NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1034567808|ref|XP_016871577|]
View 

DNA polymerase lambda isoform X11 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
BRCT_polymerase_lambda cd17715
BRCT domain of DNA polymerase lambda and similar proteins; DNA polymerase lambda, also termed ...
 41-125 6.21e-30

BRCT domain of DNA polymerase lambda and similar proteins; DNA polymerase lambda, also termed Pol Lambda, or DNA polymerase beta-2 (Pol beta2), or DNA polymerase kappa, is involved in base excision repair (BER) and is responsible for repair of lesions that give rise to abasic (AP) sites in DNA. It also contributes to DNA double-strand break repair by non-homologous end joining and homologous recombination. DNA polymerase lambda has both template-dependent and template-independent (terminal transferase) DNA polymerase activities, as well as a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity. DNA polymerase lambda contains one BRCT domain.


:

Pssm-ID: 349347  Cd Length: 80  Bit Score: 109.89  E-value: 6.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567808  41 LSSLRAHVVRTGIGRARAELFEKQIVQHGGQLCPAQGPGVTHIVVDEGMDYEralrlLRLPQLPPGAQLVKSAWLSLCLQ 120
Cdd:cd17715     1 FEGLTIHLVRTGIGRARAELFQRYIVQYGGQIVEDFGEGVTHVVVDDGMDAE-----RKVDRDPPGAQLVKSGWLSACIQ 75


                  ....*
gi 1034567808 121 ERRLV 125
Cdd:cd17715    76 EKRLV 80
 
Name Accession Description Interval E-value
BRCT_polymerase_lambda cd17715
BRCT domain of DNA polymerase lambda and similar proteins; DNA polymerase lambda, also termed ...
 41-125 6.21e-30

BRCT domain of DNA polymerase lambda and similar proteins; DNA polymerase lambda, also termed Pol Lambda, or DNA polymerase beta-2 (Pol beta2), or DNA polymerase kappa, is involved in base excision repair (BER) and is responsible for repair of lesions that give rise to abasic (AP) sites in DNA. It also contributes to DNA double-strand break repair by non-homologous end joining and homologous recombination. DNA polymerase lambda has both template-dependent and template-independent (terminal transferase) DNA polymerase activities, as well as a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity. DNA polymerase lambda contains one BRCT domain.


Pssm-ID: 349347  Cd Length: 80  Bit Score: 109.89  E-value: 6.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567808  41 LSSLRAHVVRTGIGRARAELFEKQIVQHGGQLCPAQGPGVTHIVVDEGMDYEralrlLRLPQLPPGAQLVKSAWLSLCLQ 120
Cdd:cd17715     1 FEGLTIHLVRTGIGRARAELFQRYIVQYGGQIVEDFGEGVTHVVVDDGMDAE-----RKVDRDPPGAQLVKSGWLSACIQ 75


                  ....*
gi 1034567808 121 ERRLV 125
Cdd:cd17715    76 EKRLV 80
 
Name Accession Description Interval E-value
BRCT_polymerase_lambda cd17715
BRCT domain of DNA polymerase lambda and similar proteins; DNA polymerase lambda, also termed ...
 41-125 6.21e-30

BRCT domain of DNA polymerase lambda and similar proteins; DNA polymerase lambda, also termed Pol Lambda, or DNA polymerase beta-2 (Pol beta2), or DNA polymerase kappa, is involved in base excision repair (BER) and is responsible for repair of lesions that give rise to abasic (AP) sites in DNA. It also contributes to DNA double-strand break repair by non-homologous end joining and homologous recombination. DNA polymerase lambda has both template-dependent and template-independent (terminal transferase) DNA polymerase activities, as well as a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity. DNA polymerase lambda contains one BRCT domain.


Pssm-ID: 349347  Cd Length: 80  Bit Score: 109.89  E-value: 6.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034567808  41 LSSLRAHVVRTGIGRARAELFEKQIVQHGGQLCPAQGPGVTHIVVDEGMDYEralrlLRLPQLPPGAQLVKSAWLSLCLQ 120
Cdd:cd17715     1 FEGLTIHLVRTGIGRARAELFQRYIVQYGGQIVEDFGEGVTHVVVDDGMDAE-----RKVDRDPPGAQLVKSGWLSACIQ 75


                  ....*
gi 1034567808 121 ERRLV 125
Cdd:cd17715    76 EKRLV 80
BRCT_DNA_ligase_IV_rpt1 cd17722
first BRCT domain of DNA ligase 4 (LIG4) and similar proteins; LIG4 (EC 6.5.1.1), also termed ...
 57-125 7.54e-03

first BRCT domain of DNA ligase 4 (LIG4) and similar proteins; LIG4 (EC 6.5.1.1), also termed DNA ligase IV, or polydeoxyribonucleotide synthase [ATP] 4, is involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. It is a component of the LIG4-XRCC4 complex that is responsible for the NHEJ ligation step. LIG4 contains two BRCT domains. The family corresponds to the first one.


Pssm-ID: 349354 [Multi-domain]  Cd Length: 90  Bit Score: 35.35  E-value: 7.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034567808  57 RAELfEKQIVQHGGQLCPAQGPGVTHIVVDEGMDYEralrlLRLPQLPPGAQLVKSAWLSLCLQERRLV 125
Cdd:cd17722    19 KAEL-EKLIKENGGKVVQNPGAPDTICVIAGREVVK-----VKNLIKSGGHDVVKPSWLLDCIARKELL 81
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH