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Conserved domains on  [gi|1046852755|ref|XP_017453484|]
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protein mono-ADP-ribosyltransferase PARP9 isoform X2 [Rattus norvegicus]

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 ...
 119-279 1.64e-73

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: 237.39  E-value: 1.64e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 119 GIELSVWKDDLTRHVVDAVVNAANEDLLHGGGLAGSLVKIGGSEIQEESKKWIATHGKIPVGGFAVTRAGKLPCYLIIHA 198
Cdd:cd02907     1 GIKVSVYKGDITKEKVDAIVNAANERLKHGGGVAGAISKAGGPEIQEECDKYIKKNGKLRVGEVVVTSAGKLPCKYVIHA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 199 VGPRWTVMDSQTAIGLLSVAITNILDYVTKWNtcIKTVAIPALSSGIFQFPLHLCTRIIVETIcLYFQDKQTVSNLREIH 278
Cdd:cd02907    81 VGPRWSGGSKEECEDLLYKAVLNSLEEAEELK--ATSIAIPAISSGIFGFPLDLCAEAIVEAI-KDFSESNSSSSLKEIR 157


                  .
gi 1046852755 279 L 279
Cdd:cd02907   158 L 158
Macro_SF super family cl00019
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 316-491 8.28e-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: 170.51  E-value: 8.28e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 316 VTLHIGqGLTLQIVQGCIELQTTDVIVNSGHLQDFKSGQVAQSILKRAGFEMEMELDKIKLSSDYQVVQVTKGFKLSCQY 395
Cdd:cd02903     1 YTMKIG-GITVQLVKGDITKEKTDVIVNSVSSDLLLKGGVSKAILKAAGPELQDECANQGKQPASGDVIVTSGGNLPCKY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 396 VFHVSW-HYSISKDQILKNAMKSCLERCLKRDINSISFPALGTGAINLEKSIAAKIMFEEIVAFAKEHKEKTL-TVKIVI 473
Cdd:cd02903    80 VYHVVLpHYNPGNEKTLKDIVRKCLEKAENYKMSSISFPAIGTGNLGFPKDVVAEIMIDEVLKFSSKNPSSSLkEVRFVI 159

                         170
                  ....*....|....*...
gi 1046852755 474 FPvdVETYKVFCAEMTKR 491
Cdd:cd02903   160 FP--PETLQAFSDELAKR 175
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 709-828 6.36e-42

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: 149.01  E-value: 6.36e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 709 RLFQQVPHQFCNAVCRVGFHRLYSTHNDPVYGAGIYFTKSLKKLADKARKTSSTDRLIYVFEAEVLTGSFCQGNFSNIIP 788
Cdd:cd01439     1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKADGLKEMFLARVLTGDYTQGHPGYRRP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1046852755 789 P-PLSPGALDVHDSVVDSVSNPETFVIFSGVQAMPRYLWTC 828
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 ...
 119-279 1.64e-73

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: 237.39  E-value: 1.64e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 119 GIELSVWKDDLTRHVVDAVVNAANEDLLHGGGLAGSLVKIGGSEIQEESKKWIATHGKIPVGGFAVTRAGKLPCYLIIHA 198
Cdd:cd02907     1 GIKVSVYKGDITKEKVDAIVNAANERLKHGGGVAGAISKAGGPEIQEECDKYIKKNGKLRVGEVVVTSAGKLPCKYVIHA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 199 VGPRWTVMDSQTAIGLLSVAITNILDYVTKWNtcIKTVAIPALSSGIFQFPLHLCTRIIVETIcLYFQDKQTVSNLREIH 278
Cdd:cd02907    81 VGPRWSGGSKEECEDLLYKAVLNSLEEAEELK--ATSIAIPAISSGIFGFPLDLCAEAIVEAI-KDFSESNSSSSLKEIR 157


                  .
gi 1046852755 279 L 279
Cdd:cd02907   158 L 158
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 316-491 8.28e-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: 170.51  E-value: 8.28e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 316 VTLHIGqGLTLQIVQGCIELQTTDVIVNSGHLQDFKSGQVAQSILKRAGFEMEMELDKIKLSSDYQVVQVTKGFKLSCQY 395
Cdd:cd02903     1 YTMKIG-GITVQLVKGDITKEKTDVIVNSVSSDLLLKGGVSKAILKAAGPELQDECANQGKQPASGDVIVTSGGNLPCKY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 396 VFHVSW-HYSISKDQILKNAMKSCLERCLKRDINSISFPALGTGAINLEKSIAAKIMFEEIVAFAKEHKEKTL-TVKIVI 473
Cdd:cd02903    80 VYHVVLpHYNPGNEKTLKDIVRKCLEKAENYKMSSISFPAIGTGNLGFPKDVVAEIMIDEVLKFSSKNPSSSLkEVRFVI 159

                         170
                  ....*....|....*...
gi 1046852755 474 FPvdVETYKVFCAEMTKR 491
Cdd:cd02903   160 FP--PETLQAFSDELAKR 175
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 709-828 6.36e-42

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: 149.01  E-value: 6.36e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 709 RLFQQVPHQFCNAVCRVGFHRLYSTHNDPVYGAGIYFTKSLKKLADKARKTSSTDRLIYVFEAEVLTGSFCQGNFSNIIP 788
Cdd:cd01439     1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKADGLKEMFLARVLTGDYTQGHPGYRRP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1046852755 789 P-PLSPGALDVHDSVVDSVSNPETFVIFSGVQAMPRYLWTC 828
Cdd:cd01439    81 PlKPSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
PRK00431 PRK00431
ADP-ribose-binding protein;
119-280 1.77e-41

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 149.61  E-value: 1.77e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 119 GIELSVWKDDLTRHVVDAVVNAANEDLLHGGGLAGSLVKIGGSEIQEESKKWIATHGKIPVGGFAVTRAGKLPCYLIIHA 198
Cdd:PRK00431    2 GMRIEVVQGDITELEVDAIVNAANSSLLGGGGVDGAIHRAAGPEILEECRELRQQQGPCPTGEAVITSAGRLPAKYVIHT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 199 VGPRWTVMDSQTAiGLLSVAITNILDYVTKwnTCIKTVAIPALSSGIFQFPLHLCTRIIVETIcLYFQdkQTVSNLREIH 278
Cdd:PRK00431   82 VGPVWRGGEDNEA-ELLASAYRNSLRLAAE--LGLRSIAFPAISTGVYGYPLEDAARIAVKTV-REFL--TRHKSPEEVY 155


                  ..
gi 1046852755 279 LV 280
Cdd:PRK00431  156 FV 157
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 122-280 1.09e-38

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: 141.47  E-value: 1.09e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 122 LSVWKDDLTRHVVDAVVNAANEDLLHGGGLAGSLVKIGGSEIQEESKKWIAtHGKIPVGGFAVTRAGKLPCYLIIHAVGP 201
Cdd:COG2110     1 IEIVQGDITELDVDAIVNAANSSLLGGGGVAGAIHRAAGPELLEECRRLCK-QGGCPTGEAVITPAGNLPAKYVIHTVGP 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046852755 202 RWtVMDSQTAIGLLSVAITNILDYVTKWNtcIKTVAIPALSSGIFQFPLHLCTRIIVETICLYFQDKQTvsnLREIHLV 280
Cdd:COG2110    80 VW-RGGGPSEEELLASCYRNSLELAEELG--IRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFLEEHPS---LEEVRFV 152
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 138-257 8.63e-35

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: 128.45  E-value: 8.63e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 138 VNAANEDLLHGGGLAGSLVKIGGSEIQEESKKWIAthGKIPVGGFAVTRAGKLPCYLIIHAVGPRWTVMDSQTAIGLLSV 217
Cdd:pfam01661   1 VNAANSRLLGGGGVAGAIHRAAGPELLEECRELKK--GGCPTGEAVVTPGGNLPAKYVIHTVGPTWRHGGSHGEEELLES 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1046852755 218 AITNILDYVTKWNtcIKTVAIPALSSGIFQFPLHLCTRII 257
Cdd:pfam01661  79 CYRNALALAEELG--IKSIAFPAISTGIYGFPWEEAARIA 116
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 121-257 3.33e-29

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: 113.17  E-value: 3.33e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755  121 ELSVWKDDLTRHVVDAVVNAANEDLLHGGGLAGSLVKIGGSEIQEESkKWIATHGKIPVGGFAVTRAGKLPCYLIIHAVG 200
Cdd:smart00506   1 ILKVVKGDITKPRADAIVNAANSDGAHGGGVAGAIARAAGKALSKEE-VRKLAGGECPVGTAVVTEGGNLPAKYVIHAVG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1046852755  201 PRWtVMDSQTAIGLLSVAITNILDYVTKWNtcIKTVAIPALSSGIFQFPLHLCTRII 257
Cdd:smart00506  80 PRA-SGHSKEGFELLENAYRNCLELAIELG--ITSVALPLIGTGIYGVPKDRSAQAL 133
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 326-490 4.21e-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: 102.56  E-value: 4.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 326 LQIVQGCIELQTTDVIVNSGHLQDFKSGQVAQSILKRAGFEMEMELDKIKLSSDYQV--VQVTKGFKLSCQYVFHV---S 400
Cdd:COG2110     1 IEIVQGDITELDVDAIVNAANSSLLGGGGVAGAIHRAAGPELLEECRRLCKQGGCPTgeAVITPAGNLPAKYVIHTvgpV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 401 WHYSI-SKDQILKNAMKSCLERCLKRDINSISFPALGTGAINLEKSIAAKIMFEEIVAFAKEHKEKTlTVKIVIFpvDVE 479
Cdd:COG2110    81 WRGGGpSEEELLASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFLEEHPSLE-EVRFVLF--DEE 157

                         170
                  ....*....|.
gi 1046852755 480 TYKVFCAEMTK 490
Cdd:COG2110   158 DYEAYRRALAR 168
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 353-451 1.98e-13

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: 67.59  E-value: 1.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 353 GQVAQSILKRAGFEMEMELDKIKLSS-DYQVVQVTKGFKLSCQYVFHV-----SWHYSISKDQILKNAMKSCLERCLKRD 426
Cdd:pfam01661  12 GGVAGAIHRAAGPELLEECRELKKGGcPTGEAVVTPGGNLPAKYVIHTvgptwRHGGSHGEEELLESCYRNALALAEELG 91

                          90       100
                  ....*....|....*....|....*
gi 1046852755 427 INSISFPALGTGAINLEKSIAAKIM 451
Cdd:pfam01661  92 IKSIAFPAISTGIYGFPWEEAARIA 116
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 326-451 9.63e-13

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: 66.17  E-value: 9.63e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755  326 LQIVQGCIELQTTDVIVNSGHLQDFKSGQVAQSILKRAGfEMEMELDKIKLSSDYQVVQ---VTKGFKLSCQYVFHV--- 399
Cdd:smart00506   2 LKVVKGDITKPRADAIVNAANSDGAHGGGVAGAIARAAG-KALSKEEVRKLAGGECPVGtavVTEGGNLPAKYVIHAvgp 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1046852755  400 SW-HYSISKDQILKNAMKSCLERCLKRDINSISFPALGTGAINLEKSIAAKIM 451
Cdd:smart00506  81 RAsGHSKEGFELLENAYRNCLELAIELGITSVALPLIGTGIYGVPKDRSAQAL 133
PRK04143 PRK04143
protein-ADP-ribose hydrolase;
385-482 1.31e-04

protein-ADP-ribose hydrolase;


Pssm-ID: 235225  Cd Length: 264  Bit Score: 44.59  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 385 VTKGFKLSCQYVFH----------VSwhySISKDQiLKNAMKSCLERCLKRDINSISFPALGTGAINLEKSIAAKIMFEE 454
Cdd:PRK04143  153 ITRAYNLPAKYVIHtvgpiirkqpVS---PIRADL-LASCYRSCLKLAEKAGLKSIAFCCISTGVFGFPKEEAAEIAIKT 228

                          90       100
                  ....*....|....*....|....*...
gi 1046852755 455 IVAFAKEHKEKTLTVKIVIFPVDVETYK 482
Cdd:PRK04143  229 VLSWLKENPSKLKVVFNVFTDEDLELYQ 256
 
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 ...
 119-279 1.64e-73

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: 237.39  E-value: 1.64e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 119 GIELSVWKDDLTRHVVDAVVNAANEDLLHGGGLAGSLVKIGGSEIQEESKKWIATHGKIPVGGFAVTRAGKLPCYLIIHA 198
Cdd:cd02907     1 GIKVSVYKGDITKEKVDAIVNAANERLKHGGGVAGAISKAGGPEIQEECDKYIKKNGKLRVGEVVVTSAGKLPCKYVIHA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 199 VGPRWTVMDSQTAIGLLSVAITNILDYVTKWNtcIKTVAIPALSSGIFQFPLHLCTRIIVETIcLYFQDKQTVSNLREIH 278
Cdd:cd02907    81 VGPRWSGGSKEECEDLLYKAVLNSLEEAEELK--ATSIAIPAISSGIFGFPLDLCAEAIVEAI-KDFSESNSSSSLKEIR 157


                  .
gi 1046852755 279 L 279
Cdd:cd02907   158 L 158
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 316-491 8.28e-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: 170.51  E-value: 8.28e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 316 VTLHIGqGLTLQIVQGCIELQTTDVIVNSGHLQDFKSGQVAQSILKRAGFEMEMELDKIKLSSDYQVVQVTKGFKLSCQY 395
Cdd:cd02903     1 YTMKIG-GITVQLVKGDITKEKTDVIVNSVSSDLLLKGGVSKAILKAAGPELQDECANQGKQPASGDVIVTSGGNLPCKY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 396 VFHVSW-HYSISKDQILKNAMKSCLERCLKRDINSISFPALGTGAINLEKSIAAKIMFEEIVAFAKEHKEKTL-TVKIVI 473
Cdd:cd02903    80 VYHVVLpHYNPGNEKTLKDIVRKCLEKAENYKMSSISFPAIGTGNLGFPKDVVAEIMIDEVLKFSSKNPSSSLkEVRFVI 159

                         170
                  ....*....|....*...
gi 1046852755 474 FPvdVETYKVFCAEMTKR 491
Cdd:cd02903   160 FP--PETLQAFSDELAKR 175
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 709-828 6.36e-42

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: 149.01  E-value: 6.36e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 709 RLFQQVPHQFCNAVCRVGFHRLYSTHNDPVYGAGIYFTKSLKKLADKARKTSSTDRLIYVFEAEVLTGSFCQGNFSNIIP 788
Cdd:cd01439     1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKADGLKEMFLARVLTGDYTQGHPGYRRP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1046852755 789 P-PLSPGALDVHDSVVDSVSNPETFVIFSGVQAMPRYLWTC 828
Cdd:cd01439    81 PlKPSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
PRK00431 PRK00431
ADP-ribose-binding protein;
119-280 1.77e-41

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 149.61  E-value: 1.77e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 119 GIELSVWKDDLTRHVVDAVVNAANEDLLHGGGLAGSLVKIGGSEIQEESKKWIATHGKIPVGGFAVTRAGKLPCYLIIHA 198
Cdd:PRK00431    2 GMRIEVVQGDITELEVDAIVNAANSSLLGGGGVDGAIHRAAGPEILEECRELRQQQGPCPTGEAVITSAGRLPAKYVIHT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 199 VGPRWTVMDSQTAiGLLSVAITNILDYVTKwnTCIKTVAIPALSSGIFQFPLHLCTRIIVETIcLYFQdkQTVSNLREIH 278
Cdd:PRK00431   82 VGPVWRGGEDNEA-ELLASAYRNSLRLAAE--LGLRSIAFPAISTGVYGYPLEDAARIAVKTV-REFL--TRHKSPEEVY 155


                  ..
gi 1046852755 279 LV 280
Cdd:PRK00431  156 FV 157
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 122-280 1.09e-38

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: 141.47  E-value: 1.09e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 122 LSVWKDDLTRHVVDAVVNAANEDLLHGGGLAGSLVKIGGSEIQEESKKWIAtHGKIPVGGFAVTRAGKLPCYLIIHAVGP 201
Cdd:COG2110     1 IEIVQGDITELDVDAIVNAANSSLLGGGGVAGAIHRAAGPELLEECRRLCK-QGGCPTGEAVITPAGNLPAKYVIHTVGP 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046852755 202 RWtVMDSQTAIGLLSVAITNILDYVTKWNtcIKTVAIPALSSGIFQFPLHLCTRIIVETICLYFQDKQTvsnLREIHLV 280
Cdd:COG2110    80 VW-RGGGPSEEELLASCYRNSLELAEELG--IRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFLEEHPS---LEEVRFV 152
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 138-257 8.63e-35

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: 128.45  E-value: 8.63e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 138 VNAANEDLLHGGGLAGSLVKIGGSEIQEESKKWIAthGKIPVGGFAVTRAGKLPCYLIIHAVGPRWTVMDSQTAIGLLSV 217
Cdd:pfam01661   1 VNAANSRLLGGGGVAGAIHRAAGPELLEECRELKK--GGCPTGEAVVTPGGNLPAKYVIHTVGPTWRHGGSHGEEELLES 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1046852755 218 AITNILDYVTKWNtcIKTVAIPALSSGIFQFPLHLCTRII 257
Cdd:pfam01661  79 CYRNALALAEELG--IKSIAFPAISTGIYGFPWEEAARIA 116
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 121-257 3.33e-29

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: 113.17  E-value: 3.33e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755  121 ELSVWKDDLTRHVVDAVVNAANEDLLHGGGLAGSLVKIGGSEIQEESkKWIATHGKIPVGGFAVTRAGKLPCYLIIHAVG 200
Cdd:smart00506   1 ILKVVKGDITKPRADAIVNAANSDGAHGGGVAGAIARAAGKALSKEE-VRKLAGGECPVGTAVVTEGGNLPAKYVIHAVG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1046852755  201 PRWtVMDSQTAIGLLSVAITNILDYVTKWNtcIKTVAIPALSSGIFQFPLHLCTRII 257
Cdd:smart00506  80 PRA-SGHSKEGFELLENAYRNCLELAIELG--ITSVALPLIGTGIYGVPKDRSAQAL 133
Macro_OAADPr_deacetylase cd02908
macrodomain, O-acetyl-ADP-ribose (OAADPr) family; Macrodomains are found in a variety of ...
 122-280 9.19e-27

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: 107.21  E-value: 9.19e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 122 LSVWKDDLTRHVVDAVVNAANEDLLHGGGLAGSLVKIGGSEIQEESKKWiatHGKIPVGGFAVTRAGKLPCYLIIHAVGP 201
Cdd:cd02908     2 ISLWRGDITKLEVDAIVNAANSSLLGGGGVDGAIHRAAGPELLEECRKL---GGVCPTGEAKITPGYNLPAKYVIHTVGP 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046852755 202 RWTVMDSQTAIgLLSVAITNILDYVTKWNtcIKTVAIPALSSGIFQFPLHLCTRIIVETICLYFQDKQTVSnlrEIHLV 280
Cdd:cd02908    79 IGEGGVEEEPE-LLASCYRSSLELALENG--LKSIAFPCISTGIYGYPNEEAAEIALNTVREWLEEHDKID---RIIFV 151
Macro_H2A-like cd02904
macrodomain, macroH2A-like family; Macrodomains are found in a variety of proteins with ...
 119-280 1.20e-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: 107.78  E-value: 1.20e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 119 GIELSVWKDDLTRHVVDAVVNAANEDLLHGGGLAGSLVKIGGSEIQEESKKWIATHGKIPVGGFAVTRAGKLPCYLIIHA 198
Cdd:cd02904    17 GQKLTVVQGDIASIKADAIVHPTNATFYLGGEVGSALEKAGGKEFVEEVKELRKSNGPLEVAGAAISPGHNLPAKFVIHC 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 199 VGPRWTvmdSQTAIGLLSVAITNILDYVTKWNtcIKTVAIPALSSGIFQFPLHLCTRIIVETICLYFqDKQTVSNLREIH 278
Cdd:cd02904    97 NSPSWG---SDKCEELLEKTVKNCLALADEKK--LKSVAFPSIGSGRNGFPKQTAAQTILKAISNYF-VSVMSSSLKQIY 170


                  ..
gi 1046852755 279 LV 280
Cdd:cd02904   171 FV 172
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 326-490 4.21e-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: 102.56  E-value: 4.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 326 LQIVQGCIELQTTDVIVNSGHLQDFKSGQVAQSILKRAGFEMEMELDKIKLSSDYQV--VQVTKGFKLSCQYVFHV---S 400
Cdd:COG2110     1 IEIVQGDITELDVDAIVNAANSSLLGGGGVAGAIHRAAGPELLEECRRLCKQGGCPTgeAVITPAGNLPAKYVIHTvgpV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 401 WHYSI-SKDQILKNAMKSCLERCLKRDINSISFPALGTGAINLEKSIAAKIMFEEIVAFAKEHKEKTlTVKIVIFpvDVE 479
Cdd:COG2110    81 WRGGGpSEEELLASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFLEEHPSLE-EVRFVLF--DEE 157

                         170
                  ....*....|.
gi 1046852755 480 TYKVFCAEMTK 490
Cdd:COG2110   158 DYEAYRRALAR 168
Macro_X_Nsp3-like cd21557
X-domain (or Mac1 domain) of viral non-structural protein 3 and related macrodomains; The ...
 135-250 3.14e-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: 95.70  E-value: 3.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 135 DAVVNAANEDLLHGGGLAGSLVKIGGSEIQEESkKWIATHGKIPVGGfAVTRAGKLPCYLIIHAVGPRWTvmdSQTAIGL 214
Cdd:cd21557     2 DVVVNAANENLKHGGGVAGAIYKATGGAFQKES-DYIKKNGPLKVGT-AVLLPGHGLAKNIIHVVGPRKR---KGQDDQL 76

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1046852755 215 LSVAITNILDYvtkwntcIKTVAIPALSSGIFQFPL 250
Cdd:cd21557    77 LAAAYKAVNKE-------YGSVLTPLLSAGIFGVPP 105
Macro_Af1521_BAL-like cd02907
macrodomain, Af1521-like family; Macrodomains are found in a variety of proteins with diverse ...
 323-468 8.82e-23

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: 95.63  E-value: 8.82e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 323 GLTLQIVQGCIELQTTDVIVNS--GHLQdfKSGQVAQSILKRAGFEMEMELDKI-----KLSsDYQVVqVTKGFKLSCQY 395
Cdd:cd02907     1 GIKVSVYKGDITKEKVDAIVNAanERLK--HGGGVAGAISKAGGPEIQEECDKYikkngKLR-VGEVV-VTSAGKLPCKY 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046852755 396 VFH-VSWHYSISKDQI----LKNAMKSCLERCLKRDINSISFPALGTGAINLEKSIAAKIMFEEIVAFAKEHKEKTLT 468
Cdd:cd02907    77 VIHaVGPRWSGGSKEEcedlLYKAVLNSLEEAEELKATSIAIPAISSGIFGFPLDLCAEAIVEAIKDFSESNSSSSLK 154
Macro_Ttha0132-like cd03330
Macrodomain, uncharacterized family similar to Thermus thermophilus hypothetical protein ...
 121-261 8.18e-22

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: 92.50  E-value: 8.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 121 ELSVWKDDLTRHVVDAVVNAANEDLLHGGGLAGSLVKIGGSEIQEESKKwiatHGKIPVGGFAVTRAGKLPCYLIIHAvg 200
Cdd:cd03330     1 RLIVVQGDITEQDADAIVNAANRRLLMGSGVAGAIKRKGGEEIEREAMR----KGPIRVGEAVETGAGKLPAKYVIHA-- 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046852755 201 prwTVMDSQTAIGLLSV--AITNILDYVTKWNtcIKTVAIPALSSGIFQFPLHLCTRIIVETI 261
Cdd:cd03330    75 ---AVMGMPGRSSEESIrdATRNALAKAEELG--LESVAFPAIGTGVGGFPVEEVARIMLEEI 132
Macro_SF cd02749
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 339-454 3.31e-21

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: 89.76  E-value: 3.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 339 DVIVNSGHLQDFKSGQVAQSILKRAGFEMEMELDKIKLSSDYQV--VQVTKGFKLSCQYVFHVSWHYSISKD---QILKN 413
Cdd:cd02749     1 DAIVNPANNDLYLGGGVAKAISKKAGGDLQEECEERKKNGYLKVgeVAVTKGGNLPARYIIHVVGPVASSKKktyEPLKK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1046852755 414 AMKSCLERCLKRDINSISFPALGTGAINLEKSIAAKIMFEE 454
Cdd:cd02749    81 CVKNCLSLADEKGLKSVAFPAIGTGIAGFPPEEAARIMLEA 121
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 114-293 7.94e-20

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: 87.69  E-value: 7.94e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 114 RMLTPGIELSVWKDDLTRHVVDAVVNAANEDLLHGGGLAGSLVKIGGSEIQEEskkwIATHGKIPV-GGFAVTRAGKLPC 192
Cdd:cd02903     2 TMKIGGITVQLVKGDITKEKTDVIVNSVSSDLLLKGGVSKAILKAAGPELQDE----CANQGKQPAsGDVIVTSGGNLPC 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 193 YLIIHAVGPRWtvmdSQTAIGLLSVAITNILDYVTKWNtcIKTVAIPALSSGIFQFPLHLCTRIIVETICLyFQDKQTVS 272
Cdd:cd02903    78 KYVYHVVLPHY----NPGNEKTLKDIVRKCLEKAENYK--MSSISFPAIGTGNLGFPKDVVAEIMIDEVLK-FSSKNPSS 150

                         170       180
                  ....*....|....*....|.
gi 1046852755 273 NLREIHLVSNEGPTVESFKSS 293
Cdd:cd02903   151 SLKEVRFVIFPPETLQAFSDE 171
Macro_SF cd02749
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 135-260 4.16e-19

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: 83.99  E-value: 4.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 135 DAVVNAANEDLLHGGGLAGSLVKIGGSEIQEESkKWIATHGKIPVGGFAVTRAGKLPCYLIIHAVGPRWTVMDSQTAigL 214
Cdd:cd02749     1 DAIVNPANNDLYLGGGVAKAISKKAGGDLQEEC-EERKKNGYLKVGEVAVTKGGNLPARYIIHVVGPVASSKKKTYE--P 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1046852755 215 LSVAITNILDYVTKWNtcIKTVAIPALSSGIFQFPLHLCTRIIVET 260
Cdd:cd02749    78 LKKCVKNCLSLADEKG--LKSVAFPAIGTGIAGFPPEEAARIMLEA 121
PRK04143 PRK04143
protein-ADP-ribose hydrolase;
122-271 1.19e-14

protein-ADP-ribose hydrolase;


Pssm-ID: 235225  Cd Length: 264  Bit Score: 75.02  E-value: 1.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 122 LSVWKDDLTRHVVDAVVNAANEDLL------HG------GGLAGSLVKIGGSEIQEEskkwiatHGKI-PVGGFAVTRAG 188
Cdd:PRK04143   85 IFLWQGDITRLKVDAIVNAANSRLLgcfqpnHDcidnaiHTFAGVQLRLDCAEIMTE-------QGRKeATGQAKITRAY 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 189 KLPCYLIIHAVGPRWTV-MDSQTAIGLLSVAITNILDYVTKWNtcIKTVAIPALSSGIFQFPLHLCTRIIVETICLYF-- 265
Cdd:PRK04143  158 NLPAKYVIHTVGPIIRKqPVSPIRADLLASCYRSCLKLAEKAG--LKSIAFCCISTGVFGFPKEEAAEIAIKTVLSWLke 235


                  ....*..
gi 1046852755 266 -QDKQTV 271
Cdd:PRK04143  236 nPSKLKV 242
Macro_GDAP2-like cd02905
macrodomain, GDAP2-like family; Macrodomains are found in a variety of proteins with diverse ...
 122-257 1.26e-14

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: 72.65  E-value: 1.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 122 LSVWKDDLTRHVVDAVVNAANEDLLHGGGLAGSLVKIGGSEIQEEskkwIATHGKIPVGGFAVTRAGKLPCYLIIHAVGP 201
Cdd:cd02905     3 IVLWDGDLTLLNVDAIVNSTNESLTDKSPISDRLFLAAGPELREE----LAKLGGCRTGEAKLTKGYNLPARYVIHTVGP 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046852755 202 RWTVmDSQTAI---------GLLSVAITNILdyvtkwntciKTVAIPALSSGIFQFPL----HLCTRII 257
Cdd:cd02905    79 RYNE-KYRTAAesalyscyrNVLQLAKEHKL----------RSVAFPVIHSERRGYPLedgaHIALRTV 136
Macro_OAADPr_deacetylase cd02908
macrodomain, O-acetyl-ADP-ribose (OAADPr) family; Macrodomains are found in a variety of ...
 328-482 1.48e-13

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: 69.46  E-value: 1.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 328 IVQGCIELQTTDVIVNSGHlqdfKS----GQVAQSILKRAGFEMEMELDKIKLSSDYQVVQVTKGFKLSCQYVFH----V 399
Cdd:cd02908     4 LWRGDITKLEVDAIVNAAN----SSllggGGVDGAIHRAAGPELLEECRKLGGVCPTGEAKITPGYNLPAKYVIHtvgpI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 400 SWHYSISKDQILKNAMKSCLERCLKRDINSISFPALGTGAINLEKSIAAKIMFEEIVAFAKEHkEKTLTVKIVIF-PVDV 478
Cdd:cd02908    80 GEGGVEEEPELLASCYRSSLELALENGLKSIAFPCISTGIYGYPNEEAAEIALNTVREWLEEH-DKIDRIIFVVFlDEDY 158


                  ....
gi 1046852755 479 ETYK 482
Cdd:cd02908   159 KIYE 162
Macro_H2A-like cd02904
macrodomain, macroH2A-like family; Macrodomains are found in a variety of proteins with ...
 314-490 1.87e-13

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: 69.65  E-value: 1.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 314 SNVTLHIGQGLTLqiVQGCIELQTTDVIVNSGHLQDFKSGQVAQSILKRAGFEMEMELDKI-KLSSDYQV--VQVTKGFK 390
Cdd:cd02904    10 SEKKLFLGQKLTV--VQGDIASIKADAIVHPTNATFYLGGEVGSALEKAGGKEFVEEVKELrKSNGPLEVagAAISPGHN 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 391 LSCQYVFHV---SWHYSISKDQiLKNAMKSCLERCLKRDINSISFPALGTGAINLEKSIAAKIMFEEIVAFAKEHKEKTL 467
Cdd:cd02904    88 LPAKFVIHCnspSWGSDKCEEL-LEKTVKNCLALADEKKLKSVAFPSIGSGRNGFPKQTAAQTILKAISNYFVSVMSSSL 166

                         170       180
                  ....*....|....*....|....
gi 1046852755 468 -TVKIVIFpvDVETYKVFCAEMTK 490
Cdd:cd02904   167 kQIYFVLF--DMESIGIYTSELAK 188
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 353-451 1.98e-13

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: 67.59  E-value: 1.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 353 GQVAQSILKRAGFEMEMELDKIKLSS-DYQVVQVTKGFKLSCQYVFHV-----SWHYSISKDQILKNAMKSCLERCLKRD 426
Cdd:pfam01661  12 GGVAGAIHRAAGPELLEECRELKKGGcPTGEAVVTPGGNLPAKYVIHTvgptwRHGGSHGEEELLESCYRNALALAEELG 91

                          90       100
                  ....*....|....*....|....*
gi 1046852755 427 INSISFPALGTGAINLEKSIAAKIM 451
Cdd:pfam01661  92 IKSIAFPAISTGIYGFPWEEAARIA 116
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 326-451 9.63e-13

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: 66.17  E-value: 9.63e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755  326 LQIVQGCIELQTTDVIVNSGHLQDFKSGQVAQSILKRAGfEMEMELDKIKLSSDYQVVQ---VTKGFKLSCQYVFHV--- 399
Cdd:smart00506   2 LKVVKGDITKPRADAIVNAANSDGAHGGGVAGAIARAAG-KALSKEEVRKLAGGECPVGtavVTEGGNLPAKYVIHAvgp 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1046852755  400 SW-HYSISKDQILKNAMKSCLERCLKRDINSISFPALGTGAINLEKSIAAKIM 451
Cdd:smart00506  81 RAsGHSKEGFELLENAYRNCLELAIELGITSVALPLIGTGIYGVPKDRSAQAL 133
Macro_Ttha0132-like cd03330
Macrodomain, uncharacterized family similar to Thermus thermophilus hypothetical protein ...
 326-461 5.81e-12

Macrodomain, uncharacterized family similar to Thermus thermophilus hypothetical protein Ttha0132; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Macrodomains include the yeast macrodomain Poa1 which is a phosphatase of ADP-ribose-1"-phosphate, a by-product of tRNA splicing. Some macrodomains have ADPr-unrelated binding partners such as the coronavirus SUD-N (N-terminal subdomain) and SUD-M (middle subdomain) of the SARS-unique domain (SUD) which bind G-quadruplexes (unusual nucleic-acid structures formed by consecutive guanosine nucleotides). Macrodomains regulate a wide variety of cellular and organismal processes, including DNA damage repair, signal transduction, and immune response. This family is composed of uncharacterized proteins containing a stand-alone macrodomain, similar to Thermus thermophilus hypothetical protein Ttha0132.


Pssm-ID: 394879  Cd Length: 147  Bit Score: 64.38  E-value: 5.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 326 LQIVQGCIELQTTDVIVNSGHLQDFKSGQVAQSILKRAGFEMEMELDK---IKLSSdyqvVQVTKGFKLSCQYVFHV--- 399
Cdd:cd03330     2 LIVVQGDITEQDADAIVNAANRRLLMGSGVAGAIKRKGGEEIEREAMRkgpIRVGE----AVETGAGKLPAKYVIHAavm 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046852755 400 -SWhYSISKDQIlKNAMKSCLERCLKRDINSISFPALGTGAINLEKSIAAKIMFEEIVAFAKE 461
Cdd:cd03330    78 gMP-GRSSEESI-RDATRNALAKAEELGLESVAFPAIGTGVGGFPVEEVARIMLEEIKKCDPP 138
Macro_GDAP2-like cd02905
macrodomain, GDAP2-like family; Macrodomains are found in a variety of proteins with diverse ...
 338-482 1.36e-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: 49.16  E-value: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 338 TDVIVNSGHLQDFKSGQVAQSILKRAGFEMEMELDKIKlSSDYQVVQVTKGFKLSCQYVFH-VSWHYSISKDQILKNAMK 416
Cdd:cd02905    15 VDAIVNSTNESLTDKSPISDRLFLAAGPELREELAKLG-GCRTGEAKLTKGYNLPARYVIHtVGPRYNEKYRTAAESALY 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 417 SCLERCL----KRDINSISFPALGTGAINLEKSIAAKIMFEEIVAFAKEHKEKTLTVKIVIFPVDVETYK 482
Cdd:cd02905    94 SCYRNVLqlakEHKLRSVAFPVIHSERRGYPLEDGAHIALRTVRRFLEKHGSSFEAVVFVVTEEEMETYE 163
PRK04143 PRK04143
protein-ADP-ribose hydrolase;
385-482 1.31e-04

protein-ADP-ribose hydrolase;


Pssm-ID: 235225  Cd Length: 264  Bit Score: 44.59  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046852755 385 VTKGFKLSCQYVFH----------VSwhySISKDQiLKNAMKSCLERCLKRDINSISFPALGTGAINLEKSIAAKIMFEE 454
Cdd:PRK04143  153 ITRAYNLPAKYVIHtvgpiirkqpVS---PIRADL-LASCYRSCLKLAEKAGLKSIAFCCISTGVFGFPKEEAAEIAIKT 228

                          90       100
                  ....*....|....*....|....*...
gi 1046852755 455 IVAFAKEHKEKTLTVKIVIFPVDVETYK 482
Cdd:PRK04143  229 VLSWLKENPSKLKVVFNVFTDEDLELYQ 256
 
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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