|
Name |
Accession |
Description |
Interval |
E-value |
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
42-477 |
0e+00 |
|
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are known are 3'-5' DNA-DNA helicases. These proteins are used for recombination, recombinational repair, and possibly maintenance of chromosome stability. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129701 [Multi-domain] Cd Length: 470 Bit Score: 795.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 42 YGKSLCFQYPPVYVGKIGLVISPLISLMEDQVLQLKMSNIPACFLGSAQSEN----VLTDIKLGKYRIVYVTPEYCSGNM 117
Cdd:TIGR00614 37 GGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATFLNSAQTKEqqlnVLTDLKDGKIKLLYVTPEKISASN 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 118 GLLQQLEADIGITLIAVDEAHCISEWGHDFRDSFRKLGSLKTALPMVPIVALTATASSSIREDIVRCLNLRNPQITCTGF 197
Cdd:TIGR00614 117 RLLQTLEERKGITLIAVDEAHCISQWGHDFRPDYKALGSLKQKFPNVPVMALTATASPSVREDILRQLNLLNPQIFCTSF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 198 DRPNLYLEVRRKTGNILQDLQPFLVKtsshwEFEGPT-IIYCPSRKMTQQVTGELRKLNLSCGTYHAGMSFSTRKDIHHR 276
Cdd:TIGR00614 197 DRPNLYYEVRRKTPKILEDLLRFIRK-----EFEGKSgIIYCPSRKKVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHK 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 277 FVRDEIQCVIATIAFGMGINKADIRQVIHYGAPKDMESYYQEIGRAGRDGLQSSCHVLWAPADINLNRHLLTEIRNEKFR 356
Cdd:TIGR00614 272 FQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECHLFYAPADMNRLRRLLMEEPDGNFR 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 357 LYKLKMMAKMEKYLHSSRCRRQIILSHFEDKQVQKaSLGIMGTEKCCDNCRSRLDHCYsmDDSEDTSWDFGPQAFKLLSA 436
Cdd:TIGR00614 352 TYKLKLYEMMEYCLNSSTCRRLILLSYFGEKGFNK-SFCIMGTEKCCDNCCKRLDYKT--KDVTDKVYDFGPQAQKALSA 428
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 767951195 437 VDILGEKFGIGLPILFLRGSNSQRLAD-QYRRHSLFGTGKDQ 477
Cdd:TIGR00614 429 VGRLNQKFGMGYPVDFLRGSNSQKIRDgGFRKHSLYGRGKDE 470
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
43-494 |
1.14e-165 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 491.58 E-value: 1.14e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 43 GKSLCFQYPPVYVGKIGLVISPLISLMEDQVLQLKMSNIPACFLGSAQSEN----VLTDIKLGKYRIVYVTPEYCSgNMG 118
Cdd:COG0514 44 GKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGIRAAFLNSSLSAEerreVLRALRAGELKLLYVAPERLL-NPR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 119 LLQQLeADIGITLIAVDEAHCISEWGHDFRDSFRKLGSLKTALPMVPIVALTATASSSIREDIVRCLNLRNPQITCTGFD 198
Cdd:COG0514 123 FLELL-RRLKISLFAIDEAHCISQWGHDFRPDYRRLGELRERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 199 RPNLYLEVRRKTG-NILQDLQPFLVKTSshwefEGPTIIYCPSRKMTQQVTGELRKLNLSCGTYHAGMSFSTRKDIHHRF 277
Cdd:COG0514 202 RPNLRLEVVPKPPdDKLAQLLDFLKEHP-----GGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRF 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 278 VRDEIQCVIATIAFGMGINKADIRQVIHYGAPKDMESYYQEIGRAGRDGLQSSCHVLWAPADINLNRHLLTEIRN-EKFR 356
Cdd:COG0514 277 LRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIEQSPPdEERK 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 357 LYKLKMMAKMEKYLHSSRCRRQIILSHFEDKQvqkaslgimgTEKC--CDNCRsrldhcysmddSEDTSWDFGPQAFKLL 434
Cdd:COG0514 357 RVERAKLDAMLAYAETTGCRRQFLLRYFGEEL----------AEPCgnCDNCL-----------GPPETFDGTEAAQKAL 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767951195 435 SAVDILGEKFGIGLPILFLRGSNSQRLADQ-YRRHSLFGTGKDQTESWWKAFSRQLITEGF 494
Cdd:COG0514 416 SCVYRTGQRFGAGHVIDVLRGSKNEKIRQFgHDKLSTYGIGKDLSDKEWRSVIRQLLAQLF 476
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
43-687 |
2.10e-116 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 367.89 E-value: 2.10e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 43 GKSLCFQYPPVYVGKIGLVISPLISLMEDQVLQLKMSNIPACFLGSAQSE----NVLTDIKLGKYRIVYVTPEYCSGNmG 118
Cdd:PRK11057 52 GKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVAAACLNSTQTReqqlEVMAGCRTGQIKLLYIAPERLMMD-N 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 119 LLQQLeADIGITLIAVDEAHCISEWGHDFRDSFRKLGSLKTALPMVPIVALTATASSSIREDIVRCLNLRNPQITCTGFD 198
Cdd:PRK11057 131 FLEHL-AHWNPALLAVDEAHCISQWGHDFRPEYAALGQLRQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 199 RPNLylevrRKTgnILQDLQPflvkTSSHWEF----EGPT-IIYCPSRKMTQQVTGELRKLNLSCGTYHAGMSFSTRKDI 273
Cdd:PRK11057 210 RPNI-----RYT--LVEKFKP----LDQLMRYvqeqRGKSgIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 274 HHRFVRDEIQCVIATIAFGMGINKADIRQVIHYGAPKDMESYYQEIGRAGRDGLQSSCHVLWAPADINLNRHLLTEIRNE 353
Cdd:PRK11057 279 QEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPADMAWLRRCLEEKPAG 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 354 KFRLYKLKMMAKMEKYLHSSRCRRQIILSHFEDkqvqkaslgimGTEKCCDNCRSRLDHCYSMDDSEDtswdfgpqAFKL 433
Cdd:PRK11057 359 QQQDIERHKLNAMGAFAEAQTCRRLVLLNYFGE-----------GRQEPCGNCDICLDPPKQYDGLED--------AQKA 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 434 LSAVDILGEKFGIGLPILFLRGSNSQRLAD-QYRRHSLFGTGKDQTESWWKAFSRQLITEGFLVE-VSRYNKfmkicalt 511
Cdd:PRK11057 420 LSCIYRVNQRFGMGYVVEVLRGANNQRIRDyGHDKLKVYGIGRDKSHEHWVSVIRQLIHLGLVTQnIAQHSA-------- 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 512 kkgrnwlhkantesqsliLQANEELCPkklllpssktVSSGtkehcynQVPVELSTEKKSNLEKLYSYKpcdkiSSGSNI 591
Cdd:PRK11057 492 ------------------LQLTEAARP----------VLRG-------EVSLQLAVPRIVALKPRAMQK-----SFGGNY 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 592 SKKsimvqspekaysssqpvisaqeqetqivLYGKLVEARQKHANKMDVPPAILATNKILVDMAKMRPTTVENVKRIDGV 671
Cdd:PRK11057 532 DRK----------------------------LFAKLRKLRKSIADEENIPPYVVFNDATLIEMAEQMPITASEMLSVNGV 583
|
650
....*....|....*..
gi 767951195 672 SEGKAAMLA-PLLEVIK 687
Cdd:PRK11057 584 GQRKLERFGkPFMALIR 600
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
42-198 |
4.92e-95 |
|
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: 296.69 E-value: 4.92e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 42 YGKSLCFQYPPVYVGKIGLVISPLISLMEDQVLQLKMSNIPACFLGSAQSENVLTDIKLGKYRIVYVTPEYCSGNMGLLQ 121
Cdd:cd18017 39 YGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPACFLGSAQSQNVLDDIKMGKIRVIYVTPEFVSKGLELLQ 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767951195 122 QLEAdiGITLIAVDEAHCISEWGHDFRDSFRKLGSLKTALPMVPIVALTATASSSIREDIVRCLNLRNPQITCTGFD 198
Cdd:cd18017 119 QLRN--GITLIAIDEAHCVSQWGHDFRSSYRHLGSIRNRLPNVPIVALTATATPSVRDDIIKNLNLRNPQITCTSFD 193
|
|
| DpdF |
NF041063 |
protein DpdF; |
43-354 |
1.66e-34 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 141.97 E-value: 1.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 43 GKSLCFQYPPVYVGKIG---LVISPLISLMEDQVLQLK-MSNIPACFLG------SAQSEN----VLTDIKLGKYRIVYV 108
Cdd:NF041063 170 GKSLVAQAPALLASRQGgltLVVVPTVALAIDQERRAReLLRRAGPDLGgplawhGGLSAEeraaIRQRIRDGTQRILFT 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 109 TPEycSGNMGLLQQLE--ADIG-ITLIAVDEAHCISEWGHDFRDSFRKLGSLKTALPMV-----PI--VALTATASSSIR 178
Cdd:NF041063 250 SPE--SLTGSLRPALFdaAEAGlLRYLVVDEAHLVDQWGDGFRPEFQLLAGLRRSLLRLapsgrPFrtLLLSATLTESTL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 179 E---------DIVRCLN---LRN-PQITCTGFDRPNLYLE-----VRRktgnilqdlqpfLVKtsshwefegPTIIYCPS 240
Cdd:NF041063 328 DtletlfgppGPFIVVSavqLRPePAYWVAKCDSEEERRErvleaLRH------------LPR---------PLILYVTK 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 241 RKMTQQVTGELRKLNLS-CGTYHAGMSFSTRKDIHHRFVRDEIQCVIATIAFGMGINKADIRQVIHYGAPKDMESYYQEI 319
Cdd:NF041063 387 VEDAEAWLQRLRAAGFRrVALFHGDTPDAERERLIEQWRENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEV 466
|
330 340 350
....*....|....*....|....*....|....*..
gi 767951195 320 GRAGRDGLQSSCHVLWAPADINLNRHLLTE--IRNEK 354
Cdd:NF041063 467 GRGGRDGKASLSLLIYTPDDLDIAKSLNRPklISVEK 503
|
|
| RQC |
smart00956 |
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix ... |
425-518 |
3.04e-26 |
|
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix structure; The RQC domain, found only in RecQ family enzymes, is a high affinity G4 DNA binding domain.
Pssm-ID: 214936 [Multi-domain] Cd Length: 92 Bit Score: 103.32 E-value: 3.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 425 DFGPQAFKLLSAVDILGEKFGIGLPILFLRGSNSQRLADQ-YRRHSLFGTGKDQTESWWKAFSRQLITEGFLVEvsrYNK 503
Cdd:smart00956 1 DVTEEAQKLLSCVYRTGQRFGAGHVIDVLRGSKNKKIRQKgHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLRE---DGG 77
|
90
....*....|....*
gi 767951195 504 FMKICALTKKGRNWL 518
Cdd:smart00956 78 RYPYLKLTEKARPVL 92
|
|
| HTH_40 |
pfam14493 |
Helix-turn-helix domain; This presumed domain is found at the C-terminus of a large number of ... |
725-819 |
9.00e-21 |
|
Helix-turn-helix domain; This presumed domain is found at the C-terminus of a large number of helicase proteins.
Pssm-ID: 464189 Cd Length: 89 Bit Score: 87.56 E-value: 9.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 725 SMAITYSLFQEKkMPLKSIAESRILPLMTIGMHLSQAVKAGCPLDLERAgLTPEVQKIIADVIRNPPVNSdmskISLIRM 804
Cdd:pfam14493 1 SAEITLELYKEG-LSIEEIAEERGLKESTIEGHLAELIEAGEPVDIERL-VSEEEQKEILDAIEKLGSES----LKPIKE 74
|
90
....*....|....*
gi 767951195 805 LVPENIDTYLIHMAI 819
Cdd:pfam14493 75 ALPEEISYFEIRLVL 89
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
229-326 |
1.66e-19 |
|
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: 84.57 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 229 EFEGPTIIYCPSRKMTQqvTGEL-RKLNLSCGTYHAGMSFSTRKDIHHRFVRDEIQCVIATIAFGMGINKADIRQVIHYG 307
Cdd:pfam00271 13 ERGGKVLIFSQTKKTLE--AELLlEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVINYD 90
|
90
....*....|....*....
gi 767951195 308 APKDMESYYQEIGRAGRDG 326
Cdd:pfam00271 91 LPWNPASYIQRIGRAGRAG 109
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
623-696 |
5.56e-18 |
|
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the HRDC domain cause human disease.
Pssm-ID: 128635 [Multi-domain] Cd Length: 81 Bit Score: 79.26 E-value: 5.56e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767951195 623 LYGKLVEARQKHANKMDVPPAILATNKILVDMAKMRPTTVENVKRIDGVSEGKAAMLAP-LLEVIKHFCQTNSVQ 696
Cdd:smart00341 7 LLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKdLLAVIQEASDSPSEA 81
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
620-686 |
6.88e-12 |
|
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic acid binding. Mutations in the HRDC domain cause human disease. It is interesting to note that the RecQ helicase in Deinococcus radiodurans has three tandem HRDC domains.
Pssm-ID: 425755 [Multi-domain] Cd Length: 68 Bit Score: 61.40 E-value: 6.88e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767951195 620 QIVLYGKLVEARQKHANKMDVPPAILATNKILVDMAKMRPTTVENVKRIDGVSEGKAAMLAP-LLEVI 686
Cdd:pfam00570 1 QLALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEeILAAI 68
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
42-477 |
0e+00 |
|
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are known are 3'-5' DNA-DNA helicases. These proteins are used for recombination, recombinational repair, and possibly maintenance of chromosome stability. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129701 [Multi-domain] Cd Length: 470 Bit Score: 795.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 42 YGKSLCFQYPPVYVGKIGLVISPLISLMEDQVLQLKMSNIPACFLGSAQSEN----VLTDIKLGKYRIVYVTPEYCSGNM 117
Cdd:TIGR00614 37 GGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATFLNSAQTKEqqlnVLTDLKDGKIKLLYVTPEKISASN 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 118 GLLQQLEADIGITLIAVDEAHCISEWGHDFRDSFRKLGSLKTALPMVPIVALTATASSSIREDIVRCLNLRNPQITCTGF 197
Cdd:TIGR00614 117 RLLQTLEERKGITLIAVDEAHCISQWGHDFRPDYKALGSLKQKFPNVPVMALTATASPSVREDILRQLNLLNPQIFCTSF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 198 DRPNLYLEVRRKTGNILQDLQPFLVKtsshwEFEGPT-IIYCPSRKMTQQVTGELRKLNLSCGTYHAGMSFSTRKDIHHR 276
Cdd:TIGR00614 197 DRPNLYYEVRRKTPKILEDLLRFIRK-----EFEGKSgIIYCPSRKKVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHK 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 277 FVRDEIQCVIATIAFGMGINKADIRQVIHYGAPKDMESYYQEIGRAGRDGLQSSCHVLWAPADINLNRHLLTEIRNEKFR 356
Cdd:TIGR00614 272 FQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECHLFYAPADMNRLRRLLMEEPDGNFR 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 357 LYKLKMMAKMEKYLHSSRCRRQIILSHFEDKQVQKaSLGIMGTEKCCDNCRSRLDHCYsmDDSEDTSWDFGPQAFKLLSA 436
Cdd:TIGR00614 352 TYKLKLYEMMEYCLNSSTCRRLILLSYFGEKGFNK-SFCIMGTEKCCDNCCKRLDYKT--KDVTDKVYDFGPQAQKALSA 428
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 767951195 437 VDILGEKFGIGLPILFLRGSNSQRLAD-QYRRHSLFGTGKDQ 477
Cdd:TIGR00614 429 VGRLNQKFGMGYPVDFLRGSNSQKIRDgGFRKHSLYGRGKDE 470
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
43-494 |
1.14e-165 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 491.58 E-value: 1.14e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 43 GKSLCFQYPPVYVGKIGLVISPLISLMEDQVLQLKMSNIPACFLGSAQSEN----VLTDIKLGKYRIVYVTPEYCSgNMG 118
Cdd:COG0514 44 GKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGIRAAFLNSSLSAEerreVLRALRAGELKLLYVAPERLL-NPR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 119 LLQQLeADIGITLIAVDEAHCISEWGHDFRDSFRKLGSLKTALPMVPIVALTATASSSIREDIVRCLNLRNPQITCTGFD 198
Cdd:COG0514 123 FLELL-RRLKISLFAIDEAHCISQWGHDFRPDYRRLGELRERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 199 RPNLYLEVRRKTG-NILQDLQPFLVKTSshwefEGPTIIYCPSRKMTQQVTGELRKLNLSCGTYHAGMSFSTRKDIHHRF 277
Cdd:COG0514 202 RPNLRLEVVPKPPdDKLAQLLDFLKEHP-----GGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRF 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 278 VRDEIQCVIATIAFGMGINKADIRQVIHYGAPKDMESYYQEIGRAGRDGLQSSCHVLWAPADINLNRHLLTEIRN-EKFR 356
Cdd:COG0514 277 LRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIEQSPPdEERK 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 357 LYKLKMMAKMEKYLHSSRCRRQIILSHFEDKQvqkaslgimgTEKC--CDNCRsrldhcysmddSEDTSWDFGPQAFKLL 434
Cdd:COG0514 357 RVERAKLDAMLAYAETTGCRRQFLLRYFGEEL----------AEPCgnCDNCL-----------GPPETFDGTEAAQKAL 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767951195 435 SAVDILGEKFGIGLPILFLRGSNSQRLADQ-YRRHSLFGTGKDQTESWWKAFSRQLITEGF 494
Cdd:COG0514 416 SCVYRTGQRFGAGHVIDVLRGSKNEKIRQFgHDKLSTYGIGKDLSDKEWRSVIRQLLAQLF 476
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
19-687 |
3.05e-133 |
|
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: 411.39 E-value: 3.05e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 19 GQHPMKSKLLASRCTLAI-PVLNryGKSLCFQYPPVYVGKIGLVISPLISLMEDQVLQLKMSNIPACFLGSAQS----EN 93
Cdd:TIGR01389 17 GQEEIISHVLDGRDVLVVmPTGG--GKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAAAYLNSTLSakeqQD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 94 VLTDIKLGKYRIVYVTPEycsgnmGLLQ----QLEADIGITLIAVDEAHCISEWGHDFRDSFRKLGSLKTALPMVPIVAL 169
Cdd:TIGR01389 95 IEKALVNGELKLLYVAPE------RLEQdyflNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERFPQVPRIAL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 170 TATASSSIREDIVRCLNLRNPQITCTGFDRPNLYLEVRRKTgNILQDLQPFLVKtssHWEFEGptIIYCPSRKMTQQVTG 249
Cdd:TIGR01389 169 TATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKN-NKQKFLLDYLKK---HRGQSG--IIYASSRKKVEELAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 250 ELRKLNLSCGTYHAGMSFSTRKDIHHRFVRDEIQCVIATIAFGMGINKADIRQVIHYGAPKDMESYYQEIGRAGRDGLQS 329
Cdd:TIGR01389 243 RLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDGLPA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 330 SCHVLWAPADINLNRHLLTEirNEKFRLYKLKMMAK---MEKYLHSSRCRRQIILSHFEDKQVqkaslgimgtEKC--CD 404
Cdd:TIGR01389 323 EAILLYSPADIALLKRRIEQ--SEADDDYKQIEREKlraMIAYCETQTCRRAYILRYFGENEV----------EPCgnCD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 405 NCRsrldhcysmddSEDTSWDFGPQAFKLLSAVDILGEKFGIGLPILFLRGSNSQRLaDQYR--RHSLFGTGKDQTESWW 482
Cdd:TIGR01389 391 NCL-----------DPPKSYDATVEAQKALSCVYRMGQRFGVGYIIEVLRGSKNDKI-LQKGhdQLSTYGIGKDYTQKEW 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 483 KAFSRQLITEGFLVEvsrynkfmkicaltkkgrnwlhkANTESQSLILQaneelcpkklllPSSKTVSSgtkehcyNQVP 562
Cdd:TIGR01389 459 RSLIDQLIAEGLLTE-----------------------NDEIYIGLQLT------------EAARKVLK-------NEVE 496
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 563 VELSTEKKSNLEKLYSYKpcdkissgsniskksIMVQSPEKAysssqpvisaqeqetqivLYGKLVEARQKHANKMDVPP 642
Cdd:TIGR01389 497 VLLRPFKVVAKEKTRVQK---------------NLSVGVDNA------------------LFEALRELRKEQADEQNVPP 543
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 767951195 643 AILATNKILVDMAKMRPTTVENVKRIDGVSEGKAAMLAP-LLEVIK 687
Cdd:TIGR01389 544 YVIFSDSTLREMAEKRPATLNALLKIKGVGQNKLDRYGEaFLEVIR 589
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
43-687 |
2.10e-116 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 367.89 E-value: 2.10e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 43 GKSLCFQYPPVYVGKIGLVISPLISLMEDQVLQLKMSNIPACFLGSAQSE----NVLTDIKLGKYRIVYVTPEYCSGNmG 118
Cdd:PRK11057 52 GKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVAAACLNSTQTReqqlEVMAGCRTGQIKLLYIAPERLMMD-N 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 119 LLQQLeADIGITLIAVDEAHCISEWGHDFRDSFRKLGSLKTALPMVPIVALTATASSSIREDIVRCLNLRNPQITCTGFD 198
Cdd:PRK11057 131 FLEHL-AHWNPALLAVDEAHCISQWGHDFRPEYAALGQLRQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 199 RPNLylevrRKTgnILQDLQPflvkTSSHWEF----EGPT-IIYCPSRKMTQQVTGELRKLNLSCGTYHAGMSFSTRKDI 273
Cdd:PRK11057 210 RPNI-----RYT--LVEKFKP----LDQLMRYvqeqRGKSgIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 274 HHRFVRDEIQCVIATIAFGMGINKADIRQVIHYGAPKDMESYYQEIGRAGRDGLQSSCHVLWAPADINLNRHLLTEIRNE 353
Cdd:PRK11057 279 QEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPADMAWLRRCLEEKPAG 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 354 KFRLYKLKMMAKMEKYLHSSRCRRQIILSHFEDkqvqkaslgimGTEKCCDNCRSRLDHCYSMDDSEDtswdfgpqAFKL 433
Cdd:PRK11057 359 QQQDIERHKLNAMGAFAEAQTCRRLVLLNYFGE-----------GRQEPCGNCDICLDPPKQYDGLED--------AQKA 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 434 LSAVDILGEKFGIGLPILFLRGSNSQRLAD-QYRRHSLFGTGKDQTESWWKAFSRQLITEGFLVE-VSRYNKfmkicalt 511
Cdd:PRK11057 420 LSCIYRVNQRFGMGYVVEVLRGANNQRIRDyGHDKLKVYGIGRDKSHEHWVSVIRQLIHLGLVTQnIAQHSA-------- 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 512 kkgrnwlhkantesqsliLQANEELCPkklllpssktVSSGtkehcynQVPVELSTEKKSNLEKLYSYKpcdkiSSGSNI 591
Cdd:PRK11057 492 ------------------LQLTEAARP----------VLRG-------EVSLQLAVPRIVALKPRAMQK-----SFGGNY 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 592 SKKsimvqspekaysssqpvisaqeqetqivLYGKLVEARQKHANKMDVPPAILATNKILVDMAKMRPTTVENVKRIDGV 671
Cdd:PRK11057 532 DRK----------------------------LFAKLRKLRKSIADEENIPPYVVFNDATLIEMAEQMPITASEMLSVNGV 583
|
650
....*....|....*..
gi 767951195 672 SEGKAAMLA-PLLEVIK 687
Cdd:PRK11057 584 GQRKLERFGkPFMALIR 600
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
42-198 |
4.92e-95 |
|
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: 296.69 E-value: 4.92e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 42 YGKSLCFQYPPVYVGKIGLVISPLISLMEDQVLQLKMSNIPACFLGSAQSENVLTDIKLGKYRIVYVTPEYCSGNMGLLQ 121
Cdd:cd18017 39 YGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPACFLGSAQSQNVLDDIKMGKIRVIYVTPEFVSKGLELLQ 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767951195 122 QLEAdiGITLIAVDEAHCISEWGHDFRDSFRKLGSLKTALPMVPIVALTATASSSIREDIVRCLNLRNPQITCTGFD 198
Cdd:cd18017 119 QLRN--GITLIAIDEAHCVSQWGHDFRSSYRHLGSIRNRLPNVPIVALTATATPSVRDDIIKNLNLRNPQITCTSFD 193
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
43-574 |
1.18e-80 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 283.71 E-value: 1.18e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 43 GKSLCFQYPPVYVGKIGLVISPLISLMEDQVLQLKMSNIPACFLGS----AQSENVLTDI--KLGKYRIVYVTPEYCSGN 116
Cdd:PLN03137 487 GKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQANIPAASLSAgmewAEQLEILQELssEYSKYKLLYVTPEKVAKS 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 117 MGLLQQLEADIGITLIA---VDEAHCISEWGHDFRDSFRKLGSLKTALPMVPIVALTATASSSIREDIVRCLNLRNPQIT 193
Cdd:PLN03137 567 DSLLRHLENLNSRGLLArfvIDEAHCVSQWGHDFRPDYQGLGILKQKFPNIPVLALTATATASVKEDVVQALGLVNCVVF 646
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 194 CTGFDRPNLYLEVRRKTGNILQDLQPFLvkTSSHweFEGPTIIYCPSRKMTQQVTGELRKLNLSCGTYHAGMSFSTRKDI 273
Cdd:PLN03137 647 RQSFNRPNLWYSVVPKTKKCLEDIDKFI--KENH--FDECGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFV 722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 274 HHRFVRDEIQCVIATIAFGMGINKADIRQVIHYGAPKDMESYYQEIGRAGRDGLQSSCHVLWAPADINLNRHLLTEIRNE 353
Cdd:PLN03137 723 QKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGRAGRDGQRSSCVLYYSYSDYIRVKHMISQGGVE 802
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 354 KFRL---YKLKM------------MAKMEKYLHSS-RCRRQIILSHFEDKqvqkasLGIMGTEKCCDNCRSrldhCYSMD 417
Cdd:PLN03137 803 QSPMamgYNRMAssgriletntenLLRMVSYCENEvDCRRFLQLVHFGEK------FDSTNCKKTCDNCSS----SKSLI 872
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 418 DSEDTSwdfgpQAFKLLSAVDILGEKFGIGLPILFLRGSNSQRLadQYRRH---SLFGTGKDQTESWWKAFSRQLITEGF 494
Cdd:PLN03137 873 DKDVTE-----IARQLVELVKLTGERFSSAHILEVYRGSLNQYV--KKHRHetlSLHGAGKHLSKGEASRILHYLVTEDI 945
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 495 LVE-VSRYNKFMKICALTKKGRNWLHKANTESQSLILQaneelcpkkllLPSSKTVSSGTKEHCyNQVPVELSTEKKSNL 573
Cdd:PLN03137 946 LAEdVKKSDLYGSVSSLLKVNESKAYKLFSGGQTIIMR-----------FPSSVKASKPSKFEA-TPAKGPLTSGKQSTL 1013
|
.
gi 767951195 574 E 574
Cdd:PLN03137 1014 P 1014
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
43-198 |
6.51e-71 |
|
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: 232.81 E-value: 6.51e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 43 GKSLCFQYPPVYVGKIGLVISPLISLMEDQVLQLKMSNIPACFLGSAQS----ENVLTDIKLGKYRIVYVTPEYC--SGN 116
Cdd:cd17920 39 GKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAAALNSTLSpeekREVLLRIKNGQYKLLYVTPERLlsPDF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 117 MGLLQQLEADIGITLIAVDEAHCISEWGHDFRDSFRKLGSLKTALPMVPIVALTATASSSIREDIVRCLNLRNPQITCTG 196
Cdd:cd17920 119 LELLQRLPERKRLALIVVDEAHCVSQWGHDFRPDYLRLGRLRRALPGVPILALTATATPEVREDILKRLGLRNPVIFRAS 198
|
..
gi 767951195 197 FD 198
Cdd:cd17920 199 FD 200
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
199-335 |
2.00e-69 |
|
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: 225.94 E-value: 2.00e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 199 RPNLYLEVRRKTGNILQDLQPFLVKtssHWEFEGPTIIYCPSRKMTQQVTGELRKLNLSCGTYHAGMSFSTRKDIHHRFV 278
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDLLKRIK---VEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWL 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 767951195 279 RDEIQCVIATIAFGMGINKADIRQVIHYGAPKDMESYYQEIGRAGRDGLQSSCHVLW 335
Cdd:cd18794 78 RDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
43-198 |
1.19e-42 |
|
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: 154.45 E-value: 1.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 43 GKSLCFQYPPVYVGKIGLVISPLISLMEDQVLQLKMSNIPACFLGSAQS-ENV------LTDIKlGKYRIVYVTPEYCSG 115
Cdd:cd18015 45 GKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLGISATMLNASSSkEHVkwvhaaLTDKN-SELKLLYVTPEKIAK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 116 NMGLLQQLEA--DIG-ITLIAVDEAHCISEWGHDFRDSFRKLGSLKTALPMVPIVALTATASSSIREDIVRCLNLRNPQI 192
Cdd:cd18015 124 SKRFMSKLEKayNAGrLARIAIDEVHCCSQWGHDFRPDYKKLGILKRQFPNVPILGLTATATSKVLKDVQKILCIQKCLT 203
|
....*.
gi 767951195 193 TCTGFD 198
Cdd:cd18015 204 FTASFN 209
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
43-192 |
7.75e-38 |
|
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: 140.47 E-value: 7.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 43 GKSLCFQYP----PVYVGKIGLVISPLISLMEDQVLQLKMSNIPACF---LGSAQSENVLTDIKLGKYRIVYVTPEYCSG 115
Cdd:cd18018 39 GKSLCYQLPalllRRRGPGLTLVVSPLIALMKDQVDALPRAIKAAALnssLTREERRRILEKLRAGEVKILYVSPERLVN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 116 NMG--LLQQLEadiGITLIAVDEAHCISEWGHDFRDSFRKLGS-LKTALPMVPIVALTATASSSIREDIVRCLNLRNPQI 192
Cdd:cd18018 119 ESFreLLRQTP---PISLLVVDEAHCISEWSHNFRPDYLRLCRvLRELLGAPPVLALTATATKRVVEDIASHLGIPESGV 195
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
25-198 |
5.70e-36 |
|
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: 135.34 E-value: 5.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 25 SKLLASRCTLAIPVLNryGKSLCFQYPPVYVGKIGLVISPLISLMEDQVLQLKMSNIPACFLGSAQSENVLTDI--KLGK 102
Cdd:cd18016 28 AALLGEDCFVLMPTGG--GKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPATYLTGDKTDAEATKIylQLSK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 103 ----YRIVYVTPEYCSGNMGLLQQLEADIGITLIA---VDEAHCISEWGHDFRDSFRKLGSLKTALPMVPIVALTATASS 175
Cdd:cd18016 106 kdpiIKLLYVTPEKISASNRLISTLENLYERKLLArfvIDEAHCVSQWGHDFRPDYKRLNMLRQKFPSVPMMALTATATP 185
|
170 180
....*....|....*....|...
gi 767951195 176 SIREDIVRCLNLRNPQITCTGFD 198
Cdd:cd18016 186 RVQKDILNQLKMLRPQVFTMSFN 208
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
42-190 |
9.41e-35 |
|
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: 131.82 E-value: 9.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 42 YGKSLCFQYPPVYVGKIGLVISPLISLMEDQVLQLKMSNIPACFLGSAQS----ENVLTDIK--LGKYRIVYVTPEYCSG 115
Cdd:cd18014 40 AGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIRVDSLNSKLSaqerKRIIADLEseKPQTKFLYITPEMAAT 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767951195 116 N--MGLLQQLEADIGITLIAVDEAHCISEWGHDFRDSFRKLGSLKTALPMVPIVALTATASSSIREDIVRCLNLRNP 190
Cdd:cd18014 120 SsfQPLLSSLVSRNLLSYLVVDEAHCVSQWGHDFRPDYLRLGALRSRYGHVPWVALTATATPQVQEDIFAQLRLKKP 196
|
|
| DpdF |
NF041063 |
protein DpdF; |
43-354 |
1.66e-34 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 141.97 E-value: 1.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 43 GKSLCFQYPPVYVGKIG---LVISPLISLMEDQVLQLK-MSNIPACFLG------SAQSEN----VLTDIKLGKYRIVYV 108
Cdd:NF041063 170 GKSLVAQAPALLASRQGgltLVVVPTVALAIDQERRAReLLRRAGPDLGgplawhGGLSAEeraaIRQRIRDGTQRILFT 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 109 TPEycSGNMGLLQQLE--ADIG-ITLIAVDEAHCISEWGHDFRDSFRKLGSLKTALPMV-----PI--VALTATASSSIR 178
Cdd:NF041063 250 SPE--SLTGSLRPALFdaAEAGlLRYLVVDEAHLVDQWGDGFRPEFQLLAGLRRSLLRLapsgrPFrtLLLSATLTESTL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 179 E---------DIVRCLN---LRN-PQITCTGFDRPNLYLE-----VRRktgnilqdlqpfLVKtsshwefegPTIIYCPS 240
Cdd:NF041063 328 DtletlfgppGPFIVVSavqLRPePAYWVAKCDSEEERRErvleaLRH------------LPR---------PLILYVTK 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 241 RKMTQQVTGELRKLNLS-CGTYHAGMSFSTRKDIHHRFVRDEIQCVIATIAFGMGINKADIRQVIHYGAPKDMESYYQEI 319
Cdd:NF041063 387 VEDAEAWLQRLRAAGFRrVALFHGDTPDAERERLIEQWRENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEV 466
|
330 340 350
....*....|....*....|....*....|....*..
gi 767951195 320 GRAGRDGLQSSCHVLWAPADINLNRHLLTE--IRNEK 354
Cdd:NF041063 467 GRGGRDGKASLSLLIYTPDDLDIAKSLNRPklISVEK 503
|
|
| RQC |
smart00956 |
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix ... |
425-518 |
3.04e-26 |
|
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix structure; The RQC domain, found only in RecQ family enzymes, is a high affinity G4 DNA binding domain.
Pssm-ID: 214936 [Multi-domain] Cd Length: 92 Bit Score: 103.32 E-value: 3.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 425 DFGPQAFKLLSAVDILGEKFGIGLPILFLRGSNSQRLADQ-YRRHSLFGTGKDQTESWWKAFSRQLITEGFLVEvsrYNK 503
Cdd:smart00956 1 DVTEEAQKLLSCVYRTGQRFGAGHVIDVLRGSKNKKIRQKgHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLRE---DGG 77
|
90
....*....|....*
gi 767951195 504 FMKICALTKKGRNWL 518
Cdd:smart00956 78 RYPYLKLTEKARPVL 92
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
245-326 |
2.47e-23 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 94.59 E-value: 2.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 245 QQVTGELRKLNLSCGTYHAGMSFSTRKDIHHRFVRDEIQCVIATIAFGMGINKADIRQVIHYGAPKDMESYYQEIGRAGR 324
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 767951195 325 DG 326
Cdd:smart00490 81 AG 82
|
|
| HTH_40 |
pfam14493 |
Helix-turn-helix domain; This presumed domain is found at the C-terminus of a large number of ... |
725-819 |
9.00e-21 |
|
Helix-turn-helix domain; This presumed domain is found at the C-terminus of a large number of helicase proteins.
Pssm-ID: 464189 Cd Length: 89 Bit Score: 87.56 E-value: 9.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 725 SMAITYSLFQEKkMPLKSIAESRILPLMTIGMHLSQAVKAGCPLDLERAgLTPEVQKIIADVIRNPPVNSdmskISLIRM 804
Cdd:pfam14493 1 SAEITLELYKEG-LSIEEIAEERGLKESTIEGHLAELIEAGEPVDIERL-VSEEEQKEILDAIEKLGSES----LKPIKE 74
|
90
....*....|....*
gi 767951195 805 LVPENIDTYLIHMAI 819
Cdd:pfam14493 75 ALPEEISYFEIRLVL 89
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
229-326 |
1.66e-19 |
|
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: 84.57 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 229 EFEGPTIIYCPSRKMTQqvTGEL-RKLNLSCGTYHAGMSFSTRKDIHHRFVRDEIQCVIATIAFGMGINKADIRQVIHYG 307
Cdd:pfam00271 13 ERGGKVLIFSQTKKTLE--AELLlEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVINYD 90
|
90
....*....|....*....
gi 767951195 308 APKDMESYYQEIGRAGRDG 326
Cdd:pfam00271 91 LPWNPASYIQRIGRAGRAG 109
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
42-179 |
1.03e-18 |
|
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: 84.22 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 42 YGKSLCFQYP------PVYVGKIGLVISPLISLMEDQVLQLK-----MSNIPACFLGSAQSENVLTDIKlgKYRIVYVTP 110
Cdd:pfam00270 25 SGKTLAFLLPalealdKLDNGPQALVLAPTRELAEQIYEELKklgkgLGLKVASLLGGDSRKEQLEKLK--GPDILVGTP 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767951195 111 E---YCSGNMGLLQQLEadigitLIAVDEAHCISEWGhdFRDSFRKLgsLKTALPMVPIVALTATASSSIRE 179
Cdd:pfam00270 103 GrllDLLQERKLLKNLK------LLVLDEAHRLLDMG--FGPDLEEI--LRRLPKKRQILLLSATLPRNLED 164
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
623-696 |
5.56e-18 |
|
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the HRDC domain cause human disease.
Pssm-ID: 128635 [Multi-domain] Cd Length: 81 Bit Score: 79.26 E-value: 5.56e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767951195 623 LYGKLVEARQKHANKMDVPPAILATNKILVDMAKMRPTTVENVKRIDGVSEGKAAMLAP-LLEVIKHFCQTNSVQ 696
Cdd:smart00341 7 LLRRLRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKdLLAVIQEASDSPSEA 81
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
43-207 |
3.36e-17 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 81.00 E-value: 3.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 43 GKSLCFQYPPVYVGKIG-----LVISPLISLMEDQVLQLK-----MSNIPACFLGSAQSENVLTDIKLGKYRIVYVTPEY 112
Cdd:smart00487 36 GKTLAALLPALEALKRGkggrvLVLVPTRELAEQWAEELKklgpsLGLKVVGLYGGDSKREQLRKLESGKTDILVTTPGR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 113 csgnmgLLQQLEAD----IGITLIAVDEAHCISEWGhdFRDSFRKLgsLKTALPMVPIVALTATASSSIREDIVRCLNLR 188
Cdd:smart00487 116 ------LLDLLENDklslSNVDLVILDEAHRLLDGG--FGDQLEKL--LKLLPKNVQLLLLSATPPEEIENLLELFLNDP 185
|
170
....*....|....*....
gi 767951195 189 npqITCTGFDRPNLYLEVR 207
Cdd:smart00487 186 ---VFIDVGFTPLEPIEQF 201
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
221-324 |
6.87e-16 |
|
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: 74.85 E-value: 6.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 221 LVKTSSHWEFEGPTIIYCPSRKMTQQVTGELRKLNLSCGTYHAGMSFSTRKDIHHRFVRDEIQCVIATIAFGMGINKADI 300
Cdd:cd18787 17 LLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVATDVAARGLDIPGV 96
|
90 100
....*....|....*....|....
gi 767951195 301 RQVIHYGAPKDMESYYQEIGRAGR 324
Cdd:cd18787 97 DHVINYDLPRDAEDYVHRIGRTGR 120
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
420-518 |
1.97e-15 |
|
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix structure. The RQC domain, found only in RecQ family enzymes, is a high affinity G4 DNA binding domain.
Pssm-ID: 462780 [Multi-domain] Cd Length: 108 Bit Score: 72.96 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 420 EDTSWDFGPQAFKLLSAVDILGEKFGIGLPILFLRGSNSQRLAdQYRRHSL--FGTGKDQTESWWKAFSRQLITEGFL-V 496
Cdd:pfam09382 1 PPETVDVTEEAQKILSCVYRTGQRFGAGHLIDVLRGSKNKKIR-QLGHDKLstFGIGKDLSKKEWRRIIRQLIAEGYLeV 79
|
90 100
....*....|....*....|..
gi 767951195 497 EVSRYNkfmkICALTKKGRNWL 518
Cdd:pfam09382 80 DIEFYS----VLKLTPKAREVL 97
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
234-326 |
3.90e-14 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 70.36 E-value: 3.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 234 TIIYCPSRKMTQQVTGELR-------KLNLSCGTYHAGMSFSTRKDIHHRFVRDEIQCVIATIAFGMGINKADIRQVIHY 306
Cdd:cd18797 38 TIVFCRSRKLAELLLRYLKarlveegPLASKVASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLA 117
|
90 100
....*....|....*....|
gi 767951195 307 GAPKDMESYYQEIGRAGRDG 326
Cdd:cd18797 118 GYPGSLASLWQQAGRAGRRG 137
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
620-686 |
6.88e-12 |
|
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic acid binding. Mutations in the HRDC domain cause human disease. It is interesting to note that the RecQ helicase in Deinococcus radiodurans has three tandem HRDC domains.
Pssm-ID: 425755 [Multi-domain] Cd Length: 68 Bit Score: 61.40 E-value: 6.88e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767951195 620 QIVLYGKLVEARQKHANKMDVPPAILATNKILVDMAKMRPTTVENVKRIDGVSEGKAAMLAP-LLEVI 686
Cdd:pfam00570 1 QLALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEeILAAI 68
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
197-327 |
1.76e-11 |
|
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: 62.96 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 197 FDRPNLYLEVRRKTGNILQDLQPFLVKTSSHwEFEGPTIIYCPSRKMTQQVTgelrkLNLSC-GTYHAGMSFSTRKDIHH 275
Cdd:cd18795 10 LGFNGLGIKLRVDVMNKFDSDIIVLLKIETV-SEGKPVLVFCSSRKECEKTA-----KDLAGiAFHHAGLTREDRELVEE 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767951195 276 RFVRDEIQCVIATIAFGMGIN-KAdiRQVI----HYGAPKDME-----SYYQEIGRAGRDGL 327
Cdd:cd18795 84 LFREGLIKVLVATSTLAAGVNlPA--RTVIikgtQRYDGKGYRelsplEYLQMIGRAGRPGF 143
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
234-326 |
3.68e-09 |
|
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: 60.62 E-value: 3.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 234 TIIYCPSRKMTQQVTGELRKLNLSCG------TYHAGMSFSTRKDIHHRFVRDEIQCVIATIAFGMGINKADIRQVIHYG 307
Cdd:COG1205 291 TLVFTRSRRGAELLARYARRALREPDladrvaAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAG 370
|
90
....*....|....*....
gi 767951195 308 APKDMESYYQEIGRAGRDG 326
Cdd:COG1205 371 YPGTRASFWQQAGRAGRRG 389
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
128-326 |
4.84e-09 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 59.80 E-value: 4.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 128 GITLIAVDEAHCISEWGhdFRDsfrKLGSLKTALPMVPIVALTATASSSIrEDIVRCLnLRNPQ-ITCTGFDRPN----- 201
Cdd:PLN00206 270 NVSVLVLDEVDCMLERG--FRD---QVMQIFQALSQPQVLLFSATVSPEV-EKFASSL-AKDIIlISIGNPNRPNkavkq 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 202 --LYLEVRRKTGNILQdlqpfLVKTSSHweFEGPTIIYCPSRKMTQQVTGELRKLN-LSCGTYHAGMSFSTRKDIHHRFV 278
Cdd:PLN00206 343 laIWVETKQKKQKLFD-----ILKSKQH--FKPPAVVFVSSRLGADLLANAITVVTgLKALSIHGEKSMKERREVMKSFL 415
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767951195 279 RDEIQCVIATIAFGMGINKADIRQVIHYGAPKDMESYYQEIGRAGRDG 326
Cdd:PLN00206 416 VGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMG 463
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
234-327 |
1.81e-08 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 57.85 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 234 TIIYCPSRKMTQQVTGELRKLNLSCGTYHAGMSFSTRKDIHHRFVRDEIQCVIAT-IAfGMGINKADIRQVIHYGAPKDM 312
Cdd:COG0513 244 AIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATdVA-ARGIDIDDVSHVINYDLPEDP 322
|
90
....*....|....*...
gi 767951195 313 ESYYQEIG---RAGRDGL 327
Cdd:COG0513 323 EDYVHRIGrtgRAGAEGT 340
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
337-407 |
2.23e-08 |
|
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: 51.52 E-value: 2.23e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767951195 337 PADINLNRHLLT-EIRNEKFRLYKLKMMAKMEKY-LHSSRCRRQIILSHFEDKqvqkaslgiMGTEKC--CDNCR 407
Cdd:pfam16124 1 YQDVVRLRFLIEqSEADEERKEVELQKLQAMVAYcENTTDCRRKQLLRYFGEE---------FDSEPCgnCDNCL 66
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
235-350 |
4.60e-08 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 56.37 E-value: 4.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 235 IIYCPSRKMTQQVTGELRKLNLSCGTYHAGMSFSTRKDIHHRFVRDEIQCVIATIAFGMGINKADIRQVIHYGAPKDMES 314
Cdd:PTZ00424 271 IIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPEN 350
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 767951195 315 YYQEIGRAGRDGLQSSCHVLWAPADI----NLNRHLLTEI 350
Cdd:PTZ00424 351 YIHRIGRSGRFGRKGVAINFVTPDDIeqlkEIERHYNTQI 390
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
267-326 |
5.52e-08 |
|
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: 50.78 E-value: 5.52e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 267 FSTRKDiHHRFVRDEIQCVIATIAFGMGINKADIRQVIHYGAPKDMESYYQEIGRAGRDG 326
Cdd:cd18785 9 FTNSIE-HAEEIASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGG 67
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
234-324 |
1.55e-07 |
|
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: 51.50 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 234 TIIYCPSRKMTQQVTGELRKL------NLSCGTYHAGMSFSTRKDIHHRFVRDEIQCVIATIAFGMGINKADIRQVIHYG 307
Cdd:cd18796 41 TLVFTNTRSQAERLAQRLRELcpdrvpPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIG 120
|
90
....*....|....*..
gi 767951195 308 APKDMESYYQEIGRAGR 324
Cdd:cd18796 121 SPKSVARLLQRLGRSGH 137
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|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
43-172 |
2.49e-07 |
|
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: 50.86 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 43 GKSLCFQYPPVYV----GKIGLVISPLISLMEDQ---VLQLKMSNIPACFLGSAQSENVLTDIKLGKYRIVYVTPEYCSG 115
Cdd:cd00046 13 GKTLAALLAALLLllkkGKKVLVLVPTKALALQTaerLRELFGPGIRVAVLVGGSSAEEREKNKLGDADIIIATPDMLLN 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 767951195 116 NMGLLQQLEADiGITLIAVDEAHCISEWGHDFRDSfrKLGSLKTALPMVPIVALTAT 172
Cdd:cd00046 93 LLLREDRLFLK-DLKLIIVDEAHALLIDSRGALIL--DLAVRKAGLKNAQVILLSAT 146
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| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
230-324 |
4.22e-07 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 53.74 E-value: 4.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 230 FEGPTIIYCPSRKMTQQVTgelRKLNLSCGTYHAGMSFSTRKDIHHRFVRDEIQCVIATIAFGMGInkaDI--RQVIhyg 307
Cdd:COG1202 426 YRGQTIIFTNSRRRCHEIA---RALGYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGV---DFpaSQVI--- 496
|
90 100
....*....|....*....|....*....
gi 767951195 308 apkdMES------------YYQEIGRAGR 324
Cdd:COG1202 497 ----FDSlamgiewlsvqeFHQMLGRAGR 521
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| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
116-322 |
5.49e-07 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 53.49 E-value: 5.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 116 NMGLLQQLEADIGitLIAVDEAHcisewgHDFRDSFRKLGSlktALPMVPIVALTAT--ASSSIREDIVRCLN------- 186
Cdd:COG1061 177 RRAHLDELGDRFG--LVIIDEAH------HAGAPSYRRILE---AFPAAYRLGLTATpfRSDGREILLFLFDGivyeysl 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 187 --------LRNP---QITCTGFDRPNLYLEVRRKTGNILQDLQPFLVKTSSHWEFE----GPTIIYCPSRKMTQQVTGEL 251
Cdd:COG1061 246 keaiedgyLAPPeyyGIRVDLTDERAEYDALSERLREALAADAERKDKILRELLREhpddRKTLVFCSSVDHAEALAELL 325
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767951195 252 RKLNLSCGTYHAGMSFSTRKDIHHRFVRDEIQCVIATIAFGMGINKADIRQVIHYGAPKDMESYYQEIGRA 322
Cdd:COG1061 326 NEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRG 396
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| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
235-333 |
9.92e-06 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 45.93 E-value: 9.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 235 IIYCPSRKMTQQVTGELRKLNLSCGTYHAGMSFSTRKDIHHRFVRDEIQCV--IATIAFGMGIN--KADIrqVIHYGAP- 309
Cdd:cd18793 31 LIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVflLSTKAGGVGLNltAANR--VILYDPWw 108
|
90 100
....*....|....*....|....*..
gi 767951195 310 ---KDMesyyQEIGRAGRDGLQSSCHV 333
Cdd:cd18793 109 npaVEE----QAIDRAHRIGQKKPVVV 131
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| PTZ00110 |
PTZ00110 |
helicase; Provisional |
204-354 |
2.41e-04 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 44.76 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 204 LEVRRKTGNILQDLQPFLVKTSShwefegpTIIYCPSRKMTQQVTGELRKLNLSCGTYHAgmsfsTRKDIHHRFVRDEIQ 283
Cdd:PTZ00110 357 VEEHEKRGKLKMLLQRIMRDGDK-------ILIFVETKKGADFLTKELRLDGWPALCIHG-----DKKQEERTWVLNEFK 424
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767951195 284 -----CVIATIAFGMGINKADIRQVIHYGAPKDMESYYQEIGRAGRDGLQSSCHVLWAPADINLNRHLLTEIRNEK 354
Cdd:PTZ00110 425 tgkspIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAK 500
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| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
260-323 |
2.59e-04 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 44.92 E-value: 2.59e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767951195 260 TYHAGMSFSTRKDIHHRFVRDEIQCVIATIAFGMGINKADIRQVIHYGAPKDMESYYQEIGRAG 323
Cdd:PRK09751 306 SHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
234-326 |
1.20e-03 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 42.53 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951195 234 TIIYCPSRKMTQQVTGELRKLNLSCGTYHAGMSFSTRKDIHHRFVRDEIQCVIATIAFGMGINKADIRQVIHYGAPKDME 313
Cdd:PRK11634 248 AIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSE 327
|
90
....*....|...
gi 767951195 314 SYYQEIGRAGRDG 326
Cdd:PRK11634 328 SYVHRIGRTGRAG 340
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
259-326 |
9.53e-03 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350189 [Multi-domain] Cd Length: 142 Bit Score: 37.57 E-value: 9.53e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767951195 259 GTYHAGMSFSTRKDIHHRFVRDEIQCVIATIAFGMGInkaDIRQ---VIHYGAPKDMESYYQEIGRAGRDG 326
Cdd:cd18802 68 QRKRSLMTQRKQKETLDKFRDGELNLLIATSVLEEGI---DVPAcnlVIRFDLPKTLRSYIQSRGRARAPN 135
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