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Conserved domains on  [gi|6323502|ref|NP_013573|]
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Y' element ATP-dependent helicase [Saccharomyces cerevisiae S288C]

Protein Classification

Sir1 and HELICc domain-containing protein( domain architecture ID 11672309)

Sir1 and HELICc domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 615-710 6.31e-14

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: 69.16  E-value: 6.31e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323502     615 FEIEPESKAIVVASTTNEVEELACSWRKYFRVVWIHGKLGAAEKVSRTKEFvTDGSMRVLIGTKLVTEGIDIKQLMMVIM 694
Cdd:pfam00271   10 LKKERGGKVLIFSQTKKTLEAELLLEKEGIKVARLHGDLSQEEREEILEDF-RKGKIDVLVATDVAERGLDLPDVDLVIN 88

                           90
                   ....*....|....*.
gi 6323502     695 LDNRLNIIELIQGVGR 710
Cdd:pfam00271   89 YDLPWNPASYIQRIGR 104
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 368-540 1.45e-12

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: 66.88  E-value: 1.45e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323502     368 HQLRLCHEIYMADtpSVAVQAPPGYGKTELFHLPLIALASKGDVKYVSFLFVPYTVLLANCMIRLSRCGCLNVAPVRNFI 447
Cdd:pfam00270    3 IQAEAIPAILEGR--DVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323502     448 eegcDGVTDLYvgIYDDLASTNFTdrIA---AWENIVECTFRTNNVKlgYLIVDEFHNFETEVYRQSQFGGITNLDFDAf 524
Cdd:pfam00270   81 ----GGDSRKE--QLEKLKGPDIL--VGtpgRLLDLLQERKLLKNLK--LLVLDEAHRLLDMGFGPDLEEILRRLPKKR- 149

                          170
                   ....*....|....*.
gi 6323502     525 eKAIFLSGTAPEAVAD 540
Cdd:pfam00270  150 -QILLLSATLPRNLED 164
Sir1 super family cl13110
Sir1, ORC-binding domain; This entry represents the ORC-binding domain of Sir1. Sir1 interacts ...
 13-88 2.23e-05

Sir1, ORC-binding domain; This entry represents the ORC-binding domain of Sir1. Sir1 interacts with the BAH domain of the Orc1 subunit of the origin recognition complex (ORC) resulting in the establishment of silent chromatin at HMR and HML in S.cerevisiae. The amino acids from the ORC interaction region of Sir1 are presented on a conserved, convex surface that forms a complementary interface with the Orc1 BAH domain, critical for transcriptional silencing. Proteins containing this domain also include Y' element ATP-dependent helicase protein 1, which catalyzes DNA unwinding and is involved in telomerase-independent telomere maintenance.


The actual alignment was detected with superfamily member pfam11603:

Pssm-ID: 431955  Cd Length: 120  Bit Score: 45.30  E-value: 2.23e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323502      13 NFDEFEsalNNKNDLVHCPSITLFESIPTEVRSFYEDEkSGLIKVVKFRTGAMDRKRSFEKIVVSVMVGKNVQKFL 88
Cdd:pfam11603   48 DLNELK---LENSDLIPCDSKELFEHVTTETKEFYRTE-DGFIIVNSTRTSKKKIRNAITYRVIPIRLKNKGVKYL 119
 
Name Accession Description Interval E-value
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 615-710 6.31e-14

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: 69.16  E-value: 6.31e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323502     615 FEIEPESKAIVVASTTNEVEELACSWRKYFRVVWIHGKLGAAEKVSRTKEFvTDGSMRVLIGTKLVTEGIDIKQLMMVIM 694
Cdd:pfam00271   10 LKKERGGKVLIFSQTKKTLEAELLLEKEGIKVARLHGDLSQEEREEILEDF-RKGKIDVLVATDVAERGLDLPDVDLVIN 88

                           90
                   ....*....|....*.
gi 6323502     695 LDNRLNIIELIQGVGR 710
Cdd:pfam00271   89 YDLPWNPASYIQRIGR 104
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 368-540 1.45e-12

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: 66.88  E-value: 1.45e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323502     368 HQLRLCHEIYMADtpSVAVQAPPGYGKTELFHLPLIALASKGDVKYVSFLFVPYTVLLANCMIRLSRCGCLNVAPVRNFI 447
Cdd:pfam00270    3 IQAEAIPAILEGR--DVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323502     448 eegcDGVTDLYvgIYDDLASTNFTdrIA---AWENIVECTFRTNNVKlgYLIVDEFHNFETEVYRQSQFGGITNLDFDAf 524
Cdd:pfam00270   81 ----GGDSRKE--QLEKLKGPDIL--VGtpgRLLDLLQERKLLKNLK--LLVLDEAHRLLDMGFGPDLEEILRRLPKKR- 149

                          170
                   ....*....|....*.
gi 6323502     525 eKAIFLSGTAPEAVAD 540
Cdd:pfam00270  150 -QILLLSATLPRNLED 164
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
333-712 1.50e-11

Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 68.90  E-value: 1.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323502   333 ISRVTRKRPREPKSTNDILVAGQKLFGSSFEFRDlHQLRLCHEI---YMADTPSVAVQAPPGYGKTELFhlplIALASKG 409
Cdd:COG1061   50 GRRLPEEDTERELAEAEALEAGDEASGTSFELRP-YQQEALEALlaaLERGGGRGLVVAPTGTGKTVLA----LALAAEL 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323502   410 DVKYVSFLFVPYTVLLANCMIRLSRcgclnVAPVRNFIEEGCDGVTDLYVGIYDDLASTNFTDRIAAwenivectfrtnn 489
Cdd:COG1061  125 LRGKRVLVLVPRRELLEQWAEELRR-----FLGDPLAGGGKKDSDAPITVATYQSLARRAHLDELGD------------- 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323502   490 vKLGYLIVDEFHNFETEVYRQSqfggitnldFDAFEKAIFL--SGTaPEAVADAALQRIGLTGLAKkSMDINELKRSE-- 565
Cdd:COG1061  187 -RFGLVIIDEAHHAGAPSYRRI---------LEAFPAAYRLglTAT-PFRSDGREILLFLFDGIVY-EYSLKEAIEDGyl 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323502   566 ----------DLSRGLSSYPT---RMFNLIKEKSEvplgHVHKIWKKVESqpeealklllalfEIEPESKAIVVASTTNE 632
Cdd:COG1061  255 appeyygirvDLTDERAEYDAlseRLREALAADAE----RKDKILRELLR-------------EHPDDRKTLVFCSSVDH 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323502   633 VEELACSWRKY-FRVVWIHGKLGAAEKVSRTKEFvTDGSMRVLIGTKLVTEGIDIKQLMMVIMLDNRLNIIELIQGVGR- 710
Cdd:COG1061  318 AEALAELLNEAgIRAAVVTGDTPKKEREEILEAF-RDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRg 396


                 ..
gi 6323502   711 LR 712
Cdd:COG1061  397 LR 398
HELICc smart00490
helicase superfamily c-terminal domain;
634-714 1.05e-09

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 56.45  E-value: 1.05e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323502      634 EELACSWRKY-FRVVWIHGKLGAAEKVSRTKEFvTDGSMRVLIGTKLVTEGIDIKQLMMVIMLDNRLNIIELIQGVGR-L 711
Cdd:smart00490    1 EELAELLKELgIKVARLHGGLSQEEREEILDKF-NNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRaG 79


                    ...
gi 6323502      712 RDG 714
Cdd:smart00490   80 RAG 82
DEXDc smart00487
DEAD-like helicases superfamily;
362-542 7.25e-08

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 54.42  E-value: 7.25e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323502      362 FEFRDlHQLRLCHEIyMADTPSVAVQAPPGYGKTELFHLPLIALASKGDVKYVSFLfVPYTVLLANCMIRLsrcgclnva 441
Cdd:smart00487    7 EPLRP-YQKEAIEAL-LSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVL-VPTRELAEQWAEEL--------- 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323502      442 pvRNFIEEGCDGVTDLYVGiyddlasTNFTDRIAAWEN----IVECTF----------RTNNVKLGYLIVDEFHNFETEV 507
Cdd:smart00487   75 --KKLGPSLGLKVVGLYGG-------DSKREQLRKLESgktdILVTTPgrlldllendKLSLSNVDLVILDEAHRLLDGG 145

                           170       180       190
                    ....*....|....*....|....*....|....*..
gi 6323502      508 YRQSqfggITNLDFDAFEKA--IFLSGTAPEAVADAA 542
Cdd:smart00487  146 FGDQ----LEKLLKLLPKNVqlLLLSATPPEEIENLL 178
Sir1 pfam11603
Sir1, ORC-binding domain; This entry represents the ORC-binding domain of Sir1. Sir1 interacts ...
 13-88 2.23e-05

Sir1, ORC-binding domain; This entry represents the ORC-binding domain of Sir1. Sir1 interacts with the BAH domain of the Orc1 subunit of the origin recognition complex (ORC) resulting in the establishment of silent chromatin at HMR and HML in S.cerevisiae. The amino acids from the ORC interaction region of Sir1 are presented on a conserved, convex surface that forms a complementary interface with the Orc1 BAH domain, critical for transcriptional silencing. Proteins containing this domain also include Y' element ATP-dependent helicase protein 1, which catalyzes DNA unwinding and is involved in telomerase-independent telomere maintenance.


Pssm-ID: 431955  Cd Length: 120  Bit Score: 45.30  E-value: 2.23e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323502      13 NFDEFEsalNNKNDLVHCPSITLFESIPTEVRSFYEDEkSGLIKVVKFRTGAMDRKRSFEKIVVSVMVGKNVQKFL 88
Cdd:pfam11603   48 DLNELK---LENSDLIPCDSKELFEHVTTETKEFYRTE-DGFIIVNSTRTSKKKIRNAITYRVIPIRLKNKGVKYL 119
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
 617-731 8.98e-05

C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350198 [Multi-domain]  Cd Length: 159  Bit Score: 44.26  E-value: 8.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323502   617 IEpESKAIVVASTTNEVEELACSWRKYFRVVWIHGKLGAAEKVSRTKEFvTDGSMRVLIGTKLVTEGIDIKQL-MMVIML 695
Cdd:cd18811   36 IE-ESEKLDLKAAVAMYEYLKERFRPELNVGLLHGRLKSDEKDAVMAEF-REGEVDILVSTTVIEVGVDVPNAtVMVIED 113

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 6323502   696 DNRLNIIELIQGVGRLRDGGL---CYLLSR-KNSWAARNR 731
Cdd:cd18811  114 AERFGLSQLHQLRGRVGRGDHqsyCLLVYKdPLTETAKQR 153
PTZ00424 PTZ00424
helicase 45; Provisional
 621-710 1.63e-04

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 45.59  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323502    621 SKAIVVASTTNEVEELACSWR-KYFRVVWIHGKLGAAEKVSRTKEFVTdGSMRVLIGTKLVTEGIDIKQLMMVIMLDNRL 699
Cdd:PTZ00424  268 TQAIIYCNTRRKVDYLTKKMHeRDFTVSCMHGDMDQKDRDLIMREFRS-GSTRVLITTDLLARGIDVQQVSLVINYDLPA 346

                          90
                  ....*....|.
gi 6323502    700 NIIELIQGVGR 710
Cdd:PTZ00424  347 SPENYIHRIGR 357
 
Name Accession Description Interval E-value
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 615-710 6.31e-14

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: 69.16  E-value: 6.31e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323502     615 FEIEPESKAIVVASTTNEVEELACSWRKYFRVVWIHGKLGAAEKVSRTKEFvTDGSMRVLIGTKLVTEGIDIKQLMMVIM 694
Cdd:pfam00271   10 LKKERGGKVLIFSQTKKTLEAELLLEKEGIKVARLHGDLSQEEREEILEDF-RKGKIDVLVATDVAERGLDLPDVDLVIN 88

                           90
                   ....*....|....*.
gi 6323502     695 LDNRLNIIELIQGVGR 710
Cdd:pfam00271   89 YDLPWNPASYIQRIGR 104
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 368-540 1.45e-12

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: 66.88  E-value: 1.45e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323502     368 HQLRLCHEIYMADtpSVAVQAPPGYGKTELFHLPLIALASKGDVKYVSFLFVPYTVLLANCMIRLSRCGCLNVAPVRNFI 447
Cdd:pfam00270    3 IQAEAIPAILEGR--DVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323502     448 eegcDGVTDLYvgIYDDLASTNFTdrIA---AWENIVECTFRTNNVKlgYLIVDEFHNFETEVYRQSQFGGITNLDFDAf 524
Cdd:pfam00270   81 ----GGDSRKE--QLEKLKGPDIL--VGtpgRLLDLLQERKLLKNLK--LLVLDEAHRLLDMGFGPDLEEILRRLPKKR- 149

                          170
                   ....*....|....*.
gi 6323502     525 eKAIFLSGTAPEAVAD 540
Cdd:pfam00270  150 -QILLLSATLPRNLED 164
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
333-712 1.50e-11

Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 68.90  E-value: 1.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323502   333 ISRVTRKRPREPKSTNDILVAGQKLFGSSFEFRDlHQLRLCHEI---YMADTPSVAVQAPPGYGKTELFhlplIALASKG 409
Cdd:COG1061   50 GRRLPEEDTERELAEAEALEAGDEASGTSFELRP-YQQEALEALlaaLERGGGRGLVVAPTGTGKTVLA----LALAAEL 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323502   410 DVKYVSFLFVPYTVLLANCMIRLSRcgclnVAPVRNFIEEGCDGVTDLYVGIYDDLASTNFTDRIAAwenivectfrtnn 489
Cdd:COG1061  125 LRGKRVLVLVPRRELLEQWAEELRR-----FLGDPLAGGGKKDSDAPITVATYQSLARRAHLDELGD------------- 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323502   490 vKLGYLIVDEFHNFETEVYRQSqfggitnldFDAFEKAIFL--SGTaPEAVADAALQRIGLTGLAKkSMDINELKRSE-- 565
Cdd:COG1061  187 -RFGLVIIDEAHHAGAPSYRRI---------LEAFPAAYRLglTAT-PFRSDGREILLFLFDGIVY-EYSLKEAIEDGyl 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323502   566 ----------DLSRGLSSYPT---RMFNLIKEKSEvplgHVHKIWKKVESqpeealklllalfEIEPESKAIVVASTTNE 632
Cdd:COG1061  255 appeyygirvDLTDERAEYDAlseRLREALAADAE----RKDKILRELLR-------------EHPDDRKTLVFCSSVDH 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323502   633 VEELACSWRKY-FRVVWIHGKLGAAEKVSRTKEFvTDGSMRVLIGTKLVTEGIDIKQLMMVIMLDNRLNIIELIQGVGR- 710
Cdd:COG1061  318 AEALAELLNEAgIRAAVVTGDTPKKEREEILEAF-RDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRg 396


                 ..
gi 6323502   711 LR 712
Cdd:COG1061  397 LR 398
HELICc smart00490
helicase superfamily c-terminal domain;
634-714 1.05e-09

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 56.45  E-value: 1.05e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323502      634 EELACSWRKY-FRVVWIHGKLGAAEKVSRTKEFvTDGSMRVLIGTKLVTEGIDIKQLMMVIMLDNRLNIIELIQGVGR-L 711
Cdd:smart00490    1 EELAELLKELgIKVARLHGGLSQEEREEILDKF-NNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRaG 79


                    ...
gi 6323502      712 RDG 714
Cdd:smart00490   80 RAG 82
DEXDc smart00487
DEAD-like helicases superfamily;
362-542 7.25e-08

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 54.42  E-value: 7.25e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323502      362 FEFRDlHQLRLCHEIyMADTPSVAVQAPPGYGKTELFHLPLIALASKGDVKYVSFLfVPYTVLLANCMIRLsrcgclnva 441
Cdd:smart00487    7 EPLRP-YQKEAIEAL-LSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVL-VPTRELAEQWAEEL--------- 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323502      442 pvRNFIEEGCDGVTDLYVGiyddlasTNFTDRIAAWEN----IVECTF----------RTNNVKLGYLIVDEFHNFETEV 507
Cdd:smart00487   75 --KKLGPSLGLKVVGLYGG-------DSKREQLRKLESgktdILVTTPgrlldllendKLSLSNVDLVILDEAHRLLDGG 145

                           170       180       190
                    ....*....|....*....|....*....|....*..
gi 6323502      508 YRQSqfggITNLDFDAFEKA--IFLSGTAPEAVADAA 542
Cdd:smart00487  146 FGDQ----LEKLLKLLPKNVqlLLLSATPPEEIENLL 178
Sir1 pfam11603
Sir1, ORC-binding domain; This entry represents the ORC-binding domain of Sir1. Sir1 interacts ...
 13-88 2.23e-05

Sir1, ORC-binding domain; This entry represents the ORC-binding domain of Sir1. Sir1 interacts with the BAH domain of the Orc1 subunit of the origin recognition complex (ORC) resulting in the establishment of silent chromatin at HMR and HML in S.cerevisiae. The amino acids from the ORC interaction region of Sir1 are presented on a conserved, convex surface that forms a complementary interface with the Orc1 BAH domain, critical for transcriptional silencing. Proteins containing this domain also include Y' element ATP-dependent helicase protein 1, which catalyzes DNA unwinding and is involved in telomerase-independent telomere maintenance.


Pssm-ID: 431955  Cd Length: 120  Bit Score: 45.30  E-value: 2.23e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323502      13 NFDEFEsalNNKNDLVHCPSITLFESIPTEVRSFYEDEkSGLIKVVKFRTGAMDRKRSFEKIVVSVMVGKNVQKFL 88
Cdd:pfam11603   48 DLNELK---LENSDLIPCDSKELFEHVTTETKEFYRTE-DGFIIVNSTRTSKKKIRNAITYRVIPIRLKNKGVKYL 119
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
 617-731 8.98e-05

C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350198 [Multi-domain]  Cd Length: 159  Bit Score: 44.26  E-value: 8.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323502   617 IEpESKAIVVASTTNEVEELACSWRKYFRVVWIHGKLGAAEKVSRTKEFvTDGSMRVLIGTKLVTEGIDIKQL-MMVIML 695
Cdd:cd18811   36 IE-ESEKLDLKAAVAMYEYLKERFRPELNVGLLHGRLKSDEKDAVMAEF-REGEVDILVSTTVIEVGVDVPNAtVMVIED 113

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 6323502   696 DNRLNIIELIQGVGRLRDGGL---CYLLSR-KNSWAARNR 731
Cdd:cd18811  114 AERFGLSQLHQLRGRVGRGDHqsyCLLVYKdPLTETAKQR 153
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 615-710 1.14e-04

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: 43.26  E-value: 1.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323502   615 FEIEPESKAIVVASTTNEVEELAcswrKYFR-----VVWIHGKLGAAEKVSRTKEFvTDGSMRVLIGTKLVTEGIDIKQL 689
Cdd:cd18787   22 LEKLKPGKAIIFVNTKKRVDRLA----ELLEelgikVAALHGDLSQEERERALKKF-RSGKVRVLVATDVAARGLDIPGV 96

                         90       100
                 ....*....|....*....|.
gi 6323502   690 MMVIMLDNRLNIIELIQGVGR 710
Cdd:cd18787   97 DHVINYDLPRDAEDYVHRIGR 117
PTZ00424 PTZ00424
helicase 45; Provisional
 621-710 1.63e-04

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 45.59  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323502    621 SKAIVVASTTNEVEELACSWR-KYFRVVWIHGKLGAAEKVSRTKEFVTdGSMRVLIGTKLVTEGIDIKQLMMVIMLDNRL 699
Cdd:PTZ00424  268 TQAIIYCNTRRKVDYLTKKMHeRDFTVSCMHGDMDQKDRDLIMREFRS-GSTRVLITTDLLARGIDVQQVSLVINYDLPA 346

                          90
                  ....*....|.
gi 6323502    700 NIIELIQGVGR 710
Cdd:PTZ00424  347 SPENYIHRIGR 357
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
 670-720 1.67e-04

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: 41.54  E-value: 1.67e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6323502   670 SMRVLIGTKLVTEGIDIKQLMMVIMLDNRLNIIELIQGVGRLR----DGGLCYLL 720
Cdd:cd18785   22 SLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGrggkDEGEVILF 76
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
 632-722 6.71e-04

C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350179 [Multi-domain]  Cd Length: 160  Bit Score: 41.87  E-value: 6.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323502   632 EVEELACSWRKYF---RVVWIHGKLGAAEKVSRTKEFvTDGSMRVLIGTKLVTEGIDIKQL-MMVIMLDNRLNIIELIQ- 706
Cdd:cd18792   46 SIEALAEELKELVpeaRVALLHGKMTEDEKEAVMLEF-REGEYDILVSTTVIEVGIDVPNAnTMIIEDADRFGLSQLHQl 124

                         90
                 ....*....|....*...
gi 6323502   707 -G-VGRLRDGGLCYLLSR 722
Cdd:cd18792  125 rGrVGRGKHQSYCYLLYP 142
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
616-693 3.74e-03

Superfamily II DNA and RNA helicase [Replication, recombination and repair];


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 41.29  E-value: 3.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323502   616 EIEPESKAIVVASTTNEVEELACSWRKY-FRVVWIHGKLGAAEkvsRTK---EFvTDGSMRVLIGTKLVTEGIDIKQLMM 691
Cdd:COG0513  237 RDEDPERAIVFCNTKRGADRLAEKLQKRgISAAALHGDLSQGQ---RERaldAF-RNGKIRVLVATDVAARGIDIDDVSH 312


                 ..
gi 6323502   692 VI 693
Cdd:COG0513  313 VI 314
PRK10917 PRK10917
ATP-dependent DNA helicase RecG; Provisional
 617-731 5.21e-03

ATP-dependent DNA helicase RecG; Provisional


Pssm-ID: 236794 [Multi-domain]  Cd Length: 681  Bit Score: 41.29  E-value: 5.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323502    617 IEpESKAIVVASttneVEELACSWRKYF---RVVWIHGKLGAAEKVSRTKEFVtDGSMRVLIGTKLVTEGIDIKQL-MMV 692
Cdd:PRK10917  481 IE-ESEKLDLQS----AEETYEELQEAFpelRVGLLHGRMKPAEKDAVMAAFK-AGEIDILVATTVIEVGVDVPNAtVMV 554

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 6323502    693 IMLDNRLNIIELIQ--G-VGRlrdGGL---CYLLSR-KNSWAARNR 731
Cdd:PRK10917  555 IENAERFGLAQLHQlrGrVGR---GAAqsyCVLLYKdPLSETARER 597
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
 620-712 5.99e-03

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: 37.92  E-value: 5.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323502   620 ESKAIVVASTTNEVEELAcswrKYFRVVWIHgklgAAEKVSRTKEFVTDGSM-----------RVLIGTKLVTEGIDIKQ 688
Cdd:cd18799    6 EIKTLIFCVSIEHAEFMA----EAFNEAGID----AVALNSDYSDRERGDEAlillffgelkpPILVTVDLLTTGVDIPE 77

                         90       100
                 ....*....|....*....|....*
gi 6323502   689 LMMVIMLDNRLNIIELIQGVGR-LR 712
Cdd:cd18799   78 VDNVVFLRPTESRTLFLQMLGRgLR 102
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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