NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1034631478|ref|XP_016861280|]
View 

protein mono-ADP-ribosyltransferase PARP15 isoform X7 [Homo sapiens]

Protein Classification

Macro_SF and TCCD_inducible_PARP_like domain-containing protein( domain architecture ID 10206224)

Macro_SF and TCCD_inducible_PARP_like domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 411-531 7.51e-61

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: 196.00  E-value: 7.51e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478 411 LLFHGTDADSVPYVNQHGFNRSCAGKNAVSYGKGTYFAVDASYSAKDTYSKPDSNGRKHMYVVRVLTGVFTKGRAGLVTP 490
Cdd:cd01439     1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKADGLKEMFLARVLTGDYTQGHPGYRRP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1034631478 491 PPKNPHNPTDLFDSVTNNTRSPKLFVVFFDNQAYPEYLITF 531
Cdd:cd01439    81 PLKPSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
Macro_SF super family cl00019
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 221-337 7.89e-47

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


The actual alignment was detected with superfamily member cd02903:

Pssm-ID: 469581  Cd Length: 175  Bit Score: 161.27  E-value: 7.89e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478 221 YEMKIGAITFQVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQP-HRDFIITPGGCLKCKII 299
Cdd:cd02903     1 YTMKIGGITVQLVKGDITKEKTDVIVNSVSSDLLLKGGVSKAILKAAGPELQDECANQGKQPaSGDVIVTSGGNLPCKYV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1034631478 300 IHVPGGKD-------VRKTVTSVLEECEQRKYTSVSLPAIGTGNL 337
Cdd:cd02903    81 YHVVLPHYnpgnektLKDIVRKCLEKAENYKMSSISFPAIGTGNL 125
Macro_SF super family cl00019
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 88-186 3.68e-20

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


The actual alignment was detected with superfamily member cd02903:

Pssm-ID: 469581  Cd Length: 175  Bit Score: 87.69  E-value: 3.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478  88 GLNLKLISGDVLYIWADVIVNSVPMNLqLGGGPLSRAFLQKAGPMLQKELDDRRreTEEKVGNIFMTSGCNLDCKAVLHA 167
Cdd:cd02903     7 GITVQLVKGDITKEKTDVIVNSVSSDL-LLKGGVSKAILKAAGPELQDECANQG--KQPASGDVIVTSGGNLPCKYVYHV 83

                          90
                  ....*....|....*....
gi 1034631478 168 VAPYWNNGAETSWQAFLDE 186
Cdd:cd02903    84 VLPHYNPGNEKTLKDIVRK 102
 
Name Accession Description Interval E-value
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 411-531 7.51e-61

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: 196.00  E-value: 7.51e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478 411 LLFHGTDADSVPYVNQHGFNRSCAGKNAVSYGKGTYFAVDASYSAKDTYSKPDSNGRKHMYVVRVLTGVFTKGRAGLVTP 490
Cdd:cd01439     1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKADGLKEMFLARVLTGDYTQGHPGYRRP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1034631478 491 PPKNPHNPTDLFDSVTNNTRSPKLFVVFFDNQAYPEYLITF 531
Cdd:cd01439    81 PLKPSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 221-337 7.89e-47

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: 161.27  E-value: 7.89e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478 221 YEMKIGAITFQVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQP-HRDFIITPGGCLKCKII 299
Cdd:cd02903     1 YTMKIGGITVQLVKGDITKEKTDVIVNSVSSDLLLKGGVSKAILKAAGPELQDECANQGKQPaSGDVIVTSGGNLPCKYV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1034631478 300 IHVPGGKD-------VRKTVTSVLEECEQRKYTSVSLPAIGTGNL 337
Cdd:cd02903    81 YHVVLPHYnpgnektLKDIVRKCLEKAENYKMSSISFPAIGTGNL 125
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 360-531 1.23e-26

Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes 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.


Pssm-ID: 395519 [Multi-domain]  Cd Length: 195  Bit Score: 107.03  E-value: 1.23e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478 360 EYNTIKDKFTRT-----CSSYAIEKIERIQNAFLWQSYQVKKRQMdikndhknNERLLFHGTDADSVPYVNQHGF--NRS 432
Cdd:pfam00644   3 EYQIIEKYFLSThdpthGYPLFILEIFRVQRDGEWERFQPKKKLR--------NRRLLWHGSRLTNFLGILSQGLriAPP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478 433 CAGKNAVSYGKGTYFAVDASYSAKdtYSKPD-SNGRKHMYVVRVLTG------------------VFTKGRaGLVTPPPK 493
Cdd:pfam00644  75 EAPVTGYMFGKGIYFADDASKSAN--YCPPSeAHGNGLMLLSEVALGdmnelkkadyaeklppgkHSVKGL-GKTAPESF 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1034631478 494 NPHNPTDLFDSVTNNTRS----PKLFVVFFDNQAYPEYLITF 531
Cdd:pfam00644 152 VDLDGVPLGKLVATGYDSsvllYNEYVVYNVNQVRPKYLLEV 193
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 88-186 3.68e-20

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


Pssm-ID: 394874  Cd Length: 175  Bit Score: 87.69  E-value: 3.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478  88 GLNLKLISGDVLYIWADVIVNSVPMNLqLGGGPLSRAFLQKAGPMLQKELDDRRreTEEKVGNIFMTSGCNLDCKAVLHA 167
Cdd:cd02903     7 GITVQLVKGDITKEKTDVIVNSVSSDL-LLKGGVSKAILKAAGPELQDECANQG--KQPASGDVIVTSGGNLPCKYVYHV 83

                          90
                  ....*....|....*....
gi 1034631478 168 VAPYWNNGAETSWQAFLDE 186
Cdd:cd02903    84 VLPHYNPGNEKTLKDIVRK 102
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 230-336 1.01e-17

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: 80.61  E-value: 1.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478 230 FQVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQ---PHRDFIITPGGCLKCKIIIHVPG-- 304
Cdd:COG2110     1 IEIVQGDITELDVDAIVNAANSSLLGGGGVAGAIHRAAGPELLEECRRLCKQggcPTGEAVITPAGNLPAKYVIHTVGpv 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1034631478 305 ---G-----KDVRKTVTSVLEECEQRKYTSVSLPAIGTGN 336
Cdd:COG2110    81 wrgGgpseeELLASCYRNSLELAEELGIRSIAFPAIGTGV 120
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 230-336 2.68e-17

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: 78.50  E-value: 2.68e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478  230 FQVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQ---PHRDFIITPGGCLKCKIIIHVPGG- 305
Cdd:smart00506   2 LKVVKGDITKPRADAIVNAANSDGAHGGGVAGAIARAAGKALSKEEVRKLAGgecPVGTAVVTEGGNLPAKYVIHAVGPr 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1034631478  306 ---------KDVRKTVTSVLEECEQRKYTSVSLPAIGTGN 336
Cdd:smart00506  82 asghskegfELLENAYRNCLELAIELGITSVALPLIGTGI 121
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 91-179 2.13e-16

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: 76.75  E-value: 2.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478  91 LKLISGDVLYIWADVIVNSVPMNLQLGGGpLSRAFLQKAGPMLQKELDDRRRETEEKVGNIFMTSGCNLDCKAVLHAVAP 170
Cdd:COG2110     1 IEIVQGDITELDVDAIVNAANSSLLGGGG-VAGAIHRAAGPELLEECRRLCKQGGCPTGEAVITPAGNLPAKYVIHTVGP 79


                  ....*....
gi 1034631478 171 YWNNGAETS 179
Cdd:COG2110    80 VWRGGGPSE 88
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 90-172 1.12e-11

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: 62.32  E-value: 1.12e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478   90 NLKLISGDVLYIWADVIVNSVPMNLQLGGGpLSRAFLQKAGPMLQKELDDRRRETEEKVGNIFMTSGCNLDCKAVLHAVA 169
Cdd:smart00506   1 ILKVVKGDITKPRADAIVNAANSDGAHGGG-VAGAIARAAGKALSKEEVRKLAGGECPVGTAVVTEGGNLPAKYVIHAVG 79


                   ...
gi 1034631478  170 PYW 172
Cdd:smart00506  80 PRA 82
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 107-179 1.67e-11

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: 61.43  E-value: 1.67e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034631478 107 VNSVPMNLqLGGGPLSRAFLQKAGPMLQKELDDRRREtEEKVGNIFMTSGCNLDCKAVLHAVAPYWNNGAETS 179
Cdd:pfam01661   1 VNAANSRL-LGGGGVAGAIHRAAGPELLEECRELKKG-GCPTGEAVVTPGGNLPAKYVIHTVGPTWRHGGSHG 71
PRK00431 PRK00431
ADP-ribose-binding protein;
226-335 1.70e-11

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 62.94  E-value: 1.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478 226 GAITFQVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQ----PHRDFIITPGGCLKCKIIIH 301
Cdd:PRK00431    1 MGMRIEVVQGDITELEVDAIVNAANSSLLGGGGVDGAIHRAAGPEILEECRELRQQqgpcPTGEAVITSAGRLPAKYVIH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1034631478 302 VPG-----GKD-----VRKTVTSVLEECEQRKYTSVSLPAIGTG 335
Cdd:PRK00431   81 TVGpvwrgGEDneaelLASAYRNSLRLAAELGLRSIAFPAISTG 124
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 246-335 1.99e-09

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: 55.26  E-value: 1.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478 246 VNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQPHR--DFIITPGGCLKCKIIIHVPG-----------GKDVRKTV 312
Cdd:pfam01661   1 VNAANSRLLGGGGVAGAIHRAAGPELLEECRELKKGGCPtgEAVVTPGGNLPAKYVIHTVGptwrhggshgeEELLESCY 80

                          90       100
                  ....*....|....*....|...
gi 1034631478 313 TSVLEECEQRKYTSVSLPAIGTG 335
Cdd:pfam01661  81 RNALALAEELGIKSIAFPAISTG 103
PRK00431 PRK00431
ADP-ribose-binding protein;
88-177 2.39e-09

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 56.77  E-value: 2.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478  88 GLNLKLISGDVLYIWADVIVNsvPMN-LQLGGGPLSRAFLQKAGPMLQKELDDRRRETEE-KVGNIFMTSGCNLDCKAVL 165
Cdd:PRK00431    2 GMRIEVVQGDITELEVDAIVN--AANsSLLGGGGVDGAIHRAAGPEILEECRELRQQQGPcPTGEAVITSAGRLPAKYVI 79

                          90
                  ....*....|..
gi 1034631478 166 HAVAPYWNNGAE 177
Cdd:PRK00431   80 HTVGPVWRGGED 91
 
Name Accession Description Interval E-value
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 411-531 7.51e-61

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: 196.00  E-value: 7.51e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478 411 LLFHGTDADSVPYVNQHGFNRSCAGKNAVSYGKGTYFAVDASYSAKDTYSKPDSNGRKHMYVVRVLTGVFTKGRAGLVTP 490
Cdd:cd01439     1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKADGLKEMFLARVLTGDYTQGHPGYRRP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1034631478 491 PPKNPHNPTDLFDSVTNNTRSPKLFVVFFDNQAYPEYLITF 531
Cdd:cd01439    81 PLKPSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 221-337 7.89e-47

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: 161.27  E-value: 7.89e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478 221 YEMKIGAITFQVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQP-HRDFIITPGGCLKCKII 299
Cdd:cd02903     1 YTMKIGGITVQLVKGDITKEKTDVIVNSVSSDLLLKGGVSKAILKAAGPELQDECANQGKQPaSGDVIVTSGGNLPCKYV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1034631478 300 IHVPGGKD-------VRKTVTSVLEECEQRKYTSVSLPAIGTGNL 337
Cdd:cd02903    81 YHVVLPHYnpgnektLKDIVRKCLEKAENYKMSSISFPAIGTGNL 125
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 360-531 1.23e-26

Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes 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.


Pssm-ID: 395519 [Multi-domain]  Cd Length: 195  Bit Score: 107.03  E-value: 1.23e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478 360 EYNTIKDKFTRT-----CSSYAIEKIERIQNAFLWQSYQVKKRQMdikndhknNERLLFHGTDADSVPYVNQHGF--NRS 432
Cdd:pfam00644   3 EYQIIEKYFLSThdpthGYPLFILEIFRVQRDGEWERFQPKKKLR--------NRRLLWHGSRLTNFLGILSQGLriAPP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478 433 CAGKNAVSYGKGTYFAVDASYSAKdtYSKPD-SNGRKHMYVVRVLTG------------------VFTKGRaGLVTPPPK 493
Cdd:pfam00644  75 EAPVTGYMFGKGIYFADDASKSAN--YCPPSeAHGNGLMLLSEVALGdmnelkkadyaeklppgkHSVKGL-GKTAPESF 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1034631478 494 NPHNPTDLFDSVTNNTRS----PKLFVVFFDNQAYPEYLITF 531
Cdd:pfam00644 152 VDLDGVPLGKLVATGYDSsvllYNEYVVYNVNQVRPKYLLEV 193
Macro_Af1521_BAL-like cd02907
macrodomain, Af1521-like family; Macrodomains are found in a variety of proteins with diverse ...
 228-335 1.36e-23

macrodomain, Af1521-like family; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. The macrodomains in this family show similarity to Af1521, a protein from Archaeoglobus fulgidus containing a stand-alone macrodomain. Af1521 binds ADP-ribose and exhibits phosphatase activity toward ADP-ribose-1"-monophosphate (Appr-1"-p). Also included in this family are the N-terminal (or first) macrodomains of BAL (B-aggressive lymphoma) proteins which contain multiple macrodomains, such as the first macrodomain of mono-ADP-ribosyltransferase PARP14 (PARP-14, also known as ADP-ribosyltransferase diphtheria toxin-like 8, ATRD8, B aggressive lymphoma protein 2, or BAL2). Most BAL proteins also contain a C-terminal PARP active site and are also named as PARPs. Human BAL1 (or PARP-9) was originally identified as a risk-related gene in diffuse large B-cell lymphoma that promotes malignant B-cell migration. Some BAL family proteins exhibit PARP activity. Poly (ADP-ribosyl)ation is an immediate DNA-damage-dependent post-translational modification of histones and other nuclear proteins. BAL proteins may also function as transcriptional repressors.


Pssm-ID: 394877 [Multi-domain]  Cd Length: 158  Bit Score: 97.18  E-value: 1.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478 228 ITFQVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESEC-AVLAAQ---PHRDFIITPGGCLKCKIIIHV- 302
Cdd:cd02907     2 IKVSVYKGDITKEKVDAIVNAANERLKHGGGVAGAISKAGGPEIQEECdKYIKKNgklRVGEVVVTSAGKLPCKYVIHAv 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1034631478 303 -P---GGKD------VRKTVTSVLEECEQRKYTSVSLPAIGTG 335
Cdd:cd02907    82 gPrwsGGSKeecedlLYKAVLNSLEEAEELKATSIAIPAISSG 124
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 88-186 3.68e-20

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


Pssm-ID: 394874  Cd Length: 175  Bit Score: 87.69  E-value: 3.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478  88 GLNLKLISGDVLYIWADVIVNSVPMNLqLGGGPLSRAFLQKAGPMLQKELDDRRreTEEKVGNIFMTSGCNLDCKAVLHA 167
Cdd:cd02903     7 GITVQLVKGDITKEKTDVIVNSVSSDL-LLKGGVSKAILKAAGPELQDECANQG--KQPASGDVIVTSGGNLPCKYVYHV 83

                          90
                  ....*....|....*....
gi 1034631478 168 VAPYWNNGAETSWQAFLDE 186
Cdd:cd02903    84 VLPHYNPGNEKTLKDIVRK 102
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 230-336 1.01e-17

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: 80.61  E-value: 1.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478 230 FQVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQ---PHRDFIITPGGCLKCKIIIHVPG-- 304
Cdd:COG2110     1 IEIVQGDITELDVDAIVNAANSSLLGGGGVAGAIHRAAGPELLEECRRLCKQggcPTGEAVITPAGNLPAKYVIHTVGpv 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1034631478 305 ---G-----KDVRKTVTSVLEECEQRKYTSVSLPAIGTGN 336
Cdd:COG2110    81 wrgGgpseeELLASCYRNSLELAEELGIRSIAFPAIGTGV 120
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 230-336 2.68e-17

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: 78.50  E-value: 2.68e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478  230 FQVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQ---PHRDFIITPGGCLKCKIIIHVPGG- 305
Cdd:smart00506   2 LKVVKGDITKPRADAIVNAANSDGAHGGGVAGAIARAAGKALSKEEVRKLAGgecPVGTAVVTEGGNLPAKYVIHAVGPr 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1034631478  306 ---------KDVRKTVTSVLEECEQRKYTSVSLPAIGTGN 336
Cdd:smart00506  82 asghskegfELLENAYRNCLELAIELGITSVALPLIGTGI 121
Macro_Af1521_BAL-like cd02907
macrodomain, Af1521-like family; Macrodomains are found in a variety of proteins with diverse ...
 88-175 9.94e-17

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: 77.53  E-value: 9.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478  88 GLNLKLISGDVLYIWADVIVNSVPMNLQLGGGpLSRAFLQKAGPMLQKELDD-RRRETEEKVGNIFMTSGCNLDCKAVLH 166
Cdd:cd02907     1 GIKVSVYKGDITKEKVDAIVNAANERLKHGGG-VAGAISKAGGPEIQEECDKyIKKNGKLRVGEVVVTSAGKLPCKYVIH 79


                  ....*....
gi 1034631478 167 AVAPYWNNG 175
Cdd:cd02907    80 AVGPRWSGG 88
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 91-179 2.13e-16

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: 76.75  E-value: 2.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478  91 LKLISGDVLYIWADVIVNSVPMNLQLGGGpLSRAFLQKAGPMLQKELDDRRRETEEKVGNIFMTSGCNLDCKAVLHAVAP 170
Cdd:COG2110     1 IEIVQGDITELDVDAIVNAANSSLLGGGG-VAGAIHRAAGPELLEECRRLCKQGGCPTGEAVITPAGNLPAKYVIHTVGP 79


                  ....*....
gi 1034631478 171 YWNNGAETS 179
Cdd:COG2110    80 VWRGGGPSE 88
Macro_Ttha0132-like cd03330
Macrodomain, uncharacterized family similar to Thermus thermophilus hypothetical protein ...
 230-335 4.08e-14

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: 69.77  E-value: 4.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478 230 FQVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQPHRDFIITPGGCLKCKIIIHVPGGKD-- 307
Cdd:cd03330     2 LIVVQGDITEQDADAIVNAANRRLLMGSGVAGAIKRKGGEEIEREAMRKGPIRVGEAVETGAGKLPAKYVIHAAVMGMpg 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1034631478 308 ------VRKTVTSVLEECEQRKYTSVSLPAIGTG 335
Cdd:cd03330    82 rsseesIRDATRNALAKAEELGLESVAFPAIGTG 115
Macro_SF cd02749
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 243-336 5.16e-14

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: 68.58  E-value: 5.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478 243 DVIVNSTARTFNRKSGVSRAILEGAGQAVESECA-VLAAQPHR--DFIITPGGCLKCKIIIHVPGGK---------DVRK 310
Cdd:cd02749     1 DAIVNPANNDLYLGGGVAKAISKKAGGDLQEECEeRKKNGYLKvgEVAVTKGGNLPARYIIHVVGPVasskkktyePLKK 80

                          90       100
                  ....*....|....*....|....*.
gi 1034631478 311 TVTSVLEECEQRKYTSVSLPAIGTGN 336
Cdd:cd02749    81 CVKNCLSLADEKGLKSVAFPAIGTGI 106
Macro_OAADPr_deacetylase cd02908
macrodomain, O-acetyl-ADP-ribose (OAADPr) family; Macrodomains are found in a variety of ...
 235-335 5.34e-13

macrodomain, O-acetyl-ADP-ribose (OAADPr) family; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. This family includes eukaryotic macrodomain proteins such as human MacroD1 and MacroD2, and bacterial proteins such as Escherichia coli YmdB; these have been shown to be O-acetyl-ADP-ribose (OAADPr) deacetylases that efficiently catalyze the hydrolysis of OAADPr to produce ADP-ribose and free acetate. OAADPr is a sirtuin reaction product generated from the NAD+-dependent protein deacetylation reactions and has been implicated as a signaling molecule. By acting on mono-ADP-ribosylated substrates, OAADPr deacetylases may reverse cellular ADP-ribosylation.


Pssm-ID: 438955  Cd Length: 166  Bit Score: 67.15  E-value: 5.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478 235 GDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQ-PHRDFIITPGGCLKCKIIIHV--PGGKDV--- 308
Cdd:cd02908     7 GDITKLEVDAIVNAANSSLLGGGGVDGAIHRAAGPELLEECRKLGGVcPTGEAKITPGYNLPAKYVIHTvgPIGEGGvee 86

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1034631478 309 -----RKTVTSVLEECEQRKYTSVSLPAIGTG 335
Cdd:cd02908    87 epellASCYRSSLELALENGLKSIAFPCISTG 118
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 90-172 1.12e-11

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: 62.32  E-value: 1.12e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478   90 NLKLISGDVLYIWADVIVNSVPMNLQLGGGpLSRAFLQKAGPMLQKELDDRRRETEEKVGNIFMTSGCNLDCKAVLHAVA 169
Cdd:smart00506   1 ILKVVKGDITKPRADAIVNAANSDGAHGGG-VAGAIARAAGKALSKEEVRKLAGGECPVGTAVVTEGGNLPAKYVIHAVG 79


                   ...
gi 1034631478  170 PYW 172
Cdd:smart00506  80 PRA 82
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 107-179 1.67e-11

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: 61.43  E-value: 1.67e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034631478 107 VNSVPMNLqLGGGPLSRAFLQKAGPMLQKELDDRRREtEEKVGNIFMTSGCNLDCKAVLHAVAPYWNNGAETS 179
Cdd:pfam01661   1 VNAANSRL-LGGGGVAGAIHRAAGPELLEECRELKKG-GCPTGEAVVTPGGNLPAKYVIHTVGPTWRHGGSHG 71
PRK00431 PRK00431
ADP-ribose-binding protein;
226-335 1.70e-11

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 62.94  E-value: 1.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478 226 GAITFQVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQ----PHRDFIITPGGCLKCKIIIH 301
Cdd:PRK00431    1 MGMRIEVVQGDITELEVDAIVNAANSSLLGGGGVDGAIHRAAGPEILEECRELRQQqgpcPTGEAVITSAGRLPAKYVIH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1034631478 302 VPG-----GKD-----VRKTVTSVLEECEQRKYTSVSLPAIGTG 335
Cdd:PRK00431   81 TVGpvwrgGEDneaelLASAYRNSLRLAAELGLRSIAFPAISTG 124
tankyrase_like cd01438
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ...
 351-531 2.10e-10

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: 60.68  E-value: 2.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478 351 MVQLEPGQSEYNTIKDKFTRTC-------------SSYAIEKIERIQNAFLWQSYQVKKRQMDIKNDHKNNERLLFHGTd 417
Cdd:cd01438    18 LLDLAPDDKEYQSVEEEMQSTIrehrdggnaggifNRYNIIRIQKVVNKKLRERYCHRQKEIAEENHNHHNERMLFHGS- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478 418 adsvPYVN---QHGFNRSCAGKNAVsYGKGTYFAVDASYSAKDTYSKPDSNG------------RKHMYVVRVltgvfTK 482
Cdd:cd01438    97 ----PFINaiiHKGFDERHAYIGGM-FGAGIYFAENSSKSNQYVYGIGGGTGcpthkdrscyvcHRQMLFCRV-----TL 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034631478 483 GRAGLVTPPPKNPHNPTDlFDSVTNNTRSPKL----FVVFFDNQAYPEYLITF 531
Cdd:cd01438   167 GKSFLQFSAMKMAHAPPG-HHSVIGRPSVNGLayaeYVIYRGEQAYPEYLITY 218
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 246-335 1.99e-09

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: 55.26  E-value: 1.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478 246 VNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQPHR--DFIITPGGCLKCKIIIHVPG-----------GKDVRKTV 312
Cdd:pfam01661   1 VNAANSRLLGGGGVAGAIHRAAGPELLEECRELKKGGCPtgEAVVTPGGNLPAKYVIHTVGptwrhggshgeEELLESCY 80

                          90       100
                  ....*....|....*....|...
gi 1034631478 313 TSVLEECEQRKYTSVSLPAIGTG 335
Cdd:pfam01661  81 RNALALAEELGIKSIAFPAISTG 103
PRK00431 PRK00431
ADP-ribose-binding protein;
88-177 2.39e-09

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 56.77  E-value: 2.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478  88 GLNLKLISGDVLYIWADVIVNsvPMN-LQLGGGPLSRAFLQKAGPMLQKELDDRRRETEE-KVGNIFMTSGCNLDCKAVL 165
Cdd:PRK00431    2 GMRIEVVQGDITELEVDAIVN--AANsSLLGGGGVDGAIHRAAGPEILEECRELRQQQGPcPTGEAVITSAGRLPAKYVI 79

                          90
                  ....*....|..
gi 1034631478 166 HAVAPYWNNGAE 177
Cdd:PRK00431   80 HTVGPVWRGGED 91
Macro_H2A-like cd02904
macrodomain, macroH2A-like family; Macrodomains are found in a variety of proteins with ...
 232-336 9.36e-09

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: 55.40  E-value: 9.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478 232 VATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQ----PHRDFIITPGGCLKCKIIIHV--PGG 305
Cdd:cd02904    22 VVQGDIASIKADAIVHPTNATFYLGGEVGSALEKAGGKEFVEEVKELRKSngplEVAGAAISPGHNLPAKFVIHCnsPSW 101

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1034631478 306 KDVR------KTVTSVLEECEQRKYTSVSLPAIGTGN 336
Cdd:cd02904   102 GSDKceelleKTVKNCLALADEKKLKSVAFPSIGSGR 138
Macro_GDAP2-like cd02905
macrodomain, GDAP2-like family; Macrodomains are found in a variety of proteins with diverse ...
 235-332 3.47e-08

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: 53.01  E-value: 3.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478 235 GDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQPHRDFIITPGGCLKCKIIIHVPGGKDVRKTVT- 313
Cdd:cd02905     8 GDLTLLNVDAIVNSTNESLTDKSPISDRLFLAAGPELREELAKLGGCRTGEAKLTKGYNLPARYVIHTVGPRYNEKYRTa 87

                          90       100
                  ....*....|....*....|....*....
gi 1034631478 314 ----------SVLEECEQRKYTSVSLPAI 332
Cdd:cd02905    88 aesalyscyrNVLQLAKEHKLRSVAFPVI 116
Macro_Ttha0132-like cd03330
Macrodomain, uncharacterized family similar to Thermus thermophilus hypothetical protein ...
 91-178 4.55e-08

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: 52.44  E-value: 4.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478  91 LKLISGDVLYIWADVIVNSVPMNLQLGGGpLSRAFLQKAGPMLQKELDdrrRETEEKVGNIFMTSGCNLDCKAVLHA--V 168
Cdd:cd03330     2 LIVVQGDITEQDADAIVNAANRRLLMGSG-VAGAIKRKGGEEIEREAM---RKGPIRVGEAVETGAGKLPAKYVIHAavM 77

                          90
                  ....*....|
gi 1034631478 169 APYWNNGAET 178
Cdd:cd03330    78 GMPGRSSEES 87
Macro_SF cd02749
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 104-172 1.83e-07

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: 49.70  E-value: 1.83e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034631478 104 DVIVNSVPMNLQLGGGpLSRAFLQKAGPMLQKELDDRRRETEEKVGNIFMTSGCNLDCKAVLHAVAPYW 172
Cdd:cd02749     1 DAIVNPANNDLYLGGG-VAKAISKKAGGDLQEECEERKKNGYLKVGEVAVTKGGNLPARYIIHVVGPVA 68
Macro_OAADPr_deacetylase cd02908
macrodomain, O-acetyl-ADP-ribose (OAADPr) family; Macrodomains are found in a variety of ...
 91-177 1.54e-06

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: 48.28  E-value: 1.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478  91 LKLISGDVLYIWADVIVNsvPMNLQL-GGGPLSRAFLQKAGPMLQKELddRRRETEEKVGNIFMTSGCNLDCKAVLHAVA 169
Cdd:cd02908     2 ISLWRGDITKLEVDAIVN--AANSSLlGGGGVDGAIHRAAGPELLEEC--RKLGGVCPTGEAKITPGYNLPAKYVIHTVG 77


                  ....*...
gi 1034631478 170 PYWNNGAE 177
Cdd:cd02908    78 PIGEGGVE 85
Macro_GDAP2-like cd02905
macrodomain, GDAP2-like family; Macrodomains are found in a variety of proteins with diverse ...
 96-179 1.88e-06

macrodomain, GDAP2-like family; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. This family contains proteins similar to human GDAP2, the ganglioside induced differentiation associated protein 2, whose gene is expressed at a higher level in differentiated Neuro2a cells compared with non-differentiated cells. GDAP2 contains an N-terminal macrodomain and a C-terminal Sec14p-like lipid binding domain. It is specifically expressed in brain and testis.


Pssm-ID: 394876  Cd Length: 169  Bit Score: 48.00  E-value: 1.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478  96 GDVLYIWADVIVNSVPMNLqLGGGPLSRAFLQKAGPMLQKELddrRRETEEKVGNIFMTSGCNLDCKAVLHAVAPYWN-- 173
Cdd:cd02905     8 GDLTLLNVDAIVNSTNESL-TDKSPISDRLFLAAGPELREEL---AKLGGCRTGEAKLTKGYNLPARYVIHTVGPRYNek 83


                  ....*...
gi 1034631478 174 --NGAETS 179
Cdd:cd02905    84 yrTAAESA 91
Macro_X_Nsp3-like cd21557
X-domain (or Mac1 domain) of viral non-structural protein 3 and related macrodomains; The ...
 104-170 2.19e-05

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: 44.08  E-value: 2.19e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034631478 104 DVIVNSVPMNLQLGGGpLSRAFLQKAGPMLQKELDDRRRETEEKVGNIFMTSgCNLDCKAVLHAVAP 170
Cdd:cd21557     2 DVVVNAANENLKHGGG-VAGAIYKATGGAFQKESDYIKKNGPLKVGTAVLLP-GHGLAKNIIHVVGP 66
Macro_H2A-like cd02904
macrodomain, macroH2A-like family; Macrodomains are found in a variety of proteins with ...
 88-175 4.92e-03

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: 38.45  E-value: 4.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478  88 GLNLKLISGDVLYIWADVIVNSVPMNLQLGGGpLSRAFLQKAGPMLQKELDDRRRETEE-KVGNIFMTSGCNLDCKAVLH 166
Cdd:cd02904    17 GQKLTVVQGDIASIKADAIVHPTNATFYLGGE-VGSALEKAGGKEFVEEVKELRKSNGPlEVAGAAISPGHNLPAKFVIH 95


                  ....*....
gi 1034631478 167 AVAPYWNNG 175
Cdd:cd02904    96 CNSPSWGSD 104
PRK04143 PRK04143
protein-ADP-ribose hydrolase;
235-335 6.06e-03

protein-ADP-ribose hydrolase;


Pssm-ID: 235225  Cd Length: 264  Bit Score: 38.81  E-value: 6.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034631478 235 GDIATEQVDVIVNSTARTF------NRKSgVSRAILEGAGQAVESECAVL-AAQPHRDFI----ITPGGCLKCKIIIHVP 303
Cdd:PRK04143   90 GDITRLKVDAIVNAANSRLlgcfqpNHDC-IDNAIHTFAGVQLRLDCAEImTEQGRKEATgqakITRAYNLPAKYVIHTV 168

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1034631478 304 GGKDVRKTVT------------SVLEECEQRKYTSVSLPAIGTG 335
Cdd:PRK04143  169 GPIIRKQPVSpiradllascyrSCLKLAEKAGLKSIAFCCISTG 212
 
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