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Conserved domains on  [gi|1474879996|ref|XP_026235825|]
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telomerase reverse transcriptase isoform X1 [Urocitellus parryii]

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

EC:  2.7.7.49
Gene Ontology:  GO:0003677|GO:0003721
PubMed:  32770221|9110970

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 ...
 428-560 1.96e-62

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: 208.12  E-value: 1.96e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474879996  428 QVYAFLRACLSRLVPAGLWGSRHNQRRFLRNVKRFISLGKHARLSLRELTWKMKVRDCAWLRRSPG*HCVPAAEHRLRAQ 507
Cdd:pfam12009    1 QVSAFLRAVLRKLIPLELWGSKHNKRVLLKNVDRFIRLRRFESLSLHELMQGLKVSDFPWLGLPTKNSKLSLSDFEKRQE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1474879996  508 ILAKFLFWLVDTYVVGLLRSFFYVTETTFQKNRLLFYRQS*WRRLQSVGVRQL 560
Cdd:pfam12009   81 LLAEFIYWLFDSLLIPLIRSFFYVTESSTHRNRLFYFRHDVWRKLSEPFLRKL 133
TERT cd01648
TERT: Telomerase reverse transcriptase (TERT). Telomerase is a ribonucleoprotein (RNP) that ...
 792-905 7.50e-41

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: 146.26  E-value: 7.50e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474879996  792 RYYVQCRGIPQGSVLSTLLCSLCYGDMENKLFAGVQ---QDGVLLRLVDDFLLVTPHLAQARAFLRALVQG-VPEYGCQI 867
Cdd:cd01648     12 QYYRQKVGIPQGSPLSSLLCSLYYADLENKYLSFLDvidKDSLLLRLVDDFLLITTSLDKAIKFLNLLLRGfINQYKTFV 91

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1474879996  868 NLQKTVVNFPVEseapsgaaplQLPAHCLFPWCGLLLD 905
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 ...
 428-560 1.96e-62

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: 208.12  E-value: 1.96e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474879996  428 QVYAFLRACLSRLVPAGLWGSRHNQRRFLRNVKRFISLGKHARLSLRELTWKMKVRDCAWLRRSPG*HCVPAAEHRLRAQ 507
Cdd:pfam12009    1 QVSAFLRAVLRKLIPLELWGSKHNKRVLLKNVDRFIRLRRFESLSLHELMQGLKVSDFPWLGLPTKNSKLSLSDFEKRQE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1474879996  508 ILAKFLFWLVDTYVVGLLRSFFYVTETTFQKNRLLFYRQS*WRRLQSVGVRQL 560
Cdd:pfam12009   81 LLAEFIYWLFDSLLIPLIRSFFYVTESSTHRNRLFYFRHDVWRKLSEPFLRKL 133
Telomerase_RBD smart00975
Telomerase ribonucleoprotein complex - RNA binding domain; Telomeres in most organisms are ...
 428-562 2.17e-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: 194.01  E-value: 2.17e-57
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474879996   428 QVYAFLRACLSRLVPAGLWGSRHNQRRFLRNVKRFISLGKHARLSLRELTWKMKVRDCAWLRRSPG*H-CVPAAEHRLRA 506
Cdd:smart00975    1 QVVSFLRAILRKLFPLSLWGSRHNKRVFLKNLRRFLSLGRNEKFSLQELMWGIRVSDIPWLAGSKTTTqRVSKSEHEKRQ 80

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1474879996   507 QILAKFLFWLVDTYVVGLLRSFFYVTETTFQKNRLLFYRQS*WRRLQSVGVRQLLE 562
Cdd:smart00975   81 ELLAQFVYWLFDCLVPPLLRSFFYVTESSGQKNKLLYFRHDVWKKLTRPALRRYLE 136
TERT cd01648
TERT: Telomerase reverse transcriptase (TERT). Telomerase is a ribonucleoprotein (RNP) that ...
 792-905 7.50e-41

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: 146.26  E-value: 7.50e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474879996  792 RYYVQCRGIPQGSVLSTLLCSLCYGDMENKLFAGVQ---QDGVLLRLVDDFLLVTPHLAQARAFLRALVQG-VPEYGCQI 867
Cdd:cd01648     12 QYYRQKVGIPQGSPLSSLLCSLYYADLENKYLSFLDvidKDSLLLRLVDDFLLITTSLDKAIKFLNLLLRGfINQYKTFV 91

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1474879996  868 NLQKTVVNFPVEseapsgaaplQLPAHCLFPWCGLLLD 905
Cdd:cd01648     92 NFDKTQINFSFA----------QLDSSDLIPWCGLLIN 119
RVT_1 pfam00078
Reverse transcriptase (RNA-dependent DNA polymerase); A reverse transcriptase gene is usually ...
 775-874 8.44e-09

Reverse transcriptase (RNA-dependent DNA polymerase); A reverse transcriptase gene is usually indicative of a mobile element such as a retrotransposon or retrovirus. Reverse transcriptases occur in a variety of mobile elements, including retrotransposons, retroviruses, group II introns, bacterial msDNAs, hepadnaviruses, and caulimoviruses.


Pssm-ID: 395031 [Multi-domain]  Cd Length: 189  Bit Score: 56.54  E-value: 8.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474879996  775 FDFFLRFVRSSVVRIGGRYyvQCRGIPQGSVLSTLLCSLCYGDMENKL--FAGVQqdgvLLRLVDDFLLVTPHLAQARAF 852
Cdd:pfam00078   80 FTTPPININWNGELSGGRY--EWKGLPQGLVLSPALFQLFMNELLRPLrkRAGLT----LVRYADDILIFSKSEEEHQEA 153

                           90       100
                   ....*....|....*....|..
gi 1474879996  853 LRALVQGVPEYGCQINLQKTVV 874
Cdd:pfam00078  154 LEEVLEWLKESGLKINPEKTQF 175
 
Name Accession Description Interval E-value
Telomerase_RBD pfam12009
Telomerase ribonucleoprotein complex - RNA binding domain; Telomeres in most organizms are ...
 428-560 1.96e-62

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: 208.12  E-value: 1.96e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474879996  428 QVYAFLRACLSRLVPAGLWGSRHNQRRFLRNVKRFISLGKHARLSLRELTWKMKVRDCAWLRRSPG*HCVPAAEHRLRAQ 507
Cdd:pfam12009    1 QVSAFLRAVLRKLIPLELWGSKHNKRVLLKNVDRFIRLRRFESLSLHELMQGLKVSDFPWLGLPTKNSKLSLSDFEKRQE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1474879996  508 ILAKFLFWLVDTYVVGLLRSFFYVTETTFQKNRLLFYRQS*WRRLQSVGVRQL 560
Cdd:pfam12009   81 LLAEFIYWLFDSLLIPLIRSFFYVTESSTHRNRLFYFRHDVWRKLSEPFLRKL 133
Telomerase_RBD smart00975
Telomerase ribonucleoprotein complex - RNA binding domain; Telomeres in most organisms are ...
 428-562 2.17e-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: 194.01  E-value: 2.17e-57
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474879996   428 QVYAFLRACLSRLVPAGLWGSRHNQRRFLRNVKRFISLGKHARLSLRELTWKMKVRDCAWLRRSPG*H-CVPAAEHRLRA 506
Cdd:smart00975    1 QVVSFLRAILRKLFPLSLWGSRHNKRVFLKNLRRFLSLGRNEKFSLQELMWGIRVSDIPWLAGSKTTTqRVSKSEHEKRQ 80

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1474879996   507 QILAKFLFWLVDTYVVGLLRSFFYVTETTFQKNRLLFYRQS*WRRLQSVGVRQLLE 562
Cdd:smart00975   81 ELLAQFVYWLFDCLVPPLLRSFFYVTESSGQKNKLLYFRHDVWKKLTRPALRRYLE 136
TERT cd01648
TERT: Telomerase reverse transcriptase (TERT). Telomerase is a ribonucleoprotein (RNP) that ...
 792-905 7.50e-41

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: 146.26  E-value: 7.50e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474879996  792 RYYVQCRGIPQGSVLSTLLCSLCYGDMENKLFAGVQ---QDGVLLRLVDDFLLVTPHLAQARAFLRALVQG-VPEYGCQI 867
Cdd:cd01648     12 QYYRQKVGIPQGSPLSSLLCSLYYADLENKYLSFLDvidKDSLLLRLVDDFLLITTSLDKAIKFLNLLLRGfINQYKTFV 91

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1474879996  868 NLQKTVVNFPVEseapsgaaplQLPAHCLFPWCGLLLD 905
Cdd:cd01648     92 NFDKTQINFSFA----------QLDSSDLIPWCGLLIN 119
RVT_1 pfam00078
Reverse transcriptase (RNA-dependent DNA polymerase); A reverse transcriptase gene is usually ...
 775-874 8.44e-09

Reverse transcriptase (RNA-dependent DNA polymerase); A reverse transcriptase gene is usually indicative of a mobile element such as a retrotransposon or retrovirus. Reverse transcriptases occur in a variety of mobile elements, including retrotransposons, retroviruses, group II introns, bacterial msDNAs, hepadnaviruses, and caulimoviruses.


Pssm-ID: 395031 [Multi-domain]  Cd Length: 189  Bit Score: 56.54  E-value: 8.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474879996  775 FDFFLRFVRSSVVRIGGRYyvQCRGIPQGSVLSTLLCSLCYGDMENKL--FAGVQqdgvLLRLVDDFLLVTPHLAQARAF 852
Cdd:pfam00078   80 FTTPPININWNGELSGGRY--EWKGLPQGLVLSPALFQLFMNELLRPLrkRAGLT----LVRYADDILIFSKSEEEHQEA 153

                           90       100
                   ....*....|....*....|..
gi 1474879996  853 LRALVQGVPEYGCQINLQKTVV 874
Cdd:pfam00078  154 LEEVLEWLKESGLKINPEKTQF 175
RT_Bac_retron_I cd01646
RT_Bac_retron_I: Reverse transcriptases (RTs) in bacterial retrotransposons or retrons. The ...
 798-877 2.50e-05

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: 45.78  E-value: 2.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474879996  798 RGIPQGSVLSTLLC--SLCYGD--MENKLfagvqQDGVLLRLVDDFLLVTPHLAQARAFLRALVQGVPEYGCQINLQKT- 872
Cdd:cd01646     52 NGLPIGPLTSRFLAniYLNDVDheLKSKL-----KGVDYVRYVDDIRIFADSKEEAEEILEELKEFLAELGLSLNLSKTe 126


                   ....*
gi 1474879996  873 VVNFP 877
Cdd:cd01646    127 ILPLP 131
RT_G2_intron cd01651
RT_G2_intron: Reverse transcriptases (RTs) with group II intron origin. RT transcribes DNA ...
 779-880 3.97e-05

RT_G2_intron: Reverse transcriptases (RTs) with group II intron origin. RT transcribes DNA using RNA as template. Proteins in this subfamily are found in bacterial and mitochondrial group II introns. Their most probable ancestor was a retrotransposable element with both gag-like and pol-like genes. This subfamily of proteins appears to have captured the RT sequences from transposable elements, which lack long terminal repeats (LTRs).


Pssm-ID: 238828 [Multi-domain]  Cd Length: 226  Bit Score: 46.04  E-value: 3.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474879996  779 LRFVRSSVVRIGGRYYVQCRGIPQGSVLSTLLCSLCYGDMENKLFAGVQQ----------DGVLLRLVDDFLLVTPHLAQ 848
Cdd:cd01651    106 IRKWLKAGVLEDGKLVETEKGTPQGGVISPLLANIYLHELDKFVEEKLKEyydtsdpkfrRLRYVRYADDFVIGVRGPKE 185

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1474879996  849 ARAFLRALVQGVPEYGCQINLQKT-VVNFPVES 880
Cdd:cd01651    186 AEEIKELIREFLEELGLELNPEKTrITHFKSEG 218
RT_nLTR_like cd01650
RT_nLTR: Non-LTR (long terminal repeat) retrotransposon and non-LTR retrovirus reverse ...
 799-874 2.02e-03

RT_nLTR: Non-LTR (long terminal repeat) retrotransposon and non-LTR retrovirus reverse transcriptase (RT). This subfamily contains both non-LTR retrotransposons and non-LTR retrovirus RTs. RTs catalyze the conversion of single-stranded RNA into double-stranded DNA for integration into host chromosomes. RT is a multifunctional enzyme with RNA-directed DNA polymerase, DNA directed DNA polymerase and ribonuclease hybrid (RNase H) activities.


Pssm-ID: 238827 [Multi-domain]  Cd Length: 220  Bit Score: 41.12  E-value: 2.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474879996  799 GIPQGSVLSTLLCSLCYGDMENKL--FAGVQQDGVLLRLV---DDFLLVTPHLAQARAFLRALVQG-VPEYGCQINLQKT 872
Cdd:cd01650    106 GVRQGDPLSPLLFNLALDDLLRLLnkEEEIKLGGPGITHLayaDDIVLFSEGKSRKLQELLQRLQEwSKESGLKINPSKS 185


                   ..
gi 1474879996  873 VV 874
Cdd:cd01650    186 KV 187
 
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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