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Conserved domains on  [gi|226371710|ref|NP_001139574|]
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protein mono-ADP-ribosyltransferase PARP9 isoform a [Homo sapiens]

Protein Classification

Macro_Af1521_BAL-like and Macro_BAL-like domain-containing protein( domain architecture ID 10121100)

protein containing domains Macro_Af1521_BAL-like, Macro_BAL-like, and TCCD_inducible_PARP_like

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 ...
 117-277 7.40e-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: 7.40e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 117 RIELSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQFVARYGKVSAGEIAVTGAGRLPCKQIIHA 196
Cdd:cd02907    1 GIKVSVYKGDITKEKVDAIVNAANERLKHGGGVAGAISKAGGPEIQEECDKYIKKNGKLRVGEVVVTSAGKLPCKYVIHA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 197 VGPRWMEWDKQGCTGKLQRAIVSILNYVIYKNthIKTVAIPALSSGIFQFPLNLCTKTIVETIRvSLQGKPMMSNLKEIH 276
Cdd:cd02907   81 VGPRWSGGSKEECEDLLYKAVLNSLEEAEELK--ATSIAIPAISSGIFGFPLDLCAEAIVEAIK-DFSESNSSSSLKEIR 157


                 .
gi 226371710 277 L 277
Cdd:cd02907  158 L 158
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 310-486 1.25e-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: 214.04  E-value: 1.25e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 310 NAMVVNNLTLQIVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEfLATKAKQFQrSQLVLVTKGFNLFCK 389
Cdd:cd02903    1 YTMKIGGITVQLVKGDITKEKTDVIVNSVSSDLLLKGGVSKAILKAAGPELQDE-CANQGKQPA-SGDVIVTSGGNLPCK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 390 YIYHVLWHSEFPK-PQILKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILFDEVLTFAKDHV-KHQLTVKFV 467
Cdd:cd02903   79 YVYHVVLPHYNPGnEKTLKDIVRKCLEKAENYKMSSISFPAIGTGNLGFPKDVVAEIMIDEVLKFSSKNPsSSLKEVRFV 158

                        170
                 ....*....|....*....
gi 226371710 468 IFPTdlEIYKAFSSEMAKR 486
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 ...
 702-821 2.97e-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: 2.97e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 702 RLFQQVPYQFCNVVCRVGFQRMYSTPCDPKYGAGIYFTKNLKNLAEKAKKISAADKLIYVFEAEVLTGFFCQGHPLNIVP 781
Cdd:cd01439    1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKADGLKEMFLARVLTGDYTQGHPGYRRP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 226371710 782 P-PLSPGAIDGHDSVVDNVSSPETFVIFSGMQAIPQYLWTC 821
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 ...
 117-277 7.40e-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: 7.40e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 117 RIELSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQFVARYGKVSAGEIAVTGAGRLPCKQIIHA 196
Cdd:cd02907    1 GIKVSVYKGDITKEKVDAIVNAANERLKHGGGVAGAISKAGGPEIQEECDKYIKKNGKLRVGEVVVTSAGKLPCKYVIHA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 197 VGPRWMEWDKQGCTGKLQRAIVSILNYVIYKNthIKTVAIPALSSGIFQFPLNLCTKTIVETIRvSLQGKPMMSNLKEIH 276
Cdd:cd02907   81 VGPRWSGGSKEECEDLLYKAVLNSLEEAEELK--ATSIAIPAISSGIFGFPLDLCAEAIVEAIK-DFSESNSSSSLKEIR 157


                 .
gi 226371710 277 L 277
Cdd:cd02907  158 L 158
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 310-486 1.25e-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: 214.04  E-value: 1.25e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 310 NAMVVNNLTLQIVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEfLATKAKQFQrSQLVLVTKGFNLFCK 389
Cdd:cd02903    1 YTMKIGGITVQLVKGDITKEKTDVIVNSVSSDLLLKGGVSKAILKAAGPELQDE-CANQGKQPA-SGDVIVTSGGNLPCK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 390 YIYHVLWHSEFPK-PQILKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILFDEVLTFAKDHV-KHQLTVKFV 467
Cdd:cd02903   79 YVYHVVLPHYNPGnEKTLKDIVRKCLEKAENYKMSSISFPAIGTGNLGFPKDVVAEIMIDEVLKFSSKNPsSSLKEVRFV 158

                        170
                 ....*....|....*....
gi 226371710 468 IFPTdlEIYKAFSSEMAKR 486
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 ...
 702-821 2.97e-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: 2.97e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 702 RLFQQVPYQFCNVVCRVGFQRMYSTPCDPKYGAGIYFTKNLKNLAEKAKKISAADKLIYVFEAEVLTGFFCQGHPLNIVP 781
Cdd:cd01439    1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKADGLKEMFLARVLTGDYTQGHPGYRRP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 226371710 782 P-PLSPGAIDGHDSVVDNVSSPETFVIFSGMQAIPQYLWTC 821
Cdd:cd01439   81 PlKPSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
PRK00431 PRK00431
ADP-ribose-binding protein;
118-291 5.96e-45

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 159.62  E-value: 5.96e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 118 IELSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQFVARYGKVSAGEIAVTGAGRLPCKQIIHAV 197
Cdd:PRK00431   3 MRIEVVQGDITELEVDAIVNAANSSLLGGGGVDGAIHRAAGPEILEECRELRQQQGPCPTGEAVITSAGRLPAKYVIHTV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 198 GPRWM-EWDKQgcTGKLQRAIVSILNYViyKNTHIKTVAIPALSSGIFQFPLNLCTKTIVETIRVSLQGKpmmSNLKEIH 276
Cdd:PRK00431  83 GPVWRgGEDNE--AELLASAYRNSLRLA--AELGLRSIAFPAISTGVYGYPLEDAARIAVKTVREFLTRH---KSPEEVY 155

                        170
                 ....*....|....*
gi 226371710 277 LVSNEDPTVAAFKAA 291
Cdd:PRK00431 156 FVCYDEEAYRLYERL 170
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 120-291 3.35e-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: 3.35e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 120 LSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQFVaRYGKVSAGEIAVTGAGRLPCKQIIHAVGP 199
Cdd:COG2110    1 IEIVQGDITELDVDAIVNAANSSLLGGGGVAGAIHRAAGPELLEECRRLC-KQGGCPTGEAVITPAGNLPAKYVIHTVGP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 200 RWmEWDKQGCTGKLQRAIVSILNyvIYKNTHIKTVAIPALSSGIFQFPLNLCTKTIVETIRVSLQGKPmmsNLKEIHLVS 279
Cdd:COG2110   80 VW-RGGGPSEEELLASCYRNSLE--LAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFLEEHP---SLEEVRFVL 153

                        170
                 ....*....|..
gi 226371710 280 NEDPTVAAFKAA 291
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 ...
 136-255 1.06e-37

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: 1.06e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710  136 VNAANEDLLHGGGLALALVKAGGFEIQEESKQFVAryGKVSAGEIAVTGAGRLPCKQIIHAVGPRWMEWDKQGCTGKLQR 215
Cdd:pfam01661   1 VNAANSRLLGGGGVAGAIHRAAGPELLEECRELKK--GGCPTGEAVVTPGGNLPAKYVIHTVGPTWRHGGSHGEEELLES 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 226371710  216 AIVSILNYViyKNTHIKTVAIPALSSGIFQFPLNLCTKTI 255
Cdd:pfam01661  79 CYRNALALA--EELGIKSIAFPAISTGIYGFPWEEAARIA 116
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 119-255 1.33e-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: 1.33e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710   119 ELSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQfVARYGKVSAGEIAVTGAGRLPCKQIIHAVG 198
Cdd:smart00506   1 ILKVVKGDITKPRADAIVNAANSDGAHGGGVAGAIARAAGKALSKEEVR-KLAGGECPVGTAVVTEGGNLPAKYVIHAVG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 226371710   199 PRWMEwDKQGCTGKLQRAIVSILNYVIYKNthIKTVAIPALSSGIFQFPLNLCTKTI 255
Cdd:smart00506  80 PRASG-HSKEGFELLENAYRNCLELAIELG--ITSVALPLIGTGIYGVPKDRSAQAL 133
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 319-478 4.10e-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: 4.10e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 319 LQIVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEFLAT-KAKQFQRSQLVlVTKGFNLFCKYIYHVL-- 395
Cdd:COG2110    1 IEIVQGDITELDVDAIVNAANSSLLGGGGVAGAIHRAAGPELLEECRRLcKQGGCPTGEAV-ITPAGNLPAKYVIHTVgp 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 396 -WHSEFP-KPQILKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILFDEVLTFAKDHVKHQlTVKFVIF-PTD 472
Cdd:COG2110   80 vWRGGGPsEEELLASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFLEEHPSLE-EVRFVLFdEED 158


                 ....*.
gi 226371710 473 LEIYKA 478
Cdd:COG2110  159 YEAYRR 164
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 319-446 1.04e-20

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: 1.04e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710   319 LQIVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEFLATKAKQFQRSQLVLVTKGFNLFCKYIYHVL--- 395
Cdd:smart00506   2 LKVVKGDITKPRADAIVNAANSDGAHGGGVAGAIARAAGKALSKEEVRKLAGGECPVGTAVVTEGGNLPAKYVIHAVgpr 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 226371710   396 ----WHSEFpkpQILKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEIL 446
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 ...
 335-446 3.17e-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: 3.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710  335 VNSVNPHDITVGPVAKSILQQAGVEMKSEflaTKAKQFQRSQL--VLVTKGFNLFCKYIYHV---LWHSEFPK--PQILK 407
Cdd:pfam01661   1 VNAANSRLLGGGGVAGAIHRAAGPELLEE---CRELKKGGCPTgeAVVTPGGNLPAKYVIHTvgpTWRHGGSHgeEELLE 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 226371710  408 HAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEIL 446
Cdd:pfam01661  78 SCYRNALALAEELGIKSIAFPAISTGIYGFPWEEAARIA 116
PRK04143 PRK04143
protein-ADP-ribose hydrolase;
380-477 2.29e-07

protein-ADP-ribose hydrolase;


Pssm-ID: 235225  Cd Length: 264  Bit Score: 53.06  E-value: 2.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 380 VTKGFNLFCKYIYHVLwhsefpKPQI------------LKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILF 447
Cdd:PRK04143 153 ITRAYNLPAKYVIHTV------GPIIrkqpvspiradlLASCYRSCLKLAEKAGLKSIAFCCISTGVFGFPKEEAAEIAI 226

                         90       100       110
                 ....*....|....*....|....*....|.
gi 226371710 448 DEVLTFAKDHvKHQLTVKFVIF-PTDLEIYK 477
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 ...
 117-277 7.40e-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: 7.40e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 117 RIELSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQFVARYGKVSAGEIAVTGAGRLPCKQIIHA 196
Cdd:cd02907    1 GIKVSVYKGDITKEKVDAIVNAANERLKHGGGVAGAISKAGGPEIQEECDKYIKKNGKLRVGEVVVTSAGKLPCKYVIHA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 197 VGPRWMEWDKQGCTGKLQRAIVSILNYVIYKNthIKTVAIPALSSGIFQFPLNLCTKTIVETIRvSLQGKPMMSNLKEIH 276
Cdd:cd02907   81 VGPRWSGGSKEECEDLLYKAVLNSLEEAEELK--ATSIAIPAISSGIFGFPLDLCAEAIVEAIK-DFSESNSSSSLKEIR 157


                 .
gi 226371710 277 L 277
Cdd:cd02907  158 L 158
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 310-486 1.25e-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: 214.04  E-value: 1.25e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 310 NAMVVNNLTLQIVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEfLATKAKQFQrSQLVLVTKGFNLFCK 389
Cdd:cd02903    1 YTMKIGGITVQLVKGDITKEKTDVIVNSVSSDLLLKGGVSKAILKAAGPELQDE-CANQGKQPA-SGDVIVTSGGNLPCK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 390 YIYHVLWHSEFPK-PQILKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILFDEVLTFAKDHV-KHQLTVKFV 467
Cdd:cd02903   79 YVYHVVLPHYNPGnEKTLKDIVRKCLEKAENYKMSSISFPAIGTGNLGFPKDVVAEIMIDEVLKFSSKNPsSSLKEVRFV 158

                        170
                 ....*....|....*....
gi 226371710 468 IFPTdlEIYKAFSSEMAKR 486
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 ...
 702-821 2.97e-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: 2.97e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 702 RLFQQVPYQFCNVVCRVGFQRMYSTPCDPKYGAGIYFTKNLKNLAEKAKKISAADKLIYVFEAEVLTGFFCQGHPLNIVP 781
Cdd:cd01439    1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKADGLKEMFLARVLTGDYTQGHPGYRRP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 226371710 782 P-PLSPGAIDGHDSVVDNVSSPETFVIFSGMQAIPQYLWTC 821
Cdd:cd01439   81 PlKPSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
PRK00431 PRK00431
ADP-ribose-binding protein;
118-291 5.96e-45

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 159.62  E-value: 5.96e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 118 IELSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQFVARYGKVSAGEIAVTGAGRLPCKQIIHAV 197
Cdd:PRK00431   3 MRIEVVQGDITELEVDAIVNAANSSLLGGGGVDGAIHRAAGPEILEECRELRQQQGPCPTGEAVITSAGRLPAKYVIHTV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 198 GPRWM-EWDKQgcTGKLQRAIVSILNYViyKNTHIKTVAIPALSSGIFQFPLNLCTKTIVETIRVSLQGKpmmSNLKEIH 276
Cdd:PRK00431  83 GPVWRgGEDNE--AELLASAYRNSLRLA--AELGLRSIAFPAISTGVYGYPLEDAARIAVKTVREFLTRH---KSPEEVY 155

                        170
                 ....*....|....*
gi 226371710 277 LVSNEDPTVAAFKAA 291
Cdd:PRK00431 156 FVCYDEEAYRLYERL 170
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 120-291 3.35e-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: 3.35e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 120 LSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQFVaRYGKVSAGEIAVTGAGRLPCKQIIHAVGP 199
Cdd:COG2110    1 IEIVQGDITELDVDAIVNAANSSLLGGGGVAGAIHRAAGPELLEECRRLC-KQGGCPTGEAVITPAGNLPAKYVIHTVGP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 200 RWmEWDKQGCTGKLQRAIVSILNyvIYKNTHIKTVAIPALSSGIFQFPLNLCTKTIVETIRVSLQGKPmmsNLKEIHLVS 279
Cdd:COG2110   80 VW-RGGGPSEEELLASCYRNSLE--LAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFLEEHP---SLEEVRFVL 153

                        170
                 ....*....|..
gi 226371710 280 NEDPTVAAFKAA 291
Cdd:COG2110  154 FDEEDYEAYRRA 165
Macro_SF cd02749
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 332-449 8.51e-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: 8.51e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 332 DVIVNSVNPHDITVGPVAKSILQQAGVEMKSEFLATKAKQFQRSQLVLVTKGFNLFCKYIYHVLWHSEFPKP---QILKH 408
Cdd:cd02749    1 DAIVNPANNDLYLGGGVAKAISKKAGGDLQEECEERKKNGYLKVGEVAVTKGGNLPARYIIHVVGPVASSKKktyEPLKK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 226371710 409 AMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILFDE 449
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 ...
 136-255 1.06e-37

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: 1.06e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710  136 VNAANEDLLHGGGLALALVKAGGFEIQEESKQFVAryGKVSAGEIAVTGAGRLPCKQIIHAVGPRWMEWDKQGCTGKLQR 215
Cdd:pfam01661   1 VNAANSRLLGGGGVAGAIHRAAGPELLEECRELKK--GGCPTGEAVVTPGGNLPAKYVIHTVGPTWRHGGSHGEEELLES 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 226371710  216 AIVSILNYViyKNTHIKTVAIPALSSGIFQFPLNLCTKTI 255
Cdd:pfam01661  79 CYRNALALA--EELGIKSIAFPAISTGIYGFPWEEAARIA 116
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 119-255 1.33e-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: 1.33e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710   119 ELSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQfVARYGKVSAGEIAVTGAGRLPCKQIIHAVG 198
Cdd:smart00506   1 ILKVVKGDITKPRADAIVNAANSDGAHGGGVAGAIARAAGKALSKEEVR-KLAGGECPVGTAVVTEGGNLPAKYVIHAVG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 226371710   199 PRWMEwDKQGCTGKLQRAIVSILNYVIYKNthIKTVAIPALSSGIFQFPLNLCTKTI 255
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 ...
 120-260 9.09e-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: 9.09e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 120 LSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQFvarYGKVSAGEIAVTGAGRLPCKQIIHAVGP 199
Cdd:cd02908    2 ISLWRGDITKLEVDAIVNAANSSLLGGGGVDGAIHRAAGPELLEECRKL---GGVCPTGEAKITPGYNLPAKYVIHTVGP 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226371710 200 RWmEWDKQGCTGKLQRAIVSILNYVIYKNthIKTVAIPALSSGIFQFPLNLCTKTIVETIR 260
Cdd:cd02908   79 IG-EGGVEEEPELLASCYRSSLELALENG--LKSIAFPCISTGIYGYPNEEAAEIALNTVR 136
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 319-478 4.10e-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: 4.10e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 319 LQIVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEFLAT-KAKQFQRSQLVlVTKGFNLFCKYIYHVL-- 395
Cdd:COG2110    1 IEIVQGDITELDVDAIVNAANSSLLGGGGVAGAIHRAAGPELLEECRRLcKQGGCPTGEAV-ITPAGNLPAKYVIHTVgp 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 396 -WHSEFP-KPQILKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILFDEVLTFAKDHVKHQlTVKFVIF-PTD 472
Cdd:COG2110   80 vWRGGGPsEEELLASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFLEEHPSLE-EVRFVLFdEED 158


                 ....*.
gi 226371710 473 LEIYKA 478
Cdd:COG2110  159 YEAYRR 164
Macro_H2A-like cd02904
macrodomain, macroH2A-like family; Macrodomains are found in a variety of proteins with ...
 120-278 3.03e-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: 100.85  E-value: 3.03e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 120 LSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQFVARYGKVSAGEIAVTGAGRLPCKQIIHAVGP 199
Cdd:cd02904   20 LTVVQGDIASIKADAIVHPTNATFYLGGEVGSALEKAGGKEFVEEVKELRKSNGPLEVAGAAISPGHNLPAKFVIHCNSP 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 200 RWMEWDkqgCTGKLQRAIVSILNYVIYKNthIKTVAIPALSSGIFQFPLNLCTKTIVETIR---VSLqgkpMMSNLKEIH 276
Cdd:cd02904  100 SWGSDK---CEELLEKTVKNCLALADEKK--LKSVAFPSIGSGRNGFPKQTAAQTILKAISnyfVSV----MSSSLKQIY 170


                 ..
gi 226371710 277 LV 278
Cdd:cd02904  171 FV 172
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 116-288 1.02e-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: 1.02e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 116 PRIELSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQfvaRYGKVSAGEIAVTGAGRLPCKQIIH 195
Cdd:cd02903    6 GGITVQLVKGDITKEKTDVIVNSVSSDLLLKGGVSKAILKAAGPELQDECAN---QGKQPASGDVIVTSGGNLPCKYVYH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 196 AVGPRWMEWDKQGctgkLQRAIVSILNYViyKNTHIKTVAIPALSSGIFQFPLNLCTKTIVETIRVSLQGKPmMSNLKEI 275
Cdd:cd02903   83 VVLPHYNPGNEKT----LKDIVRKCLEKA--ENYKMSSISFPAIGTGNLGFPKDVVAEIMIDEVLKFSSKNP-SSSLKEV 155

                        170
                 ....*....|...
gi 226371710 276 HLVSNEDPTVAAF 288
Cdd:cd02903  156 RFVIFPPETLQAF 168
Macro_SF cd02749
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 133-258 1.76e-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: 93.62  E-value: 1.76e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 133 DAVVNAANEDLLHGGGLALALVKAGGFEIQEESkQFVARYGKVSAGEIAVTGAGRLPCKQIIHAVGPRWMEWDKqgCTGK 212
Cdd:cd02749    1 DAIVNPANNDLYLGGGVAKAISKKAGGDLQEEC-EERKKNGYLKVGEVAVTKGGNLPARYIIHVVGPVASSKKK--TYEP 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 226371710 213 LQRAIVSILNYVIYKNthIKTVAIPALSSGIFQFPLNLCTKTIVET 258
Cdd:cd02749   78 LKKCVKNCLSLADEKG--LKSVAFPAIGTGIAGFPPEEAARIMLEA 121
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 319-446 1.04e-20

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: 1.04e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710   319 LQIVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEFLATKAKQFQRSQLVLVTKGFNLFCKYIYHVL--- 395
Cdd:smart00506   2 LKVVKGDITKPRADAIVNAANSDGAHGGGVAGAIARAAGKALSKEEVRKLAGGECPVGTAVVTEGGNLPAKYVIHAVgpr 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 226371710   396 ----WHSEFpkpQILKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEIL 446
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 ...
 133-248 1.09e-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: 1.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 133 DAVVNAANEDLLHGGGLALALVKAGGFEIQEESKqFVARYGKVSAGEIAVTgAGRLPCKQIIHAVGPRwmeWDKQGCTGK 212
Cdd:cd21557    2 DVVVNAANENLKHGGGVAGAIYKATGGAFQKESD-YIKKNGPLKVGTAVLL-PGHGLAKNIIHVVGPR---KRKGQDDQL 76

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 226371710 213 LQRAivsilnyviYKNTH--IKTVAIPALSSGIFQFPL 248
Cdd:cd21557   77 LAAA---------YKAVNkeYGSVLTPLLSAGIFGVPP 105
Macro_Ttha0132-like cd03330
Macrodomain, uncharacterized family similar to Thermus thermophilus hypothetical protein ...
 119-265 4.30e-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: 4.30e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 119 ELSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESkqfvARYGKVSAGEIAVTGAGRLPCKQIIHAVG 198
Cdd:cd03330    1 RLIVVQGDITEQDADAIVNAANRRLLMGSGVAGAIKRKGGEEIEREA----MRKGPIRVGEAVETGAGKLPAKYVIHAAV 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226371710 199 prwMEWDKQGCTGKLQRAIVSILNYVIYKNthIKTVAIPALSSGIFQFPLNLCTKTIVETIRVSLQG 265
Cdd:cd03330   77 ---MGMPGRSSEESIRDATRNALAKAEELG--LESVAFPAIGTGVGGFPVEEVARIMLEEIKKCDPP 138
Macro_OAADPr_deacetylase cd02908
macrodomain, O-acetyl-ADP-ribose (OAADPr) family; Macrodomains are found in a variety of ...
 321-479 2.10e-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: 2.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 321 IVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSE------FLAT-KAKqfqrsqlvlVTKGFNLFCKYIYH 393
Cdd:cd02908    4 LWRGDITKLEVDAIVNAANSSLLGGGGVDGAIHRAAGPELLEEcrklggVCPTgEAK---------ITPGYNLPAKYVIH 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 394 V---LWHSEFPK-PQILKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILFDEVLTFAKDHvKHQLTVKFVIF 469
Cdd:cd02908   75 TvgpIGEGGVEEePELLASCYRSSLELALENGLKSIAFPCISTGIYGYPNEEAAEIALNTVREWLEEH-DKIDRIIFVVF 153

                        170
                 ....*....|.
gi 226371710 470 -PTDLEIYKAF 479
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 ...
 335-446 3.17e-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: 3.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710  335 VNSVNPHDITVGPVAKSILQQAGVEMKSEflaTKAKQFQRSQL--VLVTKGFNLFCKYIYHV---LWHSEFPK--PQILK 407
Cdd:pfam01661   1 VNAANSRLLGGGGVAGAIHRAAGPELLEE---CRELKKGGCPTgeAVVTPGGNLPAKYVIHTvgpTWRHGGSHgeEELLE 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 226371710  408 HAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEIL 446
Cdd:pfam01661  78 SCYRNALALAEELGIKSIAFPAISTGIYGFPWEEAARIA 116
Macro_GDAP2-like cd02905
macrodomain, GDAP2-like family; Macrodomains are found in a variety of proteins with diverse ...
 120-260 3.50e-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: 3.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 120 LSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEEskqfVARYGKVSAGEIAVTGAGRLPCKQIIHAVGP 199
Cdd:cd02905    3 IVLWDGDLTLLNVDAIVNSTNESLTDKSPISDRLFLAAGPELREE----LAKLGGCRTGEAKLTKGYNLPARYVIHTVGP 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226371710 200 RWMEwdkqgctgKLQRAIVSILnYVIYKNT-------HIKTVAIPALSSGIFQFPLNLCTKTIVETIR 260
Cdd:cd02905   79 RYNE--------KYRTAAESAL-YSCYRNVlqlakehKLRSVAFPVIHSERRGYPLEDGAHIALRTVR 137
Macro_H2A-like cd02904
macrodomain, macroH2A-like family; Macrodomains are found in a variety of proteins with ...
 318-485 4.99e-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: 4.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 318 TLQIVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEFLATKAKQfqrSQL----VLVTKGFNLFCKYIYH 393
Cdd:cd02904   19 KLTVVQGDIASIKADAIVHPTNATFYLGGEVGSALEKAGGKEFVEEVKELRKSN---GPLevagAAISPGHNLPAKFVIH 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 394 V---LWHSEFPKPQiLKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEIL-------FDEVLTfakDHVKhqlT 463
Cdd:cd02904   96 CnspSWGSDKCEEL-LEKTVKNCLALADEKKLKSVAFPSIGSGRNGFPKQTAAQTIlkaisnyFVSVMS---SSLK---Q 168

                        170       180
                 ....*....|....*....|..
gi 226371710 464 VKFVIFptDLEIYKAFSSEMAK 485
Cdd:cd02904  169 IYFVLF--DMESIGIYTSELAK 188
Macro_Ttha0132-like cd03330
Macrodomain, uncharacterized family similar to Thermus thermophilus hypothetical protein ...
 319-456 1.93e-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: 1.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 319 LQIVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEFLAtkaKQFQRSQLVLVTKGFNLFCKYIYHVLWHS 398
Cdd:cd03330    2 LIVVQGDITEQDADAIVNAANRRLLMGSGVAGAIKRKGGEEIEREAMR---KGPIRVGEAVETGAGKLPAKYVIHAAVMG 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 399 EFPK--PQILKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILFDEVLTFAKD 456
Cdd:cd03330   79 MPGRssEESIRDATRNALAKAEELGLESVAFPAIGTGVGGFPVEEVARIMLEEIKKCDPP 138
PRK04143 PRK04143
protein-ADP-ribose hydrolase;
120-260 1.02e-10

protein-ADP-ribose hydrolase;


Pssm-ID: 235225  Cd Length: 264  Bit Score: 63.08  E-value: 1.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 120 LSVWKDDLTTHAVDAVVNAANEDLLhGGGLAL------ALVKAGGFEIQEESKQFVARYGKVSA-GEIAVTGAGRLPCKQ 192
Cdd:PRK04143  85 IFLWQGDITRLKVDAIVNAANSRLL-GCFQPNhdcidnAIHTFAGVQLRLDCAEIMTEQGRKEAtGQAKITRAYNLPAKY 163

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226371710 193 IIHAVGPRWMEW-----DKQgctgKLQRAIVSILNyviYKNTH-IKTVAIPALSSGIFQFPLNLCTKTIVETIR 260
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 ...
 323-478 1.91e-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: 1.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 323 QGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEFLATKAkqfQRSQLVLVTKGFNLFCKYIYHVLWhsefPK 402
Cdd:cd02905    7 DGDLTLLNVDAIVNSTNESLTDKSPISDRLFLAAGPELREELAKLGG---CRTGEAKLTKGYNLPARYVIHTVG----PR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 403 PQI---------LKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILFDEVLTFAKDHVKHQLTVKFVIFPTDL 473
Cdd:cd02905   80 YNEkyrtaaesaLYSCYRNVLQLAKEHKLRSVAFPVIHSERRGYPLEDGAHIALRTVRRFLEKHGSSFEAVVFVVTEEEM 159


                 ....*
gi 226371710 474 EIYKA 478
Cdd:cd02905  160 ETYER 164
PRK04143 PRK04143
protein-ADP-ribose hydrolase;
380-477 2.29e-07

protein-ADP-ribose hydrolase;


Pssm-ID: 235225  Cd Length: 264  Bit Score: 53.06  E-value: 2.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 380 VTKGFNLFCKYIYHVLwhsefpKPQI------------LKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILF 447
Cdd:PRK04143 153 ITRAYNLPAKYVIHTV------GPIIrkqpvspiradlLASCYRSCLKLAEKAGLKSIAFCCISTGVFGFPKEEAAEIAI 226

                         90       100       110
                 ....*....|....*....|....*....|.
gi 226371710 448 DEVLTFAKDHvKHQLTVKFVIF-PTDLEIYK 477
Cdd:PRK04143 227 KTVLSWLKEN-PSKLKVVFNVFtDEDLELYQ 256
tankyrase_like cd01438
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ...
 668-820 2.23e-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: 2.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 668 VLKVEKIDNEVLMAAFQRKKKMMEEKLHRQPVSHRLFQQVPyqFCNVVCRVGFQRMYSTpCDPKYGAGIYFTKNLKNLAE 747
Cdd:cd01438   57 IIRIQKVVNKKLRERYCHRQKEIAEENHNHHNERMLFHGSP--FINAIIHKGFDERHAY-IGGMFGAGIYFAENSSKSNQ 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371710 748 KAKKI-------SAADKLIYVFEAEVLtgfFCQ-----------GHPLNIVPPplspgaidGHDSVVDNVS----SPETF 805
Cdd:cd01438  134 YVYGIgggtgcpTHKDRSCYVCHRQML---FCRvtlgksflqfsAMKMAHAPP--------GHHSVIGRPSvnglAYAEY 202

                        170
                 ....*....|....*
gi 226371710 806 VIFSGMQAIPQYLWT 820
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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