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Conserved domains on  [gi|110625732|ref|NP_997102|]
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ADP-ribose glycohydrolase OARD1 isoform 1 [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
PubMed:  15902274|26844395
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 ...
 13-143 1.53e-68

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: 203.64  E-value: 1.53e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625732  13 RITYVKGDLFACPKTDSLAHCISEDCRMGAGIAVLFKKRFGGVQELLSQQKKS--GEVAVLKRDG--RYIYYLITKKRAS 88
Cdd:cd02901    1 KITYVKGDLFACPETKSLAHCCNCDGVMGKGIALQFKKKPGRVEELRAQCKKKllGGVAVLKRDGvkRYIYYLITKKSYG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 110625732  89 HKPTYENLQKSLEAMKSHCLKNGVTDLSMPRIGCGLDRLQWENVSAILEEVFEST 143
Cdd:cd02901   81 PKPTYEALRSSLEELREHCRENGVTSVAMPRIGCGLDGLDWEEVEPILKEVFDDR 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 ...
 13-143 1.53e-68

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: 203.64  E-value: 1.53e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625732  13 RITYVKGDLFACPKTDSLAHCISEDCRMGAGIAVLFKKRFGGVQELLSQQKKS--GEVAVLKRDG--RYIYYLITKKRAS 88
Cdd:cd02901    1 KITYVKGDLFACPETKSLAHCCNCDGVMGKGIALQFKKKPGRVEELRAQCKKKllGGVAVLKRDGvkRYIYYLITKKSYG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 110625732  89 HKPTYENLQKSLEAMKSHCLKNGVTDLSMPRIGCGLDRLQWENVSAILEEVFEST 143
Cdd:cd02901   81 PKPTYEALRSSLEELREHCRENGVTSVAMPRIGCGLDGLDWEEVEPILKEVFDDR 135
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 14-151 3.35e-13

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: 63.27  E-value: 3.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625732  14 ITYVKGDLFACpKTDSLAHCISEDCRMGAGIAVLFKKRFG-GVQELLSQQKKSGEV----AVLKRDG----RYIYYLITK 84
Cdd:COG2110    1 IEIVQGDITEL-DVDAIVNAANSSLLGGGGVAGAIHRAAGpELLEECRRLCKQGGCptgeAVITPAGnlpaKYVIHTVGP 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110625732  85 K-RASHKPTYENLQKSLEAMKSHCLKNGVTDLSMPRIGCGLDRLQWENVSAILEEVFES--------TDIKITVYT 151
Cdd:COG2110   80 VwRGGGPSEEELLASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDfleehpslEEVRFVLFD 155
tk.4 PHA02595
hypothetical protein; Provisional
 14-149 2.10e-12

hypothetical protein; Provisional


Pssm-ID: 222899  Cd Length: 154  Bit Score: 60.86  E-value: 2.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625732  14 ITYVKGD---LFACPKTDsLAH-CiseDC--RMGAGIAVLFKKRFGGVQELLSQQ-----KKSGEVAVLKRDGR----YI 78
Cdd:PHA02595   3 VDYIKGDivaLFLQGKGN-IAHgC---NCfhTMGSGIAGQLAKAFPQILEADKLTtegdvEKLGTFSVWEKYVGghkaYC 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110625732  79 YYLITKKRASHKPTYENLQKSLEAMKSHClKNGVTDLSM--PRIGCGLDRLQWENVSAILEEVfeSTDIKITV 149
Cdd:PHA02595  79 FNLYTQFDPGPNLEYSALMNCFEELNEVF-EGTLFKPTIyiPRIGAGIAGGDWDKIEAIIDEA--TPDIDIVV 148
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 13-136 9.53e-11

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: 56.16  E-value: 9.53e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625732    13 RITYVKGDLFAcPKTDSLAHCISEDCRMGAGIAVLFKKRFGGVQ---ELLSQQKK---SGEVAVL---KRDGRYIYYLIT 83
Cdd:smart00506   1 ILKVVKGDITK-PRADAIVNAANSDGAHGGGVAGAIARAAGKALskeEVRKLAGGecpVGTAVVTeggNLPAKYVIHAVG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 110625732    84 KKRASHKPT-YENLQKSLEAMKSHCLKNGVTDLSMPRIGCGLDRLQWENVSAIL 136
Cdd:smart00506  80 PRASGHSKEgFELLENAYRNCLELAIELGITSVALPLIGTGIYGVPKDRSAQAL 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 ...
 13-143 1.53e-68

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: 203.64  E-value: 1.53e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625732  13 RITYVKGDLFACPKTDSLAHCISEDCRMGAGIAVLFKKRFGGVQELLSQQKKS--GEVAVLKRDG--RYIYYLITKKRAS 88
Cdd:cd02901    1 KITYVKGDLFACPETKSLAHCCNCDGVMGKGIALQFKKKPGRVEELRAQCKKKllGGVAVLKRDGvkRYIYYLITKKSYG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 110625732  89 HKPTYENLQKSLEAMKSHCLKNGVTDLSMPRIGCGLDRLQWENVSAILEEVFEST 143
Cdd:cd02901   81 PKPTYEALRSSLEELREHCRENGVTSVAMPRIGCGLDGLDWEEVEPILKEVFDDR 135
Macro_SF cd02749
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 28-139 2.23e-33

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: 114.03  E-value: 2.23e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625732  28 DSLAHCISEDCRMGAGIAVLFKKRFGGVQE------LLSQQKKSGEVAVLKRDG---RYIYYLITKKRASHKPTYENLQK 98
Cdd:cd02749    1 DAIVNPANNDLYLGGGVAKAISKKAGGDLQeeceerKKNGYLKVGEVAVTKGGNlpaRYIIHVVGPVASSKKKTYEPLKK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 110625732  99 SLEAMKSHCLKNGVTDLSMPRIGCGLDRLQWENVSAILEEV 139
Cdd:cd02749   81 CVKNCLSLADEKGLKSVAFPAIGTGIAGFPPEEAARIMLEA 121
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 14-151 3.35e-13

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: 63.27  E-value: 3.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625732  14 ITYVKGDLFACpKTDSLAHCISEDCRMGAGIAVLFKKRFG-GVQELLSQQKKSGEV----AVLKRDG----RYIYYLITK 84
Cdd:COG2110    1 IEIVQGDITEL-DVDAIVNAANSSLLGGGGVAGAIHRAAGpELLEECRRLCKQGGCptgeAVITPAGnlpaKYVIHTVGP 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110625732  85 K-RASHKPTYENLQKSLEAMKSHCLKNGVTDLSMPRIGCGLDRLQWENVSAILEEVFES--------TDIKITVYT 151
Cdd:COG2110   80 VwRGGGPSEEELLASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDfleehpslEEVRFVLFD 155
tk.4 PHA02595
hypothetical protein; Provisional
 14-149 2.10e-12

hypothetical protein; Provisional


Pssm-ID: 222899  Cd Length: 154  Bit Score: 60.86  E-value: 2.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625732  14 ITYVKGD---LFACPKTDsLAH-CiseDC--RMGAGIAVLFKKRFGGVQELLSQQ-----KKSGEVAVLKRDGR----YI 78
Cdd:PHA02595   3 VDYIKGDivaLFLQGKGN-IAHgC---NCfhTMGSGIAGQLAKAFPQILEADKLTtegdvEKLGTFSVWEKYVGghkaYC 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110625732  79 YYLITKKRASHKPTYENLQKSLEAMKSHClKNGVTDLSM--PRIGCGLDRLQWENVSAILEEVfeSTDIKITV 149
Cdd:PHA02595  79 FNLYTQFDPGPNLEYSALMNCFEELNEVF-EGTLFKPTIyiPRIGAGIAGGDWDKIEAIIDEA--TPDIDIVV 148
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 13-136 9.53e-11

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: 56.16  E-value: 9.53e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625732    13 RITYVKGDLFAcPKTDSLAHCISEDCRMGAGIAVLFKKRFGGVQ---ELLSQQKK---SGEVAVL---KRDGRYIYYLIT 83
Cdd:smart00506   1 ILKVVKGDITK-PRADAIVNAANSDGAHGGGVAGAIARAAGKALskeEVRKLAGGecpVGTAVVTeggNLPAKYVIHAVG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 110625732    84 KKRASHKPT-YENLQKSLEAMKSHCLKNGVTDLSMPRIGCGLDRLQWENVSAIL 136
Cdd:smart00506  80 PRASGHSKEgFELLENAYRNCLELAIELGITSVALPLIGTGIYGVPKDRSAQAL 133
PHA03033 PHA03033
hypothetical protein; Provisional
 49-114 1.15e-05

hypothetical protein; Provisional


Pssm-ID: 165330  Cd Length: 142  Bit Score: 42.66  E-value: 1.15e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110625732  49 KKRFGGVQELLSQQKKSGEVAVLKRDGRYIYYLITKKRASHKPTYENLQKSLEAMKSHCLKNGVTD 114
Cdd:PHA03033  42 KKKYNSIKELKKQKKKKGEVAYIYKNNKYIIYIIIADYIEDIVDDINILRALDNFKEIIEKDKIAD 107
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 9-141 2.01e-03

macrodomain, B-aggressive lymphoma (BAL)-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 BAL (B-aggressive lymphoma) proteins, which contain one to three macrodomains. Most BAL family macrodomains belong to this family except for the most N-terminal domain in multiple-domain containing proteins. This family includes the second and third macrodomains of mono-ADP-ribosyltransferase PARP14 (PARP-14, also known as ADP-ribosyltransferase diphtheria toxin-like 8, ATRD8, B aggressive lymphoma protein 2, or BAL2). Most BAL proteins also contain a C-terminal PARP active site and are also named as PARPs. Human BAL1 (or PARP-9) was originally identified as a risk-related gene in diffuse large B-cell lymphoma that promotes malignant B-cell migration. Some BAL family proteins exhibit PARP activity. Poly (ADP-ribosyl)ation is an immediate DNA-damage-dependent post-translational modification of histones and other nuclear proteins. BAL proteins may also function as transcriptional repressors.


Pssm-ID: 394874  Cd Length: 175  Bit Score: 36.85  E-value: 2.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625732   9 PEGSRITYVKGDLfACPKTDSLAHCISEDCRMGAGIA-VLFKKRFGGVQELLSQQKK---SGEVAVLKRDG---RYIYYL 81
Cdd:cd02903    5 IGGITVQLVKGDI-TKEKTDVIVNSVSSDLLLKGGVSkAILKAAGPELQDECANQGKqpaSGDVIVTSGGNlpcKYVYHV 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110625732  82 ITkkrashkPTY-ENLQKSLEAMKSHCL----KNGVTDLSMPRIGCGLDRLQWENV-SAILEEVFE 141
Cdd:cd02903   84 VL-------PHYnPGNEKTLKDIVRKCLekaeNYKMSSISFPAIGTGNLGFPKDVVaEIMIDEVLK 142
 
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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