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Conserved domains on  [gi|795389453|ref|XP_011752947|]
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O-acetyl-ADP-ribose deacetylase 1 isoform X1 [Macaca nemestrina]

Protein Classification

macro domain-containing protein( domain architecture ID 10121048)

macro domain-containing protein functions in the recognition, interpretation, and turnover of ADP-ribose (ADPr) signaling, such as ADP-ribose 1''-phosphate phosphatase that is involved in the metabolism of ADP-ribose 1''-phosphate (Appr1p) which is produced as a consequence of tRNA splicing

CATH:  3.40.220.10
Gene Ontology:  GO:0072570|GO:0019213
PubMed:  26844395|15902274|21421074|32214744
SCOP:  4000521

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Macro_Poa1p-like cd02901
macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse ...
 13-143 7.11e-69

macrodomain, Poa1p-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 the yeast protein Poa1p, reported to be a phosphatase specific for Appr-1"-p, a tRNA splicing metabolite. Poa1p may play a role in tRNA splicing regulation.


:

Pssm-ID: 394873  Cd Length: 135  Bit Score: 204.41  E-value: 7.11e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795389453  13 RITYVKGDLFACPKTDSLAHCISEDCRMGAGIAVLFKKKFGGVQELLNQQKKS--GEVAVLKRDG--RYIYYLITKKRAS 88
Cdd:cd02901    1 KITYVKGDLFACPETKSLAHCCNCDGVMGKGIALQFKKKPGRVEELRAQCKKKllGGVAVLKRDGvkRYIYYLITKKSYG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 795389453  89 HKPTYENLQKSLEAMKSHCLKNGVTDLSMPRIGCGLDRLQWENVSAMIEEVFEAT 143
Cdd:cd02901   81 PKPTYEALRSSLEELREHCRENGVTSVAMPRIGCGLDGLDWEEVEPILKEVFDDR 135
 
Name Accession Description Interval E-value
Macro_Poa1p-like cd02901
macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse ...
 13-143 7.11e-69

macrodomain, Poa1p-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 the yeast protein Poa1p, reported to be a phosphatase specific for Appr-1"-p, a tRNA splicing metabolite. Poa1p may play a role in tRNA splicing regulation.


Pssm-ID: 394873  Cd Length: 135  Bit Score: 204.41  E-value: 7.11e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795389453  13 RITYVKGDLFACPKTDSLAHCISEDCRMGAGIAVLFKKKFGGVQELLNQQKKS--GEVAVLKRDG--RYIYYLITKKRAS 88
Cdd:cd02901    1 KITYVKGDLFACPETKSLAHCCNCDGVMGKGIALQFKKKPGRVEELRAQCKKKllGGVAVLKRDGvkRYIYYLITKKSYG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 795389453  89 HKPTYENLQKSLEAMKSHCLKNGVTDLSMPRIGCGLDRLQWENVSAMIEEVFEAT 143
Cdd:cd02901   81 PKPTYEALRSSLEELREHCRENGVTSVAMPRIGCGLDGLDWEEVEPILKEVFDDR 135
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 14-151 9.38e-13

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: 62.12  E-value: 9.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795389453  14 ITYVKGDLFACpKTDSLAHCISEDCRMGAGIAVLFKKKFG-GVQELLNQQKKSGEV----AVLKRDG----RYIYYLITK 84
Cdd:COG2110    1 IEIVQGDITEL-DVDAIVNAANSSLLGGGGVAGAIHRAAGpELLEECRRLCKQGGCptgeAVITPAGnlpaKYVIHTVGP 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 795389453  85 K-RASHKPTYENLQKSLEAMKSHCLKNGVTDLSMPRIGCGLDRLQWENVSAMIEEVFEA--------TDIKITVYT 151
Cdd:COG2110   80 VwRGGGPSEEELLASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDfleehpslEEVRFVLFD 155
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 13-130 1.41e-10

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: 55.39  E-value: 1.41e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795389453    13 RITYVKGDLFAcPKTDSLAHCISEDCRMGAGIAVLFKKKFGGVQ---ELLNQQKK---SGEVAVL---KRDGRYIYYLIT 83
Cdd:smart00506   1 ILKVVKGDITK-PRADAIVNAANSDGAHGGGVAGAIARAAGKALskeEVRKLAGGecpVGTAVVTeggNLPAKYVIHAVG 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 795389453    84 KKRASHKPT-YENLQKSLEAMKSHCLKNGVTDLSMPRIGCGLDRLQWE 130
Cdd:smart00506  80 PRASGHSKEgFELLENAYRNCLELAIELGITSVALPLIGTGIYGVPKD 127
tk.4 PHA02595
hypothetical protein; Provisional
 14-149 1.54e-10

hypothetical protein; Provisional


Pssm-ID: 222899  Cd Length: 154  Bit Score: 55.85  E-value: 1.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795389453  14 ITYVKGD---LFACPKTDsLAH-CiseDC--RMGAGIAVLFKKKFGGVQELLNQQ-----KKSGEVAVLKRDGR----YI 78
Cdd:PHA02595   3 VDYIKGDivaLFLQGKGN-IAHgC---NCfhTMGSGIAGQLAKAFPQILEADKLTtegdvEKLGTFSVWEKYVGghkaYC 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 795389453  79 YYLITKKRASHKPTYENLQKSLEAMKSHClKNGVTDLSM--PRIGCGLDRLQWENVSAMIEEVfeATDIKITV 149
Cdd:PHA02595  79 FNLYTQFDPGPNLEYSALMNCFEELNEVF-EGTLFKPTIyiPRIGAGIAGGDWDKIEAIIDEA--TPDIDIVV 148
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 40-130 5.69e-04

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: 37.54  E-value: 5.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795389453   40 MGAGIAVLFKKKFGG-----VQELLNQQKKSGEVAVL---KRDGRYIYYLI--TKKRASHKPTYENLQKSLEAMKSHCLK 109
Cdd:pfam01661  10 GGGGVAGAIHRAAGPelleeCRELKKGGCPTGEAVVTpggNLPAKYVIHTVgpTWRHGGSHGEEELLESCYRNALALAEE 89

                          90       100
                  ....*....|....*....|.
gi 795389453  110 NGVTDLSMPRIGCGLDRLQWE 130
Cdd:pfam01661  90 LGIKSIAFPAISTGIYGFPWE 110
 
Name Accession Description Interval E-value
Macro_Poa1p-like cd02901
macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse ...
 13-143 7.11e-69

macrodomain, Poa1p-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 the yeast protein Poa1p, reported to be a phosphatase specific for Appr-1"-p, a tRNA splicing metabolite. Poa1p may play a role in tRNA splicing regulation.


Pssm-ID: 394873  Cd Length: 135  Bit Score: 204.41  E-value: 7.11e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795389453  13 RITYVKGDLFACPKTDSLAHCISEDCRMGAGIAVLFKKKFGGVQELLNQQKKS--GEVAVLKRDG--RYIYYLITKKRAS 88
Cdd:cd02901    1 KITYVKGDLFACPETKSLAHCCNCDGVMGKGIALQFKKKPGRVEELRAQCKKKllGGVAVLKRDGvkRYIYYLITKKSYG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 795389453  89 HKPTYENLQKSLEAMKSHCLKNGVTDLSMPRIGCGLDRLQWENVSAMIEEVFEAT 143
Cdd:cd02901   81 PKPTYEALRSSLEELREHCRENGVTSVAMPRIGCGLDGLDWEEVEPILKEVFDDR 135
Macro_SF cd02749
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 28-139 6.18e-35

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: 117.88  E-value: 6.18e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795389453  28 DSLAHCISEDCRMGAGIAVLFKKKFGGVQE------LLNQQKKSGEVAVLKRDG---RYIYYLITKKRASHKPTYENLQK 98
Cdd:cd02749    1 DAIVNPANNDLYLGGGVAKAISKKAGGDLQeeceerKKNGYLKVGEVAVTKGGNlpaRYIIHVVGPVASSKKKTYEPLKK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 795389453  99 SLEAMKSHCLKNGVTDLSMPRIGCGLDRLQWENVSAMIEEV 139
Cdd:cd02749   81 CVKNCLSLADEKGLKSVAFPAIGTGIAGFPPEEAARIMLEA 121
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 14-151 9.38e-13

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: 62.12  E-value: 9.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795389453  14 ITYVKGDLFACpKTDSLAHCISEDCRMGAGIAVLFKKKFG-GVQELLNQQKKSGEV----AVLKRDG----RYIYYLITK 84
Cdd:COG2110    1 IEIVQGDITEL-DVDAIVNAANSSLLGGGGVAGAIHRAAGpELLEECRRLCKQGGCptgeAVITPAGnlpaKYVIHTVGP 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 795389453  85 K-RASHKPTYENLQKSLEAMKSHCLKNGVTDLSMPRIGCGLDRLQWENVSAMIEEVFEA--------TDIKITVYT 151
Cdd:COG2110   80 VwRGGGPSEEELLASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDfleehpslEEVRFVLFD 155
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 13-130 1.41e-10

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: 55.39  E-value: 1.41e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795389453    13 RITYVKGDLFAcPKTDSLAHCISEDCRMGAGIAVLFKKKFGGVQ---ELLNQQKK---SGEVAVL---KRDGRYIYYLIT 83
Cdd:smart00506   1 ILKVVKGDITK-PRADAIVNAANSDGAHGGGVAGAIARAAGKALskeEVRKLAGGecpVGTAVVTeggNLPAKYVIHAVG 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 795389453    84 KKRASHKPT-YENLQKSLEAMKSHCLKNGVTDLSMPRIGCGLDRLQWE 130
Cdd:smart00506  80 PRASGHSKEgFELLENAYRNCLELAIELGITSVALPLIGTGIYGVPKD 127
tk.4 PHA02595
hypothetical protein; Provisional
 14-149 1.54e-10

hypothetical protein; Provisional


Pssm-ID: 222899  Cd Length: 154  Bit Score: 55.85  E-value: 1.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795389453  14 ITYVKGD---LFACPKTDsLAH-CiseDC--RMGAGIAVLFKKKFGGVQELLNQQ-----KKSGEVAVLKRDGR----YI 78
Cdd:PHA02595   3 VDYIKGDivaLFLQGKGN-IAHgC---NCfhTMGSGIAGQLAKAFPQILEADKLTtegdvEKLGTFSVWEKYVGghkaYC 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 795389453  79 YYLITKKRASHKPTYENLQKSLEAMKSHClKNGVTDLSM--PRIGCGLDRLQWENVSAMIEEVfeATDIKITV 149
Cdd:PHA02595  79 FNLYTQFDPGPNLEYSALMNCFEELNEVF-EGTLFKPTIyiPRIGAGIAGGDWDKIEAIIDEA--TPDIDIVV 148
PHA03033 PHA03033
hypothetical protein; Provisional
 49-139 9.24e-07

hypothetical protein; Provisional


Pssm-ID: 165330  Cd Length: 142  Bit Score: 45.74  E-value: 9.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795389453  49 KKKFGGVQELLNQQKKSGEVAVLKRDGRYIYYLITKKRASHKPTYENLQKSLEAMKSHCLKNGVTDlSMPRIGCGLDRLQ 128
Cdd:PHA03033  42 KKKYNSIKELKKQKKKKGEVAYIYKNNKYIIYIIIADYIEDIVDDINILRALDNFKEIIEKDKIAD-IMSHMKFIEDNYE 120

                         90
                 ....*....|.
gi 795389453 129 WENVSAMIEEV 139
Cdd:PHA03033 121 TDKLLKYIRDH 131
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 9-141 1.12e-04

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: 40.31  E-value: 1.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795389453   9 PEGSRITYVKGDLfACPKTDSLAHCISEDCRMGAGIAVLFKKKFG-GVQELLNQQKK---SGEVAVLKRDG---RYIYYL 81
Cdd:cd02903    5 IGGITVQLVKGDI-TKEKTDVIVNSVSSDLLLKGGVSKAILKAAGpELQDECANQGKqpaSGDVIVTSGGNlpcKYVYHV 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 795389453  82 ITkkrashkPTY-ENLQKSLEAMKSHCL----KNGVTDLSMPRIGCGLDRLQWENV-SAMIEEVFE 141
Cdd:cd02903   84 VL-------PHYnPGNEKTLKDIVRKCLekaeNYKMSSISFPAIGTGNLGFPKDVVaEIMIDEVLK 142
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 40-130 5.69e-04

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: 37.54  E-value: 5.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795389453   40 MGAGIAVLFKKKFGG-----VQELLNQQKKSGEVAVL---KRDGRYIYYLI--TKKRASHKPTYENLQKSLEAMKSHCLK 109
Cdd:pfam01661  10 GGGGVAGAIHRAAGPelleeCRELKKGGCPTGEAVVTpggNLPAKYVIHTVgpTWRHGGSHGEEELLESCYRNALALAEE 89

                          90       100
                  ....*....|....*....|.
gi 795389453  110 NGVTDLSMPRIGCGLDRLQWE 130
Cdd:pfam01661  90 LGIKSIAFPAISTGIYGFPWE 110
 
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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