFGEKFDSTNCKKTCDNCSSSKSLIDKDVTEIARQLVELVKLT---GERFSSAHILEVYRGslnQY 910
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 524 AAKFRVAGVAVPA----LPREDLEKIIVHALLQQYLKEDYSFT-AYATI-SYLKVG-PRASLLSNEGHAVTMQ----VKR 592
Cdd:PLN03137 911 VKKHRHETLSLHGagkhLSKGEASRILHYLVTEDILAEDVKKSdLYGSVsSLLKVNeSKAYKLFSGGQTIIMRfpssVKA 990
|
570 580 590
....*....|....*....|....*....|....*
gi 1958769850 593 S-----------------TQSSVRAASPEACEVDS 610
Cdd:PLN03137 991 SkpskfeatpakgpltsgKQSTLPMATPAQPPVDL 1025
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
74-282 |
1.62e-148 |
|
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: 427.55 E-value: 1.62e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 74 PWSGKVKHVLRDVFKLQKFRPLQLETVNATMARKDIFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLQQ 153
Cdd:cd18015 1 PWSGKVKDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 154 LGISATMLNSSSSKEHVKCVHTEMMNKNSHLKLIYVTPEKIAKSKMFMSRLEKAYEAGRLTGVAVDEVHCCSQWGHDFRP 233
Cdd:cd18015 81 LGISATMLNASSSKEHVKWVHAALTDKNSELKLLYVTPEKIAKSKRFMSKLEKAYNAGRLARIAIDEVHCCSQWGHDFRP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958769850 234 DYKALGILKRQFPNISLIGLTATATNHVLKDAQKILCVEKCLTFTASFN 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 |
1.88e-126 |
|
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: 385.19 E-value: 1.88e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 80 KHVLRDVFKLQKFRPLQLETVNATMARKDIFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLQQLGISAT 159
Cdd:TIGR01389 2 QQVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 160 MLNSSSSKEHVKcvHTEMMNKNSHLKLIYVTPEKIaKSKMFMSRLEKAyeagRLTGVAVDEVHCCSQWGHDFRPDYKALG 239
Cdd:TIGR01389 82 YLNSTLSAKEQQ--DIEKALVNGELKLLYVAPERL-EQDYFLNMLQRI----PIALVAVDEAHCVSQWGHDFRPEYQRLG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 240 ILKRQFPNISLIGLTATATNHVLKDAQKILCVEKCLTFTASFNRPNLYYEVRQKPSSAEDFIENIanlinGRYKGKSGII 319
Cdd:TIGR01389 155 SLAERFPQVPRIALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKNNKQKFLLDYL-----KKHRGQSGII 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 320 YCFSQKDSEQVTISLQKLGVRAGTYHANMEPEDRTKVHTQWSANELQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYY 399
Cdd:TIGR01389 230 YASSRKKVEELAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 400 QESGRAGRDDWRADCILYYGFGDI----FRISSMVVMENVGQ---QKLYEMVSYCqNISKCRRALIAQHFDEVWNADACN 472
Cdd:TIGR01389 310 QEAGRAGRDGLPAEAILLYSPADIallkRRIEQSEADDDYKQierEKLRAMIAYC-ETQTCRRAYILRYFGENEVEPCGN 388
|
....*.
gi 1958769850 473 kmCDNC 478
Cdd:TIGR01389 389 --CDNC 392
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
80-481 |
9.49e-119 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 365.58 E-value: 9.49e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 80 KHVLRDVFKLQKFRPLQLETVNATMARKDIFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLQQLGISAT 159
Cdd:PRK11057 14 KQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVAAA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 160 MLNSSSSKEHVKCVHTEMmnKNSHLKLIYVTPEKIAKSKmFMSRLEKAyeagRLTGVAVDEVHCCSQWGHDFRPDYKALG 239
Cdd:PRK11057 94 CLNSTQTREQQLEVMAGC--RTGQIKLLYIAPERLMMDN-FLEHLAHW----NPALLAVDEAHCISQWGHDFRPEYAALG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 240 ILKRQFPNISLIGLTATATNHVLKDAQKILCVEKCLTFTASFNRPNLYYEV--RQKPssaedfIENIANLINGRyKGKSG 317
Cdd:PRK11057 167 QLRQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLveKFKP------LDQLMRYVQEQ-RGKSG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 318 IIYCFSQKDSEQVTISLQKLGVRAGTYHANMEPEDRTKVHTQWSANELQVVVATVAFGMGIDKPDVRFVIHHSMSKSMEN 397
Cdd:PRK11057 240 IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIES 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 398 YYQESGRAGRDDWRADCILYYGFGDIFRISSMVVMENVGQQ------KLYEMVSYCQnISKCRRALIAQHFDEvwnadAC 471
Cdd:PRK11057 320 YYQETGRAGRDGLPAEAMLFYDPADMAWLRRCLEEKPAGQQqdierhKLNAMGAFAE-AQTCRRLVLLNYFGE-----GR 393
|
410
....*....|..
gi 1958769850 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 |
4.37e-96 |
|
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: 292.90 E-value: 4.37e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 80 KHVLRDVFKLQKFRPLQLETVNATMARKDIFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLQQLGISAT 159
Cdd:cd17920 1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 160 MLNSSSSKEHVKcvHTEMMNKNSHLKLIYVTPEKIAkSKMFMSRLEKAYEAGRLTGVAVDEVHCCSQWGHDFRPDYKALG 239
Cdd:cd17920 81 ALNSTLSPEEKR--EVLLRIKNGQYKLLYVTPERLL-SPDFLELLQRLPERKRLALIVVDEAHCVSQWGHDFRPDYLRLG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958769850 240 ILKRQFPNISLIGLTATATNHVLKDAQKILCVEKCLTFTASFN 282
Cdd:cd17920 158 RLRRALPGVPILALTATATPEVREDILKRLGLRNPVIFRASFD 200
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
76-282 |
1.52e-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: 226.63 E-value: 1.52e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 76 SGKVKHVLRDVFKLQKFRPLQLETVNATMARKDIFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLQQLG 155
Cdd:cd18016 2 SKEMMKIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 156 ISATMLNSSSSKEHVKCVHTEMMNKNSHLKLIYVTPEKIAKSKMFMSRLEKAYEAGRLTGVAVDEVHCCSQWGHDFRPDY 235
Cdd:cd18016 82 IPATYLTGDKTDAEATKIYLQLSKKDPIIKLLYVTPEKISASNRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRPDY 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1958769850 236 KALGILKRQFPNISLIGLTATATNHVLKDAQKILCVEKCLTFTASFN 282
Cdd:cd18016 162 KRLNMLRQKFPSVPMMALTATATPRVQKDILNQLKMLRPQVFTMSFN 208
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
283-418 |
2.05e-70 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350181 [Multi-domain] Cd Length: 134 Bit Score: 223.62 E-value: 2.05e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 283 RPNLYYEVRQKPSSAEDFIEniANLINGRYKGKSGIIYCFSQKDSEQVTISLQKLGVRAGTYHANMEPEDRTKVHTQWSA 362
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDL--LKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLR 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958769850 363 NELQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESGRAGRDDWRADCILYY 418
Cdd:cd18794 79 DKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
83-282 |
2.20e-53 |
|
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: 180.74 E-value: 2.20e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 83 LRDVFKLQKFRPLQLETV-NATMARKDIFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLQQLGISATML 161
Cdd:cd18017 4 LNEYFGHSSFRPVQWKVIrSVLEERRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPACFL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 162 NSSSSKEHVKcvhtemMNKNSHLKLIYVTPEKIAKSKMFMSRLEKayeagRLTGVAVDEVHCCSQWGHDFRPDYKALGIL 241
Cdd:cd18017 84 GSAQSQNVLD------DIKMGKIRVIYVTPEFVSKGLELLQQLRN-----GITLIAIDEAHCVSQWGHDFRSSYRHLGSI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958769850 242 KRQFPNISLIGLTATATNHVLKDAQKILCVEKCLTFTASFN 282
Cdd:cd18017 153 RNRLPNVPIVALTATATPSVRDDIIKNLNLRNPQITCTSFD 193
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
81-272 |
2.71e-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: 2.71e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 81 HVLRDVFKLQKFRPLQLETVNATMARKDIFLVMPTGGGKSLCYQLPALC----SDGFTLVICPLISLMEDQLMVLQQLgI 156
Cdd:cd18018 2 KLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLlrrrGPGLTLVVSPLIALMKDQVDALPRA-I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 157 SATMLNSSSSKEHVKcvHTEMMNKNSHLKLIYVTPEKIAkSKMFMSRLEkayEAGRLTGVAVDEVHCCSQWGHDFRPDYK 236
Cdd:cd18018 81 KAAALNSSLTREERR--RILEKLRAGEVKILYVSPERLV-NESFRELLR---QTPPISLLVVDEAHCISEWSHNFRPDYL 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 1958769850 237 ALGILKRQFPNI-SLIGLTATATNHVLKDAQKILCVE 272
Cdd:cd18018 155 RLCRVLRELLGApPVLALTATATKRVVEDIASHLGIP 191
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
80-280 |
3.15e-49 |
|
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: 170.34 E-value: 3.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 80 KHVLRDVFKLQKFR-PLQletVNATMA----RKDIFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLQQL 154
Cdd:cd18014 1 RSTLKKVFGHSDFKsPLQ---EKATMAvvkgNKDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 155 GISATMLNSSSSKEHVKCVHTEMMNKNSHLKLIYVTPEKiAKSKMFMSRLEKAYEAGRLTGVAVDEVHCCSQWGHDFRPD 234
Cdd:cd18014 78 KIRVDSLNSKLSAQERKRIIADLESEKPQTKFLYITPEM-AATSSFQPLLSSLVSRNLLSYLVVDEAHCVSQWGHDFRPD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1958769850 235 YKALGILKRQFPNISLIGLTATATNHVLKDAQKILCVEK-CLTFTAS 280
Cdd:cd18014 157 YLRLGALRSRYGHVPWVALTATATPQVQEDIFAQLRLKKpVAIFKTP 203
|
|
| DpdF |
NF041063 |
protein DpdF; |
114-423 |
6.78e-43 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 165.08 E-value: 6.78e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 114 PTGGGKSLCYQLPALCS---DGFTLVICPLISL---MEDQLM-VLQQLGISATML------NSSSSKEHVKcvhtemMN- 179
Cdd:NF041063 166 PTGSGKSLVAQAPALLAsrqGGLTLVVVPTVALaidQERRAReLLRRAGPDLGGPlawhggLSAEERAAIR------QRi 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 180 KNSHLKLIYVTPEKIAKSkmFMSRLEKAYEAGRLTGVAVDEVHCCSQWGHDFRPDYKALGILKRqfpniSLIG------- 252
Cdd:NF041063 240 RDGTQRILFTSPESLTGS--LRPALFDAAEAGLLRYLVVDEAHLVDQWGDGFRPEFQLLAGLRR-----SLLRlapsgrp 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 253 -----LTATATNHVLKDAQKILCV-EKCLTFTASFNRPNLYYEVRQKPSSAEDF---IENIANLingrykGKSGIIYCFS 323
Cdd:NF041063 313 frtllLSATLTESTLDTLETLFGPpGPFIVVSAVQLRPEPAYWVAKCDSEEERRervLEALRHL------PRPLILYVTK 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 324 QKDSEQVTISLQKLGV-RAGTYHANMEPEDRTKVHTQWSANELQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQES 402
Cdd:NF041063 387 VEDAEAWLQRLRAAGFrRVALFHGDTPDAERERLIEQWRENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEV 466
|
330 340
....*....|....*....|.
gi 1958769850 403 GRAGRDDWRADCILYYGFGDI 423
Cdd:NF041063 467 GRGGRDGKASLSLLIYTPDDL 487
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
107-256 |
2.17e-28 |
|
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: 110.57 E-value: 2.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 107 KDIFLVMPTGGGKSLCYQLPALCSD----GFTLVICPLISLMEDQLMVLQQL---GISATMLNSSSSKEHVKcvhtemMN 179
Cdd:cd00046 2 ENVLITAPTGSGKTLAALLAALLLLlkkgKKVLVLVPTKALALQTAERLRELfgpGIRVAVLVGGSSAEERE------KN 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958769850 180 KNSHLKLIYVTPEKIAKSKMFMSRLEKAyeagRLTGVAVDEVHCCSQWGHDFRPDYkaLGILKRQFPNISLIGLTAT 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. ... |
93-258 |
4.08e-27 |
|
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: 107.71 E-value: 4.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 93 RPLQLETVNATMARKDIFLVMPTGGGKSLCYQLPAL------CSDGFTLVICPLISLMEDQLMVLQQLGISATMLnssss 166
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKLGKGLGLK----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 167 kehVKCVHT-----EMMNKNSHLKLIYVTPEKIAKSKMFMSRLEkayeagRLTGVAVDEVHCCSQWGhdFRPDYKAlgIL 241
Cdd:pfam00270 76 ---VASLLGgdsrkEQLEKLKGPDILVGTPGRLLDLLQERKLLK------NLKLLVLDEAHRLLDMG--FGPDLEE--IL 142
|
170
....*....|....*..
gi 1958769850 242 KRQFPNISLIGLTATAT 258
Cdd:pfam00270 143 RRLPKKRQILLLSATLP 159
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
328-408 |
7.53e-23 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 92.66 E-value: 7.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 328 EQVTISLQKLGVRAGTYHANMEPEDRTKVHTQWSANELQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESGRAGR 407
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
.
gi 1958769850 408 D 408
Cdd:smart00490 81 A 81
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
87-291 |
1.16e-22 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 96.02 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 87 FKLQKFRPLQLETVNATMAR-KDIFLVMPTGGGKSLCYQLPALC-----SDGFTLVICPLISLMEDQLMVLQQLG----- 155
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEalkrgKGGRVLVLVPTRELAEQWAEELKKLGpslgl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 156 ISATMLNSSSSKEHVKcvhtEMMNKNSHlkLIYVTPEkiakskMFMSRLEKAY-EAGRLTGVAVDEVHCCSQWGhdFRPD 234
Cdd:smart00487 84 KVVGLYGGDSKREQLR----KLESGKTD--ILVTTPG------RLLDLLENDKlSLSNVDLVILDEAHRLLDGG--FGDQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958769850 235 YKalGILKRQFPNISLIGLTATATNHVLKDAQKILcveKCLTFTASFNRPNLYYEVR 291
Cdd:smart00487 150 LE--KLLKLLPKNVQLLLLSATPPEEIENLLELFL---NDPVFIDVGFTPLEPIEQF 201
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
301-407 |
1.01e-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: 87.65 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 301 IENIANLINGRYKGKSgIIYCFSQKDSEqVTISLQKLGVRAGTYHANMEPEDRTKVHTQWSANELQVVVATVAFGMGIDK 380
Cdd:pfam00271 3 LEALLELLKKERGGKV-LIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDL 80
|
90 100
....*....|....*....|....*..
gi 1958769850 381 PDVRFVIHHSMSKSMENYYQESGRAGR 407
Cdd:pfam00271 81 PDVDLVINYDLPWNPASYIQRIGRAGR 107
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
420-479 |
4.91e-16 |
|
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: 72.71 E-value: 4.91e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958769850 420 FGDIFRISSMVVMEN-------VGQQKLYEMVSYCQNISKCRRALIAQHFDEVWNADACnKMCDNCC 479
Cdd:pfam16124 1 YQDVVRLRFLIEQSEadeerkeVELQKLQAMVAYCENTTDCRRKQLLRYFGEEFDSEPC-GNCDNCL 66
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
93-407 |
2.80e-15 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 78.91 E-value: 2.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 93 RPLQLETVNATMA-----RKDIFLVMPTGGGKSL----CYQlpALCSDGFTLVICPLISLMEdQLM--VLQQLGISATML 161
Cdd:COG1061 82 RPYQQEALEALLAalergGGRGLVVAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRRELLE-QWAeeLRRFLGDPLAGG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 162 NSSSSKEHVkcvhtemmnknshlklIYVTPEKIAKSKMFmSRLEKAYeagrlTGVAVDEVHccsqwgHDFRPDYKAlgIL 241
Cdd:COG1061 159 GKKDSDAPI----------------TVATYQSLARRAHL-DELGDRF-----GLVIIDEAH------HAGAPSYRR--IL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 242 KRqFPNISLIGLTAT----ATNHV-------------LKDA--QKILCVEKCLTFTASFNRPNLYYEVRQKP------SS 296
Cdd:COG1061 209 EA-FPAAYRLGLTATpfrsDGREIllflfdgivyeysLKEAieDGYLAPPEYYGIRVDLTDERAEYDALSERlrealaAD 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 297 AEDFIENIANLINGRYKGKSGIIYCFSQKDSEQVTISLQKLGVRAGTYHANMEPEDRTKVHTQWSANELQVVVATVAFGM 376
Cdd:COG1061 288 AERKDKILRELLREHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNE 367
|
330 340 350
....*....|....*....|....*....|.
gi 1958769850 377 GIDKPDVRFVIHHSMSKSMENYYQesgRAGR 407
Cdd:COG1061 368 GVDVPRLDVAILLRPTGSPREFIQ---RLGR 395
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
286-407 |
1.78e-13 |
|
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: 67.53 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 286 LYYEVRQKpssaEDFIENIANLINGRYKGKSgIIYCFSQKDSEQVTISLQKLGVRAGTYHANMEPEDRTKVHTQWSANEL 365
Cdd:cd18787 4 LYVVVEEE----EKKLLLLLLLLEKLKPGKA-IIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKV 78
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1958769850 366 QVVVAT-VAfGMGIDKPDVRFVIHHSMSKSMENYYQESGRAGR 407
Cdd:cd18787 79 RVLVATdVA-ARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGR 120
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
362-418 |
1.86e-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: 60.03 E-value: 1.86e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958769850 362 ANELQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESGRAGRD-DWRADCILYY 418
Cdd:cd18785 20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGgKDEGEVILFV 77
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
287-407 |
3.61e-11 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 65.55 E-value: 3.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 287 YYEVRQKpssaeDFIENIANLINgRYKGKSGIIYCFSQKDSEQVTISLQKLGVRAGTYHANMEPEDRTKVHTQWSANELQ 366
Cdd:COG0513 220 YYLVDKR-----DKLELLRRLLR-DEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIR 293
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1958769850 367 VVVAT-VAfGMGIDKPDVRFVIHHSMSKSMENYYQESGRAGR 407
Cdd:COG0513 294 VLVATdVA-ARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGR 334
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
96-407 |
4.65e-11 |
|
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: 66.01 E-value: 4.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 96 QLETVNATMARKDIFLVMPTGGGKSLCYQLPALCS-----DGFTLVICPLISLMEDQLMVLQQL------GISATMLN-- 162
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEAlledpGATALYLYPTKALARDQLRRLRELaealglGVRVATYDgd 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 163 -SSSSKEHVKcvhtemmnKNSHlkLIYVTPEKI--------AKSKMFMSRLEkaYeagrltgVAVDEVHCcsqwghdfrp 233
Cdd:COG1205 141 tPPEERRWIR--------EHPD--IVLTNPDMLhygllphhTRWARFFRNLR--Y-------VVIDEAHT---------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 234 dYK-ALG-----ILKR------------QFpnislIGLTATATN---HvlkdAQKILCVEkcltFTA------------- 279
Cdd:COG1205 192 -YRgVFGshvanVLRRlrricrhygsdpQF-----ILASATIGNpaeH----AERLTGRP----VTVvdedgsprgertf 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 280 SFNRPNLYYEVRQKPSSAEDfIENIANLIngrYKGKSGIIYCFSQKDSEQVTISLQK------LGVRAGTYHANMEPEDR 353
Cdd:COG1205 258 VLWNPPLVDDGIRRSALAEA-ARLLADLV---REGLRTLVFTRSRRGAELLARYARRalrepdLADRVAAYRAGYLPEER 333
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1958769850 354 TKVHTQWSANELQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESGRAGR 407
Cdd:COG1205 334 REIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGR 387
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
285-412 |
1.01e-09 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 57.27 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 285 NLYYEVRQKPSSAEDFIEN---IANLINgryKGKSGIIYCFSQKDSEQVT-------ISLQKLGVRAGTYHANMEPEDRT 354
Cdd:cd18797 6 NPPLLDRKDGERGSARREAarlFADLVR---AGVKTIVFCRSRKLAELLLrylkarlVEEGPLASKVASYRAGYLAEDRR 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958769850 355 KVHTQWSANELQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESGRAGRDDWRA 412
Cdd:cd18797 83 EIEAELFNGELLGVVATNALELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKDS 140
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
216-409 |
1.41e-08 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 57.98 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 216 VAVDEVHCC--SQWGHdfRPDykalGI---LKRQFPNISLIGLTATATN-HVLkdAQKILC-----------VEKCLTFT 278
Cdd:COG1202 330 VVIDEVHMLedPERGH--RLD----GLiarLKYYCPGAQWIYLSATVGNpEEL--AKKLGAklveyeerpvpLERHLTFA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 279 ASFNRPNLyyevrqkpssaedfienIANLINGRYKGKSG-------IIYCFSQKDSEQvtISlQKLGVRAGTYHANMEPE 351
Cdd:COG1202 402 DGREKIRI-----------------INKLVKREFDTKSSkgyrgqtIIFTNSRRRCHE--IA-RALGYKAAPYHAGLDYG 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958769850 352 DRTKVHTQWSANELQVVVATVAFGMGIDKPDVRfVIHHS--MSK---SMENYYQESGRAGRDD 409
Cdd:COG1202 462 ERKKVERRFADQELAAVVTTAALAAGVDFPASQ-VIFDSlaMGIewlSVQEFHQMLGRAGRPD 523
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
313-417 |
6.95e-08 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350182 [Multi-domain] Cd Length: 154 Bit Score: 52.17 E-value: 6.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 313 KGKSGIIYCFSQKDSEQVTISLqkLGVraGTYHANMEPEDRTKVHTQWSANELQVVVATVAFGMGIDKPdVRFVIHHSMS 392
Cdd:cd18795 42 EGKPVLVFCSSRKECEKTAKDL--AGI--AFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLP-ARTVIIKGTQ 116
|
90 100 110
....*....|....*....|....*....|....*..
gi 1958769850 393 K---------SMENYYQESGRAGR---DDwRADCILY 417
Cdd:cd18795 117 RydgkgyrelSPLEYLQMIGRAGRpgfDT-RGEAIIM 152
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
318-407 |
6.33e-07 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 52.14 E-value: 6.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 318 IIYCFSQKDSEQVTISLQKLGVRAGTYHANMEPEDRTKVHTQWSANELQVVVATVAFGMGIDKPDVRFVIHHSMSKSMEN 397
Cdd:PTZ00424 271 IIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPEN 350
|
90
....*....|
gi 1958769850 398 YYQESGRAGR 407
Cdd:PTZ00424 351 YIHRIGRSGR 360
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
91-256 |
3.85e-06 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 47.28 E-value: 3.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 91 KFRPLQLETVNATMA-----RKDIFLVMPTGGGKSLCY-QLPALCSDGF----TLVICPLISLMEDQLMVLQQLGISATM 160
Cdd:pfam04851 3 ELRPYQIEAIENLLEsikngQKRGLIVMATGSGKTLTAaKLIARLFKKGpikkVLFLVPRKDLLEQALEEFKKFLPNYVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 161 LNSSSSKEhvkcvhtEMMNKNSHLKLIYVTPEKIAKSKMfMSRLEKAYEAGRLtgVAVDEVHccsqwgHDFRPDYKAlgi 240
Cdd:pfam04851 83 IGEIISGD-------KKDESVDDNKIVVTTIQSLYKALE-LASLELLPDFFDV--IIIDEAH------RSGASSYRN--- 143
|
170
....*....|....*.
gi 1958769850 241 LKRQFPNISLIGLTAT 256
Cdd:pfam04851 144 ILEYFKPAFLLGLTAT 159
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
318-407 |
9.30e-06 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 48.62 E-value: 9.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 318 IIYCFSQKDSEQVTISLQKLGVRAGTYHANMEPEDRTKVHTQWSANELQVVVATVAFGMGIDKPDVRFVIHHSMSKSMEN 397
Cdd:PTZ00110 381 LIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIED 460
|
90
....*....|
gi 1958769850 398 YYQESGRAGR 407
Cdd:PTZ00110 461 YVHRIGRTGR 470
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
96-168 |
3.51e-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: 44.88 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 96 QLETVNATMARKDIFLVMPTGGGKSLCYQLP---ALCSDGFT--LVICPLISLMEDQLMVLQQL------GISATMLNSS 164
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPileALLRDPGSraLYLYPTKALAQDQLRSLRELleqlglGIRVATYDGD 84
|
....
gi 1958769850 165 SSKE 168
Cdd:cd17923 85 TPRE 88
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
92-259 |
5.02e-05 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 44.17 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 92 FRPLQLETVNATMARKDIFLV-MPTGGGKSLCYQLPAL----CSDGFTLVICPLISLMEDQLM----VLQQLGISATMLN 162
Cdd:cd17921 2 LNPIQREALRALYLSGDSVLVsAPTSSGKTLIAELAILralaTSGGKAVYIAPTRALVNQKEAdlreRFGPLGKNVGLLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 163 SSSskehvkcvhTEMMNKNSHLKLIYVTPEKIAkskmFMSRLEKAYEAGRLTGVAVDEVHCCSQwghdfrPDYKA----- 237
Cdd:cd17921 82 GDP---------SVNKLLLAEADILVATPEKLD----LLLRNGGERLIQDVRLVVVDEAHLIGD------GERGVvlell 142
|
170 180
....*....|....*....|..
gi 1958769850 238 LGILKRQFPNISLIGLTATATN 259
Cdd:cd17921 143 LSRLLRINKNARFVGLSATLPN 164
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
92-256 |
2.74e-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: 41.52 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 92 FRPLQLETVNATMA----RKDIFlVMPTGGGKSLC-YQLPALCSDGFTLVICPLISLMEDQLMVLQQLGISAT-MLNSSS 165
Cdd:cd17926 1 LRPYQEEALEAWLAhknnRRGIL-VLPTGSGKTLTaLALIAYLKELRTLIVVPTDALLDQWKERFEDFLGDSSiGLIGGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 166 SKEHVKCvhtemmnknshlKLIYV-TPEKIakskmfMSRLEKAYEAGRLTGV-AVDEVH--CCSQWGHdfrpdykalgIL 241
Cdd:cd17926 80 KKKDFDD------------ANVVVaTYQSL------SNLAEEEKDLFDQFGLlIVDEAHhlPAKTFSE----------IL 131
|
170
....*....|....*
gi 1958769850 242 KRqFPNISLIGLTAT 256
Cdd:cd17926 132 KE-LNAKYRLGLTAT 145
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
293-407 |
2.95e-04 |
|
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: 41.48 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 293 KPSSAEDFIENIANLINgryKGKSGIIYCFSQKDSEQVTISLQKL------GVRAGTYHANMEPEDRTKVHTQWSANELQ 366
Cdd:cd18796 20 AGESGADAYAEVIFLLE---RHKSTLVFTNTRSQAERLAQRLRELcpdrvpPDFIALHHGSLSRELREEVEAALKRGDLK 96
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1958769850 367 VVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESGRAGR 407
Cdd:cd18796 97 VVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
345-445 |
2.99e-04 |
|
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: 41.56 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 345 HANMEPEDRTKVHTQWSANELQVVVATVAFGMGIDKPDVR-FVIHHSMSKSMENYYQESGRAGRDDWRADCILYYGfgdi 423
Cdd:cd18811 68 HGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATvMVIEDAERFGLSQLHQLRGRVGRGDHQSYCLLVYK---- 143
|
90 100
....*....|....*....|..
gi 1958769850 424 frissmVVMENVGQQKLYEMVS 445
Cdd:cd18811 144 ------DPLTETAKQRLRVMTE 159
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
94-407 |
3.49e-04 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 43.62 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 94 PLQLETVNATMARKDIFLVMPTGGGKSLCYQLP--ALCS-----------DGFTLVICP---LISLMEDQLMVLQQLGIS 157
Cdd:PLN00206 146 PIQMQAIPAALSGRSLLVSADTGSGKTASFLVPiiSRCCtirsghpseqrNPLAMVLTPtreLCVQVEDQAKVLGKGLPF 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 158 ATMLnsssskehvkCVHTEMMNKNSH-----LKLIYVTPEKIAKskmFMSRLEKayeagRLTGVAV---DEVHCCSQWGh 229
Cdd:PLN00206 226 KTAL----------VVGGDAMPQQLYriqqgVELIVGTPGRLID---LLSKHDI-----ELDNVSVlvlDEVDCMLERG- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 230 dFRPdyKALGILkRQFPNISLIGLTATATNHVLKDAQKILcveKCLTFTA--SFNRPN-------LYYEVRQKPSSAEDF 300
Cdd:PLN00206 287 -FRD--QVMQIF-QALSQPQVLLFSATVSPEVEKFASSLA---KDIILISigNPNRPNkavkqlaIWVETKQKKQKLFDI 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 301 IENianliNGRYKgKSGIIYCFSQKDSEQVTISLQKL-GVRAGTYHANMEPEDRTKVHTQWSANELQVVVATVAFGMGID 379
Cdd:PLN00206 360 LKS-----KQHFK-PPAVVFVSSRLGADLLANAITVVtGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVD 433
|
330 340
....*....|....*....|....*...
gi 1958769850 380 KPDVRFVIHHSMSKSMENYYQESGRAGR 407
Cdd:PLN00206 434 LLRVRQVIIFDMPNTIKEYIHQIGRASR 461
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
342-407 |
1.26e-03 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 41.85 E-value: 1.26e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958769850 342 GTYHANMEPEDRTKVHTQWSANELQVVVATVAFGMGIDKPdVRFVIHHSMSK----SMEN-----YYQESGRAGR 407
Cdd:COG4581 303 AVHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMP-ARTVVFTKLSKfdgeRHRPltareFHQIAGRAGR 376
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
341-406 |
1.47e-03 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 41.83 E-value: 1.47e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958769850 341 AGTYHANMEPEDRTKVHTQWSANELQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESGRAG 406
Cdd:PRK09751 304 ARSHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
107-222 |
3.87e-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: 38.33 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769850 107 KDIFLVMPTGGGKSLCYQLPALCS------DGF-TLVICPLISLMEDQLMVLQ------QLGISATMLN---SSSSKehv 170
Cdd:cd17922 2 RNVLIAAPTGSGKTEAAFLPALSSladepeKGVqVLYISPLKALINDQERRLEepldeiDLEIPVAVRHgdtSQSEK--- 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1958769850 171 kcvhTEMMNKNSHLKLIyvTPEKIAksKMFMSRleKAYEA-GRLTGVAVDEVH 222
Cdd:cd17922 79 ----AKQLKNPPGILIT--TPESLE--LLLVNK--KLRELfAGLRYVVVDEIH 121
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
345-419 |
7.26e-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: 37.63 E-value: 7.26e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958769850 345 HANMEPEDRTKVHTQWSANELQVVVATVAFGMGIDKPDVR-FVIHHSMSKSMENYYQESGRAGRDDWRADCILYYG 419
Cdd:cd18792 67 HGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANtMIIEDADRFGLSQLHQLRGRVGRGKHQSYCYLLYP 142
|
|
| |
