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Conserved domains on  [gi|398366093|ref|NP_010492|]
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Ebs1p [Saccharomyces cerevisiae S288C]

Protein Classification

EST1 family protein( domain architecture ID 12105293)

EST1 family protein similar to Saccharomyces cerevisiae telomere elongation protein EST1 that associates with telomerase and is directly involved in telomere replication

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
EST1_DNA_bind pfam10373
Est1 DNA/RNA binding domain; Est1 is a protein which recruits or activates telomerase at the ...
228-516 2.57e-43

Est1 DNA/RNA binding domain; Est1 is a protein which recruits or activates telomerase at the site of polymerization. This is the DNA/RNA binding domain of EST1.


:

Pssm-ID: 431239  Cd Length: 279  Bit Score: 158.73  E-value: 2.57e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366093  228 SLDFFRLASLVLPSAGETYSQAGAIFLQTGNLGIAVFNFVKGMMTKMPSPVSIKNFGALMVDNKSSLNRSLHTtimNTYL 307
Cdd:pfam10373   1 ALRYYLLAILLLPSNGEPYNQLGVIALYVGNHLDAVYYFLRSLLSRNPFPTAKNNLELLFDKIRSKLEQGELK---LSPE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366093  308 QESKGPRTPAKEILEFYFLGLFGSVWSPTSWRDDTK-PNQLnngikLRHLENALYETMSARYLNNIKTIFHNLIITIGGF 386
Cdd:pfam10373  78 SLQEGTPGDLLERLISLFLYLHGKLYTPTDFSEFPElEDEV-----LKKLEILLKESLLSRYLKSRSLLLKMLLINIFAF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366093  387 HLLlkrRSDVSAKTLKDlrSNELDYLNFAFKYIAHILNDIVKESW--SENPEVSEILGMVRIINCWIKANPMVLQYSQSN 464
Cdd:pfam10373 153 ENA---KDKSSPEETKQ--FLLRLALRFFFTLFGLLLEEVNTLEAlkSFTPVATRYLPALRVYLCWLKSNPSVLEFEDKD 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 398366093  465 LEFVNALAYLINDIVKKKPSPSFSITEHIPKRTYWFEEDLMVKGLSFVNFQL 516
Cdd:pfam10373 228 EKLVDSLSDLWNELLSSTLLNSSFDVEKRPKRDYLLEEDVELKGFSPLGYRL 279
EST1 pfam10374
Telomerase activating protein Est1; Est1 is a protein which recruits or activates telomerase ...
79-214 5.48e-24

Telomerase activating protein Est1; Est1 is a protein which recruits or activates telomerase at the site of polymerization. Structurally it resembles a TPR-like repeat.


:

Pssm-ID: 463062  Cd Length: 98  Bit Score: 97.00  E-value: 5.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366093   79 SILDFSWESVHYPIFKWFQMWRNYIlfeKENKKQQTKFIDFRKMNSKMLKFFKTVQNFYVNVIntvykkydisvllpKRI 158
Cdd:pfam10374   1 KVLDLLWRKTHYPIIKWFRKWRKRL---DGNSKKKKYPVEFRKLNSKLRKFLKSAQKFYYGLI--------------QRL 63
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 398366093  159 IqdlklsdienttnvgdilavkTFNSSSPLAHLIPTLFHRCLLFLGTAYRYKTLLE 214
Cdd:pfam10374  64 V---------------------SREASSSLTALALLSCHRCLIYLGDLHRYRELLE 98
 
Name Accession Description Interval E-value
EST1_DNA_bind pfam10373
Est1 DNA/RNA binding domain; Est1 is a protein which recruits or activates telomerase at the ...
228-516 2.57e-43

Est1 DNA/RNA binding domain; Est1 is a protein which recruits or activates telomerase at the site of polymerization. This is the DNA/RNA binding domain of EST1.


Pssm-ID: 431239  Cd Length: 279  Bit Score: 158.73  E-value: 2.57e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366093  228 SLDFFRLASLVLPSAGETYSQAGAIFLQTGNLGIAVFNFVKGMMTKMPSPVSIKNFGALMVDNKSSLNRSLHTtimNTYL 307
Cdd:pfam10373   1 ALRYYLLAILLLPSNGEPYNQLGVIALYVGNHLDAVYYFLRSLLSRNPFPTAKNNLELLFDKIRSKLEQGELK---LSPE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366093  308 QESKGPRTPAKEILEFYFLGLFGSVWSPTSWRDDTK-PNQLnngikLRHLENALYETMSARYLNNIKTIFHNLIITIGGF 386
Cdd:pfam10373  78 SLQEGTPGDLLERLISLFLYLHGKLYTPTDFSEFPElEDEV-----LKKLEILLKESLLSRYLKSRSLLLKMLLINIFAF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366093  387 HLLlkrRSDVSAKTLKDlrSNELDYLNFAFKYIAHILNDIVKESW--SENPEVSEILGMVRIINCWIKANPMVLQYSQSN 464
Cdd:pfam10373 153 ENA---KDKSSPEETKQ--FLLRLALRFFFTLFGLLLEEVNTLEAlkSFTPVATRYLPALRVYLCWLKSNPSVLEFEDKD 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 398366093  465 LEFVNALAYLINDIVKKKPSPSFSITEHIPKRTYWFEEDLMVKGLSFVNFQL 516
Cdd:pfam10373 228 EKLVDSLSDLWNELLSSTLLNSSFDVEKRPKRDYLLEEDVELKGFSPLGYRL 279
EST1 pfam10374
Telomerase activating protein Est1; Est1 is a protein which recruits or activates telomerase ...
79-214 5.48e-24

Telomerase activating protein Est1; Est1 is a protein which recruits or activates telomerase at the site of polymerization. Structurally it resembles a TPR-like repeat.


Pssm-ID: 463062  Cd Length: 98  Bit Score: 97.00  E-value: 5.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366093   79 SILDFSWESVHYPIFKWFQMWRNYIlfeKENKKQQTKFIDFRKMNSKMLKFFKTVQNFYVNVIntvykkydisvllpKRI 158
Cdd:pfam10374   1 KVLDLLWRKTHYPIIKWFRKWRKRL---DGNSKKKKYPVEFRKLNSKLRKFLKSAQKFYYGLI--------------QRL 63
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 398366093  159 IqdlklsdienttnvgdilavkTFNSSSPLAHLIPTLFHRCLLFLGTAYRYKTLLE 214
Cdd:pfam10374  64 V---------------------SREASSSLTALALLSCHRCLIYLGDLHRYRELLE 98
Cas12d NF033951
type V CRISPR-associated protein Cas12d;
54-173 5.89e-03

type V CRISPR-associated protein Cas12d;


Pssm-ID: 468262  Cd Length: 1118  Bit Score: 40.28  E-value: 5.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366093   54 LTSIESQCGKSFAADLDSFDQSSISsILDFsWESVHYPIFKWFQMWRNYILFEKENKKQQTKFIDFRKMNSKMLKFFKTV 133
Cdd:NF033951  394 LVSLEKPELKKFSWINDMADREFIE-LYRL-WLSDLRSQLNEYNTYDEKISFEKKGKKKNKETKDENKWYPKLSKSIKLI 471
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 398366093  134 QNFYVNVINTVYKKY----DISVLLPKRIIQDLKLSDIENTTNV 173
Cdd:NF033951  472 PNFFGESKRERYKKFinlkDLTFSEGKNVENIIMSAEAEDLKNI 515
 
Name Accession Description Interval E-value
EST1_DNA_bind pfam10373
Est1 DNA/RNA binding domain; Est1 is a protein which recruits or activates telomerase at the ...
228-516 2.57e-43

Est1 DNA/RNA binding domain; Est1 is a protein which recruits or activates telomerase at the site of polymerization. This is the DNA/RNA binding domain of EST1.


Pssm-ID: 431239  Cd Length: 279  Bit Score: 158.73  E-value: 2.57e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366093  228 SLDFFRLASLVLPSAGETYSQAGAIFLQTGNLGIAVFNFVKGMMTKMPSPVSIKNFGALMVDNKSSLNRSLHTtimNTYL 307
Cdd:pfam10373   1 ALRYYLLAILLLPSNGEPYNQLGVIALYVGNHLDAVYYFLRSLLSRNPFPTAKNNLELLFDKIRSKLEQGELK---LSPE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366093  308 QESKGPRTPAKEILEFYFLGLFGSVWSPTSWRDDTK-PNQLnngikLRHLENALYETMSARYLNNIKTIFHNLIITIGGF 386
Cdd:pfam10373  78 SLQEGTPGDLLERLISLFLYLHGKLYTPTDFSEFPElEDEV-----LKKLEILLKESLLSRYLKSRSLLLKMLLINIFAF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366093  387 HLLlkrRSDVSAKTLKDlrSNELDYLNFAFKYIAHILNDIVKESW--SENPEVSEILGMVRIINCWIKANPMVLQYSQSN 464
Cdd:pfam10373 153 ENA---KDKSSPEETKQ--FLLRLALRFFFTLFGLLLEEVNTLEAlkSFTPVATRYLPALRVYLCWLKSNPSVLEFEDKD 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 398366093  465 LEFVNALAYLINDIVKKKPSPSFSITEHIPKRTYWFEEDLMVKGLSFVNFQL 516
Cdd:pfam10373 228 EKLVDSLSDLWNELLSSTLLNSSFDVEKRPKRDYLLEEDVELKGFSPLGYRL 279
EST1 pfam10374
Telomerase activating protein Est1; Est1 is a protein which recruits or activates telomerase ...
79-214 5.48e-24

Telomerase activating protein Est1; Est1 is a protein which recruits or activates telomerase at the site of polymerization. Structurally it resembles a TPR-like repeat.


Pssm-ID: 463062  Cd Length: 98  Bit Score: 97.00  E-value: 5.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366093   79 SILDFSWESVHYPIFKWFQMWRNYIlfeKENKKQQTKFIDFRKMNSKMLKFFKTVQNFYVNVIntvykkydisvllpKRI 158
Cdd:pfam10374   1 KVLDLLWRKTHYPIIKWFRKWRKRL---DGNSKKKKYPVEFRKLNSKLRKFLKSAQKFYYGLI--------------QRL 63
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 398366093  159 IqdlklsdienttnvgdilavkTFNSSSPLAHLIPTLFHRCLLFLGTAYRYKTLLE 214
Cdd:pfam10374  64 V---------------------SREASSSLTALALLSCHRCLIYLGDLHRYRELLE 98
Cas12d NF033951
type V CRISPR-associated protein Cas12d;
54-173 5.89e-03

type V CRISPR-associated protein Cas12d;


Pssm-ID: 468262  Cd Length: 1118  Bit Score: 40.28  E-value: 5.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366093   54 LTSIESQCGKSFAADLDSFDQSSISsILDFsWESVHYPIFKWFQMWRNYILFEKENKKQQTKFIDFRKMNSKMLKFFKTV 133
Cdd:NF033951  394 LVSLEKPELKKFSWINDMADREFIE-LYRL-WLSDLRSQLNEYNTYDEKISFEKKGKKKNKETKDENKWYPKLSKSIKLI 471
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 398366093  134 QNFYVNVINTVYKKY----DISVLLPKRIIQDLKLSDIENTTNV 173
Cdd:NF033951  472 PNFFGESKRERYKKFinlkDLTFSEGKNVENIIMSAEAEDLKNI 515
WaaY pfam06176
Lipopolysaccharide core biosynthesis protein (WaaY); This family consists of several bacterial ...
100-156 6.93e-03

Lipopolysaccharide core biosynthesis protein (WaaY); This family consists of several bacterial lipopolysaccharide core biosynthesis proteins (WaaY or RfaY). The waaY, waaQ, and waaP genes are located in the central operon of the waa (formerly rfa) locus on the chromosome of Escherichia coli. This locus contains genes whose products are involved in the assembly of the core region of the lipopolysaccharide molecule. WaaY is the enzyme that phosphorylates HepII in this system.


Pssm-ID: 283765  Cd Length: 229  Bit Score: 39.04  E-value: 6.93e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 398366093  100 RNYILFEKEN-KKQQTKFIDFRKMNSKMLKFFKTVQNFYVNVINTVYKKYDISVLLPK 156
Cdd:pfam06176   8 KGFSVFYKDNdNKYKEIFDDFLSYNFKTIKVFRNIDDTKVSLIDTDYGKYILKVFSPK 65
 
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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