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Conserved domains on  [gi|22094097|ref|NP_034399|]
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ganglioside-induced differentiation-associated protein 2 isoform 1 [Mus musculus]

Protein Classification

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

Macro_GDAP2_like and SEC14 domain-containing protein

Graphical summary

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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 ...
 55-222 1.55e-110

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: 324.57  E-value: 1.55e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094097  55 KVVLWKGDVALLNCTAIVNTSNESLTDKNPVSESIFMLAGPDLKEDLQKLKGCRTGEAKLTKGFNLAARFIIHTVGPKYK 134
Cdd:cd02905   2 KIVLWDGDLTLLNVDAIVNSTNESLTDKSPISDRLFLAAGPELREELAKLGGCRTGEAKLTKGYNLPARYVIHTVGPRYN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094097 135 SRYRTAAESSLYSCYRNVLQLAKEQSMSSVGFCVINSAKRGYPLEDATHIALRTVRRFLEIHGENIEKVVFAVSELEEAT 214
Cdd:cd02905  82 EKYRTAAESALYSCYRNVLQLAKEHKLRSVAFPVIHSERRGYPLEDGAHIALRTVRRFLEKHGSSFEAVVFVVTEEEMET 161


                ....*...
gi 22094097 215 YQKLLPLY 222
Cdd:cd02905 162 YERLLPLY 169
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
 350-481 1.86e-32

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: 120.90  E-value: 1.86e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094097   350 GRTVMVVVGRNIPV---TLIDMDKALLYFIH-VMDHIAVKEYVLVYFHTLTSDYNHLDSDFLKKLYDVVDIKYKRNLKAV 425
Cdd:pfam13716   1 GRPVLVFISKLLPSrpaSLDDLDRLLFYLLKtLSEKLKGKPFVVVVDHTGVTSENFPSLSFLKKAYDLLPRAFKKNLKAV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 22094097   426 YFVHPTFRSKVSTW-FFTTFSVSGLKDKIHHVDSLQQLFSAISPEQIDFP-PFVLEYD 481
Cdd:pfam13716  81 YVVHPSTFLRTFLKtLGSLLGSKKLRKKVHYVSSLSELWEGIDREQLPTElPGVLSYD 138
 
Name Accession Description Interval E-value
Macro_GDAP2-like cd02905
macrodomain, GDAP2-like family; Macrodomains are found in a variety of proteins with diverse ...
 55-222 1.55e-110

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: 324.57  E-value: 1.55e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094097  55 KVVLWKGDVALLNCTAIVNTSNESLTDKNPVSESIFMLAGPDLKEDLQKLKGCRTGEAKLTKGFNLAARFIIHTVGPKYK 134
Cdd:cd02905   2 KIVLWDGDLTLLNVDAIVNSTNESLTDKSPISDRLFLAAGPELREELAKLGGCRTGEAKLTKGYNLPARYVIHTVGPRYN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094097 135 SRYRTAAESSLYSCYRNVLQLAKEQSMSSVGFCVINSAKRGYPLEDATHIALRTVRRFLEIHGENIEKVVFAVSELEEAT 214
Cdd:cd02905  82 EKYRTAAESALYSCYRNVLQLAKEHKLRSVAFPVIHSERRGYPLEDGAHIALRTVRRFLEKHGSSFEAVVFVVTEEEMET 161


                ....*...
gi 22094097 215 YQKLLPLY 222
Cdd:cd02905 162 YERLLPLY 169
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 56-219 2.26e-41

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


Pssm-ID: 441713  Cd Length: 168  Bit Score: 145.70  E-value: 2.26e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094097  56 VVLWKGDVALLNCTAIVNTSNESLTDKNPVSESIFMLAGPDLKEDLQKL---KGCRTGEAKLTKGFNLAARFIIHTVGPK 132
Cdd:COG2110   1 IEIVQGDITELDVDAIVNAANSSLLGGGGVAGAIHRAAGPELLEECRRLckqGGCPTGEAVITPAGNLPAKYVIHTVGPV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094097 133 YKSRYRTAAEsSLYSCYRNVLQLAKEQSMSSVGFCVINSAKRGYPLEDATHIALRTVRRFLEIHgENIEKVVFAV-SELE 211
Cdd:COG2110  81 WRGGGPSEEE-LLASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFLEEH-PSLEEVRFVLfDEED 158


                ....*...
gi 22094097 212 EATYQKLL 219
Cdd:COG2110 159 YEAYRRAL 166
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 72-185 7.28e-39

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: 137.31  E-value: 7.28e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094097    72 VNTSNESLTDKNPVSESIFMLAGPDLKEDLQKLK--GCRTGEAKLTKGFNLAARFIIHTVGPKYKSRYRTAAESSLYSCY 149
Cdd:pfam01661   1 VNAANSRLLGGGGVAGAIHRAAGPELLEECRELKkgGCPTGEAVVTPGGNLPAKYVIHTVGPTWRHGGSHGEEELLESCY 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 22094097   150 RNVLQLAKEQSMSSVGFCVINSAKRGYPLEDATHIA 185
Cdd:pfam01661  81 RNALALAEELGIKSIAFPAISTGIYGFPWEEAARIA 116
PRK00431 PRK00431
ADP-ribose-binding protein;
55-219 1.38e-34

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 127.65  E-value: 1.38e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094097   55 KVVLWKGDVALLNCTAIVNTSNESLTDKNPVSESIFMLAGPDL----KEDLQKLKGCRTGEAKLTKGFNLAARFIIHTVG 130
Cdd:PRK00431   4 RIEVVQGDITELEVDAIVNAANSSLLGGGGVDGAIHRAAGPEIleecRELRQQQGPCPTGEAVITSAGRLPAKYVIHTVG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094097  131 PKYKSRYRTAAEsSLYSCYRNVLQLAKEQSMSSVGFCVINSAKRGYPLEDATHIALRTVRRFLEIHgENIEKVVF-AVSE 209
Cdd:PRK00431  84 PVWRGGEDNEAE-LLASAYRNSLRLAAELGLRSIAFPAISTGVYGYPLEDAARIAVKTVREFLTRH-KSPEEVYFvCYDE 161

                        170
                 ....*....|
gi 22094097  210 LEEATYQKLL 219
Cdd:PRK00431 162 EAYRLYERLL 171
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
 350-481 1.86e-32

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: 120.90  E-value: 1.86e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094097   350 GRTVMVVVGRNIPV---TLIDMDKALLYFIH-VMDHIAVKEYVLVYFHTLTSDYNHLDSDFLKKLYDVVDIKYKRNLKAV 425
Cdd:pfam13716   1 GRPVLVFISKLLPSrpaSLDDLDRLLFYLLKtLSEKLKGKPFVVVVDHTGVTSENFPSLSFLKKAYDLLPRAFKKNLKAV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 22094097   426 YFVHPTFRSKVSTW-FFTTFSVSGLKDKIHHVDSLQQLFSAISPEQIDFP-PFVLEYD 481
Cdd:pfam13716  81 YVVHPSTFLRTFLKtLGSLLGSKKLRKKVHYVSSLSELWEGIDREQLPTElPGVLSYD 138
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 334-481 6.36e-25

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: 100.45  E-value: 6.36e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094097    334 DIASLKALYQ--TGVDNCGRTVMVVVGRNIPVTLIDMDKALLYFIHVMDHIAV---KEYVLVYFHTLT----SDYNHLDS 404
Cdd:smart00516   1 ELELLKAYIPggRGYDKDGRPVLIERAGRFDLKSVTLEELLRYLVYVLEKILQeekKTGGIEGFTVIFdlkgLSMSNPDL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22094097    405 DFLKKLYDVVDIKYKRNLKAVYFVHPTFRSKVSTWFFTTFSVSGLKDKIHHVDSLQQLFSAISPEQIDFPPFVLEYD 481
Cdd:smart00516  81 SVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNDSKEELLEYIDKEQLPEELGGTL 157
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 55-182 7.71e-22

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: 91.21  E-value: 7.71e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094097     55 KVVLWKGDVALLNCTAIVNTSNESLTDKNPVSESIFMLAGPDL-KEDLQKL--KGCRTGEAKLTKGFNLAARFIIHTVGP 131
Cdd:smart00506   1 ILKVVKGDITKPRADAIVNAANSDGAHGGGVAGAIARAAGKALsKEEVRKLagGECPVGTAVVTEGGNLPAKYVIHAVGP 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 22094097    132 KYkSRYRTAAESSLYSCYRNVLQLAKEQSMSSVGFCVINSAKRGYPLEDAT 182
Cdd:smart00506  81 RA-SGHSKEGFELLENAYRNCLELAIELGITSVALPLIGTGIYGVPKDRSA 130
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 330-471 8.01e-20

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: 86.23  E-value: 8.01e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094097 330 EDLSDIASlKALYQTGVDNCGRTVMVVVGRNIPVTLIDMDKALLYFIHVMDHIAVKEYVLVYFHTLTSDY------NHLD 403
Cdd:cd00170   2 EELLELLG-GIGYLGGRDKEGRPVLVFRAGWDPPKLLDLEELLRYLVYLLEKALRELEEQVEGFVVIIDLkgfslsNLSD 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22094097 404 SDFLKKLYDVVDIKYKRNLKAVYFVHPTFRSKVSTWFFTTFSVSGLKDKIHHVDS-LQQLFSAISPEQI 471
Cdd:cd00170  81 LSLLKKLLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGSdLEELLEYIDPDQL 149
 
Name Accession Description Interval E-value
Macro_GDAP2-like cd02905
macrodomain, GDAP2-like family; Macrodomains are found in a variety of proteins with diverse ...
 55-222 1.55e-110

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: 324.57  E-value: 1.55e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094097  55 KVVLWKGDVALLNCTAIVNTSNESLTDKNPVSESIFMLAGPDLKEDLQKLKGCRTGEAKLTKGFNLAARFIIHTVGPKYK 134
Cdd:cd02905   2 KIVLWDGDLTLLNVDAIVNSTNESLTDKSPISDRLFLAAGPELREELAKLGGCRTGEAKLTKGYNLPARYVIHTVGPRYN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094097 135 SRYRTAAESSLYSCYRNVLQLAKEQSMSSVGFCVINSAKRGYPLEDATHIALRTVRRFLEIHGENIEKVVFAVSELEEAT 214
Cdd:cd02905  82 EKYRTAAESALYSCYRNVLQLAKEHKLRSVAFPVIHSERRGYPLEDGAHIALRTVRRFLEKHGSSFEAVVFVVTEEEMET 161


                ....*...
gi 22094097 215 YQKLLPLY 222
Cdd:cd02905 162 YERLLPLY 169
Macro_OAADPr_deacetylase cd02908
macrodomain, O-acetyl-ADP-ribose (OAADPr) family; Macrodomains are found in a variety of ...
 55-220 5.83e-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: 184.25  E-value: 5.83e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094097  55 KVVLWKGDVALLNCTAIVNTSNESLTDKNPVSESIFMLAGPDLKEDLQKLKG-CRTGEAKLTKGFNLAARFIIHTVGPKY 133
Cdd:cd02908   1 KISLWRGDITKLEVDAIVNAANSSLLGGGGVDGAIHRAAGPELLEECRKLGGvCPTGEAKITPGYNLPAKYVIHTVGPIG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094097 134 KSRYRTAAESsLYSCYRNVLQLAKEQSMSSVGFCVINSAKRGYPLEDATHIALRTVRRFLEIHGEnIEKVVFAV-SELEE 212
Cdd:cd02908  81 EGGVEEEPEL-LASCYRSSLELALENGLKSIAFPCISTGIYGYPNEEAAEIALNTVREWLEEHDK-IDRIIFVVfLDEDY 158


                ....*...
gi 22094097 213 ATYQKLLP 220
Cdd:cd02908 159 KIYEELLP 166
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 56-219 2.26e-41

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


Pssm-ID: 441713  Cd Length: 168  Bit Score: 145.70  E-value: 2.26e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094097  56 VVLWKGDVALLNCTAIVNTSNESLTDKNPVSESIFMLAGPDLKEDLQKL---KGCRTGEAKLTKGFNLAARFIIHTVGPK 132
Cdd:COG2110   1 IEIVQGDITELDVDAIVNAANSSLLGGGGVAGAIHRAAGPELLEECRRLckqGGCPTGEAVITPAGNLPAKYVIHTVGPV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094097 133 YKSRYRTAAEsSLYSCYRNVLQLAKEQSMSSVGFCVINSAKRGYPLEDATHIALRTVRRFLEIHgENIEKVVFAV-SELE 211
Cdd:COG2110  81 WRGGGPSEEE-LLASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDFLEEH-PSLEEVRFVLfDEED 158


                ....*...
gi 22094097 212 EATYQKLL 219
Cdd:COG2110 159 YEAYRRAL 166
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 72-185 7.28e-39

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: 137.31  E-value: 7.28e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094097    72 VNTSNESLTDKNPVSESIFMLAGPDLKEDLQKLK--GCRTGEAKLTKGFNLAARFIIHTVGPKYKSRYRTAAESSLYSCY 149
Cdd:pfam01661   1 VNAANSRLLGGGGVAGAIHRAAGPELLEECRELKkgGCPTGEAVVTPGGNLPAKYVIHTVGPTWRHGGSHGEEELLESCY 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 22094097   150 RNVLQLAKEQSMSSVGFCVINSAKRGYPLEDATHIA 185
Cdd:pfam01661  81 RNALALAEELGIKSIAFPAISTGIYGFPWEEAARIA 116
Macro_SF cd02749
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 69-188 8.28e-38

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: 134.45  E-value: 8.28e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094097  69 TAIVNTSNESLTDKNPVSESIFMLAGPDLKE---DLQKLKGCRTGEAKLTKGFNLAARFIIHTVGPKYksRYRTAAESSL 145
Cdd:cd02749   1 DAIVNPANNDLYLGGGVAKAISKKAGGDLQEeceERKKNGYLKVGEVAVTKGGNLPARYIIHVVGPVA--SSKKKTYEPL 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 22094097 146 YSCYRNVLQLAKEQSMSSVGFCVINSAKRGYPLEDATHIALRT 188
Cdd:cd02749  79 KKCVKNCLSLADEKGLKSVAFPAIGTGIAGFPPEEAARIMLEA 121
PRK00431 PRK00431
ADP-ribose-binding protein;
55-219 1.38e-34

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 127.65  E-value: 1.38e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094097   55 KVVLWKGDVALLNCTAIVNTSNESLTDKNPVSESIFMLAGPDL----KEDLQKLKGCRTGEAKLTKGFNLAARFIIHTVG 130
Cdd:PRK00431   4 RIEVVQGDITELEVDAIVNAANSSLLGGGGVDGAIHRAAGPEIleecRELRQQQGPCPTGEAVITSAGRLPAKYVIHTVG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094097  131 PKYKSRYRTAAEsSLYSCYRNVLQLAKEQSMSSVGFCVINSAKRGYPLEDATHIALRTVRRFLEIHgENIEKVVF-AVSE 209
Cdd:PRK00431  84 PVWRGGEDNEAE-LLASAYRNSLRLAAELGLRSIAFPAISTGVYGYPLEDAARIAVKTVREFLTRH-KSPEEVYFvCYDE 161

                        170
                 ....*....|
gi 22094097  210 LEEATYQKLL 219
Cdd:PRK00431 162 EAYRLYERLL 171
PRK04143 PRK04143
protein-ADP-ribose hydrolase;
55-219 3.08e-34

protein-ADP-ribose hydrolase;


Pssm-ID: 235225  Cd Length: 264  Bit Score: 129.72  E-value: 3.08e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094097   55 KVVLWKGDVALLNCTAIVNTSNESLT-----DKNPVSESIFMLAGPDLKEDLQKL---KGCR--TGEAKLTKGFNLAARF 124
Cdd:PRK04143  84 NIFLWQGDITRLKVDAIVNAANSRLLgcfqpNHDCIDNAIHTFAGVQLRLDCAEImteQGRKeaTGQAKITRAYNLPAKY 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094097  125 IIHTVGPK-YKSRYRTAAESSLYSCYRNVLQLAKEQSMSSVGFCVINSAKRGYPLEDATHIALRTVRRFLEIHGENIeKV 203
Cdd:PRK04143 164 VIHTVGPIiRKQPVSPIRADLLASCYRSCLKLAEKAGLKSIAFCCISTGVFGFPKEEAAEIAIKTVLSWLKENPSKL-KV 242

                        170
                 ....*....|....*..
gi 22094097  204 VFAV-SELEEATYQKLL 219
Cdd:PRK04143 243 VFNVfTDEDLELYQKAL 259
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
 350-481 1.86e-32

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: 120.90  E-value: 1.86e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094097   350 GRTVMVVVGRNIPV---TLIDMDKALLYFIH-VMDHIAVKEYVLVYFHTLTSDYNHLDSDFLKKLYDVVDIKYKRNLKAV 425
Cdd:pfam13716   1 GRPVLVFISKLLPSrpaSLDDLDRLLFYLLKtLSEKLKGKPFVVVVDHTGVTSENFPSLSFLKKAYDLLPRAFKKNLKAV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 22094097   426 YFVHPTFRSKVSTW-FFTTFSVSGLKDKIHHVDSLQQLFSAISPEQIDFP-PFVLEYD 481
Cdd:pfam13716  81 YVVHPSTFLRTFLKtLGSLLGSKKLRKKVHYVSSLSELWEGIDREQLPTElPGVLSYD 138
Macro_Af1521_BAL-like cd02907
macrodomain, Af1521-like family; Macrodomains are found in a variety of proteins with diverse ...
 55-194 3.42e-27

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: 106.81  E-value: 3.42e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094097  55 KVVLWKGDVALLNCTAIVNTSNESLtdKNP--VSESIFMLAGPDLKED----LQKLKGCRTGEAKLTKGFNLAARFIIHT 128
Cdd:cd02907   3 KVSVYKGDITKEKVDAIVNAANERL--KHGggVAGAISKAGGPEIQEEcdkyIKKNGKLRVGEVVVTSAGKLPCKYVIHA 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22094097 129 VGPKYKSRYRTAAESSLYSCYRNVLQLAKEQSMSSVGFCVINSAKRGYPLEDATHIALRTVRRFLE 194
Cdd:cd02907  81 VGPRWSGGSKEECEDLLYKAVLNSLEEAEELKATSIAIPAISSGIFGFPLDLCAEAIVEAIKDFSE 146
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 334-481 6.36e-25

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: 100.45  E-value: 6.36e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094097    334 DIASLKALYQ--TGVDNCGRTVMVVVGRNIPVTLIDMDKALLYFIHVMDHIAV---KEYVLVYFHTLT----SDYNHLDS 404
Cdd:smart00516   1 ELELLKAYIPggRGYDKDGRPVLIERAGRFDLKSVTLEELLRYLVYVLEKILQeekKTGGIEGFTVIFdlkgLSMSNPDL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22094097    405 DFLKKLYDVVDIKYKRNLKAVYFVHPTFRSKVSTWFFTTFSVSGLKDKIHHVDSLQQLFSAISPEQIDFPPFVLEYD 481
Cdd:smart00516  81 SVLRKILKILQDHYPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGNDSKEELLEYIDKEQLPEELGGTL 157
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 55-182 7.71e-22

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: 91.21  E-value: 7.71e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094097     55 KVVLWKGDVALLNCTAIVNTSNESLTDKNPVSESIFMLAGPDL-KEDLQKL--KGCRTGEAKLTKGFNLAARFIIHTVGP 131
Cdd:smart00506   1 ILKVVKGDITKPRADAIVNAANSDGAHGGGVAGAIARAAGKALsKEEVRKLagGECPVGTAVVTEGGNLPAKYVIHAVGP 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 22094097    132 KYkSRYRTAAESSLYSCYRNVLQLAKEQSMSSVGFCVINSAKRGYPLEDAT 182
Cdd:smart00506  81 RA-SGHSKEGFELLENAYRNCLELAIELGITSVALPLIGTGIYGVPKDRSA 130
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 330-471 8.01e-20

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: 86.23  E-value: 8.01e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094097 330 EDLSDIASlKALYQTGVDNCGRTVMVVVGRNIPVTLIDMDKALLYFIHVMDHIAVKEYVLVYFHTLTSDY------NHLD 403
Cdd:cd00170   2 EELLELLG-GIGYLGGRDKEGRPVLVFRAGWDPPKLLDLEELLRYLVYLLEKALRELEEQVEGFVVIIDLkgfslsNLSD 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22094097 404 SDFLKKLYDVVDIKYKRNLKAVYFVHPTFRSKVSTWFFTTFSVSGLKDKIHHVDS-LQQLFSAISPEQI 471
Cdd:cd00170  81 LSLLKKLLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGSdLEELLEYIDPDQL 149
Macro_H2A-like cd02904
macrodomain, macroH2A-like family; Macrodomains are found in a variety of proteins with ...
 55-211 3.66e-18

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: 82.36  E-value: 3.66e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094097  55 KVVLWKGDVALLNCTAIVNTSNESLTDKNPVSESIFMLAGPDLKEDLQKLKGCR----TGEAKLTKGFNLAARFIIHTVG 130
Cdd:cd02904  19 KLTVVQGDIASIKADAIVHPTNATFYLGGEVGSALEKAGGKEFVEEVKELRKSNgpleVAGAAISPGHNLPAKFVIHCNS 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094097 131 PKYKSryrTAAESSLYSCYRNVLQLAKEQSMSSVGFCVINSAKRGYPLEDATHIALRTVRR-FLEIHGENIEKVVFAVSE 209
Cdd:cd02904  99 PSWGS---DKCEELLEKTVKNCLALADEKKLKSVAFPSIGSGRNGFPKQTAAQTILKAISNyFVSVMSSSLKQIYFVLFD 175


                ..
gi 22094097 210 LE 211
Cdd:cd02904 176 ME 177
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 55-177 2.94e-17

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: 79.22  E-value: 2.94e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094097  55 KVVLWKGDVALLNCTAIVNTSNESLTDKNPVSESIFMLAGPDLKEDL-QKLKGCRTGEAKLTKGFNLAARFIIHTVGPKY 133
Cdd:cd02903   9 TVQLVKGDITKEKTDVIVNSVSSDLLLKGGVSKAILKAAGPELQDECaNQGKQPASGDVIVTSGGNLPCKYVYHVVLPHY 88

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 22094097 134 KSRYRTAAESSLYSCyrnvLQLAKEQSMSSVGFCVINSAKRGYP 177
Cdd:cd02903  89 NPGNEKTLKDIVRKC----LEKAENYKMSSISFPAIGTGNLGFP 128
Macro_Ttha0132-like cd03330
Macrodomain, uncharacterized family similar to Thermus thermophilus hypothetical protein ...
 55-205 7.80e-13

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: 65.92  E-value: 7.80e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094097  55 KVVLWKGDVALLNCTAIVNTSNESLTDKNPVSESIFMLAGPDLKEDLQKLKGCRTGEAKLTKGFNLAARFIIH--TVGPK 132
Cdd:cd03330   1 RLIVVQGDITEQDADAIVNAANRRLLMGSGVAGAIKRKGGEEIEREAMRKGPIRVGEAVETGAGKLPAKYVIHaaVMGMP 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22094097 133 YKSryrtaAESSLYSCYRNVLQLAKEQSMSSVGFCVINSAKRGYPLEDATHIALRTVRRFLEihgENIEKVVF 205
Cdd:cd03330  81 GRS-----SEESIRDATRNALAKAEELGLESVAFPAIGTGVGGFPVEEVARIMLEEIKKCDP---PLLEEVRL 145
Macro_X_Nsp3-like cd21557
X-domain (or Mac1 domain) of viral non-structural protein 3 and related macrodomains; The ...
 68-155 2.07e-07

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: 49.86  E-value: 2.07e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22094097  68 CTAIVNTSNESLTDKNPVSESIFMLAGPDLKE--DLQKLKG-CRTGEAKLTKGFNLAARfIIHTVGPKYKsryRTAAESS 144
Cdd:cd21557   1 EDVVVNAANENLKHGGGVAGAIYKATGGAFQKesDYIKKNGpLKVGTAVLLPGHGLAKN-IIHVVGPRKR---KGQDDQL 76

                        90
                ....*....|.
gi 22094097 145 LYSCYRNVLQL 155
Cdd:cd21557  77 LAAAYKAVNKE 87
 
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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