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Conserved domains on  [gi|1958765644|ref|XP_038962377|]
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182 kDa tankyrase-1-binding protein isoform X2 [Rattus norvegicus]

Protein Classification

Tankyrase_bdg_C domain-containing protein( domain architecture ID 10633972)

Tankyrase_bdg_C domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tankyrase_bdg_C pfam15327
Tankyrase binding protein C terminal domain; This protein domain family is found at the ...
 926-1091 1.69e-47

Tankyrase binding protein C terminal domain; This protein domain family is found at the C-terminal end of the Tankyrase binding protein in eukaryotes. The precise function of this protein is still unknown. However, it is known interacts with the enzyme tankyrase, a telomeric poly(ADP-ribose) polymerase, by binding to it. Tankyrin catalyzes poly(ADP-ribose) chain formation onto proteins. More specifically, it binds to the ankyrin domain in tankyrase. The protein domain is approximately 170 amino acids in length and contains two conserved sequence motifs: FPG and LKA.


:

Pssm-ID: 464648  Cd Length: 169  Bit Score: 167.29  E-value: 1.69e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765644  926 DFSFIEDTEILDSAMYRSRANLGRKRGHRAPAIRP-----GGTLGLSETADMDARLFQDSTEPRA-SRVPSSDEEVVEep 999
Cdd:pfam15327    1 DFSFIEQTSVLDSSALKTRAQLGKKRRRRAPPSRSlrrseAENGGPLEEEDDSAWMFKDSTEEKSpSRQEDSDEEEPE-- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765644 1000 QSRRTRMSLGTKGLKVNLFPGLSPSALKAKLRSRNRSAEEGEVTeskssqkeSSVQRSKSCKVPGL--GKPLTLPPKPEK 1077
Cdd:pfam15327   79 QSPRSERSPVTQPQRVPLFPGMDPSALKAQLRKRNESDSPGEGP--------SPSQLSKSPKSPFLpgKGPRVLPPSGEK 150

                          170
                   ....*....|....
gi 1958765644 1078 SSGSEGSSPNWLQA 1091
Cdd:pfam15327  151 ESGSEESSPQWLKE 164
 
Name Accession Description Interval E-value
Tankyrase_bdg_C pfam15327
Tankyrase binding protein C terminal domain; This protein domain family is found at the ...
 926-1091 1.69e-47

Tankyrase binding protein C terminal domain; This protein domain family is found at the C-terminal end of the Tankyrase binding protein in eukaryotes. The precise function of this protein is still unknown. However, it is known interacts with the enzyme tankyrase, a telomeric poly(ADP-ribose) polymerase, by binding to it. Tankyrin catalyzes poly(ADP-ribose) chain formation onto proteins. More specifically, it binds to the ankyrin domain in tankyrase. The protein domain is approximately 170 amino acids in length and contains two conserved sequence motifs: FPG and LKA.


Pssm-ID: 464648  Cd Length: 169  Bit Score: 167.29  E-value: 1.69e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765644  926 DFSFIEDTEILDSAMYRSRANLGRKRGHRAPAIRP-----GGTLGLSETADMDARLFQDSTEPRA-SRVPSSDEEVVEep 999
Cdd:pfam15327    1 DFSFIEQTSVLDSSALKTRAQLGKKRRRRAPPSRSlrrseAENGGPLEEEDDSAWMFKDSTEEKSpSRQEDSDEEEPE-- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765644 1000 QSRRTRMSLGTKGLKVNLFPGLSPSALKAKLRSRNRSAEEGEVTeskssqkeSSVQRSKSCKVPGL--GKPLTLPPKPEK 1077
Cdd:pfam15327   79 QSPRSERSPVTQPQRVPLFPGMDPSALKAQLRKRNESDSPGEGP--------SPSQLSKSPKSPFLpgKGPRVLPPSGEK 150

                          170
                   ....*....|....
gi 1958765644 1078 SSGSEGSSPNWLQA 1091
Cdd:pfam15327  151 ESGSEESSPQWLKE 164
 
Name Accession Description Interval E-value
Tankyrase_bdg_C pfam15327
Tankyrase binding protein C terminal domain; This protein domain family is found at the ...
 926-1091 1.69e-47

Tankyrase binding protein C terminal domain; This protein domain family is found at the C-terminal end of the Tankyrase binding protein in eukaryotes. The precise function of this protein is still unknown. However, it is known interacts with the enzyme tankyrase, a telomeric poly(ADP-ribose) polymerase, by binding to it. Tankyrin catalyzes poly(ADP-ribose) chain formation onto proteins. More specifically, it binds to the ankyrin domain in tankyrase. The protein domain is approximately 170 amino acids in length and contains two conserved sequence motifs: FPG and LKA.


Pssm-ID: 464648  Cd Length: 169  Bit Score: 167.29  E-value: 1.69e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765644  926 DFSFIEDTEILDSAMYRSRANLGRKRGHRAPAIRP-----GGTLGLSETADMDARLFQDSTEPRA-SRVPSSDEEVVEep 999
Cdd:pfam15327    1 DFSFIEQTSVLDSSALKTRAQLGKKRRRRAPPSRSlrrseAENGGPLEEEDDSAWMFKDSTEEKSpSRQEDSDEEEPE-- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958765644 1000 QSRRTRMSLGTKGLKVNLFPGLSPSALKAKLRSRNRSAEEGEVTeskssqkeSSVQRSKSCKVPGL--GKPLTLPPKPEK 1077
Cdd:pfam15327   79 QSPRSERSPVTQPQRVPLFPGMDPSALKAQLRKRNESDSPGEGP--------SPSQLSKSPKSPFLpgKGPRVLPPSGEK 150

                          170
                   ....*....|....
gi 1958765644 1078 SSGSEGSSPNWLQA 1091
Cdd:pfam15327  151 ESGSEESSPQWLKE 164
 
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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