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Conserved domains on  [gi|767925861|ref|XP_011510779|]
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protein mono-ADP-ribosyltransferase PARP15 isoform X6 [Homo sapiens]

Protein Classification

Macro_BAL-like and TCCD_inducible_PARP_like domain-containing protein( domain architecture ID 10206230)

Macro_BAL-like and TCCD_inducible_PARP_like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 181-337 1.11e-64

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: 208.65  E-value: 1.11e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861 181 QVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQP-HRDFIITPGGCLKCKIIIHVPGGKD-- 257
Cdd:cd02903   11 QLVKGDITKEKTDVIVNSVSSDLLLKGGVSKAILKAAGPELQDECANQGKQPaSGDVIVTSGGNLPCKYVYHVVLPHYnp 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861 258 -----VRKTVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVADNIIDAIVDFSSQHSTPSLKTVKVVIFQPELLNIFYD 332
Cdd:cd02903   91 gnektLKDIVRKCLEKAENYKMSSISFPAIGTGNLGFPKDVVAEIMIDEVLKFSSKNPSSSLKEVRFVIFPPETLQAFSD 170


                 ....*
gi 767925861 333 SMKKR 337
Cdd:cd02903  171 ELAKR 175
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 430-550 2.35e-60

Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. 2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD) causes pleotropic effects in mammalian species through modulating gene expression. TCCD indicible PARP (TiPARP) is a target of TCDD that may contribute to multiple responses to TCDD by modulating protein function through poly ADP-ribosylation


:

Pssm-ID: 238719 [Multi-domain]  Cd Length: 121  Bit Score: 195.23  E-value: 2.35e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861 430 LLFHGTDADSVPYVNQHGFNRSCAGKNAVSYGKGTYFAVDASYSAKDTYSKPDSNGRKHMYVVRVLTGVFTKGRAGLVTP 509
Cdd:cd01439    1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKADGLKEMFLARVLTGDYTQGHPGYRRP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 767925861 510 PPKNPHNPTDLFDSVTNNTRSPKLFVVFFDNQAYPEYLITF 550
Cdd:cd01439   81 PLKPSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
Macro super family cl46597
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 107-179 1.33e-11

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.


The actual alignment was detected with superfamily member pfam01661:

Pssm-ID: 460286  Cd Length: 116  Bit Score: 61.43  E-value: 1.33e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767925861  107 VNSVPMNLqLGGGPLSRAFLQKAGPMLQKELDDRRREtEEKVGNIFMTSGCNLDCKAVLHAVAPYWNNGAETS 179
Cdd:pfam01661   1 VNAANSRL-LGGGGVAGAIHRAAGPELLEECRELKKG-GCPTGEAVVTPGGNLPAKYVIHTVGPTWRHGGSHG 71
 
Name Accession Description Interval E-value
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 181-337 1.11e-64

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: 208.65  E-value: 1.11e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861 181 QVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQP-HRDFIITPGGCLKCKIIIHVPGGKD-- 257
Cdd:cd02903   11 QLVKGDITKEKTDVIVNSVSSDLLLKGGVSKAILKAAGPELQDECANQGKQPaSGDVIVTSGGNLPCKYVYHVVLPHYnp 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861 258 -----VRKTVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVADNIIDAIVDFSSQHSTPSLKTVKVVIFQPELLNIFYD 332
Cdd:cd02903   91 gnektLKDIVRKCLEKAENYKMSSISFPAIGTGNLGFPKDVVAEIMIDEVLKFSSKNPSSSLKEVRFVIFPPETLQAFSD 170


                 ....*
gi 767925861 333 SMKKR 337
Cdd:cd02903  171 ELAKR 175
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 430-550 2.35e-60

Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. 2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD) causes pleotropic effects in mammalian species through modulating gene expression. TCCD indicible PARP (TiPARP) is a target of TCDD that may contribute to multiple responses to TCDD by modulating protein function through poly ADP-ribosylation


Pssm-ID: 238719 [Multi-domain]  Cd Length: 121  Bit Score: 195.23  E-value: 2.35e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861 430 LLFHGTDADSVPYVNQHGFNRSCAGKNAVSYGKGTYFAVDASYSAKDTYSKPDSNGRKHMYVVRVLTGVFTKGRAGLVTP 509
Cdd:cd01439    1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKADGLKEMFLARVLTGDYTQGHPGYRRP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 767925861 510 PPKNPHNPTDLFDSVTNNTRSPKLFVVFFDNQAYPEYLITF 550
Cdd:cd01439   81 PLKPSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 379-550 1.58e-26

Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active.


Pssm-ID: 395519 [Multi-domain]  Cd Length: 195  Bit Score: 106.65  E-value: 1.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861  379 EYNTIKDKFTRT-----CSSYAIEKIERIQNAFLWQSYQVKKRQMdikndhknNERLLFHGTDADSVPYVNQHGF--NRS 451
Cdd:pfam00644   3 EYQIIEKYFLSThdpthGYPLFILEIFRVQRDGEWERFQPKKKLR--------NRRLLWHGSRLTNFLGILSQGLriAPP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861  452 CAGKNAVSYGKGTYFAVDASYSAKdtYSKPD-SNGRKHMYVVRVLTG------------------VFTKGRaGLVTPPPK 512
Cdd:pfam00644  75 EAPVTGYMFGKGIYFADDASKSAN--YCPPSeAHGNGLMLLSEVALGdmnelkkadyaeklppgkHSVKGL-GKTAPESF 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 767925861  513 NPHNPTDLFDSVTNNTRS----PKLFVVFFDNQAYPEYLITF 550
Cdd:pfam00644 152 VDLDGVPLGKLVATGYDSsvllYNEYVVYNVNQVRPKYLLEV 193
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 181-336 3.50e-25

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: 101.79  E-value: 3.50e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861 181 QVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQ---PHRDFIITPGGCLKCKIIIHVPG--- 254
Cdd:COG2110    2 EIVQGDITELDVDAIVNAANSSLLGGGGVAGAIHRAAGPELLEECRRLCKQggcPTGEAVITPAGNLPAKYVIHTVGpvw 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861 255 --G-----KDVRKTVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVADNIIDAIVDFSSQHstPSLKTVKVVIFQPELL 327
Cdd:COG2110   82 rgGgpseeELLASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFLEEH--PSLEEVRFVLFDEEDY 159


                 ....*....
gi 767925861 328 NIFYDSMKK 336
Cdd:COG2110  160 EAYRRALAR 168
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 181-296 1.81e-18

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: 81.58  E-value: 1.81e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861   181 QVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQ---PHRDFIITPGGCLKCKIIIHVPGG-- 255
Cdd:smart00506   3 KVVKGDITKPRADAIVNAANSDGAHGGGVAGAIARAAGKALSKEEVRKLAGgecPVGTAVVTEGGNLPAKYVIHAVGPra 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 767925861   256 --------KDVRKTVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVAD 296
Cdd:smart00506  83 sghskegfELLENAYRNCLELAIELGITSVALPLIGTGIYGVPKDRSAQ 131
PRK00431 PRK00431
ADP-ribose-binding protein;
182-330 3.20e-14

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 71.03  E-value: 3.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861 182 VATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQ----PHRDFIITPGGCLKCKIIIHVPG--- 254
Cdd:PRK00431   7 VVQGDITELEVDAIVNAANSSLLGGGGVDGAIHRAAGPEILEECRELRQQqgpcPTGEAVITSAGRLPAKYVIHTVGpvw 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861 255 --GKD-----VRKTVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVADNIIDAIVDFSSQHStpSLKTVKVVIFQPELL 327
Cdd:PRK00431  87 rgGEDneaelLASAYRNSLRLAAELGLRSIAFPAISTGVYGYPLEDAARIAVKTVREFLTRHK--SPEEVYFVCYDEEAY 164


                 ...
gi 767925861 328 NIF 330
Cdd:PRK00431 165 RLY 167
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 107-179 1.33e-11

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: 61.43  E-value: 1.33e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767925861  107 VNSVPMNLqLGGGPLSRAFLQKAGPMLQKELDDRRREtEEKVGNIFMTSGCNLDCKAVLHAVAPYWNNGAETS 179
Cdd:pfam01661   1 VNAANSRL-LGGGGVAGAIHRAAGPELLEECRELKKG-GCPTGEAVVTPGGNLPAKYVIHTVGPTWRHGGSHG 71
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 196-288 5.57e-10

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: 56.80  E-value: 5.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861  196 VNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQPHR--DFIITPGGCLKCKIIIHVPG-----------GKDVRKTV 262
Cdd:pfam01661   1 VNAANSRLLGGGGVAGAIHRAAGPELLEECRELKKGGCPtgEAVVTPGGNLPAKYVIHTVGptwrhggshgeEELLESCY 80

                          90       100
                  ....*....|....*....|....*.
gi 767925861  263 TSVLEECEQRKYTSVSLPAIGTGNAG 288
Cdd:pfam01661  81 RNALALAEELGIKSIAFPAISTGIYG 106
PRK00431 PRK00431
ADP-ribose-binding protein;
88-177 2.49e-09

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 56.77  E-value: 2.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861  88 GLNLKLISGDVLYIWADVIVNsvPMN-LQLGGGPLSRAFLQKAGPMLQKELDDRRRETEE-KVGNIFMTSGCNLDCKAVL 165
Cdd:PRK00431   2 GMRIEVVQGDITELEVDAIVN--AANsSLLGGGGVDGAIHRAAGPEILEECRELRQQQGPcPTGEAVITSAGRLPAKYVI 79

                         90
                 ....*....|..
gi 767925861 166 HAVAPYWNNGAE 177
Cdd:PRK00431  80 HTVGPVWRGGED 91
Macro_Ttha0132-like cd03330
Macrodomain, uncharacterized family similar to Thermus thermophilus hypothetical protein ...
 91-178 4.75e-08

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: 52.44  E-value: 4.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861  91 LKLISGDVLYIWADVIVNSVPMNLQLGGGpLSRAFLQKAGPMLQKELDdrrRETEEKVGNIFMTSGCNLDCKAVLHA--V 168
Cdd:cd03330    2 LIVVQGDITEQDADAIVNAANRRLLMGSG-VAGAIKRKGGEEIEREAM---RKGPIRVGEAVETGAGKLPAKYVIHAavM 77

                         90
                 ....*....|
gi 767925861 169 APYWNNGAET 178
Cdd:cd03330   78 GMPGRSSEES 87
 
Name Accession Description Interval E-value
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 181-337 1.11e-64

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: 208.65  E-value: 1.11e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861 181 QVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQP-HRDFIITPGGCLKCKIIIHVPGGKD-- 257
Cdd:cd02903   11 QLVKGDITKEKTDVIVNSVSSDLLLKGGVSKAILKAAGPELQDECANQGKQPaSGDVIVTSGGNLPCKYVYHVVLPHYnp 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861 258 -----VRKTVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVADNIIDAIVDFSSQHSTPSLKTVKVVIFQPELLNIFYD 332
Cdd:cd02903   91 gnektLKDIVRKCLEKAENYKMSSISFPAIGTGNLGFPKDVVAEIMIDEVLKFSSKNPSSSLKEVRFVIFPPETLQAFSD 170


                 ....*
gi 767925861 333 SMKKR 337
Cdd:cd02903  171 ELAKR 175
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 430-550 2.35e-60

Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. 2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD) causes pleotropic effects in mammalian species through modulating gene expression. TCCD indicible PARP (TiPARP) is a target of TCDD that may contribute to multiple responses to TCDD by modulating protein function through poly ADP-ribosylation


Pssm-ID: 238719 [Multi-domain]  Cd Length: 121  Bit Score: 195.23  E-value: 2.35e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861 430 LLFHGTDADSVPYVNQHGFNRSCAGKNAVSYGKGTYFAVDASYSAKDTYSKPDSNGRKHMYVVRVLTGVFTKGRAGLVTP 509
Cdd:cd01439    1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKADGLKEMFLARVLTGDYTQGHPGYRRP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 767925861 510 PPKNPHNPTDLFDSVTNNTRSPKLFVVFFDNQAYPEYLITF 550
Cdd:cd01439   81 PLKPSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
Macro_Af1521_BAL-like cd02907
macrodomain, Af1521-like family; Macrodomains are found in a variety of proteins with diverse ...
 182-315 1.41e-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: 114.12  E-value: 1.41e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861 182 VATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESEC-AVLAAQ---PHRDFIITPGGCLKCKIIIHV--P-- 253
Cdd:cd02907    6 VYKGDITKEKVDAIVNAANERLKHGGGVAGAISKAGGPEIQEECdKYIKKNgklRVGEVVVTSAGKLPCKYVIHAvgPrw 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767925861 254 -GGKD------VRKTVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVADNIIDAIVDFSSQHSTPSLK 315
Cdd:cd02907   86 sGGSKeecedlLYKAVLNSLEEAEELKATSIAIPAISSGIFGFPLDLCAEAIVEAIKDFSESNSSSSLK 154
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 379-550 1.58e-26

Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active.


Pssm-ID: 395519 [Multi-domain]  Cd Length: 195  Bit Score: 106.65  E-value: 1.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861  379 EYNTIKDKFTRT-----CSSYAIEKIERIQNAFLWQSYQVKKRQMdikndhknNERLLFHGTDADSVPYVNQHGF--NRS 451
Cdd:pfam00644   3 EYQIIEKYFLSThdpthGYPLFILEIFRVQRDGEWERFQPKKKLR--------NRRLLWHGSRLTNFLGILSQGLriAPP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861  452 CAGKNAVSYGKGTYFAVDASYSAKdtYSKPD-SNGRKHMYVVRVLTG------------------VFTKGRaGLVTPPPK 512
Cdd:pfam00644  75 EAPVTGYMFGKGIYFADDASKSAN--YCPPSeAHGNGLMLLSEVALGdmnelkkadyaeklppgkHSVKGL-GKTAPESF 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 767925861  513 NPHNPTDLFDSVTNNTRS----PKLFVVFFDNQAYPEYLITF 550
Cdd:pfam00644 152 VDLDGVPLGKLVATGYDSsvllYNEYVVYNVNQVRPKYLLEV 193
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 181-336 3.50e-25

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: 101.79  E-value: 3.50e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861 181 QVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQ---PHRDFIITPGGCLKCKIIIHVPG--- 254
Cdd:COG2110    2 EIVQGDITELDVDAIVNAANSSLLGGGGVAGAIHRAAGPELLEECRRLCKQggcPTGEAVITPAGNLPAKYVIHTVGpvw 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861 255 --G-----KDVRKTVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVADNIIDAIVDFSSQHstPSLKTVKVVIFQPELL 327
Cdd:COG2110   82 rgGgpseeELLASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFLEEH--PSLEEVRFVLFDEEDY 159


                 ....*....
gi 767925861 328 NIFYDSMKK 336
Cdd:COG2110  160 EAYRRALAR 168
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 181-296 1.81e-18

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: 81.58  E-value: 1.81e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861   181 QVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQ---PHRDFIITPGGCLKCKIIIHVPGG-- 255
Cdd:smart00506   3 KVVKGDITKPRADAIVNAANSDGAHGGGVAGAIARAAGKALSKEEVRKLAGgecPVGTAVVTEGGNLPAKYVIHAVGPra 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 767925861   256 --------KDVRKTVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVAD 296
Cdd:smart00506  83 sghskegfELLENAYRNCLELAIELGITSVALPLIGTGIYGVPKDRSAQ 131
Macro_SF cd02749
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 193-301 5.78e-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: 79.75  E-value: 5.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861 193 DVIVNSTARTFNRKSGVSRAILEGAGQAVESECA-VLAAQPHR--DFIITPGGCLKCKIIIHVPGGK---------DVRK 260
Cdd:cd02749    1 DAIVNPANNDLYLGGGVAKAISKKAGGDLQEECEeRKKNGYLKvgEVAVTKGGNLPARYIIHVVGPVasskkktyePLKK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 767925861 261 TVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVADNIIDA 301
Cdd:cd02749   81 CVKNCLSLADEKGLKSVAFPAIGTGIAGFPPEEAARIMLEA 121
Macro_H2A-like cd02904
macrodomain, macroH2A-like family; Macrodomains are found in a variety of proteins with ...
 182-336 1.10e-15

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: 75.43  E-value: 1.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861 182 VATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQ----PHRDFIITPGGCLKCKIIIHV--PGG 255
Cdd:cd02904   22 VVQGDIASIKADAIVHPTNATFYLGGEVGSALEKAGGKEFVEEVKELRKSngplEVAGAAISPGHNLPAKFVIHCnsPSW 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861 256 KDVR------KTVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVADNIIDAIVD-FSSQHSTpSLKTVKVVIFQPELLN 328
Cdd:cd02904  102 GSDKceelleKTVKNCLALADEKKLKSVAFPSIGSGRNGFPKQTAAQTILKAISNyFVSVMSS-SLKQIYFVLFDMESIG 180


                 ....*...
gi 767925861 329 IFYDSMKK 336
Cdd:cd02904  181 IYTSELAK 188
Macro_OAADPr_deacetylase cd02908
macrodomain, O-acetyl-ADP-ribose (OAADPr) family; Macrodomains are found in a variety of ...
 185-335 1.64e-14

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: 71.39  E-value: 1.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861 185 GDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQ-PHRDFIITPGGCLKCKIIIHV--PGGKDV--- 258
Cdd:cd02908    7 GDITKLEVDAIVNAANSSLLGGGGVDGAIHRAAGPELLEECRKLGGVcPTGEAKITPGYNLPAKYVIHTvgPIGEGGvee 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861 259 -----RKTVTSVLEECEQRKYTSVSLPAIGTGNAGKnPITVADNI-IDAIVDFSSQHSTPSLktVKVVIFQPELLNIFYD 332
Cdd:cd02908   87 epellASCYRSSLELALENGLKSIAFPCISTGIYGY-PNEEAAEIaLNTVREWLEEHDKIDR--IIFVVFLDEDYKIYEE 163


                 ...
gi 767925861 333 SMK 335
Cdd:cd02908  164 LLP 166
Macro_Ttha0132-like cd03330
Macrodomain, uncharacterized family similar to Thermus thermophilus hypothetical protein ...
 181-288 2.32e-14

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: 70.54  E-value: 2.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861 181 QVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQPHRDFIITPGGCLKCKIIIHVPGGKD--- 257
Cdd:cd03330    3 IVVQGDITEQDADAIVNAANRRLLMGSGVAGAIKRKGGEEIEREAMRKGPIRVGEAVETGAGKLPAKYVIHAAVMGMpgr 82

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767925861 258 -----VRKTVTSVLEECEQRKYTSVSLPAIGTGNAG 288
Cdd:cd03330   83 sseesIRDATRNALAKAEELGLESVAFPAIGTGVGG 118
PRK00431 PRK00431
ADP-ribose-binding protein;
182-330 3.20e-14

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 71.03  E-value: 3.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861 182 VATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQ----PHRDFIITPGGCLKCKIIIHVPG--- 254
Cdd:PRK00431   7 VVQGDITELEVDAIVNAANSSLLGGGGVDGAIHRAAGPEILEECRELRQQqgpcPTGEAVITSAGRLPAKYVIHTVGpvw 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861 255 --GKD-----VRKTVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVADNIIDAIVDFSSQHStpSLKTVKVVIFQPELL 327
Cdd:PRK00431  87 rgGEDneaelLASAYRNSLRLAAELGLRSIAFPAISTGVYGYPLEDAARIAVKTVREFLTRHK--SPEEVYFVCYDEEAY 164


                 ...
gi 767925861 328 NIF 330
Cdd:PRK00431 165 RLY 167
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 107-179 1.33e-11

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: 61.43  E-value: 1.33e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767925861  107 VNSVPMNLqLGGGPLSRAFLQKAGPMLQKELDDRRREtEEKVGNIFMTSGCNLDCKAVLHAVAPYWNNGAETS 179
Cdd:pfam01661   1 VNAANSRL-LGGGGVAGAIHRAAGPELLEECRELKKG-GCPTGEAVVTPGGNLPAKYVIHTVGPTWRHGGSHG 71
tankyrase_like cd01438
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ...
 370-550 1.33e-10

Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 poly-ADP-ribosylates Telomere Repeat Binding Factor 1 (TRF1) while Tankyrase 2 can poly-ADP-ribosylate itself or TRF1. The tankyrases also contain multiple ankyrin repeats that mediate protein-protein interaction (binding TRF1 and insulin-responsive aminopeptidase) and may function as a complex. Overexpression of Tank1 promotes increased telomere length when overexpressed, while overexpressed Tank2 has been shown to promote PARP cleavage- independent cell death (necrosis).


Pssm-ID: 238718 [Multi-domain]  Cd Length: 223  Bit Score: 61.45  E-value: 1.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861 370 MVQLEPGQSEYNTIKDKFTRTC-------------SSYAIEKIERIQNAFLWQSYQVKKRQMDIKNDHKNNERLLFHGTd 436
Cdd:cd01438   18 LLDLAPDDKEYQSVEEEMQSTIrehrdggnaggifNRYNIIRIQKVVNKKLRERYCHRQKEIAEENHNHHNERMLFHGS- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861 437 adsvPYVN---QHGFNRSCAGKNAVsYGKGTYFAVDASYSAKDTYSKPDSNG------------RKHMYVVRVltgvfTK 501
Cdd:cd01438   97 ----PFINaiiHKGFDERHAYIGGM-FGAGIYFAENSSKSNQYVYGIGGGTGcpthkdrscyvcHRQMLFCRV-----TL 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767925861 502 GRAGLVTPPPKNPHNPTDlFDSVTNNTRSPKL----FVVFFDNQAYPEYLITF 550
Cdd:cd01438  167 GKSFLQFSAMKMAHAPPG-HHSVIGRPSVNGLayaeYVIYRGEQAYPEYLITY 218
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 196-288 5.57e-10

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: 56.80  E-value: 5.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861  196 VNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQPHR--DFIITPGGCLKCKIIIHVPG-----------GKDVRKTV 262
Cdd:pfam01661   1 VNAANSRLLGGGGVAGAIHRAAGPELLEECRELKKGGCPtgEAVVTPGGNLPAKYVIHTVGptwrhggshgeEELLESCY 80

                          90       100
                  ....*....|....*....|....*.
gi 767925861  263 TSVLEECEQRKYTSVSLPAIGTGNAG 288
Cdd:pfam01661  81 RNALALAEELGIKSIAFPAISTGIYG 106
PRK00431 PRK00431
ADP-ribose-binding protein;
88-177 2.49e-09

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 56.77  E-value: 2.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861  88 GLNLKLISGDVLYIWADVIVNsvPMN-LQLGGGPLSRAFLQKAGPMLQKELDDRRRETEE-KVGNIFMTSGCNLDCKAVL 165
Cdd:PRK00431   2 GMRIEVVQGDITELEVDAIVN--AANsSLLGGGGVDGAIHRAAGPEILEECRELRQQQGPcPTGEAVITSAGRLPAKYVI 79

                         90
                 ....*....|..
gi 767925861 166 HAVAPYWNNGAE 177
Cdd:PRK00431  80 HTVGPVWRGGED 91
Macro_GDAP2-like cd02905
macrodomain, GDAP2-like family; Macrodomains are found in a variety of proteins with diverse ...
 180-288 2.20e-08

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: 53.78  E-value: 2.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861 180 WQvatGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQPHRDFIITPGGCLKCKIIIHVPGGKDVR 259
Cdd:cd02905    6 WD---GDLTLLNVDAIVNSTNESLTDKSPISDRLFLAAGPELREELAKLGGCRTGEAKLTKGYNLPARYVIHTVGPRYNE 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767925861 260 KTVT-----------SVLEECEQRKYTSVSLPAIGTGNAG 288
Cdd:cd02905   83 KYRTaaesalyscyrNVLQLAKEHKLRSVAFPVIHSERRG 122
Macro_Ttha0132-like cd03330
Macrodomain, uncharacterized family similar to Thermus thermophilus hypothetical protein ...
 91-178 4.75e-08

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: 52.44  E-value: 4.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861  91 LKLISGDVLYIWADVIVNSVPMNLQLGGGpLSRAFLQKAGPMLQKELDdrrRETEEKVGNIFMTSGCNLDCKAVLHA--V 168
Cdd:cd03330    2 LIVVQGDITEQDADAIVNAANRRLLMGSG-VAGAIKRKGGEEIEREAM---RKGPIRVGEAVETGAGKLPAKYVIHAavM 77

                         90
                 ....*....|
gi 767925861 169 APYWNNGAET 178
Cdd:cd03330   78 GMPGRSSEES 87
Macro_OAADPr_deacetylase cd02908
macrodomain, O-acetyl-ADP-ribose (OAADPr) family; Macrodomains are found in a variety of ...
 91-177 1.60e-06

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: 48.28  E-value: 1.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861  91 LKLISGDVLYIWADVIVNsvPMNLQL-GGGPLSRAFLQKAGPMLQKELddRRRETEEKVGNIFMTSGCNLDCKAVLHAVA 169
Cdd:cd02908    2 ISLWRGDITKLEVDAIVN--AANSSLlGGGGVDGAIHRAAGPELLEEC--RKLGGVCPTGEAKITPGYNLPAKYVIHTVG 77


                 ....*...
gi 767925861 170 PYWNNGAE 177
Cdd:cd02908   78 PIGEGGVE 85
Macro_GDAP2-like cd02905
macrodomain, GDAP2-like family; Macrodomains are found in a variety of proteins with diverse ...
 96-179 1.96e-06

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: 48.00  E-value: 1.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861  96 GDVLYIWADVIVNSVPMNLqLGGGPLSRAFLQKAGPMLQKELddrRRETEEKVGNIFMTSGCNLDCKAVLHAVAPYWN-- 173
Cdd:cd02905    8 GDLTLLNVDAIVNSTNESL-TDKSPISDRLFLAAGPELREEL---AKLGGCRTGEAKLTKGYNLPARYVIHTVGPRYNek 83


                 ....*...
gi 767925861 174 --NGAETS 179
Cdd:cd02905   84 yrTAAESA 91
Macro_X_Nsp3-like cd21557
X-domain (or Mac1 domain) of viral non-structural protein 3 and related macrodomains; The ...
 104-170 2.22e-05

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: 44.08  E-value: 2.22e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767925861 104 DVIVNSVPMNLQLGGGpLSRAFLQKAGPMLQKELDDRRRETEEKVGNIFMTSgCNLDCKAVLHAVAP 170
Cdd:cd21557    2 DVVVNAANENLKHGGG-VAGAIYKATGGAFQKESDYIKKNGPLKVGTAVLLP-GHGLAKNIIHVVGP 66
PRK04143 PRK04143
protein-ADP-ribose hydrolase;
180-330 2.37e-05

protein-ADP-ribose hydrolase;


Pssm-ID: 235225  Cd Length: 264  Bit Score: 46.13  E-value: 2.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861 180 WQvatGDIATEQVDVIVNSTARTF------NRKSgVSRAILEGAGQAVESECAVL-AAQPHRDFI----ITPGGCLKCKI 248
Cdd:PRK04143  88 WQ---GDITRLKVDAIVNAANSRLlgcfqpNHDC-IDNAIHTFAGVQLRLDCAEImTEQGRKEATgqakITRAYNLPAKY 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925861 249 IIHVPGGKDVRKTVT------------SVLEECEQRKYTSVSLPAIGTGNAGKnPITVADNI-IDAIVDFssQHSTPSLK 315
Cdd:PRK04143 164 VIHTVGPIIRKQPVSpiradllascyrSCLKLAEKAGLKSIAFCCISTGVFGF-PKEEAAEIaIKTVLSW--LKENPSKL 240

                        170
                 ....*....|....*
gi 767925861 316 TVKVVIFQPELLNIF 330
Cdd:PRK04143 241 KVVFNVFTDEDLELY 255
 
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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