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Conserved domains on  [gi|161085419|ref|NP_001097656|]
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uncharacterized protein Dmel_CG34261 [Drosophila melanogaster]

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 ...
 5-135 7.38e-61

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: 183.99  E-value: 7.38e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161085419   5 TYREINGDLFKCQRDYSMCHCVAADLRMGRGIAVKFRNKFGQLLNLQRQNVQ--PGGVAVLQDQ--QRFIYYLITKKSSW 80
Cdd:cd02901    1 KITYVKGDLFACPETKSLAHCCNCDGVMGKGIALQFKKKPGRVEELRAQCKKklLGGVAVLKRDgvKRYIYYLITKKSYG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 161085419  81 GKPTYELLQSSLIAMRKHMISHQVPKLAMPRIGCGLDGLNWPKVKEIICQVFQAD 135
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 ...
 5-135 7.38e-61

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: 183.99  E-value: 7.38e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161085419   5 TYREINGDLFKCQRDYSMCHCVAADLRMGRGIAVKFRNKFGQLLNLQRQNVQ--PGGVAVLQDQ--QRFIYYLITKKSSW 80
Cdd:cd02901    1 KITYVKGDLFACPETKSLAHCCNCDGVMGKGIALQFKKKPGRVEELRAQCKKklLGGVAVLKRDgvKRYIYYLITKKSYG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 161085419  81 GKPTYELLQSSLIAMRKHMISHQVPKLAMPRIGCGLDGLNWPKVKEIICQVFQAD 135
Cdd:cd02901   81 PKPTYEALRSSLEELREHCRENGVTSVAMPRIGCGLDGLDWEEVEPILKEVFDDR 135
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 30-143 1.22e-12

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: 61.73  E-value: 1.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161085419  30 LRMGRGIAVKFRNKFG-QLLN----LQRQN-VQPGGVAV---LQDQQRFIYYLITKKSSWGKP-TYELLQSSLIAMRKHM 99
Cdd:COG2110   24 LLGGGGVAGAIHRAAGpELLEecrrLCKQGgCPTGEAVItpaGNLPAKYVIHTVGPVWRGGGPsEEELLASCYRNSLELA 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 161085419 100 ISHQVPKLAMPRIGCGLDGLNWPKVKEIICQVFQA--------DSVELVVYN 143
Cdd:COG2110  104 EELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDfleehpslEEVRFVLFD 155
tk.4 PHA02595
hypothetical protein; Provisional
 8-144 1.34e-07

hypothetical protein; Provisional


Pssm-ID: 222899  Cd Length: 154  Bit Score: 47.76  E-value: 1.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161085419   8 EINGD---LFKcQRDYSMCHCVAADLRMGRGIAVKFRNKFGQLLNLQRQNVQpGGVAVL----------QDQQRFIYYLI 74
Cdd:PHA02595   5 YIKGDivaLFL-QGKGNIAHGCNCFHTMGSGIAGQLAKAFPQILEADKLTTE-GDVEKLgtfsvwekyvGGHKAYCFNLY 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161085419  75 TKKSSWGKPTYELLQSSLIAMRKHMISHQV-PKLAMPRIGCGLDGLNWPKVKEIICQVfqADSVELVVYNY 144
Cdd:PHA02595  83 TQFDPGPNLEYSALMNCFEELNEVFEGTLFkPTIYIPRIGAGIAGGDWDKIEAIIDEA--TPDIDIVVVEY 151
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 6-128 7.21e-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: 42.68  E-value: 7.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161085419     6 YREINGDLFKCQRDYSMcHCVAADLRMGRGIAVKFRNKFGQLL-----NLQRQNVQPGGVAVLQDQQ----RFIYYLITK 76
Cdd:smart00506   2 LKVVKGDITKPRADAIV-NAANSDGAHGGGVAGAIARAAGKALskeevRKLAGGECPVGTAVVTEGGnlpaKYVIHAVGP 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 161085419    77 KSSWGKPT-YELLQSSLIAMRKHMISHQVPKLAMPRIGCGLDGLNWPKVKEII 128
Cdd:smart00506  81 RASGHSKEgFELLENAYRNCLELAIELGITSVALPLIGTGIYGVPKDRSAQAL 133
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 30-128 2.87e-04

Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ADP-ribose (an NAD metabolite) or related ligands. Binding to ADP-ribose could be either covalent or non-covalent: in certain cases it is believed to bind non-covalently; while in other cases (such as Aprataxin) it appears to bind both non-covalently through a zinc finger motif, and covalently through a separate region of the protein. This domain is found in a number of otherwise unrelated proteins. It is found at the C-terminus of the macro-H2A histone protein 4 and also in the non-structural proteins of several types of ssRNA viruses such as NSP3 from alpha-viruses and coronaviruses. This domain is also found on its own in a family of proteins from bacteria, archaebacteria and eukaryotes. The 3D structure of the SARS-CoV Macro domain has a mixed alpha/beta fold consisting of a central seven-stranded twisted mixed beta sheet sandwiched between two alpha helices on one face, and three on the other. The final alpha-helix, located on the edge of the central beta-sheet, forms the C terminus of the protein. The crystal structure of AF1521 (a Macro domain-only protein from Archaeoglobus fulgidus) has also been reported and compared with other Macro domain containing proteins. Several Macro domain only proteins are shorter than AF1521, and appear to lack either the first strand of the beta-sheet or the C-terminal helix 5. Well conserved residues form a hydrophobic cleft and cluster around the AF1521-ADP-ribose binding site.


Pssm-ID: 460286  Cd Length: 116  Bit Score: 38.32  E-value: 2.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161085419   30 LRMGRGIAVKFRNKFGQLLN-----LQRQNVQPGGVAVL---QDQQRFIYYLI--TKKSSWGKPTYELLQSSLIAMRKHM 99
Cdd:pfam01661   8 LLGGGGVAGAIHRAAGPELLeecreLKKGGCPTGEAVVTpggNLPAKYVIHTVgpTWRHGGSHGEEELLESCYRNALALA 87

                          90       100
                  ....*....|....*....|....*....
gi 161085419  100 ISHQVPKLAMPRIGCGLDGLNWPKVKEII 128
Cdd:pfam01661  88 EELGIKSIAFPAISTGIYGFPWEEAARIA 116
 
Name Accession Description Interval E-value
Macro_Poa1p-like cd02901
macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse ...
 5-135 7.38e-61

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: 183.99  E-value: 7.38e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161085419   5 TYREINGDLFKCQRDYSMCHCVAADLRMGRGIAVKFRNKFGQLLNLQRQNVQ--PGGVAVLQDQ--QRFIYYLITKKSSW 80
Cdd:cd02901    1 KITYVKGDLFACPETKSLAHCCNCDGVMGKGIALQFKKKPGRVEELRAQCKKklLGGVAVLKRDgvKRYIYYLITKKSYG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 161085419  81 GKPTYELLQSSLIAMRKHMISHQVPKLAMPRIGCGLDGLNWPKVKEIICQVFQAD 135
Cdd:cd02901   81 PKPTYEALRSSLEELREHCRENGVTSVAMPRIGCGLDGLDWEEVEPILKEVFDDR 135
Macro_SF cd02749
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 20-128 5.85e-17

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: 71.66  E-value: 5.85e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161085419  20 YSMCHCVAADLRMGRGIAVKFRNKFGQLLNLQRQNVQP------GGVAVLQDQQ---RFIYYLITKKSSWGKPTYELLQS 90
Cdd:cd02749    1 DAIVNPANNDLYLGGGVAKAISKKAGGDLQEECEERKKngylkvGEVAVTKGGNlpaRYIIHVVGPVASSKKKTYEPLKK 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 161085419  91 SLIAMRKHMISHQVPKLAMPRIGCGLDGLNWPKVKEII 128
Cdd:cd02749   81 CVKNCLSLADEKGLKSVAFPAIGTGIAGFPPEEAARIM 118
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 30-143 1.22e-12

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: 61.73  E-value: 1.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161085419  30 LRMGRGIAVKFRNKFG-QLLN----LQRQN-VQPGGVAV---LQDQQRFIYYLITKKSSWGKP-TYELLQSSLIAMRKHM 99
Cdd:COG2110   24 LLGGGGVAGAIHRAAGpELLEecrrLCKQGgCPTGEAVItpaGNLPAKYVIHTVGPVWRGGGPsEEELLASCYRNSLELA 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 161085419 100 ISHQVPKLAMPRIGCGLDGLNWPKVKEIICQVFQA--------DSVELVVYN 143
Cdd:COG2110  104 EELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDfleehpslEEVRFVLFD 155
tk.4 PHA02595
hypothetical protein; Provisional
 8-144 1.34e-07

hypothetical protein; Provisional


Pssm-ID: 222899  Cd Length: 154  Bit Score: 47.76  E-value: 1.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161085419   8 EINGD---LFKcQRDYSMCHCVAADLRMGRGIAVKFRNKFGQLLNLQRQNVQpGGVAVL----------QDQQRFIYYLI 74
Cdd:PHA02595   5 YIKGDivaLFL-QGKGNIAHGCNCFHTMGSGIAGQLAKAFPQILEADKLTTE-GDVEKLgtfsvwekyvGGHKAYCFNLY 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161085419  75 TKKSSWGKPTYELLQSSLIAMRKHMISHQV-PKLAMPRIGCGLDGLNWPKVKEIICQVfqADSVELVVYNY 144
Cdd:PHA02595  83 TQFDPGPNLEYSALMNCFEELNEVFEGTLFkPTIYIPRIGAGIAGGDWDKIEAIIDEA--TPDIDIVVVEY 151
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 6-128 7.21e-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: 42.68  E-value: 7.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161085419     6 YREINGDLFKCQRDYSMcHCVAADLRMGRGIAVKFRNKFGQLL-----NLQRQNVQPGGVAVLQDQQ----RFIYYLITK 76
Cdd:smart00506   2 LKVVKGDITKPRADAIV-NAANSDGAHGGGVAGAIARAAGKALskeevRKLAGGECPVGTAVVTEGGnlpaKYVIHAVGP 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 161085419    77 KSSWGKPT-YELLQSSLIAMRKHMISHQVPKLAMPRIGCGLDGLNWPKVKEII 128
Cdd:smart00506  81 RASGHSKEgFELLENAYRNCLELAIELGITSVALPLIGTGIYGVPKDRSAQAL 133
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 30-128 2.87e-04

Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ADP-ribose (an NAD metabolite) or related ligands. Binding to ADP-ribose could be either covalent or non-covalent: in certain cases it is believed to bind non-covalently; while in other cases (such as Aprataxin) it appears to bind both non-covalently through a zinc finger motif, and covalently through a separate region of the protein. This domain is found in a number of otherwise unrelated proteins. It is found at the C-terminus of the macro-H2A histone protein 4 and also in the non-structural proteins of several types of ssRNA viruses such as NSP3 from alpha-viruses and coronaviruses. This domain is also found on its own in a family of proteins from bacteria, archaebacteria and eukaryotes. The 3D structure of the SARS-CoV Macro domain has a mixed alpha/beta fold consisting of a central seven-stranded twisted mixed beta sheet sandwiched between two alpha helices on one face, and three on the other. The final alpha-helix, located on the edge of the central beta-sheet, forms the C terminus of the protein. The crystal structure of AF1521 (a Macro domain-only protein from Archaeoglobus fulgidus) has also been reported and compared with other Macro domain containing proteins. Several Macro domain only proteins are shorter than AF1521, and appear to lack either the first strand of the beta-sheet or the C-terminal helix 5. Well conserved residues form a hydrophobic cleft and cluster around the AF1521-ADP-ribose binding site.


Pssm-ID: 460286  Cd Length: 116  Bit Score: 38.32  E-value: 2.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161085419   30 LRMGRGIAVKFRNKFGQLLN-----LQRQNVQPGGVAVL---QDQQRFIYYLI--TKKSSWGKPTYELLQSSLIAMRKHM 99
Cdd:pfam01661   8 LLGGGGVAGAIHRAAGPELLeecreLKKGGCPTGEAVVTpggNLPAKYVIHTVgpTWRHGGSHGEEELLESCYRNALALA 87

                          90       100
                  ....*....|....*....|....*....
gi 161085419  100 ISHQVPKLAMPRIGCGLDGLNWPKVKEII 128
Cdd:pfam01661  88 EELGIKSIAFPAISTGIYGFPWEEAARIA 116
 
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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