NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|242036899|ref|XP_002465844|]
View 

protein GDAP2 homolog [Sorghum bicolor]

Protein Classification

Macro_GDAP2_like and SEC14 domain-containing protein( domain architecture ID 10121093)

Macro_GDAP2_like and SEC14 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
Macro_GDAP2-like cd02905
macrodomain, GDAP2-like family; Macrodomains are found in a variety of proteins with diverse ...
 98-266 6.73e-99

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: 297.61  E-value: 6.73e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242036899  98 SKIYLWRGHPWSLEVDAVVNSTNENL-DEAHSSPGLHAAAGTGLAEECATLGGCRTGMAKMTNAYDLPARKVIHTVGPKY 176
Cdd:cd02905    1 RKIVLWDGDLTLLNVDAIVNSTNESLtDKSPISDRLFLAAGPELREELAKLGGCRTGEAKLTKGYNLPARYVIHTVGPRY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242036899 177 AVKYHTAAENALSHCYRSCLELLIENGLESIATGCIYTEAKNYPREPAAHVAIRTVRRFLEKQKDKITAIVFCTiSSSDT 256
Cdd:cd02905   81 NEKYRTAAESALYSCYRNVLQLAKEHKLRSVAFPVIHSERRGYPLEDGAHIALRTVRRFLEKHGSSFEAVVFVV-TEEEM 159

                        170
                 ....*....|
gi 242036899 257 EIYKRLLPLY 266
Cdd:cd02905  160 ETYERLLPLY 169
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
 425-558 5.50e-33

Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain family. This family includes ECM25 that contains a divergent CRAL-TRIO domain identified by Gallego and colleagues.


:

Pssm-ID: 463965 [Multi-domain]  Cd Length: 140  Bit Score: 123.21  E-value: 5.50e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242036899  425 GHPVMVVVGAHF---LLRCLDLERFVLYVIKEF-EPLIQKPYSIVYFHSAASLQPQPDLGFMKRLQQILGRKHQKNLHTI 500
Cdd:pfam13716   1 GRPVLVFISKLLpsrPASLDDLDRLLFYLLKTLsEKLKGKPFVVVVDHTGVTSENFPSLSFLKKAYDLLPRAFKKNLKAV 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 242036899  501 YILHPTLGLRTAV-MAMQLFVDGEVWKKVVYVDRLVQLFRYVPREQLT--IPdFVFQHDLE 558
Cdd:pfam13716  81 YVVHPSTFLRTFLkTLGSLLGSKKLRKKVHYVSSLSELWEGIDREQLPteLP-GVLSYDEE 140
 
Name Accession Description Interval E-value
Macro_GDAP2-like cd02905
macrodomain, GDAP2-like family; Macrodomains are found in a variety of proteins with diverse ...
 98-266 6.73e-99

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: 297.61  E-value: 6.73e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242036899  98 SKIYLWRGHPWSLEVDAVVNSTNENL-DEAHSSPGLHAAAGTGLAEECATLGGCRTGMAKMTNAYDLPARKVIHTVGPKY 176
Cdd:cd02905    1 RKIVLWDGDLTLLNVDAIVNSTNESLtDKSPISDRLFLAAGPELREELAKLGGCRTGEAKLTKGYNLPARYVIHTVGPRY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242036899 177 AVKYHTAAENALSHCYRSCLELLIENGLESIATGCIYTEAKNYPREPAAHVAIRTVRRFLEKQKDKITAIVFCTiSSSDT 256
Cdd:cd02905   81 NEKYRTAAESALYSCYRNVLQLAKEHKLRSVAFPVIHSERRGYPLEDGAHIALRTVRRFLEKHGSSFEAVVFVV-TEEEM 159

                        170
                 ....*....|
gi 242036899 257 EIYKRLLPLY 266
Cdd:cd02905  160 ETYERLLPLY 169
PRK04143 PRK04143
protein-ADP-ribose hydrolase;
96-263 1.06e-41

protein-ADP-ribose hydrolase;


Pssm-ID: 235225  Cd Length: 264  Bit Score: 151.29  E-value: 1.06e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242036899  96 INSKIYLWRGHPWSLEVDAVVNSTNENL-----------DEAhsspgLHAAAGTGLAEECA---TLGGCR--TGMAKMTN 159
Cdd:PRK04143  81 KYDNIFLWQGDITRLKVDAIVNAANSRLlgcfqpnhdciDNA-----IHTFAGVQLRLDCAeimTEQGRKeaTGQAKITR 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242036899 160 AYDLPARKVIHTVGPKYAvKYHTAAENA--LSHCYRSCLELLIENGLESIATGCIYTEAKNYPREPAAHVAIRTVRRFLE 237
Cdd:PRK04143 156 AYNLPAKYVIHTVGPIIR-KQPVSPIRAdlLASCYRSCLKLAEKAGLKSIAFCCISTGVFGFPKEEAAEIAIKTVLSWLK 234

                        170       180
                 ....*....|....*....|....*.
gi 242036899 238 KQKDKITaIVFCTISSSDTEIYKRLL 263
Cdd:PRK04143 235 ENPSKLK-VVFNVFTDEDLELYQKAL 259
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 100-263 1.09e-39

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: 142.62  E-value: 1.09e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242036899 100 IYLWRGHPWSLEVDAVVNSTNENL------DEAhsspgLHAAAGTGLAEECATL---GGCRTGMAKMTNAYDLPARKVIH 170
Cdd:COG2110    1 IEIVQGDITELDVDAIVNAANSSLlggggvAGA-----IHRAAGPELLEECRRLckqGGCPTGEAVITPAGNLPAKYVIH 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242036899 171 TVGPKYAVKYHTAAEnALSHCYRSCLELLIENGLESIA-----TGcIYteakNYPREPAAHVAIRTVRRFLEKQkDKITA 245
Cdd:COG2110   76 TVGPVWRGGGPSEEE-LLASCYRNSLELAEELGIRSIAfpaigTG-VG----GFPWEEAAPIAVETLRDFLEEH-PSLEE 148

                        170
                 ....*....|....*...
gi 242036899 246 IVFCTISSSDTEIYKRLL 263
Cdd:COG2110  149 VRFVLFDEEDYEAYRRAL 166
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 116-228 2.56e-36

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: 131.53  E-value: 2.56e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242036899  116 VNSTNENLDEAHS-SPGLHAAAGTGLAEECATL--GGCRTGMAKMTNAYDLPARKVIHTVGPKYAVKYHTAAENALSHCY 192
Cdd:pfam01661   1 VNAANSRLLGGGGvAGAIHRAAGPELLEECRELkkGGCPTGEAVVTPGGNLPAKYVIHTVGPTWRHGGSHGEEELLESCY 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 242036899  193 RSCLELLIENGLESIATGCIYTEAKNYPREPAAHVA 228
Cdd:pfam01661  81 RNALALAEELGIKSIAFPAISTGIYGFPWEEAARIA 116
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
 425-558 5.50e-33

Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain family. This family includes ECM25 that contains a divergent CRAL-TRIO domain identified by Gallego and colleagues.


Pssm-ID: 463965 [Multi-domain]  Cd Length: 140  Bit Score: 123.21  E-value: 5.50e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242036899  425 GHPVMVVVGAHF---LLRCLDLERFVLYVIKEF-EPLIQKPYSIVYFHSAASLQPQPDLGFMKRLQQILGRKHQKNLHTI 500
Cdd:pfam13716   1 GRPVLVFISKLLpsrPASLDDLDRLLFYLLKTLsEKLKGKPFVVVVDHTGVTSENFPSLSFLKKAYDLLPRAFKKNLKAV 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 242036899  501 YILHPTLGLRTAV-MAMQLFVDGEVWKKVVYVDRLVQLFRYVPREQLT--IPdFVFQHDLE 558
Cdd:pfam13716  81 YVVHPSTFLRTFLkTLGSLLGSKKLRKKVHYVSSLSELWEGIDREQLPteLP-GVLSYDEE 140
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 414-549 8.56e-23

Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory proteins, such as S. cerevisiae phosphatidylinositol transfer protein (Sec14p), and in lipid regulated proteins such as RhoGAPs, RhoGEFs and neurofibromin (NF1). SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 469559 [Multi-domain]  Cd Length: 156  Bit Score: 95.09  E-value: 8.56e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242036899 414 KIIYRGGVDSEGHPVMVVVGAHFLLRCLDLERFVLYVIKEFEPLIQKPYSIVYFHSA------ASLQPQPDLGFMKRLQQ 487
Cdd:cd00170   10 GIGYLGGRDKEGRPVLVFRAGWDPPKLLDLEELLRYLVYLLEKALRELEEQVEGFVViidlkgFSLSNLSDLSLLKKLLK 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 242036899 488 ILGRKHQKNLHTIYILHPTLGLRTAVMAMQLFVDGEVWKKVVYVDR-LVQLFRYVPREQLTIP 549
Cdd:cd00170   90 ILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGSdLEELLEYIDPDQLPKE 152
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 99-212 2.35e-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: 2.35e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242036899    99 KIYLWRGHPWSLEVDAVVNSTNENLdeAHSSP---GLHAAAG-TGLAEECATL--GGCRTGMAKMTNAYDLPARKVIHTV 172
Cdd:smart00506   1 ILKVVKGDITKPRADAIVNAANSDG--AHGGGvagAIARAAGkALSKEEVRKLagGECPVGTAVVTEGGNLPAKYVIHAV 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 242036899   173 GPKyAVKYHTAAENALSHCYRSCLELLIENGLESIATGCI 212
Cdd:smart00506  79 GPR-ASGHSKEGFELLENAYRNCLELAIELGITSVALPLI 117
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 406-547 3.74e-13

Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p) and in RhoGAPs, RhoGEFs and the RasGAP, neurofibromin (NF1). Lipid-binding domain. The SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 214706 [Multi-domain]  Cd Length: 158  Bit Score: 67.32  E-value: 3.74e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242036899   406 NLSDVAEMKIIYRGgVDSEGHPVMVVVGAHFLLRCLDLERFVLYVIKEFEPLIQ---KPYSIVYFHSAASLQ----PQPD 478
Cdd:smart00516   1 ELELLKAYIPGGRG-YDKDGRPVLIERAGRFDLKSVTLEELLRYLVYVLEKILQeekKTGGIEGFTVIFDLKglsmSNPD 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 242036899   479 LGFMKRLQQILGRKHQKNLHTIYILHPTLGLRTAVMAMQLFVDGEVWKKVVYVDRLVQ--LFRYVPREQLT 547
Cdd:smart00516  80 LSVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNDSKeeLLEYIDKEQLP 150
 
Name Accession Description Interval E-value
Macro_GDAP2-like cd02905
macrodomain, GDAP2-like family; Macrodomains are found in a variety of proteins with diverse ...
 98-266 6.73e-99

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: 297.61  E-value: 6.73e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242036899  98 SKIYLWRGHPWSLEVDAVVNSTNENL-DEAHSSPGLHAAAGTGLAEECATLGGCRTGMAKMTNAYDLPARKVIHTVGPKY 176
Cdd:cd02905    1 RKIVLWDGDLTLLNVDAIVNSTNESLtDKSPISDRLFLAAGPELREELAKLGGCRTGEAKLTKGYNLPARYVIHTVGPRY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242036899 177 AVKYHTAAENALSHCYRSCLELLIENGLESIATGCIYTEAKNYPREPAAHVAIRTVRRFLEKQKDKITAIVFCTiSSSDT 256
Cdd:cd02905   81 NEKYRTAAESALYSCYRNVLQLAKEHKLRSVAFPVIHSERRGYPLEDGAHIALRTVRRFLEKHGSSFEAVVFVV-TEEEM 159

                        170
                 ....*....|
gi 242036899 257 EIYKRLLPLY 266
Cdd:cd02905  160 ETYERLLPLY 169
Macro_OAADPr_deacetylase cd02908
macrodomain, O-acetyl-ADP-ribose (OAADPr) family; Macrodomains are found in a variety of ...
 99-264 5.49e-56

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: 186.18  E-value: 5.49e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242036899  99 KIYLWRGHPWSLEVDAVVNSTNENL------DEAhsspgLHAAAGTGLAEECATLGG-CRTGMAKMTNAYDLPARKVIHT 171
Cdd:cd02908    1 KISLWRGDITKLEVDAIVNAANSSLlggggvDGA-----IHRAAGPELLEECRKLGGvCPTGEAKITPGYNLPAKYVIHT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242036899 172 VGPKYAVKYHTAAENaLSHCYRSCLELLIENGLESIATGCIYTEAKNYPREPAAHVAIRTVRRFLEKQkDKITAIVFCTI 251
Cdd:cd02908   76 VGPIGEGGVEEEPEL-LASCYRSSLELALENGLKSIAFPCISTGIYGYPNEEAAEIALNTVREWLEEH-DKIDRIIFVVF 153

                        170
                 ....*....|...
gi 242036899 252 SSSDTEIYKRLLP 264
Cdd:cd02908  154 LDEDYKIYEELLP 166
PRK04143 PRK04143
protein-ADP-ribose hydrolase;
96-263 1.06e-41

protein-ADP-ribose hydrolase;


Pssm-ID: 235225  Cd Length: 264  Bit Score: 151.29  E-value: 1.06e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242036899  96 INSKIYLWRGHPWSLEVDAVVNSTNENL-----------DEAhsspgLHAAAGTGLAEECA---TLGGCR--TGMAKMTN 159
Cdd:PRK04143  81 KYDNIFLWQGDITRLKVDAIVNAANSRLlgcfqpnhdciDNA-----IHTFAGVQLRLDCAeimTEQGRKeaTGQAKITR 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242036899 160 AYDLPARKVIHTVGPKYAvKYHTAAENA--LSHCYRSCLELLIENGLESIATGCIYTEAKNYPREPAAHVAIRTVRRFLE 237
Cdd:PRK04143 156 AYNLPAKYVIHTVGPIIR-KQPVSPIRAdlLASCYRSCLKLAEKAGLKSIAFCCISTGVFGFPKEEAAEIAIKTVLSWLK 234

                        170       180
                 ....*....|....*....|....*.
gi 242036899 238 KQKDKITaIVFCTISSSDTEIYKRLL 263
Cdd:PRK04143 235 ENPSKLK-VVFNVFTDEDLELYQKAL 259
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 100-263 1.09e-39

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: 142.62  E-value: 1.09e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242036899 100 IYLWRGHPWSLEVDAVVNSTNENL------DEAhsspgLHAAAGTGLAEECATL---GGCRTGMAKMTNAYDLPARKVIH 170
Cdd:COG2110    1 IEIVQGDITELDVDAIVNAANSSLlggggvAGA-----IHRAAGPELLEECRRLckqGGCPTGEAVITPAGNLPAKYVIH 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242036899 171 TVGPKYAVKYHTAAEnALSHCYRSCLELLIENGLESIA-----TGcIYteakNYPREPAAHVAIRTVRRFLEKQkDKITA 245
Cdd:COG2110   76 TVGPVWRGGGPSEEE-LLASCYRNSLELAEELGIRSIAfpaigTG-VG----GFPWEEAAPIAVETLRDFLEEH-PSLEE 148

                        170
                 ....*....|....*...
gi 242036899 246 IVFCTISSSDTEIYKRLL 263
Cdd:COG2110  149 VRFVLFDEEDYEAYRRAL 166
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 116-228 2.56e-36

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: 131.53  E-value: 2.56e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242036899  116 VNSTNENLDEAHS-SPGLHAAAGTGLAEECATL--GGCRTGMAKMTNAYDLPARKVIHTVGPKYAVKYHTAAENALSHCY 192
Cdd:pfam01661   1 VNAANSRLLGGGGvAGAIHRAAGPELLEECRELkkGGCPTGEAVVTPGGNLPAKYVIHTVGPTWRHGGSHGEEELLESCY 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 242036899  193 RSCLELLIENGLESIATGCIYTEAKNYPREPAAHVA 228
Cdd:pfam01661  81 RNALALAEELGIKSIAFPAISTGIYGFPWEEAARIA 116
PRK00431 PRK00431
ADP-ribose-binding protein;
99-263 1.38e-34

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 128.81  E-value: 1.38e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242036899  99 KIYLWRGHPWSLEVDAVVNSTNENL------DEAhsspgLHAAAGTGLAEEC----ATLGGCRTGMAKMTNAYDLPARKV 168
Cdd:PRK00431   4 RIEVVQGDITELEVDAIVNAANSSLlggggvDGA-----IHRAAGPEILEECrelrQQQGPCPTGEAVITSAGRLPAKYV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242036899 169 IHTVGPKYAVKYHTAAENaLSHCYRSCLELLIENGLESIATGCIYTEAKNYPREPAAHVAIRTVRRFLEKQKDkITAIVF 248
Cdd:PRK00431  79 IHTVGPVWRGGEDNEAEL-LASAYRNSLRLAAELGLRSIAFPAISTGVYGYPLEDAARIAVKTVREFLTRHKS-PEEVYF 156

                        170
                 ....*....|....*
gi 242036899 249 CTISSSDTEIYKRLL 263
Cdd:PRK00431 157 VCYDEEAYRLYERLL 171
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
 425-558 5.50e-33

Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain family. This family includes ECM25 that contains a divergent CRAL-TRIO domain identified by Gallego and colleagues.


Pssm-ID: 463965 [Multi-domain]  Cd Length: 140  Bit Score: 123.21  E-value: 5.50e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242036899  425 GHPVMVVVGAHF---LLRCLDLERFVLYVIKEF-EPLIQKPYSIVYFHSAASLQPQPDLGFMKRLQQILGRKHQKNLHTI 500
Cdd:pfam13716   1 GRPVLVFISKLLpsrPASLDDLDRLLFYLLKTLsEKLKGKPFVVVVDHTGVTSENFPSLSFLKKAYDLLPRAFKKNLKAV 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 242036899  501 YILHPTLGLRTAV-MAMQLFVDGEVWKKVVYVDRLVQLFRYVPREQLT--IPdFVFQHDLE 558
Cdd:pfam13716  81 YVVHPSTFLRTFLkTLGSLLGSKKLRKKVHYVSSLSELWEGIDREQLPteLP-GVLSYDEE 140
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 414-549 8.56e-23

Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory proteins, such as S. cerevisiae phosphatidylinositol transfer protein (Sec14p), and in lipid regulated proteins such as RhoGAPs, RhoGEFs and neurofibromin (NF1). SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 469559 [Multi-domain]  Cd Length: 156  Bit Score: 95.09  E-value: 8.56e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242036899 414 KIIYRGGVDSEGHPVMVVVGAHFLLRCLDLERFVLYVIKEFEPLIQKPYSIVYFHSA------ASLQPQPDLGFMKRLQQ 487
Cdd:cd00170   10 GIGYLGGRDKEGRPVLVFRAGWDPPKLLDLEELLRYLVYLLEKALRELEEQVEGFVViidlkgFSLSNLSDLSLLKKLLK 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 242036899 488 ILGRKHQKNLHTIYILHPTLGLRTAVMAMQLFVDGEVWKKVVYVDR-LVQLFRYVPREQLTIP 549
Cdd:cd00170   90 ILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGSdLEELLEYIDPDQLPKE 152
Macro_SF cd02749
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 113-231 2.72e-22

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


Pssm-ID: 394871  Cd Length: 121  Bit Score: 92.46  E-value: 2.72e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242036899 113 DAVVNSTNENL-DEAHSSPGLHAAAGTGLAEECA---TLGGCRTGMAKMTNAYDLPARKVIHTVGPKYavKYHTAAENAL 188
Cdd:cd02749    1 DAIVNPANNDLyLGGGVAKAISKKAGGDLQEECEerkKNGYLKVGEVAVTKGGNLPARYIIHVVGPVA--SSKKKTYEPL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 242036899 189 SHCYRSCLELLIENGLESIATGCIYTEAKNYPREPAAHVAIRT 231
Cdd:cd02749   79 KKCVKNCLSLADEKGLKSVAFPAIGTGIAGFPPEEAARIMLEA 121
Macro_Af1521_BAL-like cd02907
macrodomain, Af1521-like family; Macrodomains are found in a variety of proteins with diverse ...
 99-243 1.11e-20

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: 89.09  E-value: 1.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242036899  99 KIYLWRGHPWSLEVDAVVNSTNENLDeaHSSpGLHAA----AGTGLAEEC----ATLGGCRTGMAKMTNAYDLPARKVIH 170
Cdd:cd02907    3 KVSVYKGDITKEKVDAIVNAANERLK--HGG-GVAGAiskaGGPEIQEECdkyiKKNGKLRVGEVVVTSAGKLPCKYVIH 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 242036899 171 TVGPKYAVKYHTAAENALSHCYRSCLELLIENGLESIA-----TGcIYteakNYPREPAAHVAIRTVRRFLEKQKDKI 243
Cdd:cd02907   80 AVGPRWSGGSKEECEDLLYKAVLNSLEEAEELKATSIAipaisSG-IF----GFPLDLCAEAIVEAIKDFSESNSSSS 152
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 99-212 2.35e-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: 2.35e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242036899    99 KIYLWRGHPWSLEVDAVVNSTNENLdeAHSSP---GLHAAAG-TGLAEECATL--GGCRTGMAKMTNAYDLPARKVIHTV 172
Cdd:smart00506   1 ILKVVKGDITKPRADAIVNAANSDG--AHGGGvagAIARAAGkALSKEEVRKLagGECPVGTAVVTEGGNLPAKYVIHAV 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 242036899   173 GPKyAVKYHTAAENALSHCYRSCLELLIENGLESIATGCI 212
Cdd:smart00506  79 GPR-ASGHSKEGFELLENAYRNCLELAIELGITSVALPLI 117
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 406-547 3.74e-13

Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p) and in RhoGAPs, RhoGEFs and the RasGAP, neurofibromin (NF1). Lipid-binding domain. The SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 214706 [Multi-domain]  Cd Length: 158  Bit Score: 67.32  E-value: 3.74e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242036899   406 NLSDVAEMKIIYRGgVDSEGHPVMVVVGAHFLLRCLDLERFVLYVIKEFEPLIQ---KPYSIVYFHSAASLQ----PQPD 478
Cdd:smart00516   1 ELELLKAYIPGGRG-YDKDGRPVLIERAGRFDLKSVTLEELLRYLVYVLEKILQeekKTGGIEGFTVIFDLKglsmSNPD 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 242036899   479 LGFMKRLQQILGRKHQKNLHTIYILHPTLGLRTAVMAMQLFVDGEVWKKVVYVDRLVQ--LFRYVPREQLT 547
Cdd:smart00516  80 LSVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNDSKeeLLEYIDKEQLP 150
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 112-242 3.18e-11

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: 62.27  E-value: 3.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242036899 112 VDAVVNSTN-ENLDEAHSSPGLHAAAGTGLAEECATLG-GCRTGMAKMTNAYDLPARKVIHTVGPKYAVKYHTAAENALs 189
Cdd:cd02903   22 TDVIVNSVSsDLLLKGGVSKAILKAAGPELQDECANQGkQPASGDVIVTSGGNLPCKYVYHVVLPHYNPGNEKTLKDIV- 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 242036899 190 hcyRSCLELLIENGLESIATGCIYTEAKNYPREPAAHVAIRTVRRFLEKQKDK 242
Cdd:cd02903  101 ---RKCLEKAENYKMSSISFPAIGTGNLGFPKDVVAEIMIDEVLKFSSKNPSS 150
Macro_Ttha0132-like cd03330
Macrodomain, uncharacterized family similar to Thermus thermophilus hypothetical protein ...
 109-246 1.04e-10

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: 60.14  E-value: 1.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242036899 109 SLEVDAVVNSTNENLDEAHSSPG-LHAAAGTGLAEECATLGGCRTGMAKMTNAYDLPARKVIH--TVGPKYavkyhTAAE 185
Cdd:cd03330   11 EQDADAIVNAANRRLLMGSGVAGaIKRKGGEEIEREAMRKGPIRVGEAVETGAGKLPAKYVIHaaVMGMPG-----RSSE 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 242036899 186 NALSHCYRSCLELLIENGLESIATGCIYTEAKNYPREPAAHVAIRTVRRFLEKQKDKITAI 246
Cdd:cd03330   86 ESIRDATRNALAKAEELGLESVAFPAIGTGVGGFPVEEVARIMLEEIKKCDPPLLEEVRLY 146
Macro_H2A-like cd02904
macrodomain, macroH2A-like family; Macrodomains are found in a variety of proteins with ...
 99-259 1.84e-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: 57.32  E-value: 1.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242036899  99 KIYLWRGHPWSLEVDAVVNSTNENLD---EAHSSpgLHAAAGTGLAEECATL----GGCRTGMAKMTNAYDLPARKVIHT 171
Cdd:cd02904   19 KLTVVQGDIASIKADAIVHPTNATFYlggEVGSA--LEKAGGKEFVEEVKELrksnGPLEVAGAAISPGHNLPAKFVIHC 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242036899 172 VGPKYAvkyHTAAENALSHCYRSCLELLIENGLESIATGCIYTEAKNYPREPAAHVAIRTvrrflekqkdkITAIVFCTI 251
Cdd:cd02904   97 NSPSWG---SDKCEELLEKTVKNCLALADEKKLKSVAFPSIGSGRNGFPKQTAAQTILKA-----------ISNYFVSVM 162


                 ....*...
gi 242036899 252 SSSDTEIY 259
Cdd:cd02904  163 SSSLKQIY 170
Macro_X_Nsp3-like cd21557
X-domain (or Mac1 domain) of viral non-structural protein 3 and related macrodomains; The ...
 113-198 2.87e-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: 43.70  E-value: 2.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242036899 113 DAVVNSTNENLdeahsSPG------LHAAAGTGLAEEC---ATLGGCRTGMAKMTNAYDLpARKVIHTVGPKYAVKYhta 183
Cdd:cd21557    2 DVVVNAANENL-----KHGggvagaIYKATGGAFQKESdyiKKNGPLKVGTAVLLPGHGL-AKNIIHVVGPRKRKGQ--- 72

                         90
                 ....*....|....*
gi 242036899 184 AENALSHCYRSCLEL 198
Cdd:cd21557   73 DDQLLAAAYKAVNKE 87
CRAL_TRIO pfam00650
CRAL/TRIO domain;
413-546 6.74e-05

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 43.40  E-value: 6.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242036899  413 MKIIYRGGVDSEGHPVMVVVGAHFLLRCLDLE---RFVLYV----IKEFEPLIQKPYSIVY-FH-SAASLQPQPDLGFMK 483
Cdd:pfam00650   1 GGKVYLHGRDKEGRPVLYLRLGRHDPKKSSEEelvRFLVLVleraLLLMPEGQVEGLTVIIdLKgLSLSNMDWWSISLLK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 242036899  484 RLQQILgrkhQKN----LHTIYILHPTLGLRTAVMAMQLFVDGEVWKKVVYVD--RLVQLFRYVPREQL 546
Cdd:pfam00650  81 KIIKIL----QDNyperLGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVFLKnsNEEELEKYIPPEQL 145
 
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