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Conserved domains on  [gi|55741827|ref|NP_445875|]
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telomerase reverse transcriptase [Rattus norvegicus]

Protein Classification

telomerase reverse transcriptase( domain architecture ID 10572207)

telomerase reverse transcriptase is the catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme

CATH:  1.10.10.1970|1.10.132.70
EC:  2.7.7.49
Gene Ontology:  GO:0003721|GO:0042162|GO:0070034|GO:0046872
PubMed:  32770221|9110970
SCOP:  4005451

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Telomerase_RBD pfam12009
Telomerase ribonucleoprotein complex - RNA binding domain; Telomeres in most organizms are ...
 450-581 9.08e-58

Telomerase ribonucleoprotein complex - RNA binding domain; Telomeres in most organizms are comprised of tandem simple sequence repeats. The total length of telomeric repeat sequence at each chromosome end is determined in a balance of sequence loss and sequence addition. One major influence on telomere length is the enzyme telomerase. It is a reverse transcriptase that adds these simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. The RNA binding domain of telomerase - TRBD - is made up of twelve alpha helices and two short beta sheets. How telomerase and associated regulatory factors physically interact and function with each other to maintain appropriate telomere length is poorly understood. It is known however that TRBD is involved in formation of the holoenzyme (which performs the telomere extension) in addition to recognition and binding of RNA.


:

Pssm-ID: 463428  Cd Length: 133  Bit Score: 195.03  E-value: 9.08e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741827    450 QVYGFLRACLRELVPAGLWGTRHNERRFLKNVKKFISLGKYAKLSLQELMWRVKVEDCHWLRSSPEKDTVPAAEHRLRER 529
Cdd:pfam12009    1 QVSAFLRAVLRKLIPLELWGSKHNKRVLLKNVDRFIRLRRFESLSLHELMQGLKVSDFPWLGLPTKNSKLSLSDFEKRQE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 55741827    530 ILAMFLFWLMDTYVVQLLRSFFYITETTFQKNRLFFYRKSVWSKLQSIGIRQ 581
Cdd:pfam12009   81 LLAEFIYWLFDSLLIPLIRSFFYVTESSTHRNRLFYFRHDVWRKLSEPFLRK 132
TERT cd01648
TERT: Telomerase reverse transcriptase (TERT). Telomerase is a ribonucleoprotein (RNP) that ...
 816-929 6.73e-28

TERT: Telomerase reverse transcriptase (TERT). Telomerase is a ribonucleoprotein (RNP) that synthesizes telomeric DNA repeats. The telomerase RNA subunit provides the template for synthesis of these repeats. The catalytic subunit of RNP is known as telomerase reverse transcriptase (TERT). The reverse transcriptase (RT) domain is located in the C-terminal region of the TERT polypeptide. Single amino acid substitutions in this region lead to telomere shortening and senescence. Telomerase is an enzyme that, in certain cells, maintains the physical ends of chromosomes (telomeres) during replication. In somatic cells, replication of the lagging strand requires the continual presence of an RNA primer approximately 200 nucleotides upstream, which is complementary to the template strand. Since there is a region of DNA less than 200 base pairs from the end of the chromosome where this is not possible, the chromosome is continually shortened. However, a surplus of repetitive DNA at the chromosome ends protects against the erosion of gene-encoding DNA. Telomerase is not normally expressed in somatic cells. It has been suggested that exogenous TERT may extend the lifespan of, or even immortalize, the cell. However, recent studies have shown that telomerase activity can be induced by a number of oncogenes. Conversely, the oncogene c-myc can be activated in human TERT immortalized cells. Sequence comparisons place the telomerase proteins in the RT family but reveal hallmarks that distinguish them from retroviral and retrotransposon relatives.


:

Pssm-ID: 238826  Cd Length: 119  Bit Score: 109.28  E-value: 6.73e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741827  816 RFYVQCQGIPQGSSLSTLLCSLCFGDMENKLF---AEVQQDGLLLRFVDDFLLVTPHLAHAKAFLSTLVHG-VPEYGCMI 891
Cdd:cd01648   12 QYYRQKVGIPQGSPLSSLLCSLYYADLENKYLsflDVIDKDSLLLRLVDDFLLITTSLDKAIKFLNLLLRGfINQYKTFV 91

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 55741827  892 NLQKTVVNFPVEtgalggaaphQLPAHCLFPWCGLLLD 929
Cdd:cd01648   92 NFDKTQINFSFA----------QLDSSDLIPWCGLLIN 119
 
Name Accession Description Interval E-value
Telomerase_RBD pfam12009
Telomerase ribonucleoprotein complex - RNA binding domain; Telomeres in most organizms are ...
 450-581 9.08e-58

Telomerase ribonucleoprotein complex - RNA binding domain; Telomeres in most organizms are comprised of tandem simple sequence repeats. The total length of telomeric repeat sequence at each chromosome end is determined in a balance of sequence loss and sequence addition. One major influence on telomere length is the enzyme telomerase. It is a reverse transcriptase that adds these simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. The RNA binding domain of telomerase - TRBD - is made up of twelve alpha helices and two short beta sheets. How telomerase and associated regulatory factors physically interact and function with each other to maintain appropriate telomere length is poorly understood. It is known however that TRBD is involved in formation of the holoenzyme (which performs the telomere extension) in addition to recognition and binding of RNA.


Pssm-ID: 463428  Cd Length: 133  Bit Score: 195.03  E-value: 9.08e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741827    450 QVYGFLRACLRELVPAGLWGTRHNERRFLKNVKKFISLGKYAKLSLQELMWRVKVEDCHWLRSSPEKDTVPAAEHRLRER 529
Cdd:pfam12009    1 QVSAFLRAVLRKLIPLELWGSKHNKRVLLKNVDRFIRLRRFESLSLHELMQGLKVSDFPWLGLPTKNSKLSLSDFEKRQE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 55741827    530 ILAMFLFWLMDTYVVQLLRSFFYITETTFQKNRLFFYRKSVWSKLQSIGIRQ 581
Cdd:pfam12009   81 LLAEFIYWLFDSLLIPLIRSFFYVTESSTHRNRLFYFRHDVWRKLSEPFLRK 132
Telomerase_RBD smart00975
Telomerase ribonucleoprotein complex - RNA binding domain; Telomeres in most organisms are ...
 450-584 6.75e-57

Telomerase ribonucleoprotein complex - RNA binding domain; Telomeres in most organisms are comprised of tandem simple sequence repeats. The total length of telomeric repeat sequence at each chromosome end is determined in a balance of sequence loss and sequence addition. One major influence on telomere length is the enzyme telomerase. It is a reverse transcriptase that adds these simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. The RNA binding domain of telomerase - TRBD - is made up of twelve alpha helices and two short beta sheets. How telomerase and associated regulatory factors physically interact and function with each other to maintain appropriate telomere length is poorly understood. It is known however that TRBD is involved in formation of the holoenzyme (which performs the telomere extension) in addition to recognition and binding of RNA.


Pssm-ID: 214948  Cd Length: 136  Bit Score: 192.86  E-value: 6.75e-57
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741827     450 QVYGFLRACLRELVPAGLWGTRHNERRFLKNVKKFISLGKYAKLSLQELMWRVKVEDCHWLRSSPEKDT-VPAAEHRLRE 528
Cdd:smart00975    1 QVVSFLRAILRKLFPLSLWGSRHNKRVFLKNLRRFLSLGRNEKFSLQELMWGIRVSDIPWLAGSKTTTQrVSKSEHEKRQ 80

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 55741827     529 RILAMFLFWLMDTYVVQLLRSFFYITETTFQKNRLFFYRKSVWSKLQSIGIRQQLE 584
Cdd:smart00975   81 ELLAQFVYWLFDCLVPPLLRSFFYVTESSGQKNKLLYFRHDVWKKLTRPALRRYLE 136
TERT cd01648
TERT: Telomerase reverse transcriptase (TERT). Telomerase is a ribonucleoprotein (RNP) that ...
 816-929 6.73e-28

TERT: Telomerase reverse transcriptase (TERT). Telomerase is a ribonucleoprotein (RNP) that synthesizes telomeric DNA repeats. The telomerase RNA subunit provides the template for synthesis of these repeats. The catalytic subunit of RNP is known as telomerase reverse transcriptase (TERT). The reverse transcriptase (RT) domain is located in the C-terminal region of the TERT polypeptide. Single amino acid substitutions in this region lead to telomere shortening and senescence. Telomerase is an enzyme that, in certain cells, maintains the physical ends of chromosomes (telomeres) during replication. In somatic cells, replication of the lagging strand requires the continual presence of an RNA primer approximately 200 nucleotides upstream, which is complementary to the template strand. Since there is a region of DNA less than 200 base pairs from the end of the chromosome where this is not possible, the chromosome is continually shortened. However, a surplus of repetitive DNA at the chromosome ends protects against the erosion of gene-encoding DNA. Telomerase is not normally expressed in somatic cells. It has been suggested that exogenous TERT may extend the lifespan of, or even immortalize, the cell. However, recent studies have shown that telomerase activity can be induced by a number of oncogenes. Conversely, the oncogene c-myc can be activated in human TERT immortalized cells. Sequence comparisons place the telomerase proteins in the RT family but reveal hallmarks that distinguish them from retroviral and retrotransposon relatives.


Pssm-ID: 238826  Cd Length: 119  Bit Score: 109.28  E-value: 6.73e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741827  816 RFYVQCQGIPQGSSLSTLLCSLCFGDMENKLF---AEVQQDGLLLRFVDDFLLVTPHLAHAKAFLSTLVHG-VPEYGCMI 891
Cdd:cd01648   12 QYYRQKVGIPQGSPLSSLLCSLYYADLENKYLsflDVIDKDSLLLRLVDDFLLITTSLDKAIKFLNLLLRGfINQYKTFV 91

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 55741827  892 NLQKTVVNFPVEtgalggaaphQLPAHCLFPWCGLLLD 929
Cdd:cd01648   92 NFDKTQINFSFA----------QLDSSDLIPWCGLLIN 119
 
Name Accession Description Interval E-value
Telomerase_RBD pfam12009
Telomerase ribonucleoprotein complex - RNA binding domain; Telomeres in most organizms are ...
 450-581 9.08e-58

Telomerase ribonucleoprotein complex - RNA binding domain; Telomeres in most organizms are comprised of tandem simple sequence repeats. The total length of telomeric repeat sequence at each chromosome end is determined in a balance of sequence loss and sequence addition. One major influence on telomere length is the enzyme telomerase. It is a reverse transcriptase that adds these simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. The RNA binding domain of telomerase - TRBD - is made up of twelve alpha helices and two short beta sheets. How telomerase and associated regulatory factors physically interact and function with each other to maintain appropriate telomere length is poorly understood. It is known however that TRBD is involved in formation of the holoenzyme (which performs the telomere extension) in addition to recognition and binding of RNA.


Pssm-ID: 463428  Cd Length: 133  Bit Score: 195.03  E-value: 9.08e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741827    450 QVYGFLRACLRELVPAGLWGTRHNERRFLKNVKKFISLGKYAKLSLQELMWRVKVEDCHWLRSSPEKDTVPAAEHRLRER 529
Cdd:pfam12009    1 QVSAFLRAVLRKLIPLELWGSKHNKRVLLKNVDRFIRLRRFESLSLHELMQGLKVSDFPWLGLPTKNSKLSLSDFEKRQE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 55741827    530 ILAMFLFWLMDTYVVQLLRSFFYITETTFQKNRLFFYRKSVWSKLQSIGIRQ 581
Cdd:pfam12009   81 LLAEFIYWLFDSLLIPLIRSFFYVTESSTHRNRLFYFRHDVWRKLSEPFLRK 132
Telomerase_RBD smart00975
Telomerase ribonucleoprotein complex - RNA binding domain; Telomeres in most organisms are ...
 450-584 6.75e-57

Telomerase ribonucleoprotein complex - RNA binding domain; Telomeres in most organisms are comprised of tandem simple sequence repeats. The total length of telomeric repeat sequence at each chromosome end is determined in a balance of sequence loss and sequence addition. One major influence on telomere length is the enzyme telomerase. It is a reverse transcriptase that adds these simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. The RNA binding domain of telomerase - TRBD - is made up of twelve alpha helices and two short beta sheets. How telomerase and associated regulatory factors physically interact and function with each other to maintain appropriate telomere length is poorly understood. It is known however that TRBD is involved in formation of the holoenzyme (which performs the telomere extension) in addition to recognition and binding of RNA.


Pssm-ID: 214948  Cd Length: 136  Bit Score: 192.86  E-value: 6.75e-57
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741827     450 QVYGFLRACLRELVPAGLWGTRHNERRFLKNVKKFISLGKYAKLSLQELMWRVKVEDCHWLRSSPEKDT-VPAAEHRLRE 528
Cdd:smart00975    1 QVVSFLRAILRKLFPLSLWGSRHNKRVFLKNLRRFLSLGRNEKFSLQELMWGIRVSDIPWLAGSKTTTQrVSKSEHEKRQ 80

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 55741827     529 RILAMFLFWLMDTYVVQLLRSFFYITETTFQKNRLFFYRKSVWSKLQSIGIRQQLE 584
Cdd:smart00975   81 ELLAQFVYWLFDCLVPPLLRSFFYVTESSGQKNKLLYFRHDVWKKLTRPALRRYLE 136
TERT cd01648
TERT: Telomerase reverse transcriptase (TERT). Telomerase is a ribonucleoprotein (RNP) that ...
 816-929 6.73e-28

TERT: Telomerase reverse transcriptase (TERT). Telomerase is a ribonucleoprotein (RNP) that synthesizes telomeric DNA repeats. The telomerase RNA subunit provides the template for synthesis of these repeats. The catalytic subunit of RNP is known as telomerase reverse transcriptase (TERT). The reverse transcriptase (RT) domain is located in the C-terminal region of the TERT polypeptide. Single amino acid substitutions in this region lead to telomere shortening and senescence. Telomerase is an enzyme that, in certain cells, maintains the physical ends of chromosomes (telomeres) during replication. In somatic cells, replication of the lagging strand requires the continual presence of an RNA primer approximately 200 nucleotides upstream, which is complementary to the template strand. Since there is a region of DNA less than 200 base pairs from the end of the chromosome where this is not possible, the chromosome is continually shortened. However, a surplus of repetitive DNA at the chromosome ends protects against the erosion of gene-encoding DNA. Telomerase is not normally expressed in somatic cells. It has been suggested that exogenous TERT may extend the lifespan of, or even immortalize, the cell. However, recent studies have shown that telomerase activity can be induced by a number of oncogenes. Conversely, the oncogene c-myc can be activated in human TERT immortalized cells. Sequence comparisons place the telomerase proteins in the RT family but reveal hallmarks that distinguish them from retroviral and retrotransposon relatives.


Pssm-ID: 238826  Cd Length: 119  Bit Score: 109.28  E-value: 6.73e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741827  816 RFYVQCQGIPQGSSLSTLLCSLCFGDMENKLF---AEVQQDGLLLRFVDDFLLVTPHLAHAKAFLSTLVHG-VPEYGCMI 891
Cdd:cd01648   12 QYYRQKVGIPQGSPLSSLLCSLYYADLENKYLsflDVIDKDSLLLRLVDDFLLITTSLDKAIKFLNLLLRGfINQYKTFV 91

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 55741827  892 NLQKTVVNFPVEtgalggaaphQLPAHCLFPWCGLLLD 929
Cdd:cd01648   92 NFDKTQINFSFA----------QLDSSDLIPWCGLLIN 119
RT_Bac_retron_I cd01646
RT_Bac_retron_I: Reverse transcriptases (RTs) in bacterial retrotransposons or retrons. The ...
 858-901 8.69e-03

RT_Bac_retron_I: Reverse transcriptases (RTs) in bacterial retrotransposons or retrons. The polymerase reaction of this enzyme leads to the production of a unique RNA-DNA complex called msDNA (multicopy single-stranded (ss)DNA) in which a small ssDNA branches out from a small ssRNA molecule via a 2'-5'phosphodiester linkage. Bacterial retron RTs produce cDNA corresponding to only a small portion of the retron genome.


Pssm-ID: 238824 [Multi-domain]  Cd Length: 158  Bit Score: 38.08  E-value: 8.69e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 55741827  858 RFVDDFLLVTPHLAHAKAFLSTLVHGVPEYGCMINLQKT-VVNFP 901
Cdd:cd01646   87 RYVDDIRIFADSKEEAEEILEELKEFLAELGLSLNLSKTeILPLP 131
 
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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