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Conserved domains on  [gi|1907143526|ref|XP_036018502|]
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ADP-ribose glycohydrolase MACROD2 isoform X9 [Mus musculus]

Protein Classification

macro domain-containing protein( domain architecture ID 10121116)

macro domain-containing protein functions in the recognition, interpretation, and turnover of ADP-ribose (ADPr) signaling

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Macro_OAADPr_deacetylase cd02908
macrodomain, O-acetyl-ADP-ribose (OAADPr) family; Macrodomains are found in a variety of ...
 71-198 5.36e-70

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: 218.54  E-value: 5.36e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143526  71 KVSLYRGDITLLEVDAIVNAANASLLGGGG-D---------------------------------------VIHTVGPIA 110
Cdd:cd02908     1 KISLWRGDITKLEVDAIVNAANSSLLGGGGvDgaihraagpelleecrklggvcptgeakitpgynlpakyVIHTVGPIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143526 111 RGHINGsHKEDLANCYQSSLKLVKENNLRSVAFPCISTGIYGFPNEPAAVIALGTIKEWLAKnHQEVDRIIFCVFLEVDF 190
Cdd:cd02908    81 EGGVEE-EPELLASCYRSSLELALENGLKSIAFPCISTGIYGYPNEEAAEIALNTVREWLEE-HDKIDRIIFVVFLDEDY 158


                  ....*...
gi 1907143526 191 KIYKKKMN 198
Cdd:cd02908   159 KIYEELLP 166
 
Name Accession Description Interval E-value
Macro_OAADPr_deacetylase cd02908
macrodomain, O-acetyl-ADP-ribose (OAADPr) family; Macrodomains are found in a variety of ...
 71-198 5.36e-70

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: 218.54  E-value: 5.36e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143526  71 KVSLYRGDITLLEVDAIVNAANASLLGGGG-D---------------------------------------VIHTVGPIA 110
Cdd:cd02908     1 KISLWRGDITKLEVDAIVNAANSSLLGGGGvDgaihraagpelleecrklggvcptgeakitpgynlpakyVIHTVGPIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143526 111 RGHINGsHKEDLANCYQSSLKLVKENNLRSVAFPCISTGIYGFPNEPAAVIALGTIKEWLAKnHQEVDRIIFCVFLEVDF 190
Cdd:cd02908    81 EGGVEE-EPELLASCYRSSLELALENGLKSIAFPCISTGIYGYPNEEAAEIALNTVREWLEE-HDKIDRIIFVVFLDEDY 158


                  ....*...
gi 1907143526 191 KIYKKKMN 198
Cdd:cd02908   159 KIYEELLP 166
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 72-199 1.87e-48

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: 163.04  E-value: 1.87e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143526  72 VSLYRGDITLLEVDAIVNAANASLLGGGG-D-----------------------------------------VIHTVGPI 109
Cdd:COG2110     1 IEIVQGDITELDVDAIVNAANSSLLGGGGvAgaihraagpelleecrrlckqggcptgeavitpagnlpakyVIHTVGPV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143526 110 ARGHINGShKEDLANCYQSSLKLVKENNLRSVAFPCISTGIYGFPNEPAAVIALGTIKEWLaKNHQEVDRIIFCVFLEVD 189
Cdd:COG2110    81 WRGGGPSE-EELLASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFL-EEHPSLEEVRFVLFDEED 158

                         170
                  ....*....|
gi 1907143526 190 FKIYKKKMNE 199
Cdd:COG2110   159 YEAYRRALAR 168
PRK00431 PRK00431
ADP-ribose-binding protein;
71-200 1.11e-43

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 150.76  E-value: 1.11e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143526  71 KVSLYRGDITLLEVDAIVNAANASLLGGGG-D------------------------------------------VIHTVG 107
Cdd:PRK00431    4 RIEVVQGDITELEVDAIVNAANSSLLGGGGvDgaihraagpeileecrelrqqqgpcptgeavitsagrlpakyVIHTVG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143526 108 PI-ARGHINGSHKedLANCYQSSLKLVKENNLRSVAFPCISTGIYGFPNEPAAVIALGTIKEWLAKnHQEVDRIIFCVFL 186
Cdd:PRK00431   84 PVwRGGEDNEAEL--LASAYRNSLRLAAELGLRSIAFPAISTGVYGYPLEDAARIAVKTVREFLTR-HKSPEEVYFVCYD 160

                         170
                  ....*....|....
gi 1907143526 187 EVDFKIYKKKMNEF 200
Cdd:PRK00431  161 EEAYRLYERLLTQQ 174
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 88-162 9.23e-27

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: 103.80  E-value: 9.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143526  88 VNAANASLLGGGG-----------------------------------------DVIHTVGPIARGHINGSHKEDLANCY 126
Cdd:pfam01661   1 VNAANSRLLGGGGvagaihraagpelleecrelkkggcptgeavvtpggnlpakYVIHTVGPTWRHGGSHGEEELLESCY 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907143526 127 QSSLKLVKENNLRSVAFPCISTGIYGFPNEPAAVIA 162
Cdd:pfam01661  81 RNALALAEELGIKSIAFPAISTGIYGFPWEEAARIA 116
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 71-162 3.19e-23

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: 94.68  E-value: 3.19e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143526   71 KVSLYRGDITLLEVDAIVNAANASLLGGGG------------------------------------------DVIHTVGP 108
Cdd:smart00506   1 ILKVVKGDITKPRADAIVNAANSDGAHGGGvagaiaraagkalskeevrklaggecpvgtavvteggnlpakYVIHAVGP 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907143526  109 IARGHINGSHkEDLANCYQSSLKLVKENNLRSVAFPCISTGIYGFPNEPAAVIA 162
Cdd:smart00506  81 RASGHSKEGF-ELLENAYRNCLELAIELGITSVALPLIGTGIYGVPKDRSAQAL 133
 
Name Accession Description Interval E-value
Macro_OAADPr_deacetylase cd02908
macrodomain, O-acetyl-ADP-ribose (OAADPr) family; Macrodomains are found in a variety of ...
 71-198 5.36e-70

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: 218.54  E-value: 5.36e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143526  71 KVSLYRGDITLLEVDAIVNAANASLLGGGG-D---------------------------------------VIHTVGPIA 110
Cdd:cd02908     1 KISLWRGDITKLEVDAIVNAANSSLLGGGGvDgaihraagpelleecrklggvcptgeakitpgynlpakyVIHTVGPIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143526 111 RGHINGsHKEDLANCYQSSLKLVKENNLRSVAFPCISTGIYGFPNEPAAVIALGTIKEWLAKnHQEVDRIIFCVFLEVDF 190
Cdd:cd02908    81 EGGVEE-EPELLASCYRSSLELALENGLKSIAFPCISTGIYGYPNEEAAEIALNTVREWLEE-HDKIDRIIFVVFLDEDY 158


                  ....*...
gi 1907143526 191 KIYKKKMN 198
Cdd:cd02908   159 KIYEELLP 166
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 72-199 1.87e-48

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: 163.04  E-value: 1.87e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143526  72 VSLYRGDITLLEVDAIVNAANASLLGGGG-D-----------------------------------------VIHTVGPI 109
Cdd:COG2110     1 IEIVQGDITELDVDAIVNAANSSLLGGGGvAgaihraagpelleecrrlckqggcptgeavitpagnlpakyVIHTVGPV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143526 110 ARGHINGShKEDLANCYQSSLKLVKENNLRSVAFPCISTGIYGFPNEPAAVIALGTIKEWLaKNHQEVDRIIFCVFLEVD 189
Cdd:COG2110    81 WRGGGPSE-EELLASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFL-EEHPSLEEVRFVLFDEED 158

                         170
                  ....*....|
gi 1907143526 190 FKIYKKKMNE 199
Cdd:COG2110   159 YEAYRRALAR 168
PRK00431 PRK00431
ADP-ribose-binding protein;
71-200 1.11e-43

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 150.76  E-value: 1.11e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143526  71 KVSLYRGDITLLEVDAIVNAANASLLGGGG-D------------------------------------------VIHTVG 107
Cdd:PRK00431    4 RIEVVQGDITELEVDAIVNAANSSLLGGGGvDgaihraagpeileecrelrqqqgpcptgeavitsagrlpakyVIHTVG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143526 108 PI-ARGHINGSHKedLANCYQSSLKLVKENNLRSVAFPCISTGIYGFPNEPAAVIALGTIKEWLAKnHQEVDRIIFCVFL 186
Cdd:PRK00431   84 PVwRGGEDNEAEL--LASAYRNSLRLAAELGLRSIAFPAISTGVYGYPLEDAARIAVKTVREFLTR-HKSPEEVYFVCYD 160

                         170
                  ....*....|....
gi 1907143526 187 EVDFKIYKKKMNEF 200
Cdd:PRK00431  161 EEAYRLYERLLTQQ 174
PRK04143 PRK04143
protein-ADP-ribose hydrolase;
13-199 2.70e-43

protein-ADP-ribose hydrolase;


Pssm-ID: 235225  Cd Length: 264  Bit Score: 152.83  E-value: 2.70e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143526  13 EEKERLLKMTLEERRKEYI-RDYVSLST-ILS-WKEEMKSKGQNDEENTQEapqmkkslsEKVSLYRGDITLLEVDAIVN 89
Cdd:PRK04143   32 EEQQDLLRALANVRPALPLsDEYLNLQDaYLQdENAERGVVDLKDLQPIKY---------DNIFLWQGDITRLKVDAIVN 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143526  90 AANASLLG------------------------------------GGGD-------------VIHTVGP-IARGHINGSHK 119
Cdd:PRK04143  103 AANSRLLGcfqpnhdcidnaihtfagvqlrldcaeimteqgrkeATGQakitraynlpakyVIHTVGPiIRKQPVSPIRA 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143526 120 EDLANCYQSSLKLVKENNLRSVAFPCISTGIYGFPNEPAAVIALGTIKEWLaKNHQEVDRIIFCVFLEVDFKIYKKKMNE 199
Cdd:PRK04143  183 DLLASCYRSCLKLAEKAGLKSIAFCCISTGVFGFPKEEAAEIAIKTVLSWL-KENPSKLKVVFNVFTDEDLELYQKALNK 261
Macro_Af1521_BAL-like cd02907
macrodomain, Af1521-like family; Macrodomains are found in a variety of proteins with diverse ...
 71-175 4.87e-29

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: 111.04  E-value: 4.87e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143526  71 KVSLYRGDITLLEVDAIVNAANASLLGGGG-------------------------------------------DVIHTVG 107
Cdd:cd02907     3 KVSVYKGDITKEKVDAIVNAANERLKHGGGvagaiskaggpeiqeecdkyikkngklrvgevvvtsagklpckYVIHAVG 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907143526 108 PIARGHINGSHKEDLANCYQSSLKLVKENNLRSVAFPCISTGIYGFPNEPAAVIALGTIKEWLAKNHQ 175
Cdd:cd02907    83 PRWSGGSKEECEDLLYKAVLNSLEEAEELKATSIAIPAISSGIFGFPLDLCAEAIVEAIKDFSESNSS 150
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 88-162 9.23e-27

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: 103.80  E-value: 9.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143526  88 VNAANASLLGGGG-----------------------------------------DVIHTVGPIARGHINGSHKEDLANCY 126
Cdd:pfam01661   1 VNAANSRLLGGGGvagaihraagpelleecrelkkggcptgeavvtpggnlpakYVIHTVGPTWRHGGSHGEEELLESCY 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907143526 127 QSSLKLVKENNLRSVAFPCISTGIYGFPNEPAAVIA 162
Cdd:pfam01661  81 RNALALAEELGIKSIAFPAISTGIYGFPWEEAARIA 116
Macro_GDAP2-like cd02905
macrodomain, GDAP2-like family; Macrodomains are found in a variety of proteins with diverse ...
 71-197 3.59e-25

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: 101.16  E-value: 3.59e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143526  71 KVSLYRGDITLLEVDAIVNAANASLL------------GGGGD---------------------------VIHTVGPiar 111
Cdd:cd02905     2 KIVLWDGDLTLLNVDAIVNSTNESLTdkspisdrlflaAGPELreelaklggcrtgeakltkgynlparyVIHTVGP--- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143526 112 gHINGSHK---ED-LANCYQSSLKLVKENNLRSVAFPCISTGIYGFPNEPAAVIALGTIKEWLAKNHQEVDRIIFCVfLE 187
Cdd:cd02905    79 -RYNEKYRtaaESaLYSCYRNVLQLAKEHKLRSVAFPVIHSERRGYPLEDGAHIALRTVRRFLEKHGSSFEAVVFVV-TE 156

                         170
                  ....*....|
gi 1907143526 188 VDFKIYKKKM 197
Cdd:cd02905   157 EEMETYERLL 166
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 71-162 3.19e-23

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: 94.68  E-value: 3.19e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143526   71 KVSLYRGDITLLEVDAIVNAANASLLGGGG------------------------------------------DVIHTVGP 108
Cdd:smart00506   1 ILKVVKGDITKPRADAIVNAANSDGAHGGGvagaiaraagkalskeevrklaggecpvgtavvteggnlpakYVIHAVGP 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907143526  109 IARGHINGSHkEDLANCYQSSLKLVKENNLRSVAFPCISTGIYGFPNEPAAVIA 162
Cdd:smart00506  81 RASGHSKEGF-ELLENAYRNCLELAIELGITSVALPLIGTGIYGVPKDRSAQAL 133
Macro_SF cd02749
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 85-163 1.90e-18

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: 80.91  E-value: 1.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143526  85 DAIVNAANASLLGGGG------------------------------------------DVIHTVGPIARGHinGSHKEDL 122
Cdd:cd02749     1 DAIVNPANNDLYLGGGvakaiskkaggdlqeeceerkkngylkvgevavtkggnlparYIIHVVGPVASSK--KKTYEPL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907143526 123 ANCYQSSLKLVKENNLRSVAFPCISTGIYGFPNEPAAVIAL 163
Cdd:cd02749    79 KKCVKNCLSLADEKGLKSVAFPAIGTGIAGFPPEEAARIML 119
Macro_Ttha0132-like cd03330
Macrodomain, uncharacterized family similar to Thermus thermophilus hypothetical protein ...
 71-177 1.66e-12

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: 64.76  E-value: 1.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143526  71 KVSLYRGDITLLEVDAIVNAANASLLGGGG---------------------------------------DVIH--TVGPI 109
Cdd:cd03330     1 RLIVVQGDITEQDADAIVNAANRRLLMGSGvagaikrkggeeiereamrkgpirvgeavetgagklpakYVIHaaVMGMP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907143526 110 ARghingSHKEDLANCYQSSLKLVKENNLRSVAFPCISTGIYGFPNEPAAVIALGTIKEWLAKNHQEV 177
Cdd:cd03330    81 GR-----SSEESIRDATRNALAKAEELGLESVAFPAIGTGVGGFPVEEVARIMLEEIKKCDPPLLEEV 143
Macro_H2A-like cd02904
macrodomain, macroH2A-like family; Macrodomains are found in a variety of proteins with ...
 65-167 7.30e-11

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: 61.18  E-value: 7.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143526  65 KKSLS--EKVSLYRGDITLLEVDAIVNAANASL-LG----------GGGDVIHTV-------GPIARG------------ 112
Cdd:cd02904    11 EKKLFlgQKLTVVQGDIASIKADAIVHPTNATFyLGgevgsalekaGGKEFVEEVkelrksnGPLEVAgaaispghnlpa 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907143526 113 ----HING------SHKEDLANCYQSSLKLVKENNLRSVAFPCISTGIYGFPNEPAAVIALGTIK 167
Cdd:cd02904    91 kfviHCNSpswgsdKCEELLEKTVKNCLALADEKKLKSVAFPSIGSGRNGFPKQTAAQTILKAIS 155
Macro_X_Nsp3-like cd21557
X-domain (or Mac1 domain) of viral non-structural protein 3 and related macrodomains; The ...
 85-154 1.61e-08

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: 52.56  E-value: 1.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143526  85 DAIVNAANASLLGGGG-----------------------------------------DVIHTVGPIARGHiNGSHKedLA 123
Cdd:cd21557     2 DVVVNAANENLKHGGGvagaiykatggafqkesdyikkngplkvgtavllpghglakNIIHVVGPRKRKG-QDDQL--LA 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907143526 124 NCYQSSLKLVKennlrSVAFPCISTGIYGFP 154
Cdd:cd21557    79 AAYKAVNKEYG-----SVLTPLLSAGIFGVP 104
 
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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