|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
24-581 |
2.99e-176 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 512.76 E-value: 2.99e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 24 LHAEAREVLRRLtdVADAEFHDGQYEAIRALVADRaRTVVVQRTGWGKSAVYFISSLLLRargmGPALIVSPLLSLMRDQ 103
Cdd:COG0514 1 LRDDALEVLKRV--FGYDSFRPGQEEIIEAVLAGR-DALVVMPTGGGKSLCYQLPALLLP----GLTLVVSPLIALMKDQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 104 VEAASRAGVRAAMVNSA-NVTEWDEIRTRLETDELDVLLVGPERLNNPAFREqwlpyLLPRL--GLLVIDEAHCISDWGH 180
Cdd:COG0514 74 VDALRAAGIRAAFLNSSlSAEERREVLRALRAGELKLLYVAPERLLNPRFLE-----LLRRLkiSLFAIDEAHCISQWGH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 181 DFRPDYRRIGSLIKSLPvGVPVLATTATANDRVSRDIAEQLSTDTApvHVIRGPLSRESLRLGVLTLPDEaQRIGWLLTH 260
Cdd:COG0514 149 DFRPDYRRLGELRERLP-NVPVLALTATATPRVRADIAEQLGLEDP--RVFVGSFDRPNLRLEVVPKPPD-DKLAQLLDF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 261 LNDLPG-SGIIYTLTVSAAEDTANALRASGYEVLAYTGKTDPDERLVAEQALKENRVKALVATSALGMGFDKPDLGFVVH 339
Cdd:COG0514 225 LKEHPGgSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIH 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 340 LGAPSSAVSYYQQIGRAGRGAVNADVLLLPGREDRAIWEYFATASMPNEEQalavldalaqapeglsitalearvqlrrs 419
Cdd:COG0514 305 YDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEER----------------------------- 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 420 tlelllkvldvegavvkegnywrrtsspwrydnaryaavAQARVLEQNAMLEYECTSQCRMLFLAQQLDDASAVACGRCD 499
Cdd:COG0514 356 ---------------------------------------KRVERAKLDAMLAYAETTGCRRQFLLRYFGEELAEPCGNCD 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 500 VCAGPWYPVEVPAEAQQAAQSSFNTvgvplQPRrmWPSG--LDQLMGADAPRgRLSKDEQAESGYALAR-LSDMGYGTRL 576
Cdd:COG0514 397 NCLGPPETFDGTEAAQKALSCVYRT-----GQR--FGAGhvIDVLRGSKNEK-IRQFGHDKLSTYGIGKdLSDKEWRSVI 468
|
....*
gi 896426751 577 RELLA 581
Cdd:COG0514 469 RQLLA 473
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
28-517 |
1.97e-82 |
|
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: 273.49 E-value: 1.97e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 28 AREVLRRLTDVADaeFHDGQYEAIRALVADRArTVVVQRTGWGKSAVYFISSLLLRargmGPALIVSPLLSLMRDQVEAA 107
Cdd:TIGR01389 1 AQQVLKRTFGYDD--FRPGQEEIISHVLDGRD-VLVVMPTGGGKSLCYQVPALLLK----GLTVVISPLISLMKDQVDQL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 108 SRAGVRAAMVNSA-NVTEWDEIRTRLETDELDVLLVGPERLNNPAFREqwlpyLLPR--LGLLVIDEAHCISDWGHDFRP 184
Cdd:TIGR01389 74 RAAGVAAAYLNSTlSAKEQQDIEKALVNGELKLLYVAPERLEQDYFLN-----MLQRipIALVAVDEAHCVSQWGHDFRP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 185 DYRRIGSLIKSLPvGVPVLATTATANDRVSRDIAEQLSTDTAPvHVIRGpLSRESLRLGVltLPDEA---QRIGWLLTHL 261
Cdd:TIGR01389 149 EYQRLGSLAERFP-QVPRIALTATADAETRQDIRELLRLADAN-EFITS-FDRPNLRFSV--VKKNNkqkFLLDYLKKHR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 262 NDlpgSGIIYTLTVSAAEDTANALRASGYEVLAYTGKTDPDERLVAEQALKENRVKALVATSALGMGFDKPDLGFVVHLG 341
Cdd:TIGR01389 224 GQ---SGIIYASSRKKVEELAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYD 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 342 APSSAVSYYQQIGRAGRGAVNADVLLLPGREDRAIWEYFATASMPNEEQAlavldalaqapeglsitalearvqlrrstl 421
Cdd:TIGR01389 301 MPGNLESYYQEAGRAGRDGLPAEAILLYSPADIALLKRRIEQSEADDDYK------------------------------ 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 422 elllkvlDVEGAvvkegnywrrtsspwrydnaryaavaqarvlEQNAMLEYECTSQCRMLFLAQQLDDASAVACGRCDVC 501
Cdd:TIGR01389 351 -------QIERE-------------------------------KLRAMIAYCETQTCRRAYILRYFGENEVEPCGNCDNC 392
|
490
....*....|....*.
gi 896426751 502 AGPWYPVEVPAEAQQA 517
Cdd:TIGR01389 393 LDPPKSYDATVEAQKA 408
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
30-235 |
3.73e-69 |
|
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: 225.21 E-value: 3.73e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 30 EVLRRLtdVADAEFHDGQYEAIRALVADRaRTVVVQRTGWGKSAVYFISSLLLRARGMGPALIVSPLLSLMRDQVEAASR 109
Cdd:cd18018 2 KLLRRV--FGHPSFRPGQEEAIARLLSGR-STLVVLPTGAGKSLCYQLPALLLRRRGPGLTLVVSPLIALMKDQVDALPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 110 AgVRAAMVNSANVTEWDEIR-TRLETDELDVLLVGPERLNNPAFREQWLPylLPRLGLLVIDEAHCISDWGHDFRPDYRR 188
Cdd:cd18018 79 A-IKAAALNSSLTREERRRIlEKLRAGEVKILYVSPERLVNESFRELLRQ--TPPISLLVVDEAHCISEWSHNFRPDYLR 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 896426751 189 IGSLIKSLPVGVPVLATTATANDRVSRDIAEQLstDTAPVHVIRGPL 235
Cdd:cd18018 156 LCRVLRELLGAPPVLALTATATKRVVEDIASHL--GIPESGVVRGPL 200
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
43-373 |
5.84e-65 |
|
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: 223.11 E-value: 5.84e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 43 FHDGQYEAIRALVADRaRTVVVQRTGWGKSAVYFISSLLLRargmGPALIVSPLLSLMRDQVEAASRAGVRAAMVNSANV 122
Cdd:TIGR00614 12 FRPVQLEVINAVLLGR-DCFVVMPTGGGKSLCYQLPALYSD----GITLVISPLISLMEDQVLQLQALGIPATFLNSAQT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 123 TEWD-EIRTRLETDELDVLLVGPERL-NNPAFREQWLPYLlpRLGLLVIDEAHCISDWGHDFRPDYRRIGSLIKSLPVgV 200
Cdd:TIGR00614 87 KEQQlNVLTDLKDGKIKLLYVTPEKIsASNRLLQTLEERK--GITLIAVDEAHCISQWGHDFRPDYKALGSLKQKFPN-V 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 201 PVLATTATANDRVSRDIAEQLSTDTApvHVIRGPLSRESLRLGVL-TLPDEAQRI-GWLLTHLndlPG-SGIIYTLTVSA 277
Cdd:TIGR00614 164 PVMALTATASPSVREDILRQLNLLNP--QIFCTSFDRPNLYYEVRrKTPKILEDLlRFIRKEF---EGkSGIIYCPSRKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 278 AEDTANALRASGYEVLAYTGKTDPDERLVAEQALKENRVKALVATSALGMGFDKPDLGFVVHLGAPSSAVSYYQQIGRAG 357
Cdd:TIGR00614 239 VEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRAG 318
|
330
....*....|....*.
gi 896426751 358 RGAVNADVLLLPGRED 373
Cdd:TIGR00614 319 RDGLPSECHLFYAPAD 334
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
19-368 |
8.84e-63 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 220.74 E-value: 8.84e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 19 LQADPLHAE--AREVLRRLtdVADAEFHDGQYEAIRALVADRaRTVVVQRTGWGKSAVYFISSLLLRargmGPALIVSPL 96
Cdd:PRK11057 2 AQAEVLNLEslAKQVLQET--FGYQQFRPGQQEIIDAVLSGR-DCLVVMPTGGGKSLCYQIPALVLD----GLTLVVSPL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 97 LSLMRDQVEAASRAGVRAAMVNSANVTEWD-EIRTRLETDELDVLLVGPERLNNPAFREQwLPYLlpRLGLLVIDEAHCI 175
Cdd:PRK11057 75 ISLMKDQVDQLLANGVAAACLNSTQTREQQlEVMAGCRTGQIKLLYIAPERLMMDNFLEH-LAHW--NPALLAVDEAHCI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 176 SDWGHDFRPDYRRIGSLIKSLPvGVPVLATTATANDRVSRDIAEQLSTDTAPVHVirGPLSRESLRLgvlTLPDEAQRIG 255
Cdd:PRK11057 152 SQWGHDFRPEYAALGQLRQRFP-TLPFMALTATADDTTRQDIVRLLGLNDPLIQI--SSFDRPNIRY---TLVEKFKPLD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 256 WLLTHLNDLPG-SGIIYTLTVSAAEDTANALRASGYEVLAYTGKTDPDERLVAEQALKENRVKALVATSALGMGFDKPDL 334
Cdd:PRK11057 226 QLMRYVQEQRGkSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNV 305
|
330 340 350
....*....|....*....|....*....|....
gi 896426751 335 GFVVHLGAPSSAVSYYQQIGRAGRGAVNADVLLL 368
Cdd:PRK11057 306 RFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLF 339
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
41-230 |
4.12e-58 |
|
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: 195.45 E-value: 4.12e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 41 AEFHDGQYEAIRALVADRaRTVVVQRTGWGKSAVYFISSLLLRargmGPALIVSPLLSLMRDQVEAASRAGVRAAMVNSA 120
Cdd:cd17920 11 DEFRPGQLEAINAVLAGR-DVLVVMPTGGGKSLCYQLPALLLD----GVTLVVSPLISLMQDQVDRLQQLGIRAAALNST 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 121 N-VTEWDEIRTRLETDELDVLLVGPERLNNPAFREQ-WLPYLLPRLGLLVIDEAHCISDWGHDFRPDYRRIGSLIKSLPv 198
Cdd:cd17920 86 LsPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELlQRLPERKRLALIVVDEAHCVSQWGHDFRPDYLRLGRLRRALP- 164
|
170 180 190
....*....|....*....|....*....|..
gi 896426751 199 GVPVLATTATANDRVSRDIAEQLSTDTAPVHV 230
Cdd:cd17920 165 GVPILALTATATPEVREDILKRLGLRNPVIFR 196
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
43-358 |
3.49e-42 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 165.45 E-value: 3.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 43 FHDGQYEAIRALVADrARTVVVQRTGWGKSAVYFISSLLLRargmGPALIVSPLLSLMRDQVEAASRAGVRAAMVnSANV 122
Cdd:PLN03137 461 FRPNQREIINATMSG-YDVFVLMPTGGGKSLTYQLPALICP----GITLVISPLVSLIQDQIMNLLQANIPAASL-SAGM 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 123 tEWDE---IRTRLETD--ELDVLLVGPERLNNPAFREQWLPYLLPR--LGLLVIDEAHCISDWGHDFRPDYRRIGSLIKS 195
Cdd:PLN03137 535 -EWAEqleILQELSSEysKYKLLYVTPEKVAKSDSLLRHLENLNSRglLARFVIDEAHCVSQWGHDFRPDYQGLGILKQK 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 196 LPvGVPVLATTATANDRVSRDIAEQLStdTAPVHVIRGPLSRESLRLGVL-----TLPDEAQRIgwlltHLNDLPGSGII 270
Cdd:PLN03137 614 FP-NIPVLALTATATASVKEDVVQALG--LVNCVVFRQSFNRPNLWYSVVpktkkCLEDIDKFI-----KENHFDECGII 685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 271 YTLTVSAAEDTANALRASGYEVLAYTGKTDPDERLVAEQALKENRVKALVATSALGMGFDKPDLGFVVHLGAPSSAVSYY 350
Cdd:PLN03137 686 YCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYH 765
|
....*...
gi 896426751 351 QQIGRAGR 358
Cdd:PLN03137 766 QECGRAGR 773
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
23-221 |
1.36e-37 |
|
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: 139.42 E-value: 1.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 23 PLHAEAREVLRRLTDVADaeFHDGQYEAIRALVADRaRTVVVQRTGWGKSAVYFISSLLlrarGMGPALIVSPLLSLMRD 102
Cdd:cd18015 1 PWSGKVKDTLKNVFKLEK--FRPLQLETINATMAGR-DVFLVMPTGGGKSLCYQLPALC----SDGFTLVVSPLISLMED 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 103 QVEAASRAGVRAAMVNSANVTE---WDEIRTRLETDELDVLLVGPERLNNPAFREQWLP--YLLPRLGLLVIDEAHCISD 177
Cdd:cd18015 74 QLMALKKLGISATMLNASSSKEhvkWVHAALTDKNSELKLLYVTPEKIAKSKRFMSKLEkaYNAGRLARIAIDEVHCCSQ 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 896426751 178 WGHDFRPDYRRIGSLIKSLPvGVPVLATTATANDRVSRDIAEQL 221
Cdd:cd18015 154 WGHDFRPDYKKLGILKRQFP-NVPILGLTATATSKVLKDVQKIL 196
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
43-221 |
6.44e-36 |
|
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: 134.13 E-value: 6.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 43 FHDGQYEAIRALVADRARTVVVQRTGWGKSAVYFISSLLLRARGmgpaLIVSPLLSLMRDQVEAASRAGVRAAMVNSANV 122
Cdd:cd18017 13 FRPVQWKVIRSVLEERRDNLVVMATGYGKSLCYQYPSVLLNSLT----LVISPLISLMEDQVLQLVMSNIPACFLGSAQS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 123 -TEWDEIRTrletDELDVLLVGPER-LNNPAFREQwlpyLLPRLGLLVIDEAHCISDWGHDFRPDYRRIGSLIKSLPvGV 200
Cdd:cd18017 89 qNVLDDIKM----GKIRVIYVTPEFvSKGLELLQQ----LRNGITLIAIDEAHCVSQWGHDFRSSYRHLGSIRNRLP-NV 159
|
170 180
....*....|....*....|.
gi 896426751 201 PVLATTATANDRVSRDIAEQL 221
Cdd:cd18017 160 PIVALTATATPSVRDDIIKNL 180
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
43-221 |
1.66e-32 |
|
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: 124.89 E-value: 1.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 43 FHDGQYEAIRALVADRARTVVVQRTGWGKSAVYFISSLLlrARGMgpALIVSPLLSLMRDQVEAASRAGVRAAMVNSANV 122
Cdd:cd18014 14 KSPLQEKATMAVVKGNKDVFVCMPTGAGKSLCYQLPALL--AKGI--TIVISPLIALIQDQVDHLKTLKIRVDSLNSKLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 123 T-EWDEIRTRLETD--ELDVLLVGPERLNNPAFrEQWLPYLLPR--LGLLVIDEAHCISDWGHDFRPDYRRIGSLIKSLP 197
Cdd:cd18014 90 AqERKRIIADLESEkpQTKFLYITPEMAATSSF-QPLLSSLVSRnlLSYLVVDEAHCVSQWGHDFRPDYLRLGALRSRYG 168
|
170 180
....*....|....*....|....
gi 896426751 198 vGVPVLATTATANDRVSRDIAEQL 221
Cdd:cd18014 169 -HVPWVALTATATPQVQEDIFAQL 191
|
|
| DpdF |
NF041063 |
protein DpdF; |
17-376 |
3.48e-31 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 130.42 E-value: 3.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 17 DSLQADPLHAEAREVLRRLTD-------VADAEFHD-----GQYEAIRA-LVADRARTVVVQ-RTGWGKSAVYFISSLLL 82
Cdd:NF041063 103 AAADDPPFEDVFAERLRRTLEpvpgdpfLAEALGFThyrspGQREAVRAaLLAPPGSTLIVNlPTGSGKSLVAQAPALLA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 83 RARGmGPALIVSPLLSLMRDQvEAASRAGVRAAMVNSANVTEW---------DEIRTRLETDELDVLLVGPERLNNPafr 153
Cdd:NF041063 183 SRQG-GLTLVVVPTVALAIDQ-ERRARELLRRAGPDLGGPLAWhgglsaeerAAIRQRIRDGTQRILFTSPESLTGS--- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 154 eqwlpyLLP---------RLGLLVIDEAHCISDWGHDFRPDYRRIGSLIKSL----PVGVP--VLATTATANDRvSRDIA 218
Cdd:NF041063 258 ------LRPalfdaaeagLLRYLVVDEAHLVDQWGDGFRPEFQLLAGLRRSLlrlaPSGRPfrTLLLSATLTES-TLDTL 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 219 EQLSTDTAPVHVIRGPLSRESLRLGVLTLPDEAQRIGWLLTHLNDLPGSGIIYTLTVSAAEDTANALRASGYE-VLAYTG 297
Cdd:NF041063 331 ETLFGPPGPFIVVSAVQLRPEPAYWVAKCDSEEERRERVLEALRHLPRPLILYVTKVEDAEAWLQRLRAAGFRrVALFHG 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 298 KTDPDERLVAEQALKENRVKALVATSALGMGFDKPDLGFVVHLGAPSSAVSYYQQIGRAGR-GavNADV-LLLPGREDRA 375
Cdd:NF041063 411 DTPDAERERLIEQWRENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRdG--KASLsLLIYTPDDLD 488
|
.
gi 896426751 376 I 376
Cdd:NF041063 489 I 489
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
42-221 |
2.31e-27 |
|
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: 110.30 E-value: 2.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 42 EFHDGQYEAIRALVADRaRTVVVQRTGWGKSAVYFISSLLLRargmGPALIVSPLLSLMRDQVEAASRAGVRAAMVnSAN 121
Cdd:cd18016 17 QFRTNQLEAINAALLGE-DCFVLMPTGGGKSLCYQLPACVSP----GVTVVISPLRSLIVDQVQKLTSLDIPATYL-TGD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 122 VTEWDEIRTRLETDELD----VLLVGPERLNNPAFREQWLPYLLPR--LGLLVIDEAHCISDWGHDFRPDYRRIGSLIKS 195
Cdd:cd18016 91 KTDAEATKIYLQLSKKDpiikLLYVTPEKISASNRLISTLENLYERklLARFVIDEAHCVSQWGHDFRPDYKRLNMLRQK 170
|
170 180
....*....|....*....|....*.
gi 896426751 196 LPvGVPVLATTATANDRVSRDIAEQL 221
Cdd:cd18016 171 FP-SVPMMALTATATPRVQKDILNQL 195
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
237-368 |
1.72e-24 |
|
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: 99.21 E-value: 1.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 237 RESLRLGVLTLPDEAQRIGWLLT----HLNdlpGSGIIYTLTVSAAEDTANALRASGYEVLAYTGKTDPDERLVAEQALK 312
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDLLKRikveHLG---GSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWL 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 896426751 313 ENRVKALVATSALGMGFDKPDLGFVVHLGAPSSAVSYYQQIGRAGRGAVNADVLLL 368
Cdd:cd18794 78 RDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILF 133
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
42-240 |
3.97e-23 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 97.56 E-value: 3.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 42 EFHDGQYEAIRALVADRARTVVVQRTGWGKSAVYFISSL-LLRARGMGPALIVSPLLSLMRDQVEAASRAGVRAAMVNSA 120
Cdd:smart00487 8 PLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALeALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 121 NVT--EWDEIRTRLETDELDVLLVGPERLNNPAFREqwlPYLLPRLGLLVIDEAHCISDWGhdFRPDYRRIgslIKSLPV 198
Cdd:smart00487 88 LYGgdSKREQLRKLESGKTDILVTTPGRLLDLLEND---KLSLSNVDLVILDEAHRLLDGG--FGDQLEKL---LKLLPK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 896426751 199 GVPVLATTATANDRVSRDIAEQLStdtAPVHVIRGPLSRESL 240
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFLN---DPVFIDVGFTPLEPI 198
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
47-215 |
3.83e-22 |
|
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: 93.85 E-value: 3.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 47 QYEAIRALVADRaRTVVVQRTGWGKSAVYFISSL-LLRARGMGP-ALIVSPLLSLMRDQVEAASRAGvRAAMVNSANVTE 124
Cdd:pfam00270 4 QAEAIPAILEGR-DVLVQAPTGSGKTLAFLLPALeALDKLDNGPqALVLAPTRELAEQIYEELKKLG-KGLGLKVASLLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 125 WDEIRTRLET-DELDVLLVGPERLNNPAFREQwlpyLLPRLGLLVIDEAHCISDWGhdFRPDYRRIgslIKSLPVGVPVL 203
Cdd:pfam00270 82 GDSRKEQLEKlKGPDILVGTPGRLLDLLQERK----LLKNLKLLVLDEAHRLLDMG--FGPDLEEI---LRRLPKKRQIL 152
|
170
....*....|..
gi 896426751 204 ATTATANDRVSR 215
Cdd:pfam00270 153 LLSATLPRNLED 164
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
12-489 |
1.01e-20 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 96.63 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 12 DSLRTDSLQADPLHAEAREVLRRLTDVADAEF--HDGQYEAIRALVADRA----RTVVVQRTGWGKSavYFISSLLLRAR 85
Cdd:COG1061 48 EDGRRLPEEDTERELAEAEALEAGDEASGTSFelRPYQQEALEALLAALErgggRGLVVAPTGTGKT--VLALALAAELL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 86 GMGPALIVSPLLSLMRDQVEAASRagVRAAMVNSANVTEWDEirtrletdelDVLLVGPERLNNPAFREQwlpyLLPRLG 165
Cdd:COG1061 126 RGKRVLVLVPRRELLEQWAEELRR--FLGDPLAGGGKKDSDA----------PITVATYQSLARRAHLDE----LGDRFG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 166 LLVIDEAHcisdwgHDFRPDYRRIGSLIKSlpvgVPVLATTATANDRVSRDIAEQLSTDT---------------APVHV 230
Cdd:COG1061 190 LVIIDEAH------HAGAPSYRRILEAFPA----AYRLGLTATPFRSDGREILLFLFDGIvyeyslkeaiedgylAPPEY 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 231 --IRGPLSRESLRLGVLT-------LPDEAQRIGWLLTHLNDLPGS--GIIYTLTVSAAEDTANALRASGYEVLAYTGKT 299
Cdd:COG1061 260 ygIRVDLTDERAEYDALSerlrealAADAERKDKILRELLREHPDDrkTLVFCSSVDHAEALAELLNEAGIRAAVVTGDT 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 300 DPDERLVAEQALKENRVKALVATSALGMGFDKPDLGFVVHLGAPSSAVSYYQQIGRAGRGAVN---ADVLLLPGReDRAI 376
Cdd:COG1061 340 PKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPGkedALVYDFVGN-DVPV 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 377 WEYFATASMPNEEQALAVLDALAQAPEGLSITALEARVQLRRSTLELLLKVLDVEGAVVKEGNYWRRTSSPWRYDNARYA 456
Cdd:COG1061 419 LEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALALELLEL 498
|
490 500 510
....*....|....*....|....*....|...
gi 896426751 457 AVAQARVLEQNAMLEYECTSQCRMLFLAQQLDD 489
Cdd:COG1061 499 AKAEGKAEEEEEEKELLLLLALAKLLKLLLLLL 531
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
47-381 |
1.17e-19 |
|
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: 93.75 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 47 QYEAIRALVADRArTVVVQRTGWGKSAVYFISSL--LLRARGmGPALIVSPLLSLMRDQVEAASR------AGVRAAMVN 118
Cdd:COG1205 61 QAEAIEAARAGKN-VVIATPTASGKSLAYLLPVLeaLLEDPG-ATALYLYPTKALARDQLRRLRElaealgLGVRVATYD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 119 -SANVTEWDEIRtrletDELDVLLVGPERLN------NPAFREqwlpyLLPRLGLLVIDEAHCisdwghdfrpdYR---- 187
Cdd:COG1205 139 gDTPPEERRWIR-----EHPDIVLTNPDMLHygllphHTRWAR-----FFRNLRYVVIDEAHT-----------YRgvfg 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 188 -----------RIGSLIKSLPVgvpVLATTAT-ANdrvSRDIAEQL--------STDTAP---VHVI--RGPLSRESLRL 242
Cdd:COG1205 198 shvanvlrrlrRICRHYGSDPQ---FILASATiGN---PAEHAERLtgrpvtvvDEDGSPrgeRTFVlwNPPLVDDGIRR 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 243 GVLTlpdEAQRigwLLTHLNDLPGSGIIYTLTVSAAEDTANALRAS------GYEVLAYTGKTDPDERLVAEQALKENRV 316
Cdd:COG1205 272 SALA---EAAR---LLADLVREGLRTLVFTRSRRGAELLARYARRAlrepdlADRVAAYRAGYLPEERREIERGLRSGEL 345
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896426751 317 KALVATSALGMGFDKPDLGFVVHLGAPSSAVSYYQQIGRAGRGAVNADVLLLPGreDRAIWEYFA 381
Cdd:COG1205 346 LGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVLVAG--DDPLDQYYV 408
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
279-358 |
1.01e-18 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 81.10 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 279 EDTANALRASGYEVLAYTGKTDPDERLVAEQALKENRVKALVATSALGMGFDKPDLGFVVHLGAPSSAVSYYQQIGRAGR 358
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
252-358 |
4.83e-18 |
|
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: 79.95 E-value: 4.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 252 QRIGWLLTHLNDLPGS-GIIYTLTVSAAEDTAnALRASGYEVLAYTGKTDPDERLVAEQALKENRVKALVATSALGMGFD 330
Cdd:pfam00271 1 EKLEALLELLKKERGGkVLIFSQTKKTLEAEL-LLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100
....*....|....*....|....*...
gi 896426751 331 KPDLGFVVHLGAPSSAVSYYQQIGRAGR 358
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGR 107
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
249-358 |
4.70e-14 |
|
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: 69.46 E-value: 4.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 249 DEAQRIGWLLTHL--NDLPGSGIIYTLTVSAAEDTANALRASGYEVLAYTGKTDPDERLVAEQALKENRVKALVATSALG 326
Cdd:cd18787 9 EEEEKKLLLLLLLleKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVATDVAA 88
|
90 100 110
....*....|....*....|....*....|..
gi 896426751 327 MGFDKPDLGFVVHLGAPSSAVSYYQQIGRAGR 358
Cdd:cd18787 89 RGLDIPGVDHVINYDLPRDAEDYVHRIGRTGR 120
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
290-369 |
7.52e-13 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 66.51 E-value: 7.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 290 YEVLAYTGKTDPDERLVAEQALKENRVKALVATSALGMGFDKPDLGFVVHLGAPSSAVSYYQQIGRAGRGAVNADVLLLP 369
Cdd:cd18797 67 SKVASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKDSLVILVA 146
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
67-208 |
1.72e-12 |
|
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: 65.50 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 67 TGWGKSAVYFISSLLLRARGMGPALIVSPLLSLMRDQVEA---ASRAGVRAAMVNSAnvtEWDEIRTRLETDELDVLLVG 143
Cdd:cd00046 10 TGSGKTLAALLAALLLLLKKGKKVLVLVPTKALALQTAERlreLFGPGIRVAVLVGG---SSAEEREKNKLGDADIIIAT 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896426751 144 PERLNNPafREQWLPYLLPRLGLLVIDEAHCISDWGHDFRPDYRRIgslIKSLPVGVPVLATTAT 208
Cdd:cd00046 87 PDMLLNL--LLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAV---RKAGLKNAQVILLSAT 146
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
230-358 |
2.24e-12 |
|
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: 65.36 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 230 VIRGPLSRESLRLGVLTLPDEAQRIGWLLTHLNDLpgsgiIYTLTVSAAEDTANALRASGYEVL------AYTGKTDPDE 303
Cdd:cd18796 8 VILPVAPEIFPWAGESGADAYAEVIFLLERHKSTL-----VFTNTRSQAERLAQRLRELCPDRVppdfiaLHHGSLSREL 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 896426751 304 RLVAEQALKENRVKALVATSALGMGFDKPDLGFVVHLGAPSSAVSYYQQIGRAGR 358
Cdd:cd18796 83 REEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
314-360 |
4.43e-11 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 59.25 E-value: 4.43e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 896426751 314 NRVKALVATSALGMGFDKPDLGFVVHLGAPSSAVSYYQQIGRAGRGA 360
Cdd:cd18785 21 SSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGG 67
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
29-383 |
1.63e-09 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 61.06 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 29 REVLRRLTDVADAEFHDGQYEAIRALVADRARTVVVQRTGWGKSAV--YFISSLLLRArgmGPALIVSPLLSL---MRDQ 103
Cdd:COG1204 9 EKVIEFLKERGIEELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIaeLAILKALLNG---GKALYIVPLRALaseKYRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 104 VEAA-SRAGVRAAMVNSANVTEWDEIRTRletdelDVLLVGPERL-----NNPAFreqwlpylLPRLGLLVIDEAHCISD 177
Cdd:COG1204 86 FKRDfEELGIKVGVSTGDYDSDDEWLGRY------DILVATPEKLdsllrNGPSW--------LRDVDLVVVDEAHLIDD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 178 wghDFR-PDYRRIGSLIKSLPVGVPVLATTAT-ANdrvSRDIAEQL-----STDTAPVhvirgPLSRESLRLGVLTLPDE 250
Cdd:COG1204 152 ---ESRgPTLEVLLARLRRLNPEAQIVALSATiGN---AEEIAEWLdaelvKSDWRPV-----PLNEGVLYDGVLRFDDG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 251 AQRIG----WLLTHLNDLPGSGIIYTLTVSAAEDTA----------------NALRASGYEVLAYTGKTDPDERL----- 305
Cdd:COG1204 221 SRRSKdptlALALDLLEEGGQVLVFVSSRRDAESLAkkladelkrrltpeerEELEELAEELLEVSEETHTNEKLadcle 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 306 --VA--------------EQALKENRVKALVATSALGMGfdkpdlgfvVHL--------------GAPSSAVSYYQQIGR 355
Cdd:COG1204 301 kgVAfhhaglpselrrlvEDAFREGLIKVLVATPTLAAG---------VNLparrviirdtkrggMVPIPVLEFKQMAGR 371
|
410 420 430
....*....|....*....|....*....|....
gi 896426751 356 AGR------GavNADVLLLPGREDRAIWEYFATA 383
Cdd:COG1204 372 AGRpgydpyG--EAILVAKSSDEADELFERYILG 403
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
67-359 |
3.95e-08 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 56.71 E-value: 3.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 67 TGWGKS------AVYFISSLLLRARGMGP-ALIVSPLLSLMRDQVEAASRAGVRAAMVNSAnvtEWDEIRTRLETDEL-- 137
Cdd:PTZ00110 176 TGSGKTlafllpAIVHINAQPLLRYGDGPiVLVLAPTRELAEQIREQCNKFGASSKIRNTV---AYGGVPKRGQIYALrr 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 138 --DVLLVGPERLNNpaFREQWLPYLLpRLGLLVIDEAHCISDWGhdFRPDYRRIGSLIKslpvgvP---VLATTATANDR 212
Cdd:PTZ00110 253 gvEILIACPGRLID--FLESNVTNLR-RVTYLVLDEADRMLDMG--FEPQIRKIVSQIR------PdrqTLMWSATWPKE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 213 V---SRDIAEQlstdtAPVHVIRGPL---SRESLRLGVLTLpDEAQRIGWLLTHLNDLPGSG---IIYTLTVSAAEDTAN 283
Cdd:PTZ00110 322 VqslARDLCKE-----EPVHVNVGSLdltACHNIKQEVFVV-EEHEKRGKLKMLLQRIMRDGdkiLIFVETKKGADFLTK 395
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896426751 284 ALRASGYEVLAYTGKTDPDERLVAEQALKENRVKALVATSALGMGFDKPDLGFVVHLGAPSSAVSYYQQIGRAGRG 359
Cdd:PTZ00110 396 ELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRA 471
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
35-424 |
5.01e-08 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 56.43 E-value: 5.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 35 LTDVADAEFHDGQYEAIRALVADRARTVVVQrTGWGKSAVYFISSLLLRARGMGPALIVsPLLSLMRDQVEAASRA---G 111
Cdd:PRK01172 15 LFTGNDFELYDHQRMAIEQLRKGENVIVSVP-TAAGKTLIAYSAIYETFLAGLKSIYIV-PLRSLAMEKYEELSRLrslG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 112 VRAAMvnsaNVTEWDEIRTRLETDelDVLLVGPERLNNPAFREqwlPYLLPRLGLLVIDEAHCISDwgHDFRPDYRRIGS 191
Cdd:PRK01172 93 MRVKI----SIGDYDDPPDFIKRY--DVVILTSEKADSLIHHD---PYIINDVGLIVADEIHIIGD--EDRGPTLETVLS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 192 LIKSLPVGVPVLATTATANDrvSRDIAEQLSTDTA-----PVHVIRGPLSRESLRLgvltlpDEAQR----IGWLLTHLN 262
Cdd:PRK01172 162 SARYVNPDARILALSATVSN--ANELAQWLNASLIksnfrPVPLKLGILYRKRLIL------DGYERsqvdINSLIKETV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 263 DLPGSGIIYTLTVSAAEDTA----------NALRASGYEVLAY----------------TGKTDPDERLVaEQALKENRV 316
Cdd:PRK01172 234 NDGGQVLVFVSSRKNAEDYAemliqhfpefNDFKVSSENNNVYddslnemlphgvafhhAGLSNEQRRFI-EEMFRNRYI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 317 KALVATSALGMGFDKP-------DLGFVVHLG-APSSAVSYYQQIGRAGRgavnadvlllPGREDRAIWEYFATAsmPNE 388
Cdd:PRK01172 313 KVIVATPTLAAGVNLParlvivrDITRYGNGGiRYLSNMEIKQMIGRAGR----------PGYDQYGIGYIYAAS--PAS 380
|
410 420 430
....*....|....*....|....*....|....*.
gi 896426751 389 EQalAVLDALAQAPEGLsITALEARVQLRRSTLELL 424
Cdd:PRK01172 381 YD--AAKKYLSGEPEPV-ISYMGSQRKVRFNTLAAI 413
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
300-357 |
5.94e-08 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 56.26 E-value: 5.94e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 896426751 300 DPDERLVAEQALKENRVKALVATSALGMGFDKPDLGFVVHLGAPSSAVSYYQQIGRAG 357
Cdd:COG1201 311 SREQRLEVEEALKAGELRAVVATSSLELGIDIGDVDLVIQVGSPKSVARLLQRIGRAG 368
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
137-368 |
1.33e-07 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 54.81 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 137 LDVLLVGPERLNNpafREQWLPYLLPRLGLLVIDEAHCISDWGhdFRPDYRRIgslIKSLPVGVPVLATTATANDRVsRD 216
Cdd:PRK10590 126 VDVLVATPGRLLD---LEHQNAVKLDQVEILVLDEADRMLDMG--FIHDIRRV---LAKLPAKRQNLLFSATFSDDI-KA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 217 IAEQLSTDTAPVHVIRGPLSRESLRLGVLTLpdEAQRIGWLLTHLndlPGSG-----IIYTLTVSAAEDTANALRASGYE 291
Cdd:PRK10590 197 LAEKLLHNPLEIEVARRNTASEQVTQHVHFV--DKKRKRELLSQM---IGKGnwqqvLVFTRTKHGANHLAEQLNKDGIR 271
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896426751 292 VLAYTGKTDPDERLVAEQALKENRVKALVATSALGMGFDKPDLGFVVHLGAPSSAVSYYQQIGRAGRGAVNADVLLL 368
Cdd:PRK10590 272 SAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSL 348
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
66-373 |
2.41e-07 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 53.76 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 66 RTGWGKSAVYFIS--SLLL-------RARGMGPALIVSPLLSLMRdQVEAASRAGVRAAMVNSANVT---EWDEIRTRLE 133
Cdd:PRK01297 132 QTGTGKTAAFLISiiNQLLqtpppkeRYMGEPRALIIAPTRELVV-QIAKDAAALTKYTGLNVMTFVggmDFDKQLKQLE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 134 TDELDVLLVGPERLNNpaFREQWLPYLlPRLGLLVIDEAHCISDWGhdFRPDYRRIgslIKSLPVGVP--VLATTATAND 211
Cdd:PRK01297 211 ARFCDILVATPGRLLD--FNQRGEVHL-DMVEVMVLDEADRMLDMG--FIPQVRQI---IRQTPRKEErqTLLFSATFTD 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 212 RVsRDIAEQLSTDTAPVHVIRGPLSRESLRLGVLTLPdEAQRIGWLLTHLNDLP-GSGIIYTLTVSAAEDTANALRASGY 290
Cdd:PRK01297 283 DV-MNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVA-GSDKYKLLYNLVTQNPwERVMVFANRKDEVRRIEERLVKDGI 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 291 EVLAYTGKTDPDERLVAEQALKENRVKALVATSALGMGFDKPDLGFVVHLGAPSSAVSYYQQIGRAGRGAVNADVLLLPG 370
Cdd:PRK01297 361 NAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAG 440
|
...
gi 896426751 371 RED 373
Cdd:PRK01297 441 EDD 443
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
267-374 |
8.88e-07 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 52.16 E-value: 8.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 267 SGIIYTLTVSAAEDTANALRASGYEVLAYTGKTDPDERLVAEQALKENRVKALVATSALGMGFDKPDLGFVVHLGAPSSA 346
Cdd:PRK11634 247 AAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDS 326
|
90 100
....*....|....*....|....*....
gi 896426751 347 VSYYQQIGRAGR-GAVNADVLLLPGREDR 374
Cdd:PRK11634 327 ESYVHRIGRTGRaGRAGRALLFVENRERR 355
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
47-177 |
9.28e-07 |
|
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: 49.57 E-value: 9.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 47 QYEAIRALVADRARTVVVQRTGWGKSAVYFISSLLLRARGMGPALIVSPLLSL----MRDQVEAASRAGVRAAMVNSanv 122
Cdd:cd17921 6 QREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATSGGKAVYIAPTRALvnqkEADLRERFGPLGKNVGLLTG--- 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 896426751 123 tewDEIRTRLETDELDVLLVGPERLNNPAFReqWLPYLLPRLGLLVIDEAHCISD 177
Cdd:cd17921 83 ---DPSVNKLLLAEADILVATPEKLDLLLRN--GGERLIQDVRLVVVDEAHLIGD 132
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
47-173 |
2.46e-06 |
|
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: 48.35 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 47 QYEAIRALVADRArTVVVQRTGWGKSAVYFISSL--LLRARGmGPALIVSPLLSLMRDQVEAASRagVRAAMVNSANVTE 124
Cdd:cd17923 5 QAEAIEAARAGRS-VVVTTGTASGKSLCYQLPILeaLLRDPG-SRALYLYPTKALAQDQLRSLRE--LLEQLGLGIRVAT 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 896426751 125 WD-----EIRTRLETDELDVLLVGPERLNNPAFR-EQWLPYLLPRLGLLVIDEAH 173
Cdd:cd17923 81 YDgdtprEERRAIIRNPPRILLTNPDMLHYALLPhHDRWARFLRNLRYVVLDEAH 135
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
286-357 |
8.13e-06 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 49.54 E-value: 8.13e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896426751 286 RASGYEVL---AYTGKTDPDERLVAEQALKENRVKALVATSALGMGFDKPDLGFVVHLGAPSSAVSYYQQIGRAG 357
Cdd:PRK09751 295 RVQSSDVFiarSHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
42-189 |
4.11e-05 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 44.59 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 42 EFHDGQYEAIRALVA----DRARTVVVQRTGWGKSAVYF-ISSLLLRARGMGPALIVSPLLSLMRDQVEAASRAGVRAAM 116
Cdd:pfam04851 3 ELRPYQIEAIENLLEsiknGQKRGLIVMATGSGKTLTAAkLIARLFKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYVE 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896426751 117 VNsanvTEWDEIRTRLETDELDVLLVGPERLNNPaFREQWLPYLLPRLGLLVIDEAHcisdwgHDFRPDYRRI 189
Cdd:pfam04851 83 IG----EIISGDKKDESVDDNKIVVTTIQSLYKA-LELASLELLPDFFDVIIIDEAH------RSGASSYRNI 144
|
|
| HTH_ICLR |
smart00346 |
helix_turn_helix isocitrate lyase regulation; |
385-438 |
9.70e-05 |
|
helix_turn_helix isocitrate lyase regulation;
Pssm-ID: 214629 [Multi-domain] Cd Length: 91 Bit Score: 41.80 E-value: 9.70e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 896426751 385 MPNEEQALAVLDALAQAPEGLSITALEARVQLRRSTLELLLKVLDVEGAVVKEG 438
Cdd:smart00346 1 IQSLERGLAVLRALAEEPGGLTLAELAERLGLSKSTAHRLLNTLQELGYVEQDG 54
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
267-358 |
1.58e-04 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350186 [Multi-domain] Cd Length: 116 Bit Score: 41.78 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 267 SGIIYTLTVSAAEDTANALRASGYEVLAYTGKTDPDERLVAEQALKENR---VKALVATSALGMGFDKPDLGFVVHLGAP 343
Cdd:cd18799 8 KTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDEALILLFFGelkPPILVTVDLLTTGVDIPEVDNVVFLRPT 87
|
90
....*....|....*
gi 896426751 344 SSAVSYYQQIGRAGR 358
Cdd:cd18799 88 ESRTLFLQMLGRGLR 102
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
273-368 |
3.46e-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: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 273 LTVSAAEDTANALR---ASGYEVLAYTGKTDPDERLVAEQALKENRVKALVATSALGMGFDKPDLGFVVHLGAPSSAVSY 349
Cdd:cd18811 42 LDLKAAVAMYEYLKerfRPELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQ 121
|
90 100
....*....|....*....|
gi 896426751 350 YQQI-GRAGRGAVNADVLLL 368
Cdd:cd18811 122 LHQLrGRVGRGDHQSYCLLV 141
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
61-358 |
3.97e-04 |
|
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
Pssm-ID: 187770 [Multi-domain] Cd Length: 353 Bit Score: 43.19 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 61 TVVVQRTGWGKS-AVYFISSLLLRARGMGPALIVSPLLSLMRDQ----VEAASRAGVRAAMVNSANVT------EWDEIR 129
Cdd:cd09639 2 LVIEAPTGYGKTeAALLWALHSLKSQKADRVIIALPTRATINAMyrraKEAFGETGLYHSSILSSRIKemgdseEFEHLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 130 TRLETDELDVLLvGPERLNNPafrEQWLPYLLPRLG------------LLVIDEAHcisdwghdFRPDYRRiGSLIKSLP 197
Cdd:cd09639 82 PLYIHSNDTLFL-DPITVCTI---DQVLKSVFGEFGhyeftlasiansLLIFDEVH--------FYDEYTL-ALILAVLE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 198 V----GVPVLATTATANDRVSR-----DIAEQLST-DTAPVHvirgpLSRESLRLGVlTLPDEAQrIGWLLTHLNDlPGS 267
Cdd:cd09639 149 VlkdnDVPILLMSATLPKFLKEyaekiGYVEENEPlDLKPNE-----RAPFIKIESD-KVGEISS-LERLLEFIKK-GGS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 268 GIIYTLTVSAAEDTANALRASGYEV--------LAYTGKTDPDERLVAEQALKENRVkaLVATSALGMGFDKpDLGFVVH 339
Cdd:cd09639 221 VAIIVNTVDRAQEFYQQLKEKGPEEeimlihsrFTEKDRAKKEAELLLEFKKSEKFV--IVATQVIEASLDI-SVDVMIT 297
|
330
....*....|....*....
gi 896426751 340 LGAPSSAVsyyqqIGRAGR 358
Cdd:cd09639 298 ELAPIDSL-----IQRLGR 311
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
232-358 |
5.80e-04 |
|
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB 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: 350176 [Multi-domain] Cd Length: 153 Bit Score: 41.08 E-value: 5.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 232 RGPLSRESLRLGVLTlPDEAQRIGWLLT-HLNDlpGSGIIYTLTVSAAEDTANALRASgyevlAYTGKTDPDERLVAEQA 310
Cdd:cd18789 18 GLGAHRKRRLLAAMN-PNKLRALEELLKrHEQG--DKIIVFTDNVEALYRYAKRLLKP-----FITGETPQSEREEILQN 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 896426751 311 LKENRVKALVATSALGMGFDKPDLGFVVHLGapSSAVSYYQQIGRAGR 358
Cdd:cd18789 90 FREGEYNTLVVSKVGDEGIDLPEANVAIQIS--GHGGSRRQEAQRLGR 135
|
|
| DEXHc_Snf |
cd17919 |
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ... |
68-187 |
7.89e-04 |
|
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350677 [Multi-domain] Cd Length: 182 Bit Score: 41.01 E-value: 7.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 68 GWGKS--AVYFISSLLLRARGMGPALIVSPLLSLMRDQVEAASRA-GVRAAMVNSANVTEwDEIRTRLETDELDVLLVGP 144
Cdd:cd17919 29 GLGKTlqAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTpDLRVVVYHGSQRER-AQIRAKEKLDKFDVVLTTY 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 896426751 145 ERLNNPAFREQWLPYllprlGLLVIDEAHCISDWG-------HDFRPDYR 187
Cdd:cd17919 108 ETLRRDKASLRKFRW-----DLVVVDEAHRLKNPKsqlskalKALRAKRR 152
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
167-359 |
8.03e-04 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 42.62 E-value: 8.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 167 LVIDEAHCISDWGhdFRPDYRRIG--------SLIKSlpvgvpvlattATANDRVSRDIAEQLSTDtaPVHVIRGPLSRE 238
Cdd:PRK11192 151 LILDEADRMLDMG--FAQDIETIAaetrwrkqTLLFS-----------ATLEGDAVQDFAERLLND--PVEVEAEPSRRE 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 239 slRLGVLT---LPDEAQRIGWLLTHL--NDLPGSGIIYTLTVSAAEDTANALRASGYEVLAYTGKTDPDERLVAEQALKE 313
Cdd:PRK11192 216 --RKKIHQwyyRADDLEHKTALLCHLlkQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTD 293
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 896426751 314 NRVKALVATSALGMGFDKPDLGFVVHLGAPSSAVSYYQQIGRAGRG 359
Cdd:PRK11192 294 GRVNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRA 339
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
47-177 |
1.24e-03 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type 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: 350786 [Multi-domain] Cd Length: 177 Bit Score: 40.40 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 47 QYEAIRALVADRARTVVVQRTGWGKSAVYFISSLLLRARGmGPALIVSPLLSL-------MRDQVEAASRAGVRAAMVNS 119
Cdd:cd18028 6 QAEAVRAGLLKGENLLISIPTASGKTLIAEMAMVNTLLEG-GKALYLVPLRALasekyeeFKKLEEIGLKVGISTGDYDE 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896426751 120 --ANVTEWDEIRTRLEtdELDVLL-VGPERLNNpafreqwlpyllprLGLLVIDEAHCISD 177
Cdd:cd18028 85 ddEWLGDYDIIVATYE--KFDSLLrHSPSWLRD--------------VGVVVVDEIHLISD 129
|
|
| HTH_IclR |
pfam09339 |
IclR helix-turn-helix domain; |
391-438 |
2.85e-03 |
|
IclR helix-turn-helix domain;
Pssm-ID: 430539 [Multi-domain] Cd Length: 52 Bit Score: 36.23 E-value: 2.85e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 896426751 391 ALAVLDALAQAPEGLSITALEARVQLRRSTLELLLKVLDVEGAVVKEG 438
Cdd:pfam09339 5 ALAILDALAEAPGPLTLTEIARRTGLPKSTAHRLLQTLVELGYVEQDP 52
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
51-366 |
3.68e-03 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 40.70 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 51 IRAL---VADRARTVVVQ-RTGWGKSAVYFISSL--LLRARGMGP-------ALIVSPL----LSLMRDQVEAASRAGVR 113
Cdd:PRK04537 35 IQALtlpVALPGGDVAGQaQTGTGKTLAFLVAVMnrLLSRPALADrkpedprALILAPTrelaIQIHKDAVKFGADLGLR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 114 AAMVNSAnvTEWDEIRTRLETDeLDVLLVGPERLNNpaFREQWLPYLLPRLGLLVIDEAHCISDWGhdFRPDYRrigSLI 193
Cdd:PRK04537 115 FALVYGG--VDYDKQRELLQQG-VDVIIATPGRLID--YVKQHKVVSLHACEICVLDEADRMFDLG--FIKDIR---FLL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 194 KSLP--VGVPVLATTATANDRV------SRDIAEQLSTDTAPVHVIRgplSRESLrlgvlTLPDEAQRIGWLLTHLNDLP 265
Cdd:PRK04537 185 RRMPerGTRQTLLFSATLSHRVlelayeHMNEPEKLVVETETITAAR---VRQRI-----YFPADEEKQTLLLGLLSRSE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 266 GS-GIIYTLTVSAAEDTANALRASGYEVLAYTGKTDPDERLVAEQALKENRVKALVATSALGMGFDKPDLGFVVHLGAPS 344
Cdd:PRK04537 257 GArTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVYNYDLPF 336
|
330 340
....*....|....*....|..
gi 896426751 345 SAVSYYQQIGRAGRGAVNADVL 366
Cdd:PRK04537 337 DAEDYVHRIGRTARLGEEGDAI 358
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
160-358 |
4.10e-03 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 40.19 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 160 LLPRLGLLVIDEAHCISDWGhdFRPdyrRIGSLIKSLPVGVPVLATTATANDRVsRDIAEQLSTDTAPVHVIRGPLSRES 239
Cdd:PTZ00424 167 RVDDLKLFILDEADEMLSRG--FKG---QIYDVFKKLPPDVQVALFSATMPNEI-LELTTKFMRDPKRILVKKDELTLEG 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896426751 240 LRLGVLTLPDEAqrigWLLTHLNDLPGS-----GIIYTLTVSAAEDTANALRASGYEVLAYTGKTDPDERLVAEQALKEN 314
Cdd:PTZ00424 241 IRQFYVAVEKEE----WKFDTLCDLYETltitqAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSG 316
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 896426751 315 RVKALVATSALGMGFDKPDLGFVVHLGAPSSAVSYYQQIGRAGR 358
Cdd:PTZ00424 317 STRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGR 360
|
|
| |
