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Conserved domains on  [gi|24654167|ref|NP_725583|]
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Poly(ADP-ribose) polymerase family member 16 [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ARTD15_N pfam18084
ARTD15 N-terminal domain; This is the N-terminal domain of poly ADP-ribose polymerase (PARP16 ...
 53-132 9.97e-22

ARTD15 N-terminal domain; This is the N-terminal domain of poly ADP-ribose polymerase (PARP16 also known as ARTD15) present in homo sapiens. ARTDs catalyze the formation of branched or unbranched chains of ADP-ribose units on protein side chains. The N-terminal domain of ARTD15 does not share any obvious sequence similarity with the regulatory domains of ARTD1-4. The N-terminal domain arrangement in both ARTD15 and ARTD1-3 suggests a regulatory role through different mechanisms.


:

Pssm-ID: 465641  Cd Length: 81  Bit Score: 87.63  E-value: 9.97e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654167    53 RRLQDDFLGCEALWTIFMAAAWSYRYRTRLRPFPSHWN-----TIDLVFNTLGDAPRLEVLQQQLMHCdyqaCSPNVVRL 127
Cdd:pfam18084   1 EALQRDLLAADLKWSLFVAAAQSYRYDSVLRPFPPQFIkedekDIDALREVVSDLPSLEELLLANLND----LDPDVIDL 76


                  ....*
gi 24654167   128 LTDIL 132
Cdd:pfam18084  77 LHWVL 81
 
Name Accession Description Interval E-value
ARTD15_N pfam18084
ARTD15 N-terminal domain; This is the N-terminal domain of poly ADP-ribose polymerase (PARP16 ...
 53-132 9.97e-22

ARTD15 N-terminal domain; This is the N-terminal domain of poly ADP-ribose polymerase (PARP16 also known as ARTD15) present in homo sapiens. ARTDs catalyze the formation of branched or unbranched chains of ADP-ribose units on protein side chains. The N-terminal domain of ARTD15 does not share any obvious sequence similarity with the regulatory domains of ARTD1-4. The N-terminal domain arrangement in both ARTD15 and ARTD1-3 suggests a regulatory role through different mechanisms.


Pssm-ID: 465641  Cd Length: 81  Bit Score: 87.63  E-value: 9.97e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654167    53 RRLQDDFLGCEALWTIFMAAAWSYRYRTRLRPFPSHWN-----TIDLVFNTLGDAPRLEVLQQQLMHCdyqaCSPNVVRL 127
Cdd:pfam18084   1 EALQRDLLAADLKWSLFVAAAQSYRYDSVLRPFPPQFIkedekDIDALREVVSDLPSLEELLLANLND----LDPDVIDL 76


                  ....*
gi 24654167   128 LTDIL 132
Cdd:pfam18084  77 LHWVL 81
 
Name Accession Description Interval E-value
ARTD15_N pfam18084
ARTD15 N-terminal domain; This is the N-terminal domain of poly ADP-ribose polymerase (PARP16 ...
 53-132 9.97e-22

ARTD15 N-terminal domain; This is the N-terminal domain of poly ADP-ribose polymerase (PARP16 also known as ARTD15) present in homo sapiens. ARTDs catalyze the formation of branched or unbranched chains of ADP-ribose units on protein side chains. The N-terminal domain of ARTD15 does not share any obvious sequence similarity with the regulatory domains of ARTD1-4. The N-terminal domain arrangement in both ARTD15 and ARTD1-3 suggests a regulatory role through different mechanisms.


Pssm-ID: 465641  Cd Length: 81  Bit Score: 87.63  E-value: 9.97e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24654167    53 RRLQDDFLGCEALWTIFMAAAWSYRYRTRLRPFPSHWN-----TIDLVFNTLGDAPRLEVLQQQLMHCdyqaCSPNVVRL 127
Cdd:pfam18084   1 EALQRDLLAADLKWSLFVAAAQSYRYDSVLRPFPPQFIkedekDIDALREVVSDLPSLEELLLANLND----LDPDVIDL 76


                  ....*
gi 24654167   128 LTDIL 132
Cdd:pfam18084  77 LHWVL 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.
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