NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2018162991|ref|WP_208223339|]
View 

macro domain-containing protein [Salegentibacter sp. BDJ18]

Protein Classification

macro domain-containing protein( domain architecture ID 11450017)

macro domain-containing protein functions as a mono-ADP-ribosylhydrolase, similar to Saccharomyces cerevisiae 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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 10-174 5.51e-74

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: 219.28  E-value: 5.51e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018162991  10 IEVFQGDIANLpNVEAVVNAANAQLTTGGGVAGAIHRAAGPKLYEECKPL---APIAPGEAVITGAYNLPNKYVIHCLGP 86
Cdd:COG2110     1 IEIVQGDITEL-DVDAIVNAANSSLLGGGGVAGAIHRAAGPELLEECRRLckqGGCPTGEAVITPAGNLPAKYVIHTVGP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018162991  87 VY-GKDKSENKLLENCYKNVLKRAEEKKVKSVAFPAISTGAFGYPIKEATKISFNTILAEIPKLKHLQKLKFVLFSEADL 165
Cdd:COG2110    80 VWrGGGPSEEELLASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFLEEHPSLEEVRFVLFDEEDY 159


                  ....*....
gi 2018162991 166 EIYETMLAE 174
Cdd:COG2110   160 EAYRRALAR 168
 
Name Accession Description Interval E-value
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 10-174 5.51e-74

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: 219.28  E-value: 5.51e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018162991  10 IEVFQGDIANLpNVEAVVNAANAQLTTGGGVAGAIHRAAGPKLYEECKPL---APIAPGEAVITGAYNLPNKYVIHCLGP 86
Cdd:COG2110     1 IEIVQGDITEL-DVDAIVNAANSSLLGGGGVAGAIHRAAGPELLEECRRLckqGGCPTGEAVITPAGNLPAKYVIHTVGP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018162991  87 VY-GKDKSENKLLENCYKNVLKRAEEKKVKSVAFPAISTGAFGYPIKEATKISFNTILAEIPKLKHLQKLKFVLFSEADL 165
Cdd:COG2110    80 VWrGGGPSEEELLASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFLEEHPSLEEVRFVLFDEEDY 159


                  ....*....
gi 2018162991 166 EIYETMLAE 174
Cdd:COG2110   160 EAYRRALAR 168
Macro_OAADPr_deacetylase cd02908
macrodomain, O-acetyl-ADP-ribose (OAADPr) family; Macrodomains are found in a variety of ...
 10-172 1.18e-72

macrodomain, O-acetyl-ADP-ribose (OAADPr) 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. This family includes eukaryotic macrodomain proteins such as human MacroD1 and MacroD2, and bacterial proteins such as Escherichia coli YmdB; these have been shown to be O-acetyl-ADP-ribose (OAADPr) deacetylases that efficiently catalyze the hydrolysis of OAADPr to produce ADP-ribose and free acetate. OAADPr is a sirtuin reaction product generated from the NAD+-dependent protein deacetylation reactions and has been implicated as a signaling molecule. By acting on mono-ADP-ribosylated substrates, OAADPr deacetylases may reverse cellular ADP-ribosylation.


Pssm-ID: 438955  Cd Length: 166  Bit Score: 215.84  E-value: 1.18e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018162991  10 IEVFQGDIANLPnVEAVVNAANAQLTTGGGVAGAIHRAAGPKLYEECKPLAPIAP-GEAVITGAYNLPNKYVIHCLGPVY 88
Cdd:cd02908     2 ISLWRGDITKLE-VDAIVNAANSSLLGGGGVDGAIHRAAGPELLEECRKLGGVCPtGEAKITPGYNLPAKYVIHTVGPIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018162991  89 GKDKSEN-KLLENCYKNVLKRAEEKKVKSVAFPAISTGAFGYPIKEATKISFNTILAEIPKLKHLQKLKFVLFSEADLEI 167
Cdd:cd02908    81 EGGVEEEpELLASCYRSSLELALENGLKSIAFPCISTGIYGYPNEEAAEIALNTVREWLEEHDKIDRIIFVVFLDEDYKI 160


                  ....*
gi 2018162991 168 YETML 172
Cdd:cd02908   161 YEELL 165
PRK00431 PRK00431
ADP-ribose-binding protein;
8-175 8.46e-70

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 208.93  E-value: 8.46e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018162991   8 IEIEVFQGDIANLPnVEAVVNAANAQLTTGGGVAGAIHRAAGPKLYEECKPL----APIAPGEAVITGAYNLPNKYVIHC 83
Cdd:PRK00431    3 MRIEVVQGDITELE-VDAIVNAANSSLLGGGGVDGAIHRAAGPEILEECRELrqqqGPCPTGEAVITSAGRLPAKYVIHT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018162991  84 LGPVYGKDKSENK-LLENCYKNVLKRAEEKKVKSVAFPAISTGAFGYPIKEATKISFNTILAEIPKLKHLQKLKFVLFSE 162
Cdd:PRK00431   82 VGPVWRGGEDNEAeLLASAYRNSLRLAAELGLRSIAFPAISTGVYGYPLEDAARIAVKTVREFLTRHKSPEEVYFVCYDE 161

                         170
                  ....*....|...
gi 2018162991 163 ADLEIYETMLAEM 175
Cdd:PRK00431  162 EAYRLYERLLTQQ 174
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 27-137 4.93e-52

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: 161.96  E-value: 4.93e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018162991  27 VNAANAQLTTGGGVAGAIHRAAGPKLYEECKPL--APIAPGEAVITGAYNLPNKYVIHCLGPVY--GKDKSENKLLENCY 102
Cdd:pfam01661   1 VNAANSRLLGGGGVAGAIHRAAGPELLEECRELkkGGCPTGEAVVTPGGNLPAKYVIHTVGPTWrhGGSHGEEELLESCY 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2018162991 103 KNVLKRAEEKKVKSVAFPAISTGAFGYPIKEATKI 137
Cdd:pfam01661  81 RNALALAEELGIKSIAFPAISTGIYGFPWEEAARI 115
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 9-137 3.77e-42

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: 137.44  E-value: 3.77e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018162991    9 EIEVFQGDIANLPnVEAVVNAANAQLTTGGGVAGAIHRAAGPKLY-EECKPLAP--IAPGEAVITGAYNLPNKYVIHCLG 85
Cdd:smart00506   1 ILKVVKGDITKPR-ADAIVNAANSDGAHGGGVAGAIARAAGKALSkEEVRKLAGgeCPVGTAVVTEGGNLPAKYVIHAVG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2018162991   86 PVYGKD-KSENKLLENCYKNVLKRAEEKKVKSVAFPAISTGAFGYPIKEATKI 137
Cdd:smart00506  80 PRASGHsKEGFELLENAYRNCLELAIELGITSVALPLIGTGIYGVPKDRSAQA 132
 
Name Accession Description Interval E-value
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 10-174 5.51e-74

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: 219.28  E-value: 5.51e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018162991  10 IEVFQGDIANLpNVEAVVNAANAQLTTGGGVAGAIHRAAGPKLYEECKPL---APIAPGEAVITGAYNLPNKYVIHCLGP 86
Cdd:COG2110     1 IEIVQGDITEL-DVDAIVNAANSSLLGGGGVAGAIHRAAGPELLEECRRLckqGGCPTGEAVITPAGNLPAKYVIHTVGP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018162991  87 VY-GKDKSENKLLENCYKNVLKRAEEKKVKSVAFPAISTGAFGYPIKEATKISFNTILAEIPKLKHLQKLKFVLFSEADL 165
Cdd:COG2110    80 VWrGGGPSEEELLASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFLEEHPSLEEVRFVLFDEEDY 159


                  ....*....
gi 2018162991 166 EIYETMLAE 174
Cdd:COG2110   160 EAYRRALAR 168
Macro_OAADPr_deacetylase cd02908
macrodomain, O-acetyl-ADP-ribose (OAADPr) family; Macrodomains are found in a variety of ...
 10-172 1.18e-72

macrodomain, O-acetyl-ADP-ribose (OAADPr) 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. This family includes eukaryotic macrodomain proteins such as human MacroD1 and MacroD2, and bacterial proteins such as Escherichia coli YmdB; these have been shown to be O-acetyl-ADP-ribose (OAADPr) deacetylases that efficiently catalyze the hydrolysis of OAADPr to produce ADP-ribose and free acetate. OAADPr is a sirtuin reaction product generated from the NAD+-dependent protein deacetylation reactions and has been implicated as a signaling molecule. By acting on mono-ADP-ribosylated substrates, OAADPr deacetylases may reverse cellular ADP-ribosylation.


Pssm-ID: 438955  Cd Length: 166  Bit Score: 215.84  E-value: 1.18e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018162991  10 IEVFQGDIANLPnVEAVVNAANAQLTTGGGVAGAIHRAAGPKLYEECKPLAPIAP-GEAVITGAYNLPNKYVIHCLGPVY 88
Cdd:cd02908     2 ISLWRGDITKLE-VDAIVNAANSSLLGGGGVDGAIHRAAGPELLEECRKLGGVCPtGEAKITPGYNLPAKYVIHTVGPIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018162991  89 GKDKSEN-KLLENCYKNVLKRAEEKKVKSVAFPAISTGAFGYPIKEATKISFNTILAEIPKLKHLQKLKFVLFSEADLEI 167
Cdd:cd02908    81 EGGVEEEpELLASCYRSSLELALENGLKSIAFPCISTGIYGYPNEEAAEIALNTVREWLEEHDKIDRIIFVVFLDEDYKI 160


                  ....*
gi 2018162991 168 YETML 172
Cdd:cd02908   161 YEELL 165
PRK00431 PRK00431
ADP-ribose-binding protein;
8-175 8.46e-70

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 208.93  E-value: 8.46e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018162991   8 IEIEVFQGDIANLPnVEAVVNAANAQLTTGGGVAGAIHRAAGPKLYEECKPL----APIAPGEAVITGAYNLPNKYVIHC 83
Cdd:PRK00431    3 MRIEVVQGDITELE-VDAIVNAANSSLLGGGGVDGAIHRAAGPEILEECRELrqqqGPCPTGEAVITSAGRLPAKYVIHT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018162991  84 LGPVYGKDKSENK-LLENCYKNVLKRAEEKKVKSVAFPAISTGAFGYPIKEATKISFNTILAEIPKLKHLQKLKFVLFSE 162
Cdd:PRK00431   82 VGPVWRGGEDNEAeLLASAYRNSLRLAAELGLRSIAFPAISTGVYGYPLEDAARIAVKTVREFLTRHKSPEEVYFVCYDE 161

                         170
                  ....*....|...
gi 2018162991 163 ADLEIYETMLAEM 175
Cdd:PRK00431  162 EAYRLYERLLTQQ 174
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 27-137 4.93e-52

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: 161.96  E-value: 4.93e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018162991  27 VNAANAQLTTGGGVAGAIHRAAGPKLYEECKPL--APIAPGEAVITGAYNLPNKYVIHCLGPVY--GKDKSENKLLENCY 102
Cdd:pfam01661   1 VNAANSRLLGGGGVAGAIHRAAGPELLEECRELkkGGCPTGEAVVTPGGNLPAKYVIHTVGPTWrhGGSHGEEELLESCY 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2018162991 103 KNVLKRAEEKKVKSVAFPAISTGAFGYPIKEATKI 137
Cdd:pfam01661  81 RNALALAEELGIKSIAFPAISTGIYGFPWEEAARI 115
Macro_Af1521_BAL-like cd02907
macrodomain, Af1521-like family; Macrodomains are found in a variety of proteins with diverse ...
 7-160 8.64e-52

macrodomain, Af1521-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. The macrodomains in this family show similarity to Af1521, a protein from Archaeoglobus fulgidus containing a stand-alone macrodomain. Af1521 binds ADP-ribose and exhibits phosphatase activity toward ADP-ribose-1"-monophosphate (Appr-1"-p). Also included in this family are the N-terminal (or first) macrodomains of BAL (B-aggressive lymphoma) proteins which contain multiple macrodomains, such as the first macrodomain 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: 394877 [Multi-domain]  Cd Length: 158  Bit Score: 162.66  E-value: 8.64e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018162991   7 NIEIEVFQGDIANLpNVEAVVNAANAQLTTGGGVAGAIHRAAGPKLYEEC----KPLAPIAPGEAVITGAYNLPNKYVIH 82
Cdd:cd02907     1 GIKVSVYKGDITKE-KVDAIVNAANERLKHGGGVAGAISKAGGPEIQEECdkyiKKNGKLRVGEVVVTSAGKLPCKYVIH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018162991  83 CLGPVYGKDKSEN--KLLENCYKNVLKRAEEKKVKSVAFPAISTGAFGYPIKEATKISFNTILaEIPKLKHLQKLKFVLF 160
Cdd:cd02907    80 AVGPRWSGGSKEEceDLLYKAVLNSLEEAEELKATSIAIPAISSGIFGFPLDLCAEAIVEAIK-DFSESNSSSSLKEIRL 158
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 9-137 3.77e-42

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: 137.44  E-value: 3.77e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018162991    9 EIEVFQGDIANLPnVEAVVNAANAQLTTGGGVAGAIHRAAGPKLY-EECKPLAP--IAPGEAVITGAYNLPNKYVIHCLG 85
Cdd:smart00506   1 ILKVVKGDITKPR-ADAIVNAANSDGAHGGGVAGAIARAAGKALSkEEVRKLAGgeCPVGTAVVTEGGNLPAKYVIHAVG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2018162991   86 PVYGKD-KSENKLLENCYKNVLKRAEEKKVKSVAFPAISTGAFGYPIKEATKI 137
Cdd:smart00506  80 PRASGHsKEGFELLENAYRNCLELAIELGITSVALPLIGTGIYGVPKDRSAQA 132
PRK04143 PRK04143
protein-ADP-ribose hydrolase;
5-174 1.32e-40

protein-ADP-ribose hydrolase;


Pssm-ID: 235225  Cd Length: 264  Bit Score: 137.42  E-value: 1.32e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018162991   5 IQNIEIEVFQGDIANLpNVEAVVNAANAQLTtG------GGVAGAIHRAAGPKLYEECKPLA-----PIAPGEAVITGAY 73
Cdd:PRK04143   80 IKYDNIFLWQGDITRL-KVDAIVNAANSRLL-GcfqpnhDCIDNAIHTFAGVQLRLDCAEIMteqgrKEATGQAKITRAY 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018162991  74 NLPNKYVIHCLGPVYGKDKS---ENKLLENCYKNVLKRAEEKKVKSVAFPAISTGAFGYPIKEATKISFNTILAEIPKLK 150
Cdd:PRK04143  158 NLPAKYVIHTVGPIIRKQPVspiRADLLASCYRSCLKLAEKAGLKSIAFCCISTGVFGFPKEEAAEIAIKTVLSWLKENP 237

                         170       180
                  ....*....|....*....|....
gi 2018162991 151 HLQKLKFVLFSEADLEIYETMLAE 174
Cdd:PRK04143  238 SKLKVVFNVFTDEDLELYQKALNK 261
Macro_Ttha0132-like cd03330
Macrodomain, uncharacterized family similar to Thermus thermophilus hypothetical protein ...
 9-149 3.29e-38

Macrodomain, uncharacterized family similar to Thermus thermophilus hypothetical protein Ttha0132; 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. This family is composed of uncharacterized proteins containing a stand-alone macrodomain, similar to Thermus thermophilus hypothetical protein Ttha0132.


Pssm-ID: 394879  Cd Length: 147  Bit Score: 127.93  E-value: 3.29e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018162991   9 EIEVFQGDIANLpNVEAVVNAANAQLTTGGGVAGAIHRAAGPKLYEECKPLAPIAPGEAVITGAYNLPNKYVIHClgPVY 88
Cdd:cd03330     1 RLIVVQGDITEQ-DADAIVNAANRRLLMGSGVAGAIKRKGGEEIEREAMRKGPIRVGEAVETGAGKLPAKYVIHA--AVM 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2018162991  89 GKD-KSENKLLENCYKNVLKRAEEKKVKSVAFPAISTGAFGYPIKEATKIsfntILAEIPKL 149
Cdd:cd03330    78 GMPgRSSEESIRDATRNALAKAEELGLESVAFPAIGTGVGGFPVEEVARI----MLEEIKKC 135
Macro_H2A-like cd02904
macrodomain, macroH2A-like family; Macrodomains are found in a variety of proteins with ...
 12-173 1.09e-37

macrodomain, macroH2A-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 are similar to macroH2A, a variant of the major-type core histone H2A, which contains an N-terminal H2A domain and a C-terminal nonhistone macrodomain. Histone macroH2A is enriched on the inactive X chromosome of mammalian female cells. It does not bind poly ADP-ribose, but does bind the monomeric SirT1 metabolite O-acetyl-ADP-ribose (OAADPR) with high affinity through its macrodomain. This family also includes the ADP-ribose binding macrodomain of the macroH2A variant, macroH2A1.1. The macroH2A1.1 isoform inhibits PARP1-dependent DNA-damage induced chromatin dynamics. The putative ADP-ribose binding pocket of the human macroH2A2 macrodomain exhibits marked structural differences compared with the macroH2A1.1 variant.


Pssm-ID: 394875  Cd Length: 188  Bit Score: 127.82  E-value: 1.09e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018162991  12 VFQGDIANLpNVEAVVNAANAQLTTGGGVAGAIHRAAGPKLYEECKPLA----PIAPGEAVITGAYNLPNKYVIHCLGPV 87
Cdd:cd02904    22 VVQGDIASI-KADAIVHPTNATFYLGGEVGSALEKAGGKEFVEEVKELRksngPLEVAGAAISPGHNLPAKFVIHCNSPS 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018162991  88 YGKDKSENKLlENCYKNVLKRAEEKKVKSVAFPAISTGAFGYPIKEATKisfnTILAEIPKL------KHLQKLKFVLFS 161
Cdd:cd02904   101 WGSDKCEELL-EKTVKNCLALADEKKLKSVAFPSIGSGRNGFPKQTAAQ----TILKAISNYfvsvmsSSLKQIYFVLFD 175

                         170
                  ....*....|..
gi 2018162991 162 EADLEIYETMLA 173
Cdd:cd02904   176 MESIGIYTSELA 187
Macro_GDAP2-like cd02905
macrodomain, GDAP2-like family; Macrodomains are found in a variety of proteins with diverse ...
 10-172 1.39e-37

macrodomain, GDAP2-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. This family contains proteins similar to human GDAP2, the ganglioside induced differentiation associated protein 2, whose gene is expressed at a higher level in differentiated Neuro2a cells compared with non-differentiated cells. GDAP2 contains an N-terminal macrodomain and a C-terminal Sec14p-like lipid binding domain. It is specifically expressed in brain and testis.


Pssm-ID: 394876  Cd Length: 169  Bit Score: 126.97  E-value: 1.39e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018162991  10 IEVFQGDIANLpNVEAVVNAANAQLTTGGGVAGAIHRAAGPKLYEECKPLAPIAPGEAVITGAYNLPNKYVIHCLGPVYg 89
Cdd:cd02905     3 IVLWDGDLTLL-NVDAIVNSTNESLTDKSPISDRLFLAAGPELREELAKLGGCRTGEAKLTKGYNLPARYVIHTVGPRY- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018162991  90 KDK----SENKlLENCYKNVLKRAEEKKVKSVAFPAISTGAFGYPIKEATKISFNTI--LAEipklKHLQKLKFVLF--S 161
Cdd:cd02905    81 NEKyrtaAESA-LYSCYRNVLQLAKEHKLRSVAFPVIHSERRGYPLEDGAHIALRTVrrFLE----KHGSSFEAVVFvvT 155

                         170
                  ....*....|.
gi 2018162991 162 EADLEIYETML 172
Cdd:cd02905   156 EEEMETYERLL 166
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 4-160 1.14e-35

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: 122.36  E-value: 1.14e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018162991   4 TIQNIEIEVFQGDIANLpNVEAVVNAANAQLTTGGGVAGAIHRAAGPKLYEECKPLAP-IAPGEAVITGAYNLPNKYVIH 82
Cdd:cd02903     4 KIGGITVQLVKGDITKE-KTDVIVNSVSSDLLLKGGVSKAILKAAGPELQDECANQGKqPASGDVIVTSGGNLPCKYVYH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018162991  83 CLGPVYGKDKSenKLLENCYKNVLKRAEEKKVKSVAFPAISTGAFGYPIKEATKISFNTIL--AEIPKLKHLQKLKFVLF 160
Cdd:cd02903    83 VVLPHYNPGNE--KTLKDIVRKCLEKAENYKMSSISFPAIGTGNLGFPKDVVAEIMIDEVLkfSSKNPSSSLKEVRFVIF 160
Macro_SF cd02749
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 25-141 2.14e-35

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: 119.81  E-value: 2.14e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018162991  25 AVVNAANAQLTTGGGVAGAIHRAAGPKLYEEC---KPLAPIAPGEAVITGAYNLPNKYVIHCLGPVYGKDKSENKLLENC 101
Cdd:cd02749     2 AIVNPANNDLYLGGGVAKAISKKAGGDLQEECeerKKNGYLKVGEVAVTKGGNLPARYIIHVVGPVASSKKKTYEPLKKC 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2018162991 102 YKNVLKRAEEKKVKSVAFPAISTGAFGYPIKEATKISFNT 141
Cdd:cd02749    82 VKNCLSLADEKGLKSVAFPAIGTGIAGFPPEEAARIMLEA 121
Macro_X_Nsp3-like cd21557
X-domain (or Mac1 domain) of viral non-structural protein 3 and related macrodomains; The ...
 24-144 1.39e-26

X-domain (or Mac1 domain) of viral non-structural protein 3 and related macrodomains; The X-domain, also called Mac1, is the macrodomain found in riboviral non-structural protein 3 (Nsp3), including the Nsp3 of Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV) as well as SARS-CoV-2, and other coronaviruses (alpha-, beta-, gamma-, and deltacoronavirus), among others. The SARS-CoV-2 Nsp3 Mac1 is highly conserved among all CoVs, and binds to and hydrolyzes mono-ADP-ribose (MAR) from target proteins. It appears to counter host-mediated antiviral ADP-ribosylation, a post-translational modification that is part of the host response to viral infections. Mac1 is essential for pathogenesis in multiple animal models of CoV infection, implicating it as a virulence factor and potential therapeutic target. Assays show that the de-MARylating activity leads to a rapid loss of substrate, and that Mac1 could not hydrolyze poly-ADP-ribose; thus, Mac1 is a MAR-hydrolase (mono-ADP ribosylhydrolase). Mac1 was originally named ADP-ribose-1"-phosphatase (ADRP) based on data demonstrating that it could remove the phosphate group from ADP-ribose-1"-phosphate; however, activity was modest and was unclear why this would impact a virus infection. This family also includes the X-domain of Avian infectious bronchitis virus (IBV) strain Beaudette coronavirus that does not bind ADP-ribose; the triple glycine sequence found in the X-domains of SARS-CoV and human coronavirus 229E (HCoV229E), which are involved in ADP-ribose binding, is not conserved in the IBV X-domain. SARS-CoVs have two other macrodomains referred to as the SUD-N (N-terminal subdomain, or Mac2) and SUD-M (middle SUD subdomain, or Mac3) of the SARS-unique domain (SUD), which also do not bind ADP-ribose; these bind G-quadruplexes (unusual nucleic-acid structures formed by consecutive guanosine nucleotides). SARS-CoV SUD-N and SUD-M are not included in this group.


Pssm-ID: 438957  Cd Length: 127  Bit Score: 97.63  E-value: 1.39e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018162991  24 EAVVNAANAQLTTGGGVAGAIHRAAGPKLYEEC---KPLAPIAPGEAVITGAYNLPNKyVIHCLGPVYGKDKSEnKLLEN 100
Cdd:cd21557     2 DVVVNAANENLKHGGGVAGAIYKATGGAFQKESdyiKKNGPLKVGTAVLLPGHGLAKN-IIHVVGPRKRKGQDD-QLLAA 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2018162991 101 CYKNVLKRaeekkVKSVAFPAISTGAFGYPIKEatkiSFNTILA 144
Cdd:cd21557    80 AYKAVNKE-----YGSVLTPLLSAGIFGVPPEQ----SLNALLD 114
Macro_Poa1p-like cd02901
macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse ...
 14-133 9.98e-06

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: 43.01  E-value: 9.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018162991  14 QGDIANLPNVEAVVNAANAQLTTGGGVAGAI-HRAAGPKLYEE-CKPLAPIA----PGEAVITGAYNLPNKYvihclgpv 87
Cdd:cd02901     6 KGDLFACPETKSLAHCCNCDGVMGKGIALQFkKKPGRVEELRAqCKKKLLGGvavlKRDGVKRYIYYLITKK-------- 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2018162991  88 YGKDKSENKLLENCYKNVLKRAEEKKVKSVAFPAISTGAFGYPIKE 133
Cdd:cd02901    78 SYGPKPTYEALRSSLEELREHCRENGVTSVAMPRIGCGLDGLDWEE 123
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH