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Conserved domains on  [gi|2228568364|ref|NP_001392227|]
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protein mono-ADP-ribosyltransferase PARP9 isoform b [Mus musculus]

Protein Classification

macro domain-containing protein( domain architecture ID 10121109)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Macro_Af1521_BAL-like cd02907
macrodomain, Af1521-like family; Macrodomains are found in a variety of proteins with diverse ...
 83-243 4.67e-75

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: 241.24  E-value: 4.67e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364  83 GIELSVWKDDLTRHVVDAVVNAANENLLHGSGLAGSLVKTGGFEIQEESKRIIANVGKISVGGIAITGAGRLPCHLIIHA 162
Cdd:cd02907     1 GIKVSVYKGDITKEKVDAIVNAANERLKHGGGVAGAISKAGGPEIQEECDKYIKKNGKLRVGEVVVTSAGKLPCKYVIHA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 163 VGPRWTVTNSQTAIELLKFAIRNILDYVTKYdlRIKTVAIPALSSGIFQFPLDLCTSIILETIRlYFQDKQMFGNLREIH 242
Cdd:cd02907    81 VGPRWSGGSKEECEDLLYKAVLNSLEEAEEL--KATSIAIPAISSGIFGFPLDLCAEAIVEAIK-DFSESNSSSSLKEIR 157


                  .
gi 2228568364 243 L 243
Cdd:cd02907   158 L 158
Macro_SF super family cl00019
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 285-455 3.44e-49

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.


The actual alignment was detected with superfamily member cd02903:

Pssm-ID: 469581  Cd Length: 175  Bit Score: 171.28  E-value: 3.44e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 285 GRGLTLQIVQGCIEMQTTDVIVNSGYMQDFKSGRVAQSILRQAGVEMEKELDKVNLSTDYQEVWVTKGFKLSCQYVFHVA 364
Cdd:cd02903     5 IGGITVQLVKGDITKEKTDVIVNSVSSDLLLKGGVSKAILKAAGPELQDECANQGKQPASGDVIVTSGGNLPCKYVYHVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 365 W-HSQINKYQILKDAMKSCLEKCLKPDINSISFPALGTGLMDLKKSTAAQIMFEEVFAFAKEHKEKTL-TVKIVIFPvdV 442
Cdd:cd02903    85 LpHYNPGNEKTLKDIVRKCLEKAENYKMSSISFPAIGTGNLGFPKDVVAEIMIDEVLKFSSKNPSSSLkEVRFVIFP--P 162

                         170
                  ....*....|...
gi 2228568364 443 ETYKIFYAEMTKR 455
Cdd:cd02903   163 ETLQAFSDELAKR 175
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 673-792 1.50e-40

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: 144.77  E-value: 1.50e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 673 RLFQQVPHQFCNTVCRVGFHRMYSTSYNPVYGAGIYFTKSLKNLADKVKKTSSTDKLIYVFEAEVLTGSFCQGNSSNIIP 752
Cdd:cd01439     1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKADGLKEMFLARVLTGDYTQGHPGYRRP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2228568364 753 P-PLSPGALDVNDSVVDNVSSPETIVVFNGMQAMPLYLWTC 792
Cdd:cd01439    81 PlKPSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
 
Name Accession Description Interval E-value
Macro_Af1521_BAL-like cd02907
macrodomain, Af1521-like family; Macrodomains are found in a variety of proteins with diverse ...
 83-243 4.67e-75

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: 241.24  E-value: 4.67e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364  83 GIELSVWKDDLTRHVVDAVVNAANENLLHGSGLAGSLVKTGGFEIQEESKRIIANVGKISVGGIAITGAGRLPCHLIIHA 162
Cdd:cd02907     1 GIKVSVYKGDITKEKVDAIVNAANERLKHGGGVAGAISKAGGPEIQEECDKYIKKNGKLRVGEVVVTSAGKLPCKYVIHA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 163 VGPRWTVTNSQTAIELLKFAIRNILDYVTKYdlRIKTVAIPALSSGIFQFPLDLCTSIILETIRlYFQDKQMFGNLREIH 242
Cdd:cd02907    81 VGPRWSGGSKEECEDLLYKAVLNSLEEAEEL--KATSIAIPAISSGIFGFPLDLCAEAIVEAIK-DFSESNSSSSLKEIR 157


                  .
gi 2228568364 243 L 243
Cdd:cd02907   158 L 158
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 285-455 3.44e-49

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: 171.28  E-value: 3.44e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 285 GRGLTLQIVQGCIEMQTTDVIVNSGYMQDFKSGRVAQSILRQAGVEMEKELDKVNLSTDYQEVWVTKGFKLSCQYVFHVA 364
Cdd:cd02903     5 IGGITVQLVKGDITKEKTDVIVNSVSSDLLLKGGVSKAILKAAGPELQDECANQGKQPASGDVIVTSGGNLPCKYVYHVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 365 W-HSQINKYQILKDAMKSCLEKCLKPDINSISFPALGTGLMDLKKSTAAQIMFEEVFAFAKEHKEKTL-TVKIVIFPvdV 442
Cdd:cd02903    85 LpHYNPGNEKTLKDIVRKCLEKAENYKMSSISFPAIGTGNLGFPKDVVAEIMIDEVLKFSSKNPSSSLkEVRFVIFP--P 162

                         170
                  ....*....|...
gi 2228568364 443 ETYKIFYAEMTKR 455
Cdd:cd02903   163 ETLQAFSDELAKR 175
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 86-257 2.30e-41

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: 149.17  E-value: 2.30e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364  86 LSVWKDDLTRHVVDAVVNAANENLLHGSGLAGSLVKTGGFEIQEESKRIIANvGKISVGGIAITGAGRLPCHLIIHAVGP 165
Cdd:COG2110     1 IEIVQGDITELDVDAIVNAANSSLLGGGGVAGAIHRAAGPELLEECRRLCKQ-GGCPTGEAVITPAGNLPAKYVIHTVGP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 166 RWtVTNSQTAIELLKFAIRNILDYVTKYDlrIKTVAIPALSSGIFQFPLDLCTSIILETIRLYFQDkqmFGNLREIHLVS 245
Cdd:COG2110    80 VW-RGGGPSEEELLASCYRNSLELAEELG--IRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFLEE---HPSLEEVRFVL 153

                         170
                  ....*....|..
gi 2228568364 246 NEDPTVASFKSA 257
Cdd:COG2110   154 FDEEDYEAYRRA 165
PRK00431 PRK00431
ADP-ribose-binding protein;
83-264 6.39e-41

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 148.07  E-value: 6.39e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364  83 GIELSVWKDDLTRHVVDAVVNAANENLLHGSGLAGSLVKTGGFEIQEESKRIIANVGKISVGGIAITGAGRLPCHLIIHA 162
Cdd:PRK00431    2 GMRIEVVQGDITELEVDAIVNAANSSLLGGGGVDGAIHRAAGPEILEECRELRQQQGPCPTGEAVITSAGRLPAKYVIHT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 163 VGPRWTVTNSQTAiELLKFAIRNILDYVTkyDLRIKTVAIPALSSGIFQFPLDLCTSIILETIRLYFQDKqmfGNLREIH 242
Cdd:PRK00431   82 VGPVWRGGEDNEA-ELLASAYRNSLRLAA--ELGLRSIAFPAISTGVYGYPLEDAARIAVKTVREFLTRH---KSPEEVY 155

                         170       180
                  ....*....|....*....|..
gi 2228568364 243 LVSNEDPTVASFKSASESILGR 264
Cdd:PRK00431  156 FVCYDEEAYRLYERLLTQQGDE 177
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 673-792 1.50e-40

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: 144.77  E-value: 1.50e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 673 RLFQQVPHQFCNTVCRVGFHRMYSTSYNPVYGAGIYFTKSLKNLADKVKKTSSTDKLIYVFEAEVLTGSFCQGNSSNIIP 752
Cdd:cd01439     1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKADGLKEMFLARVLTGDYTQGHPGYRRP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2228568364 753 P-PLSPGALDVNDSVVDNVSSPETIVVFNGMQAMPLYLWTC 792
Cdd:cd01439    81 PlKPSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 102-221 6.62e-40

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: 142.70  E-value: 6.62e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 102 VNAANENLLHGSGLAGSLVKTGGFEIQEESKRIIAnvGKISVGGIAITGAGRLPCHLIIHAVGPRWTVTNSQTAIELLKF 181
Cdd:pfam01661   1 VNAANSRLLGGGGVAGAIHRAAGPELLEECRELKK--GGCPTGEAVVTPGGNLPAKYVIHTVGPTWRHGGSHGEEELLES 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2228568364 182 AIRNILDYVTKYDlrIKTVAIPALSSGIFQFPLDLCTSII 221
Cdd:pfam01661  79 CYRNALALAEELG--IKSIAFPAISTGIYGFPWEEAARIA 116
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 85-221 5.44e-32

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: 120.87  E-value: 5.44e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364   85 ELSVWKDDLTRHVVDAVVNAANENLLHGSGLAGSLVKTGGFEIQEESKRiIANVGKISVGGIAITGAGRLPCHLIIHAVG 164
Cdd:smart00506   1 ILKVVKGDITKPRADAIVNAANSDGAHGGGVAGAIARAAGKALSKEEVR-KLAGGECPVGTAVVTEGGNLPAKYVIHAVG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2228568364  165 PRWtVTNSQTAIELLKFAIRNILDYVtkYDLRIKTVAIPALSSGIFQFPLDLCTSII 221
Cdd:smart00506  80 PRA-SGHSKEGFELLENAYRNCLELA--IELGITSVALPLIGTGIYGVPKDRSAQAL 133
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 290-454 5.57e-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: 102.18  E-value: 5.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 290 LQIVQGCIEMQTTDVIVN----SGYMqdfksGR-VAQSILRQAGVEMEKELDKVNLSTDYQ--EVWVTKGFKLSCQYVFH 362
Cdd:COG2110     1 IEIVQGDITELDVDAIVNaansSLLG-----GGgVAGAIHRAAGPELLEECRRLCKQGGCPtgEAVITPAGNLPAKYVIH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 363 VA---WHSQI-NKYQILKDAMKSCLEKCLKPDINSISFPALGTGLMDLKKSTAAQIMFEEVFAFAKEHKEKTlTVKIVIF 438
Cdd:COG2110    76 TVgpvWRGGGpSEEELLASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFLEEHPSLE-EVRFVLF 154

                         170
                  ....*....|....*.
gi 2228568364 439 pvDVETYKIFYAEMTK 454
Cdd:COG2110   155 --DEEDYEAYRRALAR 168
PRK00431 PRK00431
ADP-ribose-binding protein;
286-458 1.61e-20

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 89.52  E-value: 1.61e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 286 RGLTLQIVQGCIEMQTTDVIVN----SGYMqdfkSGRVAQSILRQAGVEMEKELDKVNLSTDY---QEVWVTKGFKLSCQ 358
Cdd:PRK00431    1 MGMRIEVVQGDITELEVDAIVNaansSLLG----GGGVDGAIHRAAGPEILEECRELRQQQGPcptGEAVITSAGRLPAK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 359 YVFHVA---WH-SQINKYQILKDAMKSCLEKCLKPDINSISFPALGTGLMDLKKSTAAQIMFEEVFAFAKEHKektlTVK 434
Cdd:PRK00431   77 YVIHTVgpvWRgGEDNEAELLASAYRNSLRLAAELGLRSIAFPAISTGVYGYPLEDAARIAVKTVREFLTRHK----SPE 152

                         170       180
                  ....*....|....*....|....*
gi 2228568364 435 IVIF-PVDVETYKIFYAEMTKRSNE 458
Cdd:PRK00431  153 EVYFvCYDEEAYRLYERLLTQQGDE 177
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 317-415 4.71e-14

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: 69.13  E-value: 4.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 317 GRVAQSILRQAGVEMEKELDK-VNLSTDYQEVWVTKGFKLSCQYVFHVA------WHSQiNKYQILKDAMKSCLEKCLKP 389
Cdd:pfam01661  12 GGVAGAIHRAAGPELLEECRElKKGGCPTGEAVVTPGGNLPAKYVIHTVgptwrhGGSH-GEEELLESCYRNALALAEEL 90

                          90       100
                  ....*....|....*....|....*.
gi 2228568364 390 DINSISFPALGTGLMDLKKSTAAQIM 415
Cdd:pfam01661  91 GIKSIAFPAISTGIYGFPWEEAARIA 116
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 290-415 5.20e-12

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: 63.86  E-value: 5.20e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364  290 LQIVQGCIEMQTTDVIVNSGyMQDFKSGR-VAQSILRQAGVEMEKE-LDKVN-LSTDYQEVWVTKGFKLSCQYVFHV--- 363
Cdd:smart00506   2 LKVVKGDITKPRADAIVNAA-NSDGAHGGgVAGAIARAAGKALSKEeVRKLAgGECPVGTAVVTEGGNLPAKYVIHAvgp 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2228568364  364 -AWHSQINKYQILKDAMKSCLEKCLKPDINSISFPALGTGLMDLKKSTAAQIM 415
Cdd:smart00506  81 rASGHSKEGFELLENAYRNCLELAIELGITSVALPLIGTGIYGVPKDRSAQAL 133
 
Name Accession Description Interval E-value
Macro_Af1521_BAL-like cd02907
macrodomain, Af1521-like family; Macrodomains are found in a variety of proteins with diverse ...
 83-243 4.67e-75

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: 241.24  E-value: 4.67e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364  83 GIELSVWKDDLTRHVVDAVVNAANENLLHGSGLAGSLVKTGGFEIQEESKRIIANVGKISVGGIAITGAGRLPCHLIIHA 162
Cdd:cd02907     1 GIKVSVYKGDITKEKVDAIVNAANERLKHGGGVAGAISKAGGPEIQEECDKYIKKNGKLRVGEVVVTSAGKLPCKYVIHA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 163 VGPRWTVTNSQTAIELLKFAIRNILDYVTKYdlRIKTVAIPALSSGIFQFPLDLCTSIILETIRlYFQDKQMFGNLREIH 242
Cdd:cd02907    81 VGPRWSGGSKEECEDLLYKAVLNSLEEAEEL--KATSIAIPAISSGIFGFPLDLCAEAIVEAIK-DFSESNSSSSLKEIR 157


                  .
gi 2228568364 243 L 243
Cdd:cd02907   158 L 158
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 285-455 3.44e-49

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: 171.28  E-value: 3.44e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 285 GRGLTLQIVQGCIEMQTTDVIVNSGYMQDFKSGRVAQSILRQAGVEMEKELDKVNLSTDYQEVWVTKGFKLSCQYVFHVA 364
Cdd:cd02903     5 IGGITVQLVKGDITKEKTDVIVNSVSSDLLLKGGVSKAILKAAGPELQDECANQGKQPASGDVIVTSGGNLPCKYVYHVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 365 W-HSQINKYQILKDAMKSCLEKCLKPDINSISFPALGTGLMDLKKSTAAQIMFEEVFAFAKEHKEKTL-TVKIVIFPvdV 442
Cdd:cd02903    85 LpHYNPGNEKTLKDIVRKCLEKAENYKMSSISFPAIGTGNLGFPKDVVAEIMIDEVLKFSSKNPSSSLkEVRFVIFP--P 162

                         170
                  ....*....|...
gi 2228568364 443 ETYKIFYAEMTKR 455
Cdd:cd02903   163 ETLQAFSDELAKR 175
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 86-257 2.30e-41

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: 149.17  E-value: 2.30e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364  86 LSVWKDDLTRHVVDAVVNAANENLLHGSGLAGSLVKTGGFEIQEESKRIIANvGKISVGGIAITGAGRLPCHLIIHAVGP 165
Cdd:COG2110     1 IEIVQGDITELDVDAIVNAANSSLLGGGGVAGAIHRAAGPELLEECRRLCKQ-GGCPTGEAVITPAGNLPAKYVIHTVGP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 166 RWtVTNSQTAIELLKFAIRNILDYVTKYDlrIKTVAIPALSSGIFQFPLDLCTSIILETIRLYFQDkqmFGNLREIHLVS 245
Cdd:COG2110    80 VW-RGGGPSEEELLASCYRNSLELAEELG--IRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFLEE---HPSLEEVRFVL 153

                         170
                  ....*....|..
gi 2228568364 246 NEDPTVASFKSA 257
Cdd:COG2110   154 FDEEDYEAYRRA 165
PRK00431 PRK00431
ADP-ribose-binding protein;
83-264 6.39e-41

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 148.07  E-value: 6.39e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364  83 GIELSVWKDDLTRHVVDAVVNAANENLLHGSGLAGSLVKTGGFEIQEESKRIIANVGKISVGGIAITGAGRLPCHLIIHA 162
Cdd:PRK00431    2 GMRIEVVQGDITELEVDAIVNAANSSLLGGGGVDGAIHRAAGPEILEECRELRQQQGPCPTGEAVITSAGRLPAKYVIHT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 163 VGPRWTVTNSQTAiELLKFAIRNILDYVTkyDLRIKTVAIPALSSGIFQFPLDLCTSIILETIRLYFQDKqmfGNLREIH 242
Cdd:PRK00431   82 VGPVWRGGEDNEA-ELLASAYRNSLRLAA--ELGLRSIAFPAISTGVYGYPLEDAARIAVKTVREFLTRH---KSPEEVY 155

                         170       180
                  ....*....|....*....|..
gi 2228568364 243 LVSNEDPTVASFKSASESILGR 264
Cdd:PRK00431  156 FVCYDEEAYRLYERLLTQQGDE 177
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 673-792 1.50e-40

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: 144.77  E-value: 1.50e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 673 RLFQQVPHQFCNTVCRVGFHRMYSTSYNPVYGAGIYFTKSLKNLADKVKKTSSTDKLIYVFEAEVLTGSFCQGNSSNIIP 752
Cdd:cd01439     1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKADGLKEMFLARVLTGDYTQGHPGYRRP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2228568364 753 P-PLSPGALDVNDSVVDNVSSPETIVVFNGMQAMPLYLWTC 792
Cdd:cd01439    81 PlKPSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 102-221 6.62e-40

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: 142.70  E-value: 6.62e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 102 VNAANENLLHGSGLAGSLVKTGGFEIQEESKRIIAnvGKISVGGIAITGAGRLPCHLIIHAVGPRWTVTNSQTAIELLKF 181
Cdd:pfam01661   1 VNAANSRLLGGGGVAGAIHRAAGPELLEECRELKK--GGCPTGEAVVTPGGNLPAKYVIHTVGPTWRHGGSHGEEELLES 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2228568364 182 AIRNILDYVTKYDlrIKTVAIPALSSGIFQFPLDLCTSII 221
Cdd:pfam01661  79 CYRNALALAEELG--IKSIAFPAISTGIYGFPWEEAARIA 116
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 85-221 5.44e-32

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: 120.87  E-value: 5.44e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364   85 ELSVWKDDLTRHVVDAVVNAANENLLHGSGLAGSLVKTGGFEIQEESKRiIANVGKISVGGIAITGAGRLPCHLIIHAVG 164
Cdd:smart00506   1 ILKVVKGDITKPRADAIVNAANSDGAHGGGVAGAIARAAGKALSKEEVR-KLAGGECPVGTAVVTEGGNLPAKYVIHAVG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2228568364  165 PRWtVTNSQTAIELLKFAIRNILDYVtkYDLRIKTVAIPALSSGIFQFPLDLCTSII 221
Cdd:smart00506  80 PRA-SGHSKEGFELLENAYRNCLELA--IELGITSVALPLIGTGIYGVPKDRSAQAL 133
Macro_OAADPr_deacetylase cd02908
macrodomain, O-acetyl-ADP-ribose (OAADPr) family; Macrodomains are found in a variety of ...
 86-226 3.21e-28

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: 111.45  E-value: 3.21e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364  86 LSVWKDDLTRHVVDAVVNAANENLLHGSGLAGSLVKTGGFEIQEESKRIIanvGKISVGGIAITGAGRLPCHLIIHAVGP 165
Cdd:cd02908     2 ISLWRGDITKLEVDAIVNAANSSLLGGGGVDGAIHRAAGPELLEECRKLG---GVCPTGEAKITPGYNLPAKYVIHTVGP 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2228568364 166 RWTVTNSQTAiELLKFAIRNILDYVTKYDlrIKTVAIPALSSGIFQFPLDLCTSIILETIR 226
Cdd:cd02908    79 IGEGGVEEEP-ELLASCYRSSLELALENG--LKSIAFPCISTGIYGYPNEEAAEIALNTVR 136
Macro_Ttha0132-like cd03330
Macrodomain, uncharacterized family similar to Thermus thermophilus hypothetical protein ...
 85-244 3.09e-26

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: 105.21  E-value: 3.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364  85 ELSVWKDDLTRHVVDAVVNAANENLLHGSGLAGSLVKTGGFEIQEESKRIianvGKISVGGIAITGAGRLPCHLIIHAVG 164
Cdd:cd03330     1 RLIVVQGDITEQDADAIVNAANRRLLMGSGVAGAIKRKGGEEIEREAMRK----GPIRVGEAVETGAGKLPAKYVIHAAV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 165 -PRWtvtnSQTAIELLKFAIRNILDYVTkyDLRIKTVAIPALSSGIFQFPLDLCTSIILETIRlyfqdKQMFGNLREIHL 243
Cdd:cd03330    77 mGMP----GRSSEESIRDATRNALAKAE--ELGLESVAFPAIGTGVGGFPVEEVARIMLEEIK-----KCDPPLLEEVRL 145


                  .
gi 2228568364 244 V 244
Cdd:cd03330   146 Y 146
Macro_H2A-like cd02904
macrodomain, macroH2A-like family; Macrodomains are found in a variety of proteins with ...
 78-244 4.74e-26

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: 105.86  E-value: 4.74e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364  78 RTLIPGIELSVWKDDLTRHVVDAVVNAANENLLHGSGLAGSLVKTGGFEIQEESKRIIANVGKISVGGIAITGAGRLPCH 157
Cdd:cd02904    12 KKLFLGQKLTVVQGDIASIKADAIVHPTNATFYLGGEVGSALEKAGGKEFVEEVKELRKSNGPLEVAGAAISPGHNLPAK 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 158 LIIHAVGPRWTVTNSQtaiELLKFAIRNILDYVTKYDLriKTVAIPALSSGIFQFPLDLCTSIILETIRLYFQDkQMFGN 237
Cdd:cd02904    92 FVIHCNSPSWGSDKCE---ELLEKTVKNCLALADEKKL--KSVAFPSIGSGRNGFPKQTAAQTILKAISNYFVS-VMSSS 165


                  ....*..
gi 2228568364 238 LREIHLV 244
Cdd:cd02904   166 LKQIYFV 172
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 290-454 5.57e-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: 102.18  E-value: 5.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 290 LQIVQGCIEMQTTDVIVN----SGYMqdfksGR-VAQSILRQAGVEMEKELDKVNLSTDYQ--EVWVTKGFKLSCQYVFH 362
Cdd:COG2110     1 IEIVQGDITELDVDAIVNaansSLLG-----GGgVAGAIHRAAGPELLEECRRLCKQGGCPtgEAVITPAGNLPAKYVIH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 363 VA---WHSQI-NKYQILKDAMKSCLEKCLKPDINSISFPALGTGLMDLKKSTAAQIMFEEVFAFAKEHKEKTlTVKIVIF 438
Cdd:COG2110    76 TVgpvWRGGGpSEEELLASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFLEEHPSLE-EVRFVLF 154

                         170
                  ....*....|....*.
gi 2228568364 439 pvDVETYKIFYAEMTK 454
Cdd:COG2110   155 --DEEDYEAYRRALAR 168
Macro_SF cd02749
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 303-418 1.17e-23

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: 96.70  E-value: 1.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 303 DVIVNSGYMQDFKSGRVAQSILRQAGVEMEKE--LDKVNLSTDYQEVWVTKGFKLSCQYVFHVAWHSQINK---YQILKD 377
Cdd:cd02749     1 DAIVNPANNDLYLGGGVAKAISKKAGGDLQEEceERKKNGYLKVGEVAVTKGGNLPARYIIHVVGPVASSKkktYEPLKK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2228568364 378 AMKSCLEKCLKPDINSISFPALGTGLMDLKKSTAAQIMFEE 418
Cdd:cd02749    81 CVKNCLSLADEKGLKSVAFPAIGTGIAGFPPEEAARIMLEA 121
Macro_X_Nsp3-like cd21557
X-domain (or Mac1 domain) of viral non-structural protein 3 and related macrodomains; The ...
 99-215 5.58e-23

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: 94.93  E-value: 5.58e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364  99 DAVVNAANENLLHGSGLAGSL-VKTGGfEIQEESKRIIANvGKISVGGIAItgagrLPCHL----IIHAVGPRwtvTNSQ 173
Cdd:cd21557     2 DVVVNAANENLKHGGGVAGAIyKATGG-AFQKESDYIKKN-GPLKVGTAVL-----LPGHGlaknIIHVVGPR---KRKG 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2228568364 174 TAIELLKFAIRNILDYvtkydlrIKTVAIPALSSGIFQFPLD 215
Cdd:cd21557    72 QDDQLLAAAYKAVNKE-------YGSVLTPLLSAGIFGVPPE 106
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 81-257 1.54e-21

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: 92.70  E-value: 1.54e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364  81 IPGIELSVWKDDLTRHVVDAVVNAANENLLHGSGLAGSLVKTGGFEIQEEskriIANVGK-ISVGGIAITGAGRLPCHLI 159
Cdd:cd02903     5 IGGITVQLVKGDITKEKTDVIVNSVSSDLLLKGGVSKAILKAAGPELQDE----CANQGKqPASGDVIVTSGGNLPCKYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 160 IHAVGPRWtvtnSQTAIELLKFAIRNILDYVTKYDLriKTVAIPALSSGIFQFPLDLCTSIILETIRLYFQDKQMfGNLR 239
Cdd:cd02903    81 YHVVLPHY----NPGNEKTLKDIVRKCLEKAENYKM--SSISFPAIGTGNLGFPKDVVAEIMIDEVLKFSSKNPS-SSLK 153

                         170
                  ....*....|....*...
gi 2228568364 240 EIHLVSNEDPTVASFKSA 257
Cdd:cd02903   154 EVRFVIFPPETLQAFSDE 171
Macro_Af1521_BAL-like cd02907
macrodomain, Af1521-like family; Macrodomains are found in a variety of proteins with diverse ...
 287-432 2.34e-21

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: 91.40  E-value: 2.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 287 GLTLQIVQGCIEMQTTDVIVNS--GYMQdfKSGRVAQSILRQAGVEMEKELDKV-----NLSTDyqEVWVTKGFKLSCQY 359
Cdd:cd02907     1 GIKVSVYKGDITKEKVDAIVNAanERLK--HGGGVAGAISKAGGPEIQEECDKYikkngKLRVG--EVVVTSAGKLPCKY 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2228568364 360 VFHVA---WH--SQINKYQILKDAMKSCLEKCLKPDINSISFPALGTGLMDLKKSTAAQIMFEEVFAFAKEHKEKTLT 432
Cdd:cd02907    77 VIHAVgprWSggSKEECEDLLYKAVLNSLEEAEELKATSIAIPAISSGIFGFPLDLCAEAIVEAIKDFSESNSSSSLK 154
Macro_SF cd02749
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 99-224 1.51e-20

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: 87.84  E-value: 1.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364  99 DAVVNAANENLLHGSGLAGSLVKTGGFEIQEESKRIIANvGKISVGGIAITGAGRLPCHLIIHAVGPRWtvTNSQTAIEL 178
Cdd:cd02749     1 DAIVNPANNDLYLGGGVAKAISKKAGGDLQEECEERKKN-GYLKVGEVAVTKGGNLPARYIIHVVGPVA--SSKKKTYEP 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2228568364 179 LKFAIRNILDYVTKYDlrIKTVAIPALSSGIFQFPLDLCTSIILET 224
Cdd:cd02749    78 LKKCVKNCLSLADEKG--LKSVAFPAIGTGIAGFPPEEAARIMLEA 121
PRK00431 PRK00431
ADP-ribose-binding protein;
286-458 1.61e-20

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 89.52  E-value: 1.61e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 286 RGLTLQIVQGCIEMQTTDVIVN----SGYMqdfkSGRVAQSILRQAGVEMEKELDKVNLSTDY---QEVWVTKGFKLSCQ 358
Cdd:PRK00431    1 MGMRIEVVQGDITELEVDAIVNaansSLLG----GGGVDGAIHRAAGPEILEECRELRQQQGPcptGEAVITSAGRLPAK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 359 YVFHVA---WH-SQINKYQILKDAMKSCLEKCLKPDINSISFPALGTGLMDLKKSTAAQIMFEEVFAFAKEHKektlTVK 434
Cdd:PRK00431   77 YVIHTVgpvWRgGEDNEAELLASAYRNSLRLAAELGLRSIAFPAISTGVYGYPLEDAARIAVKTVREFLTRHK----SPE 152

                         170       180
                  ....*....|....*....|....*
gi 2228568364 435 IVIF-PVDVETYKIFYAEMTKRSNE 458
Cdd:PRK00431  153 EVYFvCYDEEAYRLYERLLTQQGDE 177
Macro_GDAP2-like cd02905
macrodomain, GDAP2-like family; Macrodomains are found in a variety of proteins with diverse ...
 86-230 3.62e-19

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: 85.36  E-value: 3.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364  86 LSVWKDDLTRHVVDAVVNAANENLLHGSGLAGSLVKTGGFEIQEEskriIANVGKISVGGIAITGAGRLPCHLIIHAVGP 165
Cdd:cd02905     3 IVLWDGDLTLLNVDAIVNSTNESLTDKSPISDRLFLAAGPELREE----LAKLGGCRTGEAKLTKGYNLPARYVIHTVGP 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2228568364 166 RWTVtNSQTAIE-LLKFAIRNILDYVTkyDLRIKTVAIPALSSGIFQFPLDLCTSIILETIRLYFQ 230
Cdd:cd02905    79 RYNE-KYRTAAEsALYSCYRNVLQLAK--EHKLRSVAFPVIHSERRGYPLEDGAHIALRTVRRFLE 141
PRK04143 PRK04143
protein-ADP-ribose hydrolase;
86-229 1.50e-17

protein-ADP-ribose hydrolase;


Pssm-ID: 235225  Cd Length: 264  Bit Score: 83.49  E-value: 1.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364  86 LSVWKDDLTRHVVDAVVNAANENLL------HG------SGLAGSLVKTGGFEIQEESKRIIAnvgkisVGGIAITGAGR 153
Cdd:PRK04143   85 IFLWQGDITRLKVDAIVNAANSRLLgcfqpnHDcidnaiHTFAGVQLRLDCAEIMTEQGRKEA------TGQAKITRAYN 158

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2228568364 154 LPCHLIIHAVGPRWTVTN-SQTAIELLKFAIRNILDYVTKYdlRIKTVAIPALSSGIFQFPLDLCTSIILETIRLYF 229
Cdd:PRK04143  159 LPAKYVIHTVGPIIRKQPvSPIRADLLASCYRSCLKLAEKA--GLKSIAFCCISTGVFGFPKEEAAEIAIKTVLSWL 233
Macro_OAADPr_deacetylase cd02908
macrodomain, O-acetyl-ADP-ribose (OAADPr) family; Macrodomains are found in a variety of ...
 292-452 7.39e-16

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: 76.01  E-value: 7.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 292 IVQGCIEMQTTDVIVNS-------GymqdfksGRVAQSILRQAGVEMEKELDKVNLSTDYQEVWVTKGFKLSCQYVFHV- 363
Cdd:cd02908     4 LWRGDITKLEVDAIVNAanssllgG-------GGVDGAIHRAAGPELLEECRKLGGVCPTGEAKITPGYNLPAKYVIHTv 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 364 --AWHSQINK-YQILKDAMKSCLEKCLKPDINSISFPALGTGLMDLKKSTAAQIMFEEVfafaKEHKEKTLTVKIVIFPV 440
Cdd:cd02908    77 gpIGEGGVEEePELLASCYRSSLELALENGLKSIAFPCISTGIYGYPNEEAAEIALNTV----REWLEEHDKIDRIIFVV 152

                         170
                  ....*....|...
gi 2228568364 441 -DVETYKIFYAEM 452
Cdd:cd02908   153 fLDEDYKIYEELL 165
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 317-415 4.71e-14

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: 69.13  E-value: 4.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 317 GRVAQSILRQAGVEMEKELDK-VNLSTDYQEVWVTKGFKLSCQYVFHVA------WHSQiNKYQILKDAMKSCLEKCLKP 389
Cdd:pfam01661  12 GGVAGAIHRAAGPELLEECRElKKGGCPTGEAVVTPGGNLPAKYVIHTVgptwrhGGSH-GEEELLESCYRNALALAEEL 90

                          90       100
                  ....*....|....*....|....*.
gi 2228568364 390 DINSISFPALGTGLMDLKKSTAAQIM 415
Cdd:pfam01661  91 GIKSIAFPAISTGIYGFPWEEAARIA 116
Macro_Ttha0132-like cd03330
Macrodomain, uncharacterized family similar to Thermus thermophilus hypothetical protein ...
 290-425 3.76e-13

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: 67.46  E-value: 3.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 290 LQIVQGCIEMQTTDVIVNSGYMQDFKSGRVAQSILRQAGVEMEKELDKVNLsTDYQEVWVTKGFKLSCQYVFHVA----- 364
Cdd:cd03330     2 LIVVQGDITEQDADAIVNAANRRLLMGSGVAGAIKRKGGEEIEREAMRKGP-IRVGEAVETGAGKLPAKYVIHAAvmgmp 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2228568364 365 WHSQInkyQILKDAMKSCLEKCLKPDINSISFPALGTGLMDLKKSTAAQIMFEEVFAFAKE 425
Cdd:cd03330    81 GRSSE---ESIRDATRNALAKAEELGLESVAFPAIGTGVGGFPVEEVARIMLEEIKKCDPP 138
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 290-415 5.20e-12

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: 63.86  E-value: 5.20e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364  290 LQIVQGCIEMQTTDVIVNSGyMQDFKSGR-VAQSILRQAGVEMEKE-LDKVN-LSTDYQEVWVTKGFKLSCQYVFHV--- 363
Cdd:smart00506   2 LKVVKGDITKPRADAIVNAA-NSDGAHGGgVAGAIARAAGKALSKEeVRKLAgGECPVGTAVVTEGGNLPAKYVIHAvgp 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2228568364  364 -AWHSQINKYQILKDAMKSCLEKCLKPDINSISFPALGTGLMDLKKSTAAQIM 415
Cdd:smart00506  81 rASGHSKEGFELLENAYRNCLELAIELGITSVALPLIGTGIYGVPKDRSAQAL 133
Macro_H2A-like cd02904
macrodomain, macroH2A-like family; Macrodomains are found in a variety of proteins with ...
 278-454 9.16e-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: 61.95  E-value: 9.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 278 STMTLRIGRGLTLqiVQGCIEMQTTDVIV---NSGYmqDFKsGRVAQSILRQAGVEME---KELDKVNLSTDYQEVWVTK 351
Cdd:cd02904    10 SEKKLFLGQKLTV--VQGDIASIKADAIVhptNATF--YLG-GEVGSALEKAGGKEFVeevKELRKSNGPLEVAGAAISP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 352 GFKLSCQYVFHV---AWHSQiNKYQILKDAMKSCLEKCLKPDINSISFPALGTGLMDLKKSTAAQIMFEEVFAFAKEHKE 428
Cdd:cd02904    85 GHNLPAKFVIHCnspSWGSD-KCEELLEKTVKNCLALADEKKLKSVAFPSIGSGRNGFPKQTAAQTILKAISNYFVSVMS 163

                         170       180
                  ....*....|....*....|....*..
gi 2228568364 429 KTL-TVKIVIFpvDVETYKIFYAEMTK 454
Cdd:cd02904   164 SSLkQIYFVLF--DMESIGIYTSELAK 188
PRK04143 PRK04143
protein-ADP-ribose hydrolase;
349-446 5.54e-06

protein-ADP-ribose hydrolase;


Pssm-ID: 235225  Cd Length: 264  Bit Score: 48.82  E-value: 5.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 349 VTKGFKLSCQYVFHVAwHSQINKYQI-------LKDAMKSCLEKCLKPDINSISFPALGTGLMDLKKSTAAQIMFEEVFA 421
Cdd:PRK04143  153 ITRAYNLPAKYVIHTV-GPIIRKQPVspiradlLASCYRSCLKLAEKAGLKSIAFCCISTGVFGFPKEEAAEIAIKTVLS 231

                          90       100
                  ....*....|....*....|....*
gi 2228568364 422 FAKEHKEKTLTVKIVIFPVDVETYK 446
Cdd:PRK04143  232 WLKENPSKLKVVFNVFTDEDLELYQ 256
Macro_GDAP2-like cd02905
macrodomain, GDAP2-like family; Macrodomains are found in a variety of proteins with diverse ...
 302-446 1.25e-05

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: 46.46  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568364 302 TDVIVNSGYMQDFKSGRVAQSILRQAGVEMEKELDKvNLSTDYQEVWVTKGFKLSCQYVFHV---AWHSqinKYQI---- 374
Cdd:cd02905    15 VDAIVNSTNESLTDKSPISDRLFLAAGPELREELAK-LGGCRTGEAKLTKGYNLPARYVIHTvgpRYNE---KYRTaaes 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2228568364 375 -LKDAMKSCLEKCLKPDINSISFPALGTGLMDLKKSTAAQIMFEEVFAFAKEHKEKTLTVKIVIFPVDVETYK 446
Cdd:cd02905    91 aLYSCYRNVLQLAKEHKLRSVAFPVIHSERRGYPLEDGAHIALRTVRRFLEKHGSSFEAVVFVVTEEEMETYE 163
 
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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