NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1381448489|ref|XP_024651089|]
View 

O-acetyl-ADP-ribose deacetylase 1 isoform X2 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 10-139 1.34e-67

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: 200.94  E-value: 1.34e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381448489  10 ITYVKGDLFACPKTDSLAHCISEDCRMGAGIAVLFKKKFGGVQELLNQQKKS--GEVAVLKRDG--RYIYYLITKKRASH 85
Cdd:cd02901     2 ITYVKGDLFACPETKSLAHCCNCDGVMGKGIALQFKKKPGRVEELRAQCKKKllGGVAVLKRDGvkRYIYYLITKKSYGP 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1381448489  86 KPTYENLQKSLEAMKSHCLKNGVTDLSMPRIGCGLDRLQWENVSAMIEEVFEAT 139
Cdd:cd02901    82 KPTYEALRSSLEELREHCRENGVTSVAMPRIGCGLDGLDWEEVEPILKEVFDDR 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 ...
 10-139 1.34e-67

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: 200.94  E-value: 1.34e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381448489  10 ITYVKGDLFACPKTDSLAHCISEDCRMGAGIAVLFKKKFGGVQELLNQQKKS--GEVAVLKRDG--RYIYYLITKKRASH 85
Cdd:cd02901     2 ITYVKGDLFACPETKSLAHCCNCDGVMGKGIALQFKKKPGRVEELRAQCKKKllGGVAVLKRDGvkRYIYYLITKKSYGP 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1381448489  86 KPTYENLQKSLEAMKSHCLKNGVTDLSMPRIGCGLDRLQWENVSAMIEEVFEAT 139
Cdd:cd02901    82 KPTYEALRSSLEELREHCRENGVTSVAMPRIGCGLDGLDWEEVEPILKEVFDDR 135
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 10-147 8.43e-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: 8.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381448489  10 ITYVKGDLFACpKTDSLAHCISEDCRMGAGIAVLFKKKFG-GVQELLNQQKKSGEV----AVLKRDG----RYIYYLITK 80
Cdd:COG2110     1 IEIVQGDITEL-DVDAIVNAANSSLLGGGGVAGAIHRAAGpELLEECRRLCKQGGCptgeAVITPAGnlpaKYVIHTVGP 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1381448489  81 K-RASHKPTYENLQKSLEAMKSHCLKNGVTDLSMPRIGCGLDRLQWENVSAMIEEVFEA--------TDIKITVYT 147
Cdd:COG2110    80 VwRGGGPSEEELLASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDfleehpslEEVRFVLFD 155
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 10-126 2.27e-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: 55.00  E-value: 2.27e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381448489   10 ITYVKGDLFAcPKTDSLAHCISEDCRMGAGIAVLFKKKFGGVQ---ELLNQQKK---SGEVAVL---KRDGRYIYYLITK 80
Cdd:smart00506   2 LKVVKGDITK-PRADAIVNAANSDGAHGGGVAGAIARAAGKALskeEVRKLAGGecpVGTAVVTeggNLPAKYVIHAVGP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1381448489   81 KRASHKPT-YENLQKSLEAMKSHCLKNGVTDLSMPRIGCGLDRLQWE 126
Cdd:smart00506  81 RASGHSKEgFELLENAYRNCLELAIELGITSVALPLIGTGIYGVPKD 127
tk.4 PHA02595
hypothetical protein; Provisional
 10-145 2.61e-10

hypothetical protein; Provisional


Pssm-ID: 222899  Cd Length: 154  Bit Score: 55.08  E-value: 2.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381448489  10 ITYVKGD---LFACPKTDsLAH-CiseDC--RMGAGIAVLFKKKFGGVQELLNQQ-----KKSGEVAVLKRDGR----YI 74
Cdd:PHA02595    3 VDYIKGDivaLFLQGKGN-IAHgC---NCfhTMGSGIAGQLAKAFPQILEADKLTtegdvEKLGTFSVWEKYVGghkaYC 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1381448489  75 YYLITKKRASHKPTYENLQKSLEAMKSHClKNGVTDLSM--PRIGCGLDRLQWENVSAMIEEVfeATDIKITV 145
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 ...
 36-126 5.85e-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: 37.16  E-value: 5.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381448489  36 MGAGIAVLFKKKFGG-----VQELLNQQKKSGEVAVL---KRDGRYIYYLI--TKKRASHKPTYENLQKSLEAMKSHCLK 105
Cdd:pfam01661  10 GGGGVAGAIHRAAGPelleeCRELKKGGCPTGEAVVTpggNLPAKYVIHTVgpTWRHGGSHGEEELLESCYRNALALAEE 89

                          90       100
                  ....*....|....*....|.
gi 1381448489 106 NGVTDLSMPRIGCGLDRLQWE 126
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 ...
 10-139 1.34e-67

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: 200.94  E-value: 1.34e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381448489  10 ITYVKGDLFACPKTDSLAHCISEDCRMGAGIAVLFKKKFGGVQELLNQQKKS--GEVAVLKRDG--RYIYYLITKKRASH 85
Cdd:cd02901     2 ITYVKGDLFACPETKSLAHCCNCDGVMGKGIALQFKKKPGRVEELRAQCKKKllGGVAVLKRDGvkRYIYYLITKKSYGP 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1381448489  86 KPTYENLQKSLEAMKSHCLKNGVTDLSMPRIGCGLDRLQWENVSAMIEEVFEAT 139
Cdd:cd02901    82 KPTYEALRSSLEELREHCRENGVTSVAMPRIGCGLDGLDWEEVEPILKEVFDDR 135
Macro_SF cd02749
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 24-135 1.60e-34

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: 116.73  E-value: 1.60e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381448489  24 DSLAHCISEDCRMGAGIAVLFKKKFGGVQE------LLNQQKKSGEVAVLKRDG---RYIYYLITKKRASHKPTYENLQK 94
Cdd:cd02749     1 DAIVNPANNDLYLGGGVAKAISKKAGGDLQeeceerKKNGYLKVGEVAVTKGGNlpaRYIIHVVGPVASSKKKTYEPLKK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1381448489  95 SLEAMKSHCLKNGVTDLSMPRIGCGLDRLQWENVSAMIEEV 135
Cdd:cd02749    81 CVKNCLSLADEKGLKSVAFPAIGTGIAGFPPEEAARIMLEA 121
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 10-147 8.43e-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: 8.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381448489  10 ITYVKGDLFACpKTDSLAHCISEDCRMGAGIAVLFKKKFG-GVQELLNQQKKSGEV----AVLKRDG----RYIYYLITK 80
Cdd:COG2110     1 IEIVQGDITEL-DVDAIVNAANSSLLGGGGVAGAIHRAAGpELLEECRRLCKQGGCptgeAVITPAGnlpaKYVIHTVGP 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1381448489  81 K-RASHKPTYENLQKSLEAMKSHCLKNGVTDLSMPRIGCGLDRLQWENVSAMIEEVFEA--------TDIKITVYT 147
Cdd:COG2110    80 VwRGGGPSEEELLASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRDfleehpslEEVRFVLFD 155
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 10-126 2.27e-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: 55.00  E-value: 2.27e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381448489   10 ITYVKGDLFAcPKTDSLAHCISEDCRMGAGIAVLFKKKFGGVQ---ELLNQQKK---SGEVAVL---KRDGRYIYYLITK 80
Cdd:smart00506   2 LKVVKGDITK-PRADAIVNAANSDGAHGGGVAGAIARAAGKALskeEVRKLAGGecpVGTAVVTeggNLPAKYVIHAVGP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1381448489   81 KRASHKPT-YENLQKSLEAMKSHCLKNGVTDLSMPRIGCGLDRLQWE 126
Cdd:smart00506  81 RASGHSKEgFELLENAYRNCLELAIELGITSVALPLIGTGIYGVPKD 127
tk.4 PHA02595
hypothetical protein; Provisional
 10-145 2.61e-10

hypothetical protein; Provisional


Pssm-ID: 222899  Cd Length: 154  Bit Score: 55.08  E-value: 2.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381448489  10 ITYVKGD---LFACPKTDsLAH-CiseDC--RMGAGIAVLFKKKFGGVQELLNQQ-----KKSGEVAVLKRDGR----YI 74
Cdd:PHA02595    3 VDYIKGDivaLFLQGKGN-IAHgC---NCfhTMGSGIAGQLAKAFPQILEADKLTtegdvEKLGTFSVWEKYVGghkaYC 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1381448489  75 YYLITKKRASHKPTYENLQKSLEAMKSHClKNGVTDLSM--PRIGCGLDRLQWENVSAMIEEVfeATDIKITV 145
Cdd:PHA02595   79 FNLYTQFDPGPNLEYSALMNCFEELNEVF-EGTLFKPTIyiPRIGAGIAGGDWDKIEAIIDEA--TPDIDIVV 148
PHA03033 PHA03033
hypothetical protein; Provisional
 45-135 1.42e-06

hypothetical protein; Provisional


Pssm-ID: 165330  Cd Length: 142  Bit Score: 44.97  E-value: 1.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381448489  45 KKKFGGVQELLNQQKKSGEVAVLKRDGRYIYYLITKKRASHKPTYENLQKSLEAMKSHCLKNGVTDlSMPRIGCGLDRLQ 124
Cdd:PHA03033   42 KKKYNSIKELKKQKKKKGEVAYIYKNNKYIIYIIIADYIEDIVDDINILRALDNFKEIIEKDKIAD-IMSHMKFIEDNYE 120

                          90
                  ....*....|.
gi 1381448489 125 WENVSAMIEEV 135
Cdd:PHA03033  121 TDKLLKYIRDH 131
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 10-137 2.73e-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: 39.16  E-value: 2.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381448489  10 ITYVKGDLfACPKTDSLAHCISEDCRMGAGIAVLFKKKFG-GVQELLNQQKK---SGEVAVLKRDG---RYIYYLITkkr 82
Cdd:cd02903    10 VQLVKGDI-TKEKTDVIVNSVSSDLLLKGGVSKAILKAAGpELQDECANQGKqpaSGDVIVTSGGNlpcKYVYHVVL--- 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1381448489  83 ashkPTY-ENLQKSLEAMKSHCL----KNGVTDLSMPRIGCGLDRLQWENV-SAMIEEVFE 137
Cdd:cd02903    86 ----PHYnPGNEKTLKDIVRKCLekaeNYKMSSISFPAIGTGNLGFPKDVVaEIMIDEVLK 142
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 36-126 5.85e-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: 37.16  E-value: 5.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381448489  36 MGAGIAVLFKKKFGG-----VQELLNQQKKSGEVAVL---KRDGRYIYYLI--TKKRASHKPTYENLQKSLEAMKSHCLK 105
Cdd:pfam01661  10 GGGGVAGAIHRAAGPelleeCRELKKGGCPTGEAVVTpggNLPAKYVIHTVgpTWRHGGSHGEEELLESCYRNALALAEE 89

                          90       100
                  ....*....|....*....|.
gi 1381448489 106 NGVTDLSMPRIGCGLDRLQWE 126
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH