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Conserved domains on  [gi|2325215035|ref|NP_001400522|]
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ADP-ribose glycohydrolase OARD1 isoform 2 [Mus musculus]

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 ...
 1-104 1.39e-49

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: 153.95  E-value: 1.39e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2325215035   1 MGAGIAVLFKKRFGGVQELLSQQKKS--GEVAVLKRDG--RYIYYLITKKRASHKPTYENLQKSLEAMKSHCLKNGVTDL 76
Cdd:cd02901    28 MGKGIALQFKKKPGRVEELRAQCKKKllGGVAVLKRDGvkRYIYYLITKKSYGPKPTYEALRSSLEELREHCRENGVTSV 107

                          90       100
                  ....*....|....*....|....*...
gi 2325215035  77 SMPRIGCGLDRLQWENVSAILEEVFEST 104
Cdd:cd02901   108 AMPRIGCGLDGLDWEEVEPILKEVFDDR 135
 
Name Accession Description Interval E-value
Macro_Poa1p-like cd02901
macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse ...
 1-104 1.39e-49

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: 153.95  E-value: 1.39e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2325215035   1 MGAGIAVLFKKRFGGVQELLSQQKKS--GEVAVLKRDG--RYIYYLITKKRASHKPTYENLQKSLEAMKSHCLKNGVTDL 76
Cdd:cd02901    28 MGKGIALQFKKKPGRVEELRAQCKKKllGGVAVLKRDGvkRYIYYLITKKSYGPKPTYEALRSSLEELREHCRENGVTSV 107

                          90       100
                  ....*....|....*....|....*...
gi 2325215035  77 SMPRIGCGLDRLQWENVSAILEEVFEST 104
Cdd:cd02901   108 AMPRIGCGLDGLDWEEVEPILKEVFDDR 135
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 1-112 1.20e-09

O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441713  Cd Length: 168  Bit Score: 52.49  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2325215035   1 MGAGIAVLFKKRFG-GVQELLSQQKKSGEV----AVLKRDG----RYIYYLITKK-RASHKPTYENLQKSLEAMKSHCLK 70
Cdd:COG2110    26 GGGGVAGAIHRAAGpELLEECRRLCKQGGCptgeAVITPAGnlpaKYVIHTVGPVwRGGGPSEEELLASCYRNSLELAEE 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2325215035  71 NGVTDLSMPRIGCGLDRLQWENVSAILEEVFES--------TDIKITVYT 112
Cdd:COG2110   106 LGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDfleehpslEEVRFVLFD 155
tk.4 PHA02595
hypothetical protein; Provisional
 1-110 1.60e-09

hypothetical protein; Provisional


Pssm-ID: 222899  Cd Length: 154  Bit Score: 52.00  E-value: 1.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2325215035   1 MGAGIAVLFKKRFGGVQELLSQQ-----KKSGEVAVLKRDGR----YIYYLITKKRASHKPTYENLQKSLEAMKSHClKN 71
Cdd:PHA02595   31 MGSGIAGQLAKAFPQILEADKLTtegdvEKLGTFSVWEKYVGghkaYCFNLYTQFDPGPNLEYSALMNCFEELNEVF-EG 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2325215035  72 GVTDLSM--PRIGCGLDRLQWENVSAILEEVfeSTDIKITV 110
Cdd:PHA02595  110 TLFKPTIyiPRIGAGIAGGDWDKIEAIIDEA--TPDIDIVV 148
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 1-97 2.66e-06

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: 43.06  E-value: 2.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2325215035    1 MGAGIAVLFKKRFGGVQ---ELLSQQKK---SGEVAVL---KRDGRYIYYLITKKRASHKPT-YENLQKSLEAMKSHCLK 70
Cdd:smart00506  27 HGGGVAGAIARAAGKALskeEVRKLAGGecpVGTAVVTeggNLPAKYVIHAVGPRASGHSKEgFELLENAYRNCLELAIE 106

                           90       100
                   ....*....|....*....|....*..
gi 2325215035   71 NGVTDLSMPRIGCGLDRLQWENVSAIL 97
Cdd:smart00506 107 LGITSVALPLIGTGIYGVPKDRSAQAL 133
 
Name Accession Description Interval E-value
Macro_Poa1p-like cd02901
macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse ...
 1-104 1.39e-49

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: 153.95  E-value: 1.39e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2325215035   1 MGAGIAVLFKKRFGGVQELLSQQKKS--GEVAVLKRDG--RYIYYLITKKRASHKPTYENLQKSLEAMKSHCLKNGVTDL 76
Cdd:cd02901    28 MGKGIALQFKKKPGRVEELRAQCKKKllGGVAVLKRDGvkRYIYYLITKKSYGPKPTYEALRSSLEELREHCRENGVTSV 107

                          90       100
                  ....*....|....*....|....*...
gi 2325215035  77 SMPRIGCGLDRLQWENVSAILEEVFEST 104
Cdd:cd02901   108 AMPRIGCGLDGLDWEEVEPILKEVFDDR 135
Macro_SF cd02749
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 1-100 2.50e-28

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: 99.39  E-value: 2.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2325215035   1 MGAGIAVLFKKRFGGVQE------LLSQQKKSGEVAVLKRDG---RYIYYLITKKRASHKPTYENLQKSLEAMKSHCLKN 71
Cdd:cd02749    13 LGGGVAKAISKKAGGDLQeeceerKKNGYLKVGEVAVTKGGNlpaRYIIHVVGPVASSKKKTYEPLKKCVKNCLSLADEK 92

                          90       100
                  ....*....|....*....|....*....
gi 2325215035  72 GVTDLSMPRIGCGLDRLQWENVSAILEEV 100
Cdd:cd02749    93 GLKSVAFPAIGTGIAGFPPEEAARIMLEA 121
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 1-112 1.20e-09

O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441713  Cd Length: 168  Bit Score: 52.49  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2325215035   1 MGAGIAVLFKKRFG-GVQELLSQQKKSGEV----AVLKRDG----RYIYYLITKK-RASHKPTYENLQKSLEAMKSHCLK 70
Cdd:COG2110    26 GGGGVAGAIHRAAGpELLEECRRLCKQGGCptgeAVITPAGnlpaKYVIHTVGPVwRGGGPSEEELLASCYRNSLELAEE 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2325215035  71 NGVTDLSMPRIGCGLDRLQWENVSAILEEVFES--------TDIKITVYT 112
Cdd:COG2110   106 LGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDfleehpslEEVRFVLFD 155
tk.4 PHA02595
hypothetical protein; Provisional
 1-110 1.60e-09

hypothetical protein; Provisional


Pssm-ID: 222899  Cd Length: 154  Bit Score: 52.00  E-value: 1.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2325215035   1 MGAGIAVLFKKRFGGVQELLSQQ-----KKSGEVAVLKRDGR----YIYYLITKKRASHKPTYENLQKSLEAMKSHClKN 71
Cdd:PHA02595   31 MGSGIAGQLAKAFPQILEADKLTtegdvEKLGTFSVWEKYVGghkaYCFNLYTQFDPGPNLEYSALMNCFEELNEVF-EG 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2325215035  72 GVTDLSM--PRIGCGLDRLQWENVSAILEEVfeSTDIKITV 110
Cdd:PHA02595  110 TLFKPTIyiPRIGAGIAGGDWDKIEAIIDEA--TPDIDIVV 148
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 1-97 2.66e-06

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: 43.06  E-value: 2.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2325215035    1 MGAGIAVLFKKRFGGVQ---ELLSQQKK---SGEVAVL---KRDGRYIYYLITKKRASHKPT-YENLQKSLEAMKSHCLK 70
Cdd:smart00506  27 HGGGVAGAIARAAGKALskeEVRKLAGGecpVGTAVVTeggNLPAKYVIHAVGPRASGHSKEgFELLENAYRNCLELAIE 106

                           90       100
                   ....*....|....*....|....*..
gi 2325215035   71 NGVTDLSMPRIGCGLDRLQWENVSAIL 97
Cdd:smart00506 107 LGITSVALPLIGTGIYGVPKDRSAQAL 133
PHA03033 PHA03033
hypothetical protein; Provisional
 10-75 9.78e-06

hypothetical protein; Provisional


Pssm-ID: 165330  Cd Length: 142  Bit Score: 41.89  E-value: 9.78e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2325215035  10 KKRFGGVQELLSQQKKSGEVAVLKRDGRYIYYLITKKRASHKPTYENLQKSLEAMKSHCLKNGVTD 75
Cdd:PHA03033   42 KKKYNSIKELKKQKKKKGEVAYIYKNNKYIIYIIIADYIEDIVDDINILRALDNFKEIIEKDKIAD 107
 
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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