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Conserved domains on  [gi|13359215|dbj|BAB33341|]
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KIAA1671 protein, partial [Homo sapiens]

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 ...
 186-355 1.06e-74

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: 228.53  E-value: 1.06e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13359215   186 DFSFIDQTSVLDSSALKTRVQLSKRSRRRAPISHSLRRSRFSESEsrsPLEDETDNTWMFKDSTEEKSPRK-EESDEEET 264
Cdd:pfam15327   1 DFSFIEQTSVLDSSALKTRAQLGKKRRRRAPPSRSLRRSEAENGG---PLEEEDDSAWMFKDSTEEKSPSRqEDSDEEEP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13359215   265 AS--KAERTPVSHPQRMPAFPGMDPAVLKAQLHKRPEVDSPGETPSWAPQPKSPKSPFQPGVlGSRVLPSSMDKDERSDE 342
Cdd:pfam15327  78 EQspRSERSPVTQPQRVPLFPGMDPSALKAQLRKRNESDSPGEGPSPSQLSKSPKSPFLPGK-GPRVLPPSGEKESGSEE 156

                         170
                  ....*....|...
gi 13359215   343 PSPQWLKELKSKK 355
Cdd:pfam15327 157 SSPQWLKELKSKK 169
 
Name Accession Description Interval E-value
Tankyrase_bdg_C pfam15327
Tankyrase binding protein C terminal domain; This protein domain family is found at the ...
 186-355 1.06e-74

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: 228.53  E-value: 1.06e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13359215   186 DFSFIDQTSVLDSSALKTRVQLSKRSRRRAPISHSLRRSRFSESEsrsPLEDETDNTWMFKDSTEEKSPRK-EESDEEET 264
Cdd:pfam15327   1 DFSFIEQTSVLDSSALKTRAQLGKKRRRRAPPSRSLRRSEAENGG---PLEEEDDSAWMFKDSTEEKSPSRqEDSDEEEP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13359215   265 AS--KAERTPVSHPQRMPAFPGMDPAVLKAQLHKRPEVDSPGETPSWAPQPKSPKSPFQPGVlGSRVLPSSMDKDERSDE 342
Cdd:pfam15327  78 EQspRSERSPVTQPQRVPLFPGMDPSALKAQLRKRNESDSPGEGPSPSQLSKSPKSPFLPGK-GPRVLPPSGEKESGSEE 156

                         170
                  ....*....|...
gi 13359215   343 PSPQWLKELKSKK 355
Cdd:pfam15327 157 SSPQWLKELKSKK 169
 
Name Accession Description Interval E-value
Tankyrase_bdg_C pfam15327
Tankyrase binding protein C terminal domain; This protein domain family is found at the ...
 186-355 1.06e-74

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: 228.53  E-value: 1.06e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13359215   186 DFSFIDQTSVLDSSALKTRVQLSKRSRRRAPISHSLRRSRFSESEsrsPLEDETDNTWMFKDSTEEKSPRK-EESDEEET 264
Cdd:pfam15327   1 DFSFIEQTSVLDSSALKTRAQLGKKRRRRAPPSRSLRRSEAENGG---PLEEEDDSAWMFKDSTEEKSPSRqEDSDEEEP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13359215   265 AS--KAERTPVSHPQRMPAFPGMDPAVLKAQLHKRPEVDSPGETPSWAPQPKSPKSPFQPGVlGSRVLPSSMDKDERSDE 342
Cdd:pfam15327  78 EQspRSERSPVTQPQRVPLFPGMDPSALKAQLRKRNESDSPGEGPSPSQLSKSPKSPFLPGK-GPRVLPPSGEKESGSEE 156

                         170
                  ....*....|...
gi 13359215   343 PSPQWLKELKSKK 355
Cdd:pfam15327 157 SSPQWLKELKSKK 169
 
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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