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Conserved domains on  [gi|613504124|sp|Q460N3|]
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RecName: Full=Protein mono-ADP-ribosyltransferase PARP15; AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 7; Short=ARTD7; AltName: Full=B-aggressive lymphoma protein 3; AltName: Full=Poly [ADP-ribose] polymerase 15; Short=PARP-15

Protein Classification

macro domain-containing protein; serine/threonine-protein kinase( domain architecture ID 10206230)

macro domain-containing protein functions in the recognition, interpretation, and turnover of ADP-ribose (ADPr) signaling| serine/threonine-protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 297-463 1.52e-68

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: 221.74  E-value: 1.52e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 297 YEMKIGAITFQVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQP-HRDFIITPGGCLKCKII 375
Cdd:cd02903    1 YTMKIGGITVQLVKGDITKEKTDVIVNSVSSDLLLKGGVSKAILKAAGPELQDECANQGKQPaSGDVIVTSGGNLPCKYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 376 IHVPGGKD-------VRKTVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVADNIIDAIVDFSSQHSTPSLKTVKVVIF 448
Cdd:cd02903   81 YHVVLPHYnpgnektLKDIVRKCLEKAENYKMSSISFPAIGTGNLGFPKDVVAEIMIDEVLKFSSKNPSSSLKEVRFVIF 160

                        170
                 ....*....|....*
gi 613504124 449 QPELLNIFYDSMKKR 463
Cdd:cd02903  161 PPETLQAFSDELAKR 175
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 556-676 3.03e-59

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: 194.85  E-value: 3.03e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 556 LLFHGTDADSVPYVNQHGFNRSCAGKNAVSYGKGTYFAVDASYSAKDTYSKPDSNGRKHMYVVRVLTGVFTKGRAGLVTP 635
Cdd:cd01439    1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKADGLKEMFLARVLTGDYTQGHPGYRRP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 613504124 636 PPKNPHNPTDLFDSVTNNTRSPKLFVVFFDNQAYPEYLITF 676
Cdd:cd01439   81 PLKPSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
Macro_SF super family cl00019
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 88-263 1.76e-45

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: 159.73  E-value: 1.76e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124  88 GLNLKLISGDVLYIWADVIVNSVPMNLqLGGGPLSRAFLQKAGPMLQKELDDRRreTEEKVGNIFMTSGCNLDCKAVLHA 167
Cdd:cd02903    7 GITVQLVKGDITKEKTDVIVNSVSSDL-LLKGGVSKAILKAAGPELQDECANQG--KQPASGDVIVTSGGNLPCKYVYHV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 168 VAPYWNNGAEtswQIMANIIKKCLTTVEVLSFSSITFPMIGTGSLQFPKAVFAKLILSEVFEYSSSTRPITspLQEVHFL 247
Cdd:cd02903   84 VLPHYNPGNE---KTLKDIVRKCLEKAENYKMSSISFPAIGTGNLGFPKDVVAEIMIDEVLKFSSKNPSSS--LKEVRFV 158

                        170
                 ....*....|....*.
gi 613504124 248 VYtnDDEGCQAFLDEF 263
Cdd:cd02903  159 IF--PPETLQAFSDEL 172
 
Name Accession Description Interval E-value
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 297-463 1.52e-68

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: 221.74  E-value: 1.52e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 297 YEMKIGAITFQVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQP-HRDFIITPGGCLKCKII 375
Cdd:cd02903    1 YTMKIGGITVQLVKGDITKEKTDVIVNSVSSDLLLKGGVSKAILKAAGPELQDECANQGKQPaSGDVIVTSGGNLPCKYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 376 IHVPGGKD-------VRKTVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVADNIIDAIVDFSSQHSTPSLKTVKVVIF 448
Cdd:cd02903   81 YHVVLPHYnpgnektLKDIVRKCLEKAENYKMSSISFPAIGTGNLGFPKDVVAEIMIDEVLKFSSKNPSSSLKEVRFVIF 160

                        170
                 ....*....|....*
gi 613504124 449 QPELLNIFYDSMKKR 463
Cdd:cd02903  161 PPETLQAFSDELAKR 175
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 556-676 3.03e-59

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: 194.85  E-value: 3.03e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 556 LLFHGTDADSVPYVNQHGFNRSCAGKNAVSYGKGTYFAVDASYSAKDTYSKPDSNGRKHMYVVRVLTGVFTKGRAGLVTP 635
Cdd:cd01439    1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKADGLKEMFLARVLTGDYTQGHPGYRRP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 613504124 636 PPKNPHNPTDLFDSVTNNTRSPKLFVVFFDNQAYPEYLITF 676
Cdd:cd01439   81 PLKPSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 88-263 1.76e-45

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: 159.73  E-value: 1.76e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124  88 GLNLKLISGDVLYIWADVIVNSVPMNLqLGGGPLSRAFLQKAGPMLQKELDDRRreTEEKVGNIFMTSGCNLDCKAVLHA 167
Cdd:cd02903    7 GITVQLVKGDITKEKTDVIVNSVSSDL-LLKGGVSKAILKAAGPELQDECANQG--KQPASGDVIVTSGGNLPCKYVYHV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 168 VAPYWNNGAEtswQIMANIIKKCLTTVEVLSFSSITFPMIGTGSLQFPKAVFAKLILSEVFEYSSSTRPITspLQEVHFL 247
Cdd:cd02903   84 VLPHYNPGNE---KTLKDIVRKCLEKAENYKMSSISFPAIGTGNLGFPKDVVAEIMIDEVLKFSSKNPSSS--LKEVRFV 158

                        170
                 ....*....|....*.
gi 613504124 248 VYtnDDEGCQAFLDEF 263
Cdd:cd02903  159 IF--PPETLQAFSDEL 172
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 91-262 2.51e-30

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: 117.20  E-value: 2.51e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124  91 LKLISGDVLYIWADVIVNSVPMNLQLGGGpLSRAFLQKAGPMLQKELDDRRRETEEKVGNIFMTSGCNLDCKAVLHAVAP 170
Cdd:COG2110    1 IEIVQGDITELDVDAIVNAANSSLLGGGG-VAGAIHRAAGPELLEECRRLCKQGGCPTGEAVITPAGNLPAKYVIHTVGP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 171 YWNNGAETSWQIMANIIKKCLTTVEVLSFSSITFPMIGTGSLQFPKAVFAKLILSEVFEYssstRPITSPLQEVHFLVYT 250
Cdd:COG2110   80 VWRGGGPSEEELLASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDF----LEEHPSLEEVRFVLFD 155

                        170
                 ....*....|...
gi 613504124 251 NDD-EGCQAFLDE 262
Cdd:COG2110  156 EEDyEAYRRALAR 168
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 505-676 2.10e-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: 2.10e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124  505 EYNTIKDKFTRT-----CSSYAIEKIERIQNAFLWQSYQVKKRQMdikndhknNERLLFHGTDADSVPYVNQHGF--NRS 577
Cdd:pfam00644   3 EYQIIEKYFLSThdpthGYPLFILEIFRVQRDGEWERFQPKKKLR--------NRRLLWHGSRLTNFLGILSQGLriAPP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124  578 CAGKNAVSYGKGTYFAVDASYSAKdtYSKPD-SNGRKHMYVVRVLTG------------------VFTKGRaGLVTPPPK 638
Cdd:pfam00644  75 EAPVTGYMFGKGIYFADDASKSAN--YCPPSeAHGNGLMLLSEVALGdmnelkkadyaeklppgkHSVKGL-GKTAPESF 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 613504124  639 NPHNPTDLFDSVTNNTRS----PKLFVVFFDNQAYPEYLITF 676
Cdd:pfam00644 152 VDLDGVPLGKLVATGYDSsvllYNEYVVYNVNQVRPKYLLEV 193
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 306-462 3.33e-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: 3.33e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 306 FQVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQ---PHRDFIITPGGCLKCKIIIHVPG-- 380
Cdd:COG2110    1 IEIVQGDITELDVDAIVNAANSSLLGGGGVAGAIHRAAGPELLEECRRLCKQggcPTGEAVITPAGNLPAKYVIHTVGpv 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 381 ---G-----KDVRKTVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVADNIIDAIVDFSSQHstPSLKTVKVVIFQPEL 452
Cdd:COG2110   81 wrgGgpseeELLASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFLEEH--PSLEEVRFVLFDEED 158

                        170
                 ....*....|
gi 613504124 453 LNIFYDSMKK 462
Cdd:COG2110  159 YEAYRRALAR 168
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 90-223 1.58e-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: 90.83  E-value: 1.58e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124    90 NLKLISGDVLYIWADVIVNSVPMNLQLGGGpLSRAFLQKAGPMLQKELDDRRRETEEKVGNIFMTSGCNLDCKAVLHAVA 169
Cdd:smart00506   1 ILKVVKGDITKPRADAIVNAANSDGAHGGG-VAGAIARAAGKALSKEEVRKLAGGECPVGTAVVTEGGNLPAKYVIHAVG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 613504124   170 PYWNNGAETSWQIMANIIKKCLTTVEVLSFSSITFPMIGTGSLQFPKAVFAKLI 223
Cdd:smart00506  80 PRASGHSKEGFELLENAYRNCLELAIELGITSVALPLIGTGIYGVPKDRSAQAL 133
PRK00431 PRK00431
ADP-ribose-binding protein;
88-265 2.64e-20

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 88.75  E-value: 2.64e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124  88 GLNLKLISGDVLYIWADVIVNsvPMN-LQLGGGPLSRAFLQKAGPMLQKELDDRRRETEE-KVGNIFMTSGCNLDCKAVL 165
Cdd:PRK00431   2 GMRIEVVQGDITELEVDAIVN--AANsSLLGGGGVDGAIHRAAGPEILEECRELRQQQGPcPTGEAVITSAGRLPAKYVI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 166 HAVAPYWNNGAETSWQIMANIIKKCLTTVEVLSFSSITFPMIGTGSLQFPKAVFAKLILSEVFEYSsstrPITSPLQEVH 245
Cdd:PRK00431  80 HTVGPVWRGGEDNEAELLASAYRNSLRLAAELGLRSIAFPAISTGVYGYPLEDAARIAVKTVREFL----TRHKSPEEVY 155

                        170       180
                 ....*....|....*....|
gi 613504124 246 FLVYtnDDEGCQAFLDEFTN 265
Cdd:PRK00431 156 FVCY--DEEAYRLYERLLTQ 173
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 306-422 4.16e-19

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: 83.89  E-value: 4.16e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124   306 FQVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQ---PHRDFIITPGGCLKCKIIIHVPGG- 381
Cdd:smart00506   2 LKVVKGDITKPRADAIVNAANSDGAHGGGVAGAIARAAGKALSKEEVRKLAGgecPVGTAVVTEGGNLPAKYVIHAVGPr 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 613504124   382 ---------KDVRKTVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVAD 422
Cdd:smart00506  82 asghskegfELLENAYRNCLELAIELGITSVALPLIGTGIYGVPKDRSAQ 131
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 107-223 3.07e-18

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: 80.69  E-value: 3.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124  107 VNSVPMNLqLGGGPLSRAFLQKAGPMLQKELDDRRREtEEKVGNIFMTSGCNLDCKAVLHAVAPYWNNGA-ETSWQIMAN 185
Cdd:pfam01661   1 VNAANSRL-LGGGGVAGAIHRAAGPELLEECRELKKG-GCPTGEAVVTPGGNLPAKYVIHTVGPTWRHGGsHGEEELLES 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 613504124  186 IIKKCLTTVEVLSFSSITFPMIGTGSLQFPKAVFAKLI 223
Cdd:pfam01661  79 CYRNALALAEELGIKSIAFPAISTGIYGFPWEEAARIA 116
PRK00431 PRK00431
ADP-ribose-binding protein;
302-456 8.95e-15

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 72.95  E-value: 8.95e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 302 GAITFQVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQ----PHRDFIITPGGCLKCKIIIH 377
Cdd:PRK00431   1 MGMRIEVVQGDITELEVDAIVNAANSSLLGGGGVDGAIHRAAGPEILEECRELRQQqgpcPTGEAVITSAGRLPAKYVIH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 378 VPG-----GKD-----VRKTVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVADNIIDAIVDFSSQHStpSLKTVKVVI 447
Cdd:PRK00431  81 TVGpvwrgGEDneaelLASAYRNSLRLAAELGLRSIAFPAISTGVYGYPLEDAARIAVKTVREFLTRHK--SPEEVYFVC 158


                 ....*....
gi 613504124 448 FQPELLNIF 456
Cdd:PRK00431 159 YDEEAYRLY 167
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 322-414 7.00e-10

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: 56.80  E-value: 7.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124  322 VNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQPHR--DFIITPGGCLKCKIIIHVPG-----------GKDVRKTV 388
Cdd:pfam01661   1 VNAANSRLLGGGGVAGAIHRAAGPELLEECRELKKGGCPtgEAVVTPGGNLPAKYVIHTVGptwrhggshgeEELLESCY 80

                          90       100
                  ....*....|....*....|....*.
gi 613504124  389 TSVLEECEQRKYTSVSLPAIGTGNAG 414
Cdd:pfam01661  81 RNALALAEELGIKSIAFPAISTGIYG 106
 
Name Accession Description Interval E-value
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 297-463 1.52e-68

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: 221.74  E-value: 1.52e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 297 YEMKIGAITFQVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQP-HRDFIITPGGCLKCKII 375
Cdd:cd02903    1 YTMKIGGITVQLVKGDITKEKTDVIVNSVSSDLLLKGGVSKAILKAAGPELQDECANQGKQPaSGDVIVTSGGNLPCKYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 376 IHVPGGKD-------VRKTVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVADNIIDAIVDFSSQHSTPSLKTVKVVIF 448
Cdd:cd02903   81 YHVVLPHYnpgnektLKDIVRKCLEKAENYKMSSISFPAIGTGNLGFPKDVVAEIMIDEVLKFSSKNPSSSLKEVRFVIF 160

                        170
                 ....*....|....*
gi 613504124 449 QPELLNIFYDSMKKR 463
Cdd:cd02903  161 PPETLQAFSDELAKR 175
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 556-676 3.03e-59

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: 194.85  E-value: 3.03e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 556 LLFHGTDADSVPYVNQHGFNRSCAGKNAVSYGKGTYFAVDASYSAKDTYSKPDSNGRKHMYVVRVLTGVFTKGRAGLVTP 635
Cdd:cd01439    1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKADGLKEMFLARVLTGDYTQGHPGYRRP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 613504124 636 PPKNPHNPTDLFDSVTNNTRSPKLFVVFFDNQAYPEYLITF 676
Cdd:cd01439   81 PLKPSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 88-263 1.76e-45

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: 159.73  E-value: 1.76e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124  88 GLNLKLISGDVLYIWADVIVNSVPMNLqLGGGPLSRAFLQKAGPMLQKELDDRRreTEEKVGNIFMTSGCNLDCKAVLHA 167
Cdd:cd02903    7 GITVQLVKGDITKEKTDVIVNSVSSDL-LLKGGVSKAILKAAGPELQDECANQG--KQPASGDVIVTSGGNLPCKYVYHV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 168 VAPYWNNGAEtswQIMANIIKKCLTTVEVLSFSSITFPMIGTGSLQFPKAVFAKLILSEVFEYSSSTRPITspLQEVHFL 247
Cdd:cd02903   84 VLPHYNPGNE---KTLKDIVRKCLEKAENYKMSSISFPAIGTGNLGFPKDVVAEIMIDEVLKFSSKNPSSS--LKEVRFV 158

                        170
                 ....*....|....*.
gi 613504124 248 VYtnDDEGCQAFLDEF 263
Cdd:cd02903  159 IF--PPETLQAFSDEL 172
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 91-262 2.51e-30

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: 117.20  E-value: 2.51e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124  91 LKLISGDVLYIWADVIVNSVPMNLQLGGGpLSRAFLQKAGPMLQKELDDRRRETEEKVGNIFMTSGCNLDCKAVLHAVAP 170
Cdd:COG2110    1 IEIVQGDITELDVDAIVNAANSSLLGGGG-VAGAIHRAAGPELLEECRRLCKQGGCPTGEAVITPAGNLPAKYVIHTVGP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 171 YWNNGAETSWQIMANIIKKCLTTVEVLSFSSITFPMIGTGSLQFPKAVFAKLILSEVFEYssstRPITSPLQEVHFLVYT 250
Cdd:COG2110   80 VWRGGGPSEEELLASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDF----LEEHPSLEEVRFVLFD 155

                        170
                 ....*....|...
gi 613504124 251 NDD-EGCQAFLDE 262
Cdd:COG2110  156 EEDyEAYRRALAR 168
Macro_Af1521_BAL-like cd02907
macrodomain, Af1521-like family; Macrodomains are found in a variety of proteins with diverse ...
 304-441 3.61e-30

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: 116.44  E-value: 3.61e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 304 ITFQVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESEC-AVLAAQ---PHRDFIITPGGCLKCKIIIHV- 378
Cdd:cd02907    2 IKVSVYKGDITKEKVDAIVNAANERLKHGGGVAGAISKAGGPEIQEECdKYIKKNgklRVGEVVVTSAGKLPCKYVIHAv 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613504124 379 -P---GGKD------VRKTVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVADNIIDAIVDFSSQHSTPSLK 441
Cdd:cd02907   82 gPrwsGGSKeecedlLYKAVLNSLEEAEELKATSIAIPAISSGIFGFPLDLCAEAIVEAIKDFSESNSSSSLK 154
Macro_Af1521_BAL-like cd02907
macrodomain, Af1521-like family; Macrodomains are found in a variety of proteins with diverse ...
 88-246 5.66e-30

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: 115.67  E-value: 5.66e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124  88 GLNLKLISGDVLYIWADVIVNSVPMNLQLGGGpLSRAFLQKAGPMLQKELDD-RRRETEEKVGNIFMTSGCNLDCKAVLH 166
Cdd:cd02907    1 GIKVSVYKGDITKEKVDAIVNAANERLKHGGG-VAGAISKAGGPEIQEECDKyIKKNGKLRVGEVVVTSAGKLPCKYVIH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 167 AVAPYWNNG-AETSWQIMANIIKKCLTTVEVLSFSSITFPMIGTGSLQFPKAVFAKLILSEVFEYSSSTRPitSPLQEVH 245
Cdd:cd02907   80 AVGPRWSGGsKEECEDLLYKAVLNSLEEAEELKATSIAIPAISSGIFGFPLDLCAEAIVEAIKDFSESNSS--SSLKEIR 157


                 .
gi 613504124 246 F 246
Cdd:cd02907  158 L 158
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 505-676 2.10e-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: 2.10e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124  505 EYNTIKDKFTRT-----CSSYAIEKIERIQNAFLWQSYQVKKRQMdikndhknNERLLFHGTDADSVPYVNQHGF--NRS 577
Cdd:pfam00644   3 EYQIIEKYFLSThdpthGYPLFILEIFRVQRDGEWERFQPKKKLR--------NRRLLWHGSRLTNFLGILSQGLriAPP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124  578 CAGKNAVSYGKGTYFAVDASYSAKdtYSKPD-SNGRKHMYVVRVLTG------------------VFTKGRaGLVTPPPK 638
Cdd:pfam00644  75 EAPVTGYMFGKGIYFADDASKSAN--YCPPSeAHGNGLMLLSEVALGdmnelkkadyaeklppgkHSVKGL-GKTAPESF 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 613504124  639 NPHNPTDLFDSVTNNTRS----PKLFVVFFDNQAYPEYLITF 676
Cdd:pfam00644 152 VDLDGVPLGKLVATGYDSsvllYNEYVVYNVNQVRPKYLLEV 193
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 306-462 3.33e-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: 3.33e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 306 FQVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQ---PHRDFIITPGGCLKCKIIIHVPG-- 380
Cdd:COG2110    1 IEIVQGDITELDVDAIVNAANSSLLGGGGVAGAIHRAAGPELLEECRRLCKQggcPTGEAVITPAGNLPAKYVIHTVGpv 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 381 ---G-----KDVRKTVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVADNIIDAIVDFSSQHstPSLKTVKVVIFQPEL 452
Cdd:COG2110   81 wrgGgpseeELLASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFLEEH--PSLEEVRFVLFDEED 158

                        170
                 ....*....|
gi 613504124 453 LNIFYDSMKK 462
Cdd:COG2110  159 YEAYRRALAR 168
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 90-223 1.58e-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: 90.83  E-value: 1.58e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124    90 NLKLISGDVLYIWADVIVNSVPMNLQLGGGpLSRAFLQKAGPMLQKELDDRRRETEEKVGNIFMTSGCNLDCKAVLHAVA 169
Cdd:smart00506   1 ILKVVKGDITKPRADAIVNAANSDGAHGGG-VAGAIARAAGKALSKEEVRKLAGGECPVGTAVVTEGGNLPAKYVIHAVG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 613504124   170 PYWNNGAETSWQIMANIIKKCLTTVEVLSFSSITFPMIGTGSLQFPKAVFAKLI 223
Cdd:smart00506  80 PRASGHSKEGFELLENAYRNCLELAIELGITSVALPLIGTGIYGVPKDRSAQAL 133
PRK00431 PRK00431
ADP-ribose-binding protein;
88-265 2.64e-20

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 88.75  E-value: 2.64e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124  88 GLNLKLISGDVLYIWADVIVNsvPMN-LQLGGGPLSRAFLQKAGPMLQKELDDRRRETEE-KVGNIFMTSGCNLDCKAVL 165
Cdd:PRK00431   2 GMRIEVVQGDITELEVDAIVN--AANsSLLGGGGVDGAIHRAAGPEILEECRELRQQQGPcPTGEAVITSAGRLPAKYVI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 166 HAVAPYWNNGAETSWQIMANIIKKCLTTVEVLSFSSITFPMIGTGSLQFPKAVFAKLILSEVFEYSsstrPITSPLQEVH 245
Cdd:PRK00431  80 HTVGPVWRGGEDNEAELLASAYRNSLRLAAELGLRSIAFPAISTGVYGYPLEDAARIAVKTVREFL----TRHKSPEEVY 155

                        170       180
                 ....*....|....*....|
gi 613504124 246 FLVYtnDDEGCQAFLDEFTN 265
Cdd:PRK00431 156 FVCY--DEEAYRLYERLLTQ 173
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 306-422 4.16e-19

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: 83.89  E-value: 4.16e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124   306 FQVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQ---PHRDFIITPGGCLKCKIIIHVPGG- 381
Cdd:smart00506   2 LKVVKGDITKPRADAIVNAANSDGAHGGGVAGAIARAAGKALSKEEVRKLAGgecPVGTAVVTEGGNLPAKYVIHAVGPr 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 613504124   382 ---------KDVRKTVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVAD 422
Cdd:smart00506  82 asghskegfELLENAYRNCLELAIELGITSVALPLIGTGIYGVPKDRSAQ 131
Macro_SF cd02749
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 104-226 2.42e-18

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: 81.29  E-value: 2.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 104 DVIVNSVPMNLQLGGGpLSRAFLQKAGPMLQKELDDRRRETEEKVGNIFMTSGCNLDCKAVLHAVAPYWnNGAETSWQIM 183
Cdd:cd02749    1 DAIVNPANNDLYLGGG-VAKAISKKAGGDLQEECEERKKNGYLKVGEVAVTKGGNLPARYIIHVVGPVA-SSKKKTYEPL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 613504124 184 ANIIKKCLTTVEVLSFSSITFPMIGTGSLQFPKAVFAKLILSE 226
Cdd:cd02749   79 KKCVKNCLSLADEKGLKSVAFPAIGTGIAGFPPEEAARIMLEA 121
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 107-223 3.07e-18

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: 80.69  E-value: 3.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124  107 VNSVPMNLqLGGGPLSRAFLQKAGPMLQKELDDRRREtEEKVGNIFMTSGCNLDCKAVLHAVAPYWNNGA-ETSWQIMAN 185
Cdd:pfam01661   1 VNAANSRL-LGGGGVAGAIHRAAGPELLEECRELKKG-GCPTGEAVVTPGGNLPAKYVIHTVGPTWRHGGsHGEEELLES 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 613504124  186 IIKKCLTTVEVLSFSSITFPMIGTGSLQFPKAVFAKLI 223
Cdd:pfam01661  79 CYRNALALAEELGIKSIAFPAISTGIYGFPWEEAARIA 116
Macro_SF cd02749
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 319-427 7.31e-18

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: 79.75  E-value: 7.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 319 DVIVNSTARTFNRKSGVSRAILEGAGQAVESECA-VLAAQPHR--DFIITPGGCLKCKIIIHVPGGK---------DVRK 386
Cdd:cd02749    1 DAIVNPANNDLYLGGGVAKAISKKAGGDLQEECEeRKKNGYLKvgEVAVTKGGNLPARYIIHVVGPVasskkktyePLKK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 613504124 387 TVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVADNIIDA 427
Cdd:cd02749   81 CVKNCLSLADEKGLKSVAFPAIGTGIAGFPPEEAARIMLEA 121
Macro_H2A-like cd02904
macrodomain, macroH2A-like family; Macrodomains are found in a variety of proteins with ...
 88-249 5.49e-17

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: 79.67  E-value: 5.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124  88 GLNLKLISGDVLYIWADVIVNSVPMNLQLGGGpLSRAFLQKAGPMLQKELDDRRRETEE-KVGNIFMTSGCNLDCKAVLH 166
Cdd:cd02904   17 GQKLTVVQGDIASIKADAIVHPTNATFYLGGE-VGSALEKAGGKEFVEEVKELRKSNGPlEVAGAAISPGHNLPAKFVIH 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 167 AVAPYWnnGAETSWQIMANIIKKCLTTVEVLSFSSITFPMIGTGSLQFPKAVFAKLILSEVFEYSSSTrpITSPLQEVHF 246
Cdd:cd02904   96 CNSPSW--GSDKCEELLEKTVKNCLALADEKKLKSVAFPSIGSGRNGFPKQTAAQTILKAISNYFVSV--MSSSLKQIYF 171


                 ...
gi 613504124 247 LVY 249
Cdd:cd02904  172 VLF 174
Macro_OAADPr_deacetylase cd02908
macrodomain, O-acetyl-ADP-ribose (OAADPr) family; Macrodomains are found in a variety of ...
 91-254 2.58e-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: 76.78  E-value: 2.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124  91 LKLISGDVLYIWADVIVNsvPMNLQL-GGGPLSRAFLQKAGPMLQKELddRRRETEEKVGNIFMTSGCNLDCKAVLHAVA 169
Cdd:cd02908    2 ISLWRGDITKLEVDAIVN--AANSSLlGGGGVDGAIHRAAGPELLEEC--RKLGGVCPTGEAKITPGYNLPAKYVIHTVG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 170 PYWNNGAETSWQIMANIIKKCLTTVEVLSFSSITFPMIGTGSLQFPKAVFAKLILSEVFEYSSSTRPITsplqEVHFLVY 249
Cdd:cd02908   78 PIGEGGVEEEPELLASCYRSSLELALENGLKSIAFPCISTGIYGYPNEEAAEIALNTVREWLEEHDKID----RIIFVVF 153


                 ....*
gi 613504124 250 TNDDE 254
Cdd:cd02908  154 LDEDY 158
Macro_H2A-like cd02904
macrodomain, macroH2A-like family; Macrodomains are found in a variety of proteins with ...
 308-462 1.70e-15

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: 75.04  E-value: 1.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 308 VATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQ----PHRDFIITPGGCLKCKIIIHV--PGG 381
Cdd:cd02904   22 VVQGDIASIKADAIVHPTNATFYLGGEVGSALEKAGGKEFVEEVKELRKSngplEVAGAAISPGHNLPAKFVIHCnsPSW 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 382 KDVR------KTVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVADNIIDAIVDFSSQHSTPSLKTVKVVIFQPELLNI 455
Cdd:cd02904  102 GSDKceelleKTVKNCLALADEKKLKSVAFPSIGSGRNGFPKQTAAQTILKAISNYFVSVMSSSLKQIYFVLFDMESIGI 181


                 ....*..
gi 613504124 456 FYDSMKK 462
Cdd:cd02904  182 YTSELAK 188
PRK00431 PRK00431
ADP-ribose-binding protein;
302-456 8.95e-15

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 72.95  E-value: 8.95e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 302 GAITFQVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQ----PHRDFIITPGGCLKCKIIIH 377
Cdd:PRK00431   1 MGMRIEVVQGDITELEVDAIVNAANSSLLGGGGVDGAIHRAAGPEILEECRELRQQqgpcPTGEAVITSAGRLPAKYVIH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 378 VPG-----GKD-----VRKTVTSVLEECEQRKYTSVSLPAIGTGNAGKNPITVADNIIDAIVDFSSQHStpSLKTVKVVI 447
Cdd:PRK00431  81 TVGpvwrgGEDneaelLASAYRNSLRLAAELGLRSIAFPAISTGVYGYPLEDAARIAVKTVREFLTRHK--SPEEVYFVC 158


                 ....*....
gi 613504124 448 FQPELLNIF 456
Cdd:PRK00431 159 YDEEAYRLY 167
Macro_Ttha0132-like cd03330
Macrodomain, uncharacterized family similar to Thermus thermophilus hypothetical protein ...
 306-414 1.02e-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: 71.70  E-value: 1.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 306 FQVATGDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQPHRDFIITPGGCLKCKIIIHVPGGKD-- 383
Cdd:cd03330    2 LIVVQGDITEQDADAIVNAANRRLLMGSGVAGAIKRKGGEEIEREAMRKGPIRVGEAVETGAGKLPAKYVIHAAVMGMpg 81

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 613504124 384 ------VRKTVTSVLEECEQRKYTSVSLPAIGTGNAG 414
Cdd:cd03330   82 rsseesIRDATRNALAKAEELGLESVAFPAIGTGVGG 118
Macro_OAADPr_deacetylase cd02908
macrodomain, O-acetyl-ADP-ribose (OAADPr) family; Macrodomains are found in a variety of ...
 311-461 2.10e-14

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: 71.39  E-value: 2.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 311 GDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQ-PHRDFIITPGGCLKCKIIIHV--PGGKDV--- 384
Cdd:cd02908    7 GDITKLEVDAIVNAANSSLLGGGGVDGAIHRAAGPELLEECRKLGGVcPTGEAKITPGYNLPAKYVIHTvgPIGEGGvee 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 385 -----RKTVTSVLEECEQRKYTSVSLPAIGTGNAGKnPITVADNI-IDAIVDFSSQHSTPSLktVKVVIFQPELLNIFYD 458
Cdd:cd02908   87 epellASCYRSSLELALENGLKSIAFPCISTGIYGY-PNEEAAEIaLNTVREWLEEHDKIDR--IIFVVFLDEDYKIYEE 163


                 ...
gi 613504124 459 SMK 461
Cdd:cd02908  164 LLP 166
Macro_Ttha0132-like cd03330
Macrodomain, uncharacterized family similar to Thermus thermophilus hypothetical protein ...
 91-246 3.75e-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: 70.16  E-value: 3.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124  91 LKLISGDVLYIWADVIVNSVPMNLQLGGGpLSRAFLQKAGPMLQKELDdrrRETEEKVGNIFMTSGCNLDCKAVLHA--V 168
Cdd:cd03330    2 LIVVQGDITEQDADAIVNAANRRLLMGSG-VAGAIKRKGGEEIEREAM---RKGPIRVGEAVETGAGKLPAKYVIHAavM 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613504124 169 APYWNNGAETswqiMANIIKKCLTTVEVLSFSSITFPMIGTGSLQFPKAVFAKLILSEVFEYSSstrpitSPLQEVHF 246
Cdd:cd03330   78 GMPGRSSEES----IRDATRNALAKAEELGLESVAFPAIGTGVGGFPVEEVARIMLEEIKKCDP------PLLEEVRL 145
tankyrase_like cd01438
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ...
 496-676 1.49e-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: 61.45  E-value: 1.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 496 MVQLEPGQSEYNTIKDKFTRTC-------------SSYAIEKIERIQNAFLWQSYQVKKRQMDIKNDHKNNERLLFHGTd 562
Cdd:cd01438   18 LLDLAPDDKEYQSVEEEMQSTIrehrdggnaggifNRYNIIRIQKVVNKKLRERYCHRQKEIAEENHNHHNERMLFHGS- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 563 adsvPYVN---QHGFNRSCAGKNAVsYGKGTYFAVDASYSAKDTYSKPDSNG------------RKHMYVVRVltgvfTK 627
Cdd:cd01438   97 ----PFINaiiHKGFDERHAYIGGM-FGAGIYFAENSSKSNQYVYGIGGGTGcpthkdrscyvcHRQMLFCRV-----TL 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 613504124 628 GRAGLVTPPPKNPHNPTDlFDSVTNNTRSPKL----FVVFFDNQAYPEYLITF 676
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 ...
 322-414 7.00e-10

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: 56.80  E-value: 7.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124  322 VNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQPHR--DFIITPGGCLKCKIIIHVPG-----------GKDVRKTV 388
Cdd:pfam01661   1 VNAANSRLLGGGGVAGAIHRAAGPELLEECRELKKGGCPtgEAVVTPGGNLPAKYVIHTVGptwrhggshgeEELLESCY 80

                          90       100
                  ....*....|....*....|....*.
gi 613504124  389 TSVLEECEQRKYTSVSLPAIGTGNAG 414
Cdd:pfam01661  81 RNALALAEELGIKSIAFPAISTGIYG 106
Macro_GDAP2-like cd02905
macrodomain, GDAP2-like family; Macrodomains are found in a variety of proteins with diverse ...
 311-414 3.07e-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: 53.78  E-value: 3.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 311 GDIATEQVDVIVNSTARTFNRKSGVSRAILEGAGQAVESECAVLAAQPHRDFIITPGGCLKCKIIIHVPGGKDVRKTVT- 389
Cdd:cd02905    8 GDLTLLNVDAIVNSTNESLTDKSPISDRLFLAAGPELREELAKLGGCRTGEAKLTKGYNLPARYVIHTVGPRYNEKYRTa 87

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 613504124 390 ----------SVLEECEQRKYTSVSLPAIGTGNAG 414
Cdd:cd02905   88 aesalyscyrNVLQLAKEHKLRSVAFPVIHSERRG 122
PRK04143 PRK04143
protein-ADP-ribose hydrolase;
91-230 9.63e-08

protein-ADP-ribose hydrolase;


Pssm-ID: 235225  Cd Length: 264  Bit Score: 53.83  E-value: 9.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124  91 LKLISGDVLYIW--------ADVIVNSVpmNLQLGG------GPLSRAFLQKAGPMLQKELDDRRRET--EEKVGNIFMT 154
Cdd:PRK04143  77 LQPIKYDNIFLWqgditrlkVDAIVNAA--NSRLLGcfqpnhDCIDNAIHTFAGVQLRLDCAEIMTEQgrKEATGQAKIT 154

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613504124 155 SGCNLDCKAVLHAVAPYWNNG--AETSWQIMANIIKKCLTTVEVLSFSSITFPMIGTGSLQFPKAVFAKLILSEVFEY 230
Cdd:PRK04143 155 RAYNLPAKYVIHTVGPIIRKQpvSPIRADLLASCYRSCLKLAEKAGLKSIAFCCISTGVFGFPKEEAAEIAIKTVLSW 232
Macro_GDAP2-like cd02905
macrodomain, GDAP2-like family; Macrodomains are found in a variety of proteins with diverse ...
 96-215 2.90e-07

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: 50.70  E-value: 2.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124  96 GDVLYIWADVIVNSVPMNLqLGGGPLSRAFLQKAGPMLQKELddrRRETEEKVGNIFMTSGCNLDCKAVLHAVAPYWN-- 173
Cdd:cd02905    8 GDLTLLNVDAIVNSTNESL-TDKSPISDRLFLAAGPELREEL---AKLGGCRTGEAKLTKGYNLPARYVIHTVGPRYNek 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 613504124 174 --NGAETSWQimaNIIKKCLTTVEVLSFSSITFPMIGTGSLQFP 215
Cdd:cd02905   84 yrTAAESALY---SCYRNVLQLAKEHKLRSVAFPVIHSERRGYP 124
Macro_X_Nsp3-like cd21557
X-domain (or Mac1 domain) of viral non-structural protein 3 and related macrodomains; The ...
 104-210 4.97e-06

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: 46.39  E-value: 4.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 104 DVIVNSVPMNLQLGGGpLSRAFLQKAGPMLQKELDDRRRETEEKVGNIFMTSgCNLDCKAVLHAVAPywNNGAETSWQIM 183
Cdd:cd21557    2 DVVVNAANENLKHGGG-VAGAIYKATGGAFQKESDYIKKNGPLKVGTAVLLP-GHGLAKNIIHVVGP--RKRKGQDDQLL 77

                         90       100
                 ....*....|....*....|....*..
gi 613504124 184 ANIIKKCLTtvevlSFSSITFPMIGTG 210
Cdd:cd21557   78 AAAYKAVNK-----EYGSVLTPLLSAG 99
PRK04143 PRK04143
protein-ADP-ribose hydrolase;
311-456 6.18e-05

protein-ADP-ribose hydrolase;


Pssm-ID: 235225  Cd Length: 264  Bit Score: 45.36  E-value: 6.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 311 GDIATEQVDVIVNSTARTF------NRKSgVSRAILEGAGQAVESECAVL-AAQPHRDFI----ITPGGCLKCKIIIHVP 379
Cdd:PRK04143  90 GDITRLKVDAIVNAANSRLlgcfqpNHDC-IDNAIHTFAGVQLRLDCAEImTEQGRKEATgqakITRAYNLPAKYVIHTV 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613504124 380 GGKDVRKTVT------------SVLEECEQRKYTSVSLPAIGTGNAGKnPITVADNI-IDAIVDFssQHSTPSLKTVKVV 446
Cdd:PRK04143 169 GPIIRKQPVSpiradllascyrSCLKLAEKAGLKSIAFCCISTGVFGF-PKEEAAEIaIKTVLSW--LKENPSKLKVVFN 245

                        170
                 ....*....|
gi 613504124 447 IFQPELLNIF 456
Cdd:PRK04143 246 VFTDEDLELY 255
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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