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Conserved domains on  [gi|226371714|ref|NP_001139576|]
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protein mono-ADP-ribosyltransferase PARP9 isoform b [Homo sapiens]

Protein Classification

macro domain-containing protein( domain architecture ID 10121100)

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 ...
 82-242 5.13e-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: 240.86  E-value: 5.13e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714  82 RIELSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQFVARYGKVSAGEIAVTGAGRLPCKQIIHA 161
Cdd:cd02907    1 GIKVSVYKGDITKEKVDAIVNAANERLKHGGGVAGAISKAGGPEIQEECDKYIKKNGKLRVGEVVVTSAGKLPCKYVIHA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714 162 VGPRWMEWDKQGCTGKLQRAIVSILNYVIYKNthIKTVAIPALSSGIFQFPLNLCTKTIVETIRvSLQGKPMMSNLKEIH 241
Cdd:cd02907   81 VGPRWSGGSKEECEDLLYKAVLNSLEEAEELK--ATSIAIPAISSGIFGFPLDLCAEAIVEAIK-DFSESNSSSSLKEIR 157


                 .
gi 226371714 242 L 242
Cdd:cd02907  158 L 158
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 275-451 1.04e-64

macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Members of this family show similarity to BAL (B-aggressive lymphoma) proteins, which contain one to three macrodomains. Most BAL family macrodomains belong to this family except for the most N-terminal domain in multiple-domain containing proteins. This family includes the second and third macrodomains of mono-ADP-ribosyltransferase PARP14 (PARP-14, also known as ADP-ribosyltransferase diphtheria toxin-like 8, ATRD8, B aggressive lymphoma protein 2, or BAL2). Most BAL proteins also contain a C-terminal PARP active site and are also named as PARPs. Human BAL1 (or PARP-9) was originally identified as a risk-related gene in diffuse large B-cell lymphoma that promotes malignant B-cell migration. Some BAL family proteins exhibit PARP activity. Poly (ADP-ribosyl)ation is an immediate DNA-damage-dependent post-translational modification of histones and other nuclear proteins. BAL proteins may also function as transcriptional repressors.


:

Pssm-ID: 394874  Cd Length: 175  Bit Score: 213.65  E-value: 1.04e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714 275 NAMVVNNLTLQIVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEfLATKAKQFQrSQLVLVTKGFNLFCK 354
Cdd:cd02903    1 YTMKIGGITVQLVKGDITKEKTDVIVNSVSSDLLLKGGVSKAILKAAGPELQDE-CANQGKQPA-SGDVIVTSGGNLPCK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714 355 YIYHVLWHSEFPK-PQILKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILFDEVLTFAKDHV-KHQLTVKFV 432
Cdd:cd02903   79 YVYHVVLPHYNPGnEKTLKDIVRKCLEKAENYKMSSISFPAIGTGNLGFPKDVVAEIMIDEVLKFSSKNPsSSLKEVRFV 158

                        170
                 ....*....|....*....
gi 226371714 433 IFPTdlEIYKAFSSEMAKR 451
Cdd:cd02903  159 IFPP--ETLQAFSDELAKR 175
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 667-786 2.40e-52

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: 177.90  E-value: 2.40e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714 667 RLFQQVPYQFCNVVCRVGFQRMYSTPCDPKYGAGIYFTKNLKNLAEKAKKISAADKLIYVFEAEVLTGFFCQGHPLNIVP 746
Cdd:cd01439    1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKADGLKEMFLARVLTGDYTQGHPGYRRP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 226371714 747 P-PLSPGAIDGHDSVVDNVSSPETFVIFSGMQAIPQYLWTC 786
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 ...
 82-242 5.13e-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: 240.86  E-value: 5.13e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714  82 RIELSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQFVARYGKVSAGEIAVTGAGRLPCKQIIHA 161
Cdd:cd02907    1 GIKVSVYKGDITKEKVDAIVNAANERLKHGGGVAGAISKAGGPEIQEECDKYIKKNGKLRVGEVVVTSAGKLPCKYVIHA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714 162 VGPRWMEWDKQGCTGKLQRAIVSILNYVIYKNthIKTVAIPALSSGIFQFPLNLCTKTIVETIRvSLQGKPMMSNLKEIH 241
Cdd:cd02907   81 VGPRWSGGSKEECEDLLYKAVLNSLEEAEELK--ATSIAIPAISSGIFGFPLDLCAEAIVEAIK-DFSESNSSSSLKEIR 157


                 .
gi 226371714 242 L 242
Cdd:cd02907  158 L 158
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 275-451 1.04e-64

macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Members of this family show similarity to BAL (B-aggressive lymphoma) proteins, which contain one to three macrodomains. Most BAL family macrodomains belong to this family except for the most N-terminal domain in multiple-domain containing proteins. This family includes the second and third macrodomains of mono-ADP-ribosyltransferase PARP14 (PARP-14, also known as ADP-ribosyltransferase diphtheria toxin-like 8, ATRD8, B aggressive lymphoma protein 2, or BAL2). Most BAL proteins also contain a C-terminal PARP active site and are also named as PARPs. Human BAL1 (or PARP-9) was originally identified as a risk-related gene in diffuse large B-cell lymphoma that promotes malignant B-cell migration. Some BAL family proteins exhibit PARP activity. Poly (ADP-ribosyl)ation is an immediate DNA-damage-dependent post-translational modification of histones and other nuclear proteins. BAL proteins may also function as transcriptional repressors.


Pssm-ID: 394874  Cd Length: 175  Bit Score: 213.65  E-value: 1.04e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714 275 NAMVVNNLTLQIVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEfLATKAKQFQrSQLVLVTKGFNLFCK 354
Cdd:cd02903    1 YTMKIGGITVQLVKGDITKEKTDVIVNSVSSDLLLKGGVSKAILKAAGPELQDE-CANQGKQPA-SGDVIVTSGGNLPCK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714 355 YIYHVLWHSEFPK-PQILKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILFDEVLTFAKDHV-KHQLTVKFV 432
Cdd:cd02903   79 YVYHVVLPHYNPGnEKTLKDIVRKCLEKAENYKMSSISFPAIGTGNLGFPKDVVAEIMIDEVLKFSSKNPsSSLKEVRFV 158

                        170
                 ....*....|....*....
gi 226371714 433 IFPTdlEIYKAFSSEMAKR 451
Cdd:cd02903  159 IFPP--ETLQAFSDELAKR 175
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 667-786 2.40e-52

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: 177.90  E-value: 2.40e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714 667 RLFQQVPYQFCNVVCRVGFQRMYSTPCDPKYGAGIYFTKNLKNLAEKAKKISAADKLIYVFEAEVLTGFFCQGHPLNIVP 746
Cdd:cd01439    1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKADGLKEMFLARVLTGDYTQGHPGYRRP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 226371714 747 P-PLSPGAIDGHDSVVDNVSSPETFVIFSGMQAIPQYLWTC 786
Cdd:cd01439   81 PlKPSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
PRK00431 PRK00431
ADP-ribose-binding protein;
83-256 5.21e-45

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 159.62  E-value: 5.21e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714  83 IELSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQFVARYGKVSAGEIAVTGAGRLPCKQIIHAV 162
Cdd:PRK00431   3 MRIEVVQGDITELEVDAIVNAANSSLLGGGGVDGAIHRAAGPEILEECRELRQQQGPCPTGEAVITSAGRLPAKYVIHTV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714 163 GPRWM-EWDKQgcTGKLQRAIVSILNYViyKNTHIKTVAIPALSSGIFQFPLNLCTKTIVETIRVSLQGKpmmSNLKEIH 241
Cdd:PRK00431  83 GPVWRgGEDNE--AELLASAYRNSLRLA--AELGLRSIAFPAISTGVYGYPLEDAARIAVKTVREFLTRH---KSPEEVY 155

                        170
                 ....*....|....*
gi 226371714 242 LVSNEDPTVAAFKAA 256
Cdd:PRK00431 156 FVCYDEEAYRLYERL 170
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 85-256 3.05e-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: 148.79  E-value: 3.05e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714  85 LSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQFVaRYGKVSAGEIAVTGAGRLPCKQIIHAVGP 164
Cdd:COG2110    1 IEIVQGDITELDVDAIVNAANSSLLGGGGVAGAIHRAAGPELLEECRRLC-KQGGCPTGEAVITPAGNLPAKYVIHTVGP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714 165 RWmEWDKQGCTGKLQRAIVSILNyvIYKNTHIKTVAIPALSSGIFQFPLNLCTKTIVETIRVSLQGKPmmsNLKEIHLVS 244
Cdd:COG2110   80 VW-RGGGPSEEELLASCYRNSLE--LAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFLEEHP---SLEEVRFVL 153

                        170
                 ....*....|..
gi 226371714 245 NEDPTVAAFKAA 256
Cdd:COG2110  154 FDEEDYEAYRRA 165
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 101-220 9.93e-38

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: 136.54  E-value: 9.93e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714  101 VNAANEDLLHGGGLALALVKAGGFEIQEESKQFVAryGKVSAGEIAVTGAGRLPCKQIIHAVGPRWMEWDKQGCTGKLQR 180
Cdd:pfam01661   1 VNAANSRLLGGGGVAGAIHRAAGPELLEECRELKK--GGCPTGEAVVTPGGNLPAKYVIHTVGPTWRHGGSHGEEELLES 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 226371714  181 AIVSILNYViyKNTHIKTVAIPALSSGIFQFPLNLCTKTI 220
Cdd:pfam01661  79 CYRNALALA--EELGIKSIAFPAISTGIYGFPWEEAARIA 116
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 84-220 1.26e-30

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: 117.02  E-value: 1.26e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714    84 ELSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQfVARYGKVSAGEIAVTGAGRLPCKQIIHAVG 163
Cdd:smart00506   1 ILKVVKGDITKPRADAIVNAANSDGAHGGGVAGAIARAAGKALSKEEVR-KLAGGECPVGTAVVTEGGNLPAKYVIHAVG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 226371714   164 PRWMEwDKQGCTGKLQRAIVSILNYVIYKNthIKTVAIPALSSGIFQFPLNLCTKTI 220
Cdd:smart00506  80 PRASG-HSKEGFELLENAYRNCLELAIELG--ITSVALPLIGTGIYGVPKDRSAQAL 133
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 284-443 3.91e-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: 3.91e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714 284 LQIVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEFLAT-KAKQFQRSQLVlVTKGFNLFCKYIYHVL-- 360
Cdd:COG2110    1 IEIVQGDITELDVDAIVNAANSSLLGGGGVAGAIHRAAGPELLEECRRLcKQGGCPTGEAV-ITPAGNLPAKYVIHTVgp 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714 361 -WHSEFP-KPQILKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILFDEVLTFAKDHVKHQlTVKFVIF-PTD 437
Cdd:COG2110   80 vWRGGGPsEEELLASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFLEEHPSLE-EVRFVLFdEED 158


                 ....*.
gi 226371714 438 LEIYKA 443
Cdd:COG2110  159 YEAYRR 164
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 284-411 9.93e-21

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: 88.90  E-value: 9.93e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714   284 LQIVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEFLATKAKQFQRSQLVLVTKGFNLFCKYIYHVL--- 360
Cdd:smart00506   2 LKVVKGDITKPRADAIVNAANSDGAHGGGVAGAIARAAGKALSKEEVRKLAGGECPVGTAVVTEGGNLPAKYVIHAVgpr 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 226371714   361 ----WHSEFpkpQILKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEIL 411
Cdd:smart00506  82 asghSKEGF---ELLENAYRNCLELAIELGITSVALPLIGTGIYGVPKDRSAQAL 133
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 300-411 3.03e-15

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: 72.60  E-value: 3.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714  300 VNSVNPHDITVGPVAKSILQQAGVEMKSEflaTKAKQFQRSQL--VLVTKGFNLFCKYIYHV---LWHSEFPK--PQILK 372
Cdd:pfam01661   1 VNAANSRLLGGGGVAGAIHRAAGPELLEE---CRELKKGGCPTgeAVVTPGGNLPAKYVIHTvgpTWRHGGSHgeEELLE 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 226371714  373 HAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEIL 411
Cdd:pfam01661  78 SCYRNALALAEELGIKSIAFPAISTGIYGFPWEEAARIA 116
PRK04143 PRK04143
protein-ADP-ribose hydrolase;
345-442 2.23e-07

protein-ADP-ribose hydrolase;


Pssm-ID: 235225  Cd Length: 264  Bit Score: 53.06  E-value: 2.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714 345 VTKGFNLFCKYIYHVLwhsefpKPQI------------LKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILF 412
Cdd:PRK04143 153 ITRAYNLPAKYVIHTV------GPIIrkqpvspiradlLASCYRSCLKLAEKAGLKSIAFCCISTGVFGFPKEEAAEIAI 226

                         90       100       110
                 ....*....|....*....|....*....|.
gi 226371714 413 DEVLTFAKDHvKHQLTVKFVIF-PTDLEIYK 442
Cdd:PRK04143 227 KTVLSWLKEN-PSKLKVVFNVFtDEDLELYQ 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 ...
 82-242 5.13e-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: 240.86  E-value: 5.13e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714  82 RIELSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQFVARYGKVSAGEIAVTGAGRLPCKQIIHA 161
Cdd:cd02907    1 GIKVSVYKGDITKEKVDAIVNAANERLKHGGGVAGAISKAGGPEIQEECDKYIKKNGKLRVGEVVVTSAGKLPCKYVIHA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714 162 VGPRWMEWDKQGCTGKLQRAIVSILNYVIYKNthIKTVAIPALSSGIFQFPLNLCTKTIVETIRvSLQGKPMMSNLKEIH 241
Cdd:cd02907   81 VGPRWSGGSKEECEDLLYKAVLNSLEEAEELK--ATSIAIPAISSGIFGFPLDLCAEAIVEAIK-DFSESNSSSSLKEIR 157


                 .
gi 226371714 242 L 242
Cdd:cd02907  158 L 158
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 275-451 1.04e-64

macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Members of this family show similarity to BAL (B-aggressive lymphoma) proteins, which contain one to three macrodomains. Most BAL family macrodomains belong to this family except for the most N-terminal domain in multiple-domain containing proteins. This family includes the second and third macrodomains of mono-ADP-ribosyltransferase PARP14 (PARP-14, also known as ADP-ribosyltransferase diphtheria toxin-like 8, ATRD8, B aggressive lymphoma protein 2, or BAL2). Most BAL proteins also contain a C-terminal PARP active site and are also named as PARPs. Human BAL1 (or PARP-9) was originally identified as a risk-related gene in diffuse large B-cell lymphoma that promotes malignant B-cell migration. Some BAL family proteins exhibit PARP activity. Poly (ADP-ribosyl)ation is an immediate DNA-damage-dependent post-translational modification of histones and other nuclear proteins. BAL proteins may also function as transcriptional repressors.


Pssm-ID: 394874  Cd Length: 175  Bit Score: 213.65  E-value: 1.04e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714 275 NAMVVNNLTLQIVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEfLATKAKQFQrSQLVLVTKGFNLFCK 354
Cdd:cd02903    1 YTMKIGGITVQLVKGDITKEKTDVIVNSVSSDLLLKGGVSKAILKAAGPELQDE-CANQGKQPA-SGDVIVTSGGNLPCK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714 355 YIYHVLWHSEFPK-PQILKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILFDEVLTFAKDHV-KHQLTVKFV 432
Cdd:cd02903   79 YVYHVVLPHYNPGnEKTLKDIVRKCLEKAENYKMSSISFPAIGTGNLGFPKDVVAEIMIDEVLKFSSKNPsSSLKEVRFV 158

                        170
                 ....*....|....*....
gi 226371714 433 IFPTdlEIYKAFSSEMAKR 451
Cdd:cd02903  159 IFPP--ETLQAFSDELAKR 175
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 667-786 2.40e-52

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: 177.90  E-value: 2.40e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714 667 RLFQQVPYQFCNVVCRVGFQRMYSTPCDPKYGAGIYFTKNLKNLAEKAKKISAADKLIYVFEAEVLTGFFCQGHPLNIVP 746
Cdd:cd01439    1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKADGLKEMFLARVLTGDYTQGHPGYRRP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 226371714 747 P-PLSPGAIDGHDSVVDNVSSPETFVIFSGMQAIPQYLWTC 786
Cdd:cd01439   81 PlKPSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
PRK00431 PRK00431
ADP-ribose-binding protein;
83-256 5.21e-45

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 159.62  E-value: 5.21e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714  83 IELSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQFVARYGKVSAGEIAVTGAGRLPCKQIIHAV 162
Cdd:PRK00431   3 MRIEVVQGDITELEVDAIVNAANSSLLGGGGVDGAIHRAAGPEILEECRELRQQQGPCPTGEAVITSAGRLPAKYVIHTV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714 163 GPRWM-EWDKQgcTGKLQRAIVSILNYViyKNTHIKTVAIPALSSGIFQFPLNLCTKTIVETIRVSLQGKpmmSNLKEIH 241
Cdd:PRK00431  83 GPVWRgGEDNE--AELLASAYRNSLRLA--AELGLRSIAFPAISTGVYGYPLEDAARIAVKTVREFLTRH---KSPEEVY 155

                        170
                 ....*....|....*
gi 226371714 242 LVSNEDPTVAAFKAA 256
Cdd:PRK00431 156 FVCYDEEAYRLYERL 170
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 85-256 3.05e-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: 148.79  E-value: 3.05e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714  85 LSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQFVaRYGKVSAGEIAVTGAGRLPCKQIIHAVGP 164
Cdd:COG2110    1 IEIVQGDITELDVDAIVNAANSSLLGGGGVAGAIHRAAGPELLEECRRLC-KQGGCPTGEAVITPAGNLPAKYVIHTVGP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714 165 RWmEWDKQGCTGKLQRAIVSILNyvIYKNTHIKTVAIPALSSGIFQFPLNLCTKTIVETIRVSLQGKPmmsNLKEIHLVS 244
Cdd:COG2110   80 VW-RGGGPSEEELLASCYRNSLE--LAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFLEEHP---SLEEVRFVL 153

                        170
                 ....*....|..
gi 226371714 245 NEDPTVAAFKAA 256
Cdd:COG2110  154 FDEEDYEAYRRA 165
Macro_SF cd02749
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 297-414 9.52e-41

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: 145.62  E-value: 9.52e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714 297 DVIVNSVNPHDITVGPVAKSILQQAGVEMKSEFLATKAKQFQRSQLVLVTKGFNLFCKYIYHVLWHSEFPKP---QILKH 373
Cdd:cd02749    1 DAIVNPANNDLYLGGGVAKAISKKAGGDLQEECEERKKNGYLKVGEVAVTKGGNLPARYIIHVVGPVASSKKktyEPLKK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 226371714 374 AMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILFDE 414
Cdd:cd02749   81 CVKNCLSLADEKGLKSVAFPAIGTGIAGFPPEEAARIMLEA 121
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 101-220 9.93e-38

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: 136.54  E-value: 9.93e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714  101 VNAANEDLLHGGGLALALVKAGGFEIQEESKQFVAryGKVSAGEIAVTGAGRLPCKQIIHAVGPRWMEWDKQGCTGKLQR 180
Cdd:pfam01661   1 VNAANSRLLGGGGVAGAIHRAAGPELLEECRELKK--GGCPTGEAVVTPGGNLPAKYVIHTVGPTWRHGGSHGEEELLES 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 226371714  181 AIVSILNYViyKNTHIKTVAIPALSSGIFQFPLNLCTKTI 220
Cdd:pfam01661  79 CYRNALALA--EELGIKSIAFPAISTGIYGFPWEEAARIA 116
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 84-220 1.26e-30

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: 117.02  E-value: 1.26e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714    84 ELSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQfVARYGKVSAGEIAVTGAGRLPCKQIIHAVG 163
Cdd:smart00506   1 ILKVVKGDITKPRADAIVNAANSDGAHGGGVAGAIARAAGKALSKEEVR-KLAGGECPVGTAVVTEGGNLPAKYVIHAVG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 226371714   164 PRWMEwDKQGCTGKLQRAIVSILNYVIYKNthIKTVAIPALSSGIFQFPLNLCTKTI 220
Cdd:smart00506  80 PRASG-HSKEGFELLENAYRNCLELAIELG--ITSVALPLIGTGIYGVPKDRSAQAL 133
Macro_OAADPr_deacetylase cd02908
macrodomain, O-acetyl-ADP-ribose (OAADPr) family; Macrodomains are found in a variety of ...
 85-225 8.65e-30

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: 115.69  E-value: 8.65e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714  85 LSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQFvarYGKVSAGEIAVTGAGRLPCKQIIHAVGP 164
Cdd:cd02908    2 ISLWRGDITKLEVDAIVNAANSSLLGGGGVDGAIHRAAGPELLEECRKL---GGVCPTGEAKITPGYNLPAKYVIHTVGP 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226371714 165 RWmEWDKQGCTGKLQRAIVSILNYVIYKNthIKTVAIPALSSGIFQFPLNLCTKTIVETIR 225
Cdd:cd02908   79 IG-EGGVEEEPELLASCYRSSLELALENG--LKSIAFPCISTGIYGYPNEEAAEIALNTVR 136
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 284-443 3.91e-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: 3.91e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714 284 LQIVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEFLAT-KAKQFQRSQLVlVTKGFNLFCKYIYHVL-- 360
Cdd:COG2110    1 IEIVQGDITELDVDAIVNAANSSLLGGGGVAGAIHRAAGPELLEECRRLcKQGGCPTGEAV-ITPAGNLPAKYVIHTVgp 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714 361 -WHSEFP-KPQILKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILFDEVLTFAKDHVKHQlTVKFVIF-PTD 437
Cdd:COG2110   80 vWRGGGPsEEELLASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFLEEHPSLE-EVRFVLFdEED 158


                 ....*.
gi 226371714 438 LEIYKA 443
Cdd:COG2110  159 YEAYRR 164
Macro_H2A-like cd02904
macrodomain, macroH2A-like family; Macrodomains are found in a variety of proteins with ...
 85-243 3.17e-24

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: 100.47  E-value: 3.17e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714  85 LSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQFVARYGKVSAGEIAVTGAGRLPCKQIIHAVGP 164
Cdd:cd02904   20 LTVVQGDIASIKADAIVHPTNATFYLGGEVGSALEKAGGKEFVEEVKELRKSNGPLEVAGAAISPGHNLPAKFVIHCNSP 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714 165 RWMEWDkqgCTGKLQRAIVSILNYVIYKNthIKTVAIPALSSGIFQFPLNLCTKTIVETIR---VSLqgkpMMSNLKEIH 241
Cdd:cd02904  100 SWGSDK---CEELLEKTVKNCLALADEKK--LKSVAFPSIGSGRNGFPKQTAAQTILKAISnyfVSV----MSSSLKQIY 170


                 ..
gi 226371714 242 LV 243
Cdd:cd02904  171 FV 172
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 81-253 1.08e-23

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: 98.86  E-value: 1.08e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714  81 PRIELSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQfvaRYGKVSAGEIAVTGAGRLPCKQIIH 160
Cdd:cd02903    6 GGITVQLVKGDITKEKTDVIVNSVSSDLLLKGGVSKAILKAAGPELQDECAN---QGKQPASGDVIVTSGGNLPCKYVYH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714 161 AVGPRWMEWDKQGctgkLQRAIVSILNYViyKNTHIKTVAIPALSSGIFQFPLNLCTKTIVETIRVSLQGKPmMSNLKEI 240
Cdd:cd02903   83 VVLPHYNPGNEKT----LKDIVRKCLEKA--ENYKMSSISFPAIGTGNLGFPKDVVAEIMIDEVLKFSSKNP-SSSLKEV 155

                        170
                 ....*....|...
gi 226371714 241 HLVSNEDPTVAAF 253
Cdd:cd02903  156 RFVIFPPETLQAF 168
Macro_SF cd02749
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 98-223 1.96e-22

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: 93.23  E-value: 1.96e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714  98 DAVVNAANEDLLHGGGLALALVKAGGFEIQEESkQFVARYGKVSAGEIAVTGAGRLPCKQIIHAVGPRWMEWDKqgCTGK 177
Cdd:cd02749    1 DAIVNPANNDLYLGGGVAKAISKKAGGDLQEEC-EERKKNGYLKVGEVAVTKGGNLPARYIIHVVGPVASSKKK--TYEP 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 226371714 178 LQRAIVSILNYVIYKNthIKTVAIPALSSGIFQFPLNLCTKTIVET 223
Cdd:cd02749   78 LKKCVKNCLSLADEKG--LKSVAFPAIGTGIAGFPPEEAARIMLEA 121
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 284-411 9.93e-21

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: 88.90  E-value: 9.93e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714   284 LQIVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEFLATKAKQFQRSQLVLVTKGFNLFCKYIYHVL--- 360
Cdd:smart00506   2 LKVVKGDITKPRADAIVNAANSDGAHGGGVAGAIARAAGKALSKEEVRKLAGGECPVGTAVVTEGGNLPAKYVIHAVgpr 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 226371714   361 ----WHSEFpkpQILKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEIL 411
Cdd:smart00506  82 asghSKEGF---ELLENAYRNCLELAIELGITSVALPLIGTGIYGVPKDRSAQAL 133
Macro_X_Nsp3-like cd21557
X-domain (or Mac1 domain) of viral non-structural protein 3 and related macrodomains; The ...
 98-213 1.05e-20

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: 88.38  E-value: 1.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714  98 DAVVNAANEDLLHGGGLALALVKAGGFEIQEESKqFVARYGKVSAGEIAVTgAGRLPCKQIIHAVGPRwmeWDKQGCTGK 177
Cdd:cd21557    2 DVVVNAANENLKHGGGVAGAIYKATGGAFQKESD-YIKKNGPLKVGTAVLL-PGHGLAKNIIHVVGPR---KRKGQDDQL 76

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 226371714 178 LQRAivsilnyviYKNTH--IKTVAIPALSSGIFQFPL 213
Cdd:cd21557   77 LAAA---------YKAVNkeYGSVLTPLLSAGIFGVPP 105
Macro_Ttha0132-like cd03330
Macrodomain, uncharacterized family similar to Thermus thermophilus hypothetical protein ...
 84-230 4.10e-20

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: 87.49  E-value: 4.10e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714  84 ELSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESkqfvARYGKVSAGEIAVTGAGRLPCKQIIHAVG 163
Cdd:cd03330    1 RLIVVQGDITEQDADAIVNAANRRLLMGSGVAGAIKRKGGEEIEREA----MRKGPIRVGEAVETGAGKLPAKYVIHAAV 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226371714 164 prwMEWDKQGCTGKLQRAIVSILNYVIYKNthIKTVAIPALSSGIFQFPLNLCTKTIVETIRVSLQG 230
Cdd:cd03330   77 ---MGMPGRSSEESIRDATRNALAKAEELG--LESVAFPAIGTGVGGFPVEEVARIMLEEIKKCDPP 138
Macro_OAADPr_deacetylase cd02908
macrodomain, O-acetyl-ADP-ribose (OAADPr) family; Macrodomains are found in a variety of ...
 286-444 2.00e-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: 77.55  E-value: 2.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714 286 IVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSE------FLAT-KAKqfqrsqlvlVTKGFNLFCKYIYH 358
Cdd:cd02908    4 LWRGDITKLEVDAIVNAANSSLLGGGGVDGAIHRAAGPELLEEcrklggVCPTgEAK---------ITPGYNLPAKYVIH 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714 359 V---LWHSEFPK-PQILKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILFDEVLTFAKDHvKHQLTVKFVIF 434
Cdd:cd02908   75 TvgpIGEGGVEEePELLASCYRSSLELALENGLKSIAFPCISTGIYGYPNEEAAEIALNTVREWLEEH-DKIDRIIFVVF 153

                        170
                 ....*....|.
gi 226371714 435 -PTDLEIYKAF 444
Cdd:cd02908  154 lDEDYKIYEEL 164
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 300-411 3.03e-15

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: 72.60  E-value: 3.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714  300 VNSVNPHDITVGPVAKSILQQAGVEMKSEflaTKAKQFQRSQL--VLVTKGFNLFCKYIYHV---LWHSEFPK--PQILK 372
Cdd:pfam01661   1 VNAANSRLLGGGGVAGAIHRAAGPELLEE---CRELKKGGCPTgeAVVTPGGNLPAKYVIHTvgpTWRHGGSHgeEELLE 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 226371714  373 HAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEIL 411
Cdd:pfam01661  78 SCYRNALALAEELGIKSIAFPAISTGIYGFPWEEAARIA 116
Macro_GDAP2-like cd02905
macrodomain, GDAP2-like family; Macrodomains are found in a variety of proteins with diverse ...
 85-225 3.33e-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: 71.11  E-value: 3.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714  85 LSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEEskqfVARYGKVSAGEIAVTGAGRLPCKQIIHAVGP 164
Cdd:cd02905    3 IVLWDGDLTLLNVDAIVNSTNESLTDKSPISDRLFLAAGPELREE----LAKLGGCRTGEAKLTKGYNLPARYVIHTVGP 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226371714 165 RWMEwdkqgctgKLQRAIVSILnYVIYKNT-------HIKTVAIPALSSGIFQFPLNLCTKTIVETIR 225
Cdd:cd02905   79 RYNE--------KYRTAAESAL-YSCYRNVlqlakehKLRSVAFPVIHSERRGYPLEDGAHIALRTVR 137
Macro_H2A-like cd02904
macrodomain, macroH2A-like family; Macrodomains are found in a variety of proteins with ...
 283-450 5.33e-12

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: 65.41  E-value: 5.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714 283 TLQIVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEFLATKAKQfqrSQL----VLVTKGFNLFCKYIYH 358
Cdd:cd02904   19 KLTVVQGDIASIKADAIVHPTNATFYLGGEVGSALEKAGGKEFVEEVKELRKSN---GPLevagAAISPGHNLPAKFVIH 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714 359 V---LWHSEFPKPQiLKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEIL-------FDEVLTfakDHVKhqlT 428
Cdd:cd02904   96 CnspSWGSDKCEEL-LEKTVKNCLALADEKKLKSVAFPSIGSGRNGFPKQTAAQTIlkaisnyFVSVMS---SSLK---Q 168

                        170       180
                 ....*....|....*....|..
gi 226371714 429 VKFVIFptDLEIYKAFSSEMAK 450
Cdd:cd02904  169 IYFVLF--DMESIGIYTSELAK 188
Macro_Ttha0132-like cd03330
Macrodomain, uncharacterized family similar to Thermus thermophilus hypothetical protein ...
 284-421 1.84e-11

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: 62.84  E-value: 1.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714 284 LQIVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEFLAtkaKQFQRSQLVLVTKGFNLFCKYIYHVLWHS 363
Cdd:cd03330    2 LIVVQGDITEQDADAIVNAANRRLLMGSGVAGAIKRKGGEEIEREAMR---KGPIRVGEAVETGAGKLPAKYVIHAAVMG 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714 364 EFPK--PQILKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILFDEVLTFAKD 421
Cdd:cd03330   79 MPGRssEESIRDATRNALAKAEELGLESVAFPAIGTGVGGFPVEEVARIMLEEIKKCDPP 138
PRK04143 PRK04143
protein-ADP-ribose hydrolase;
85-225 1.00e-10

protein-ADP-ribose hydrolase;


Pssm-ID: 235225  Cd Length: 264  Bit Score: 63.08  E-value: 1.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714  85 LSVWKDDLTTHAVDAVVNAANEDLLhGGGLAL------ALVKAGGFEIQEESKQFVARYGKVSA-GEIAVTGAGRLPCKQ 157
Cdd:PRK04143  85 IFLWQGDITRLKVDAIVNAANSRLL-GCFQPNhdcidnAIHTFAGVQLRLDCAEIMTEQGRKEAtGQAKITRAYNLPAKY 163

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226371714 158 IIHAVGPRWMEW-----DKQgctgKLQRAIVSILNyviYKNTH-IKTVAIPALSSGIFQFPLNLCTKTIVETIR 225
Cdd:PRK04143 164 VIHTVGPIIRKQpvspiRAD----LLASCYRSCLK---LAEKAgLKSIAFCCISTGVFGFPKEEAAEIAIKTVL 230
Macro_GDAP2-like cd02905
macrodomain, GDAP2-like family; Macrodomains are found in a variety of proteins with diverse ...
 288-443 1.82e-09

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: 57.63  E-value: 1.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714 288 QGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEFLATKAkqfQRSQLVLVTKGFNLFCKYIYHVLWhsefPK 367
Cdd:cd02905    7 DGDLTLLNVDAIVNSTNESLTDKSPISDRLFLAAGPELREELAKLGG---CRTGEAKLTKGYNLPARYVIHTVG----PR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714 368 PQI---------LKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILFDEVLTFAKDHVKHQLTVKFVIFPTDL 438
Cdd:cd02905   80 YNEkyrtaaesaLYSCYRNVLQLAKEHKLRSVAFPVIHSERRGYPLEDGAHIALRTVRRFLEKHGSSFEAVVFVVTEEEM 159


                 ....*
gi 226371714 439 EIYKA 443
Cdd:cd02905  160 ETYER 164
PRK04143 PRK04143
protein-ADP-ribose hydrolase;
345-442 2.23e-07

protein-ADP-ribose hydrolase;


Pssm-ID: 235225  Cd Length: 264  Bit Score: 53.06  E-value: 2.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714 345 VTKGFNLFCKYIYHVLwhsefpKPQI------------LKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILF 412
Cdd:PRK04143 153 ITRAYNLPAKYVIHTV------GPIIrkqpvspiradlLASCYRSCLKLAEKAGLKSIAFCCISTGVFGFPKEEAAEIAI 226

                         90       100       110
                 ....*....|....*....|....*....|.
gi 226371714 413 DEVLTFAKDHvKHQLTVKFVIF-PTDLEIYK 442
Cdd:PRK04143 227 KTVLSWLKEN-PSKLKVVFNVFtDEDLELYQ 256
tankyrase_like cd01438
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ...
 633-785 2.12e-04

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


Pssm-ID: 238718 [Multi-domain]  Cd Length: 223  Bit Score: 43.35  E-value: 2.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714 633 VLKVEKIDNEVLMAAFQRKKKMMEEKLHRQPVSHRLFQQVPyqFCNVVCRVGFQRMYSTpCDPKYGAGIYFTKNLKNLAE 712
Cdd:cd01438   57 IIRIQKVVNKKLRERYCHRQKEIAEENHNHHNERMLFHGSP--FINAIIHKGFDERHAY-IGGMFGAGIYFAENSSKSNQ 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371714 713 KAKKI-------SAADKLIYVFEAEVLtgfFCQ-----------GHPLNIVPPplspgaidGHDSVVDNVS----SPETF 770
Cdd:cd01438  134 YVYGIgggtgcpTHKDRSCYVCHRQML---FCRvtlgksflqfsAMKMAHAPP--------GHHSVIGRPSvnglAYAEY 202

                        170
                 ....*....|....*
gi 226371714 771 VIFSGMQAIPQYLWT 785
Cdd:cd01438  203 VIYRGEQAYPEYLIT 217
 
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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