NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1917118665|ref|NP_001374809|]
View 

protein mono-ADP-ribosyltransferase PARP9 isoform f [Homo sapiens]

Protein Classification

macro domain-containing protein( domain architecture ID 10121103)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 2.53e-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: 240.08  E-value: 2.53e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 117 RIELSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQFVARYGKVSAGEIAVTGAGRLPCKQIIHA 196
Cdd:cd02907     1 GIKVSVYKGDITKEKVDAIVNAANERLKHGGGVAGAISKAGGPEIQEECDKYIKKNGKLRVGEVVVTSAGKLPCKYVIHA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 197 VGPRWMEWDKQGCTGKLQRAIVSILNYVIYKNthIKTVAIPALSSGIFQFPLNLCTKTIVETIRvSLQGKPMMSNLKEIH 276
Cdd:cd02907    81 VGPRWSGGSKEECEDLLYKAVLNSLEEAEELK--ATSIAIPAISSGIFGFPLDLCAEAIVEAIK-DFSESNSSSSLKEIR 157


                  .
gi 1917118665 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 9.66e-65

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: 212.88  E-value: 9.66e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 310 NAMVVNNLTLQIVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEfLATKAKQFQrSQLVLVTKGFNLFCK 389
Cdd:cd02903     1 YTMKIGGITVQLVKGDITKEKTDVIVNSVSSDLLLKGGVSKAILKAAGPELQDE-CANQGKQPA-SGDVIVTSGGNLPCK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 390 YIYHVLWHSEFPK-PQILKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILFDEVLTFAKDHV-KHQLTVKFV 467
Cdd:cd02903    79 YVYHVVLPHYNPGnEKTLKDIVRKCLEKAENYKMSSISFPAIGTGNLGFPKDVVAEIMIDEVLKFSSKNPsSSLKEVRFV 158

                         170
                  ....*....|....*....
gi 1917118665 468 IFPTdlEIYKAFSSEMAKR 486
Cdd:cd02903   159 IFPP--ETLQAFSDELAKR 175
ADP_ribosyl super family cl00283
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 702-730 2.14e-05

ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. Bacterial toxins are cytoplasmic and catalyze the transfer of a single ADP_ribose unit to eukaryotic elongation factor 2, halting protein synthesis and killing the cell. Poly(ADP-ribose) polymerases (PARPS 1-3, VPARP, tankyrase) catalyze the addition of up to 100 ADP_ribose units from NAD+. PARPs 1 and 2 are localized in the nucleaus, bind DNA, and are activated by DNA damage. VPARP is part of the vault ribonucleoprotein complex. Tankyrases regulates telomere length in part through poy(ADP_ribosylation) of telomere repeat binding factor 1 (TRF1). Poly(ADP-ribose) polymerase catalyses the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active.


The actual alignment was detected with superfamily member cd01439:

Pssm-ID: 444809 [Multi-domain]  Cd Length: 121  Bit Score: 44.23  E-value: 2.14e-05
                          10        20
                  ....*....|....*....|....*....
gi 1917118665 702 RLFQQVPYQFCNVVCRVGFQRMYSTPCGR 730
Cdd:cd01439     1 LLFHGTSADAVEAICRHGFDRRFCGKHGT 29
 
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 2.53e-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: 240.08  E-value: 2.53e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 117 RIELSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQFVARYGKVSAGEIAVTGAGRLPCKQIIHA 196
Cdd:cd02907     1 GIKVSVYKGDITKEKVDAIVNAANERLKHGGGVAGAISKAGGPEIQEECDKYIKKNGKLRVGEVVVTSAGKLPCKYVIHA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 197 VGPRWMEWDKQGCTGKLQRAIVSILNYVIYKNthIKTVAIPALSSGIFQFPLNLCTKTIVETIRvSLQGKPMMSNLKEIH 276
Cdd:cd02907    81 VGPRWSGGSKEECEDLLYKAVLNSLEEAEELK--ATSIAIPAISSGIFGFPLDLCAEAIVEAIK-DFSESNSSSSLKEIR 157


                  .
gi 1917118665 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 9.66e-65

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: 212.88  E-value: 9.66e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 310 NAMVVNNLTLQIVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEfLATKAKQFQrSQLVLVTKGFNLFCK 389
Cdd:cd02903     1 YTMKIGGITVQLVKGDITKEKTDVIVNSVSSDLLLKGGVSKAILKAAGPELQDE-CANQGKQPA-SGDVIVTSGGNLPCK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 390 YIYHVLWHSEFPK-PQILKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILFDEVLTFAKDHV-KHQLTVKFV 467
Cdd:cd02903    79 YVYHVVLPHYNPGnEKTLKDIVRKCLEKAENYKMSSISFPAIGTGNLGFPKDVVAEIMIDEVLKFSSKNPsSSLKEVRFV 158

                         170
                  ....*....|....*....
gi 1917118665 468 IFPTdlEIYKAFSSEMAKR 486
Cdd:cd02903   159 IFPP--ETLQAFSDELAKR 175
PRK00431 PRK00431
ADP-ribose-binding protein;
118-291 3.50e-45

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 159.62  E-value: 3.50e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 118 IELSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQFVARYGKVSAGEIAVTGAGRLPCKQIIHAV 197
Cdd:PRK00431    3 MRIEVVQGDITELEVDAIVNAANSSLLGGGGVDGAIHRAAGPEILEECRELRQQQGPCPTGEAVITSAGRLPAKYVIHTV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 198 GPRWM-EWDKQgcTGKLQRAIVSILNYViyKNTHIKTVAIPALSSGIFQFPLNLCTKTIVETIRVSLQGKpmmSNLKEIH 276
Cdd:PRK00431   83 GPVWRgGEDNE--AELLASAYRNSLRLA--AELGLRSIAFPAISTGVYGYPLEDAARIAVKTVREFLTRH---KSPEEVY 155

                         170
                  ....*....|....*
gi 1917118665 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 2.28e-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: 2.28e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 120 LSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQFVaRYGKVSAGEIAVTGAGRLPCKQIIHAVGP 199
Cdd:COG2110     1 IEIVQGDITELDVDAIVNAANSSLLGGGGVAGAIHRAAGPELLEECRRLC-KQGGCPTGEAVITPAGNLPAKYVIHTVGP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 200 RWmEWDKQGCTGKLQRAIVSILNyvIYKNTHIKTVAIPALSSGIFQFPLNLCTKTIVETIRVSLQGKPmmsNLKEIHLVS 279
Cdd:COG2110    80 VW-RGGGPSEEELLASCYRNSLE--LAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFLEEHP---SLEEVRFVL 153

                         170
                  ....*....|..
gi 1917118665 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 8.19e-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: 8.19e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 136 VNAANEDLLHGGGLALALVKAGGFEIQEESKQFVAryGKVSAGEIAVTGAGRLPCKQIIHAVGPRWMEWDKQGCTGKLQR 215
Cdd:pfam01661   1 VNAANSRLLGGGGVAGAIHRAAGPELLEECRELKK--GGCPTGEAVVTPGGNLPAKYVIHTVGPTWRHGGSHGEEELLES 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1917118665 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 1.12e-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: 1.12e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665  119 ELSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQfVARYGKVSAGEIAVTGAGRLPCKQIIHAVG 198
Cdd:smart00506   1 ILKVVKGDITKPRADAIVNAANSDGAHGGGVAGAIARAAGKALSKEEVR-KLAGGECPVGTAVVTEGGNLPAKYVIHAVG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1917118665  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 3.50e-25

O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441713  Cd Length: 168  Bit Score: 102.56  E-value: 3.50e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 319 LQIVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEFLAT-KAKQFQRSQLVlVTKGFNLFCKYIYHVL-- 395
Cdd:COG2110     1 IEIVQGDITELDVDAIVNAANSSLLGGGGVAGAIHRAAGPELLEECRRLcKQGGCPTGEAV-ITPAGNLPAKYVIHTVgp 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 396 -WHSEFP-KPQILKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILFDEVLTFAKDHVKHQlTVKFVIF-PTD 472
Cdd:COG2110    80 vWRGGGPsEEELLASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFLEEHPSLE-EVRFVLFdEED 158


                  ....*.
gi 1917118665 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 8.94e-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: 8.94e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665  319 LQIVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEFLATKAKQFQRSQLVLVTKGFNLFCKYIYHVL--- 395
Cdd:smart00506   2 LKVVKGDITKPRADAIVNAANSDGAHGGGVAGAIARAAGKALSKEEVRKLAGGECPVGTAVVTEGGNLPAKYVIHAVgpr 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1917118665  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 2.74e-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: 2.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 335 VNSVNPHDITVGPVAKSILQQAGVEMKSEflaTKAKQFQRSQL--VLVTKGFNLFCKYIYHV---LWHSEFPK--PQILK 407
Cdd:pfam01661   1 VNAANSRLLGGGGVAGAIHRAAGPELLEE---CRELKKGGCPTgeAVVTPGGNLPAKYVIHTvgpTWRHGGSHgeEELLE 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1917118665 408 HAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEIL 446
Cdd:pfam01661  78 SCYRNALALAEELGIKSIAFPAISTGIYGFPWEEAARIA 116
PRK04143 PRK04143
protein-ADP-ribose hydrolase;
380-477 2.63e-07

protein-ADP-ribose hydrolase;


Pssm-ID: 235225  Cd Length: 264  Bit Score: 52.68  E-value: 2.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 380 VTKGFNLFCKYIYHVLwhsefpKPQI------------LKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILF 447
Cdd:PRK04143  153 ITRAYNLPAKYVIHTV------GPIIrkqpvspiradlLASCYRSCLKLAEKAGLKSIAFCCISTGVFGFPKEEAAEIAI 226

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1917118665 448 DEVLTFAKDHvKHQLTVKFVIF-PTDLEIYK 477
Cdd:PRK04143  227 KTVLSWLKEN-PSKLKVVFNVFtDEDLELYQ 256
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 702-730 2.14e-05

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: 44.23  E-value: 2.14e-05
                          10        20
                  ....*....|....*....|....*....
gi 1917118665 702 RLFQQVPYQFCNVVCRVGFQRMYSTPCGR 730
Cdd:cd01439     1 LLFHGTSADAVEAICRHGFDRRFCGKHGT 29
 
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 2.53e-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: 240.08  E-value: 2.53e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 117 RIELSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQFVARYGKVSAGEIAVTGAGRLPCKQIIHA 196
Cdd:cd02907     1 GIKVSVYKGDITKEKVDAIVNAANERLKHGGGVAGAISKAGGPEIQEECDKYIKKNGKLRVGEVVVTSAGKLPCKYVIHA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 197 VGPRWMEWDKQGCTGKLQRAIVSILNYVIYKNthIKTVAIPALSSGIFQFPLNLCTKTIVETIRvSLQGKPMMSNLKEIH 276
Cdd:cd02907    81 VGPRWSGGSKEECEDLLYKAVLNSLEEAEELK--ATSIAIPAISSGIFGFPLDLCAEAIVEAIK-DFSESNSSSSLKEIR 157


                  .
gi 1917118665 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 9.66e-65

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: 212.88  E-value: 9.66e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 310 NAMVVNNLTLQIVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEfLATKAKQFQrSQLVLVTKGFNLFCK 389
Cdd:cd02903     1 YTMKIGGITVQLVKGDITKEKTDVIVNSVSSDLLLKGGVSKAILKAAGPELQDE-CANQGKQPA-SGDVIVTSGGNLPCK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 390 YIYHVLWHSEFPK-PQILKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILFDEVLTFAKDHV-KHQLTVKFV 467
Cdd:cd02903    79 YVYHVVLPHYNPGnEKTLKDIVRKCLEKAENYKMSSISFPAIGTGNLGFPKDVVAEIMIDEVLKFSSKNPsSSLKEVRFV 158

                         170
                  ....*....|....*....
gi 1917118665 468 IFPTdlEIYKAFSSEMAKR 486
Cdd:cd02903   159 IFPP--ETLQAFSDELAKR 175
PRK00431 PRK00431
ADP-ribose-binding protein;
118-291 3.50e-45

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 159.62  E-value: 3.50e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 118 IELSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQFVARYGKVSAGEIAVTGAGRLPCKQIIHAV 197
Cdd:PRK00431    3 MRIEVVQGDITELEVDAIVNAANSSLLGGGGVDGAIHRAAGPEILEECRELRQQQGPCPTGEAVITSAGRLPAKYVIHTV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 198 GPRWM-EWDKQgcTGKLQRAIVSILNYViyKNTHIKTVAIPALSSGIFQFPLNLCTKTIVETIRVSLQGKpmmSNLKEIH 276
Cdd:PRK00431   83 GPVWRgGEDNE--AELLASAYRNSLRLA--AELGLRSIAFPAISTGVYGYPLEDAARIAVKTVREFLTRH---KSPEEVY 155

                         170
                  ....*....|....*
gi 1917118665 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 2.28e-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: 2.28e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 120 LSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQFVaRYGKVSAGEIAVTGAGRLPCKQIIHAVGP 199
Cdd:COG2110     1 IEIVQGDITELDVDAIVNAANSSLLGGGGVAGAIHRAAGPELLEECRRLC-KQGGCPTGEAVITPAGNLPAKYVIHTVGP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 200 RWmEWDKQGCTGKLQRAIVSILNyvIYKNTHIKTVAIPALSSGIFQFPLNLCTKTIVETIRVSLQGKPmmsNLKEIHLVS 279
Cdd:COG2110    80 VW-RGGGPSEEELLASCYRNSLE--LAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFLEEHP---SLEEVRFVL 153

                         170
                  ....*....|..
gi 1917118665 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 8.53e-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: 145.23  E-value: 8.53e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 332 DVIVNSVNPHDITVGPVAKSILQQAGVEMKSEFLATKAKQFQRSQLVLVTKGFNLFCKYIYHVLWHSEFPKP---QILKH 408
Cdd:cd02749     1 DAIVNPANNDLYLGGGVAKAISKKAGGDLQEECEERKKNGYLKVGEVAVTKGGNLPARYIIHVVGPVASSKKktyEPLKK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1917118665 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 8.19e-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: 8.19e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 136 VNAANEDLLHGGGLALALVKAGGFEIQEESKQFVAryGKVSAGEIAVTGAGRLPCKQIIHAVGPRWMEWDKQGCTGKLQR 215
Cdd:pfam01661   1 VNAANSRLLGGGGVAGAIHRAAGPELLEECRELKK--GGCPTGEAVVTPGGNLPAKYVIHTVGPTWRHGGSHGEEELLES 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1917118665 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 1.12e-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: 1.12e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665  119 ELSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQfVARYGKVSAGEIAVTGAGRLPCKQIIHAVG 198
Cdd:smart00506   1 ILKVVKGDITKPRADAIVNAANSDGAHGGGVAGAIARAAGKALSKEEVR-KLAGGECPVGTAVVTEGGNLPAKYVIHAVG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1917118665  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 7.67e-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: 7.67e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 120 LSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQFvarYGKVSAGEIAVTGAGRLPCKQIIHAVGP 199
Cdd:cd02908     2 ISLWRGDITKLEVDAIVNAANSSLLGGGGVDGAIHRAAGPELLEECRKL---GGVCPTGEAKITPGYNLPAKYVIHTVGP 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1917118665 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 3.50e-25

O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441713  Cd Length: 168  Bit Score: 102.56  E-value: 3.50e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 319 LQIVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEFLAT-KAKQFQRSQLVlVTKGFNLFCKYIYHVL-- 395
Cdd:COG2110     1 IEIVQGDITELDVDAIVNAANSSLLGGGGVAGAIHRAAGPELLEECRRLcKQGGCPTGEAV-ITPAGNLPAKYVIHTVgp 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 396 -WHSEFP-KPQILKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILFDEVLTFAKDHVKHQlTVKFVIF-PTD 472
Cdd:COG2110    80 vWRGGGPsEEELLASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFLEEHPSLE-EVRFVLFdEED 158


                  ....*.
gi 1917118665 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 2.55e-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: 2.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 120 LSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQFVARYGKVSAGEIAVTGAGRLPCKQIIHAVGP 199
Cdd:cd02904    20 LTVVQGDIASIKADAIVHPTNATFYLGGEVGSALEKAGGKEFVEEVKELRKSNGPLEVAGAAISPGHNLPAKFVIHCNSP 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 200 RWMEWDkqgCTGKLQRAIVSILNYVIYKNthIKTVAIPALSSGIFQFPLNLCTKTIVETIR---VSLqgkpMMSNLKEIH 276
Cdd:cd02904   100 SWGSDK---CEELLEKTVKNCLALADEKK--LKSVAFPSIGSGRNGFPKQTAAQTILKAISnyfVSV----MSSSLKQIY 170


                  ..
gi 1917118665 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 1.43e-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: 98.09  E-value: 1.43e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 116 PRIELSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQfvaRYGKVSAGEIAVTGAGRLPCKQIIH 195
Cdd:cd02903     6 GGITVQLVKGDITKEKTDVIVNSVSSDLLLKGGVSKAILKAAGPELQDECAN---QGKQPASGDVIVTSGGNLPCKYVYH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 196 AVGPRWMEWDKQGctgkLQRAIVSILNYViyKNTHIKTVAIPALSSGIFQFPLNLCTKTIVETIRVSLQGKPmMSNLKEI 275
Cdd:cd02903    83 VVLPHYNPGNEKT----LKDIVRKCLEKA--ENYKMSSISFPAIGTGNLGFPKDVVAEIMIDEVLKFSSKNP-SSSLKEV 155

                         170
                  ....*....|...
gi 1917118665 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 1.97e-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: 1.97e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 133 DAVVNAANEDLLHGGGLALALVKAGGFEIQEESkQFVARYGKVSAGEIAVTGAGRLPCKQIIHAVGPRWMEWDKqgCTGK 212
Cdd:cd02749     1 DAIVNPANNDLYLGGGVAKAISKKAGGDLQEEC-EERKKNGYLKVGEVAVTKGGNLPARYIIHVVGPVASSKKK--TYEP 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1917118665 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 8.94e-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: 8.94e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665  319 LQIVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEFLATKAKQFQRSQLVLVTKGFNLFCKYIYHVL--- 395
Cdd:smart00506   2 LKVVKGDITKPRADAIVNAANSDGAHGGGVAGAIARAAGKALSKEEVRKLAGGECPVGTAVVTEGGNLPAKYVIHAVgpr 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1917118665  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 9.42e-21

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: 9.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 133 DAVVNAANEDLLHGGGLALALVKAGGFEIQEESKqFVARYGKVSAGEIAVTgAGRLPCKQIIHAVGPRwmeWDKQGCTGK 212
Cdd:cd21557     2 DVVVNAANENLKHGGGVAGAIYKATGGAFQKESD-YIKKNGPLKVGTAVLL-PGHGLAKNIIHVVGPR---KRKGQDDQL 76

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1917118665 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 3.69e-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: 3.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 119 ELSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESkqfvARYGKVSAGEIAVTGAGRLPCKQIIHAVG 198
Cdd:cd03330     1 RLIVVQGDITEQDADAIVNAANRRLLMGSGVAGAIKRKGGEEIEREA----MRKGPIRVGEAVETGAGKLPAKYVIHAAV 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1917118665 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 1.80e-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: 1.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 321 IVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSE------FLAT-KAKqfqrsqlvlVTKGFNLFCKYIYH 393
Cdd:cd02908     4 LWRGDITKLEVDAIVNAANSSLLGGGGVDGAIHRAAGPELLEEcrklggVCPTgEAK---------ITPGYNLPAKYVIH 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 394 V---LWHSEFPK-PQILKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILFDEVLTFAKDHvKHQLTVKFVIF 469
Cdd:cd02908    75 TvgpIGEGGVEEePELLASCYRSSLELALENGLKSIAFPCISTGIYGYPNEEAAEIALNTVREWLEEH-DKIDRIIFVVF 153

                         170
                  ....*....|.
gi 1917118665 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 2.74e-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: 2.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 335 VNSVNPHDITVGPVAKSILQQAGVEMKSEflaTKAKQFQRSQL--VLVTKGFNLFCKYIYHV---LWHSEFPK--PQILK 407
Cdd:pfam01661   1 VNAANSRLLGGGGVAGAIHRAAGPELLEE---CRELKKGGCPTgeAVVTPGGNLPAKYVIHTvgpTWRHGGSHgeEELLE 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1917118665 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 2.99e-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: 2.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 120 LSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEEskqfVARYGKVSAGEIAVTGAGRLPCKQIIHAVGP 199
Cdd:cd02905     3 IVLWDGDLTLLNVDAIVNSTNESLTDKSPISDRLFLAAGPELREE----LAKLGGCRTGEAKLTKGYNLPARYVIHTVGP 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1917118665 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 4.09e-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: 4.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 318 TLQIVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEFLATKAKQfqrSQL----VLVTKGFNLFCKYIYH 393
Cdd:cd02904    19 KLTVVQGDIASIKADAIVHPTNATFYLGGEVGSALEKAGGKEFVEEVKELRKSN---GPLevagAAISPGHNLPAKFVIH 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 394 V---LWHSEFPKPQiLKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEIL-------FDEVLTfakDHVKhqlT 463
Cdd:cd02904    96 CnspSWGSDKCEEL-LEKTVKNCLALADEKKLKSVAFPSIGSGRNGFPKQTAAQTIlkaisnyFVSVMS---SSLK---Q 168

                         170       180
                  ....*....|....*....|..
gi 1917118665 464 VKFVIFptDLEIYKAFSSEMAK 485
Cdd:cd02904   169 IYFVLF--DMESIGIYTSELAK 188
Macro_Ttha0132-like cd03330
Macrodomain, uncharacterized family similar to Thermus thermophilus hypothetical protein ...
 319-456 1.66e-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: 1.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 319 LQIVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEFLAtkaKQFQRSQLVLVTKGFNLFCKYIYHVLWHS 398
Cdd:cd03330     2 LIVVQGDITEQDADAIVNAANRRLLMGSGVAGAIKRKGGEEIEREAMR---KGPIRVGEAVETGAGKLPAKYVIHAAVMG 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 399 EFPK--PQILKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILFDEVLTFAKD 456
Cdd:cd03330    79 MPGRssEESIRDATRNALAKAEELGLESVAFPAIGTGVGGFPVEEVARIMLEEIKKCDPP 138
PRK04143 PRK04143
protein-ADP-ribose hydrolase;
120-260 1.38e-10

protein-ADP-ribose hydrolase;


Pssm-ID: 235225  Cd Length: 264  Bit Score: 62.69  E-value: 1.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 120 LSVWKDDLTTHAVDAVVNAANEDLLhGGGLAL------ALVKAGGFEIQEESKQFVARYGKVSA-GEIAVTGAGRLPCKQ 192
Cdd:PRK04143   85 IFLWQGDITRLKVDAIVNAANSRLL-GCFQPNhdcidnAIHTFAGVQLRLDCAEIMTEQGRKEAtGQAKITRAYNLPAKY 163

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1917118665 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 1.63e-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: 1.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 323 QGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEFLATKAkqfQRSQLVLVTKGFNLFCKYIYHVLWhsefPK 402
Cdd:cd02905     7 DGDLTLLNVDAIVNSTNESLTDKSPISDRLFLAAGPELREELAKLGG---CRTGEAKLTKGYNLPARYVIHTVG----PR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 403 PQI---------LKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILFDEVLTFAKDHVKHQLTVKFVIFPTDL 473
Cdd:cd02905    80 YNEkyrtaaesaLYSCYRNVLQLAKEHKLRSVAFPVIHSERRGYPLEDGAHIALRTVRRFLEKHGSSFEAVVFVVTEEEM 159


                  ....*
gi 1917118665 474 EIYKA 478
Cdd:cd02905   160 ETYER 164
PRK04143 PRK04143
protein-ADP-ribose hydrolase;
380-477 2.63e-07

protein-ADP-ribose hydrolase;


Pssm-ID: 235225  Cd Length: 264  Bit Score: 52.68  E-value: 2.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118665 380 VTKGFNLFCKYIYHVLwhsefpKPQI------------LKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILF 447
Cdd:PRK04143  153 ITRAYNLPAKYVIHTV------GPIIrkqpvspiradlLASCYRSCLKLAEKAGLKSIAFCCISTGVFGFPKEEAAEIAI 226

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1917118665 448 DEVLTFAKDHvKHQLTVKFVIF-PTDLEIYK 477
Cdd:PRK04143  227 KTVLSWLKEN-PSKLKVVFNVFtDEDLELYQ 256
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 702-730 2.14e-05

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: 44.23  E-value: 2.14e-05
                          10        20
                  ....*....|....*....|....*....
gi 1917118665 702 RLFQQVPYQFCNVVCRVGFQRMYSTPCGR 730
Cdd:cd01439     1 LLFHGTSADAVEAICRHGFDRRFCGKHGT 29
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH