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Conserved domains on  [gi|1046354238|ref|NP_001316625|]
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ADP-ribose glycohydrolase OARD1 isoform d [Homo sapiens]

Protein Classification

macro domain-containing protein( domain architecture ID 1211)

macro domain-containing protein functions in the recognition, interpretation, and turnover of ADP-ribose (ADPr) signaling

CATH:  3.40.220.10
Gene Ontology:  GO:0072570
PubMed:  26844395|15902274
SCOP:  4000521

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Macro_SF super family cl00019
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 13-61 2.22e-23

macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Macrodomains include the yeast macrodomain Poa1 which is a phosphatase of ADP-ribose-1"-phosphate, a by-product of tRNA splicing. Some macrodomains have ADPr-unrelated binding partners such as the coronavirus SUD-N (N-terminal subdomain) and SUD-M (middle subdomain) of the SARS-unique domain (SUD) which bind G-quadruplexes (unusual nucleic-acid structures formed by consecutive guanosine nucleotides). Macrodomains regulate a wide variety of cellular and organismal processes, including DNA damage repair, signal transduction, and immune response.


The actual alignment was detected with superfamily member cd02901:

Pssm-ID: 469581  Cd Length: 135  Bit Score: 85.77  E-value: 2.22e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1046354238  13 RITYVKGDLFACPKTDSLAHCISEDCRMGAGIAVLFKKKFGGVQELLNQ 61
Cdd:cd02901     1 KITYVKGDLFACPETKSLAHCCNCDGVMGKGIALQFKKKPGRVEELRAQ 49
 
Name Accession Description Interval E-value
Macro_Poa1p-like cd02901
macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse ...
 13-61 2.22e-23

macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Members of this family show similarity to the yeast protein Poa1p, reported to be a phosphatase specific for Appr-1"-p, a tRNA splicing metabolite. Poa1p may play a role in tRNA splicing regulation.


Pssm-ID: 394873  Cd Length: 135  Bit Score: 85.77  E-value: 2.22e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1046354238  13 RITYVKGDLFACPKTDSLAHCISEDCRMGAGIAVLFKKKFGGVQELLNQ 61
Cdd:cd02901     1 KITYVKGDLFACPETKSLAHCCNCDGVMGKGIALQFKKKPGRVEELRAQ 49
 
Name Accession Description Interval E-value
Macro_Poa1p-like cd02901
macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse ...
 13-61 2.22e-23

macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Members of this family show similarity to the yeast protein Poa1p, reported to be a phosphatase specific for Appr-1"-p, a tRNA splicing metabolite. Poa1p may play a role in tRNA splicing regulation.


Pssm-ID: 394873  Cd Length: 135  Bit Score: 85.77  E-value: 2.22e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1046354238  13 RITYVKGDLFACPKTDSLAHCISEDCRMGAGIAVLFKKKFGGVQELLNQ 61
Cdd:cd02901     1 KITYVKGDLFACPETKSLAHCCNCDGVMGKGIALQFKKKPGRVEELRAQ 49
Macro_SF cd02749
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 28-57 3.75e-05

macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Macrodomains include the yeast macrodomain Poa1 which is a phosphatase of ADP-ribose-1"-phosphate, a by-product of tRNA splicing. Some macrodomains have ADPr-unrelated binding partners such as the coronavirus SUD-N (N-terminal subdomain) and SUD-M (middle subdomain) of the SARS-unique domain (SUD) which bind G-quadruplexes (unusual nucleic-acid structures formed by consecutive guanosine nucleotides). Macrodomains regulate a wide variety of cellular and organismal processes, including DNA damage repair, signal transduction, and immune response.


Pssm-ID: 394871  Cd Length: 121  Bit Score: 38.53  E-value: 3.75e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1046354238  28 DSLAHCISEDCRMGAGIAVLFKKKFGGVQE 57
Cdd:cd02749     1 DAIVNPANNDLYLGGGVAKAISKKAGGDLQ 30
 
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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