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Conserved domains on  [gi|1046354244|ref|NP_001316622|]
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ADP-ribose glycohydrolase OARD1 isoform c [Homo sapiens]

Protein Classification

macro domain-containing protein( domain architecture ID 10121048)

macro domain-containing protein functions in the recognition, interpretation, and turnover of ADP-ribose (ADPr) signaling, such as ADP-ribose 1''-phosphate phosphatase that is involved in the metabolism of ADP-ribose 1''-phosphate (Appr1p) which is produced as a consequence of tRNA splicing

CATH:  3.40.220.10
Gene Ontology:  GO:0072570|GO:0019213
PubMed:  26844395|15902274|21421074|32214744
SCOP:  4000521

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Macro_Poa1p-like cd02901
macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse ...
 13-81 1.07e-31

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: 107.34  E-value: 1.07e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046354244  13 RITYVKGDLFACPKTDSLAHCISEDCRMGAGIAVLFKKKFGGVQELLNQQKKS--GEVAVLKRDG--RYIYYL 81
Cdd:cd02901     1 KITYVKGDLFACPETKSLAHCCNCDGVMGKGIALQFKKKPGRVEELRAQCKKKllGGVAVLKRDGvkRYIYYL 73
 
Name Accession Description Interval E-value
Macro_Poa1p-like cd02901
macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse ...
 13-81 1.07e-31

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: 107.34  E-value: 1.07e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046354244  13 RITYVKGDLFACPKTDSLAHCISEDCRMGAGIAVLFKKKFGGVQELLNQQKKS--GEVAVLKRDG--RYIYYL 81
Cdd:cd02901     1 KITYVKGDLFACPETKSLAHCCNCDGVMGKGIALQFKKKPGRVEELRAQCKKKllGGVAVLKRDGvkRYIYYL 73
PHA03033 PHA03033
hypothetical protein; Provisional
 49-81 5.92e-06

hypothetical protein; Provisional


Pssm-ID: 165330  Cd Length: 142  Bit Score: 41.50  E-value: 5.92e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1046354244  49 KKKFGGVQELLNQQKKSGEVAVLKRDGRYIYYL 81
Cdd:PHA03033   42 KKKYNSIKELKKQKKKKGEVAYIYKNNKYIIYI 74
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 13-57 8.59e-03

Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by reciprocal PSI-BLAST searches (unpublished results, and Pehrson _ Fuji).


Pssm-ID: 214701  Cd Length: 133  Bit Score: 32.66  E-value: 8.59e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1046354244   13 RITYVKGDLFAcPKTDSLAHCISEDCRMGAGIAVLFKKKFGGVQE 57
Cdd:smart00506   1 ILKVVKGDITK-PRADAIVNAANSDGAHGGGVAGAIARAAGKALS 44
 
Name Accession Description Interval E-value
Macro_Poa1p-like cd02901
macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse ...
 13-81 1.07e-31

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: 107.34  E-value: 1.07e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046354244  13 RITYVKGDLFACPKTDSLAHCISEDCRMGAGIAVLFKKKFGGVQELLNQQKKS--GEVAVLKRDG--RYIYYL 81
Cdd:cd02901     1 KITYVKGDLFACPETKSLAHCCNCDGVMGKGIALQFKKKPGRVEELRAQCKKKllGGVAVLKRDGvkRYIYYL 73
Macro_SF cd02749
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 28-83 9.65e-12

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: 56.25  E-value: 9.65e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046354244  28 DSLAHCISEDCRMGAGIAVLFKKKFGGVQE------LLNQQKKSGEVAVLKRDG---RYIYYLDW 83
Cdd:cd02749     1 DAIVNPANNDLYLGGGVAKAISKKAGGDLQeeceerKKNGYLKVGEVAVTKGGNlpaRYIIHVVG 65
PHA03033 PHA03033
hypothetical protein; Provisional
 49-81 5.92e-06

hypothetical protein; Provisional


Pssm-ID: 165330  Cd Length: 142  Bit Score: 41.50  E-value: 5.92e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1046354244  49 KKKFGGVQELLNQQKKSGEVAVLKRDGRYIYYL 81
Cdd:PHA03033   42 KKKYNSIKELKKQKKKKGEVAYIYKNNKYIIYI 74
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 13-57 8.59e-03

Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by reciprocal PSI-BLAST searches (unpublished results, and Pehrson _ Fuji).


Pssm-ID: 214701  Cd Length: 133  Bit Score: 32.66  E-value: 8.59e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1046354244   13 RITYVKGDLFAcPKTDSLAHCISEDCRMGAGIAVLFKKKFGGVQE 57
Cdd:smart00506   1 ILKVVKGDITK-PRADAIVNAANSDGAHGGGVAGAIARAAGKALS 44
 
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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