NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|28574784|ref|NP_788556|]
View 

uncharacterized protein Dmel_CG33056, isoform A [Drosophila melanogaster]

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 ...
 160-290 4.22e-47

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: 155.87  E-value: 4.22e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574784 160 QITEARGNLFSAPENYALVHSVSADFAMCAGINLQFRCKFGQVDELKRQHKH--TGNVAVL--EQDGRHIYNLVTKERSH 235
Cdd:cd02901   1 KITYVKGDLFACPETKSLAHCCNCDGVMGKGIALQFKKKPGRVEELRAQCKKklLGGVAVLkrDGVKRYIYYLITKKSYG 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 28574784 236 EKCTYAALYYALLAMREHMREHGVTKLAIPRLGCGIDRLDWLRVRSLLDLVFAED 290
Cdd:cd02901  81 PKPTYEALRSSLEELREHCRENGVTSVAMPRIGCGLDGLDWEEVEPILKEVFDDR 135
Macro_Poa1p-like cd02901
macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse ...
 5-135 5.83e-47

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: 155.49  E-value: 5.83e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574784   5 KIVESKLDIFHAPQTHSLAHAVeSSFTAERGTLAWQFALIYGDVDELRQRSVSR--GNCAVLEHNA--RFIYYLVTKSSL 80
Cdd:cd02901   1 KITYVKGDLFACPETKSLAHCC-NCDGVMGKGIALQFKKKPGRVEELRAQCKKKllGGVAVLKRDGvkRYIYYLITKKSY 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 28574784  81 YEASTYGDVQAALICMREHMRNHEITKVAMPRICCGNDGLEWKHVKRLVQQTFSQ 135
Cdd:cd02901  80 GPKPTYEALRSSLEELREHCRENGVTSVAMPRIGCGLDGLDWEEVEPILKEVFDD 134
 
Name Accession Description Interval E-value
Macro_Poa1p-like cd02901
macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse ...
 160-290 4.22e-47

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: 155.87  E-value: 4.22e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574784 160 QITEARGNLFSAPENYALVHSVSADFAMCAGINLQFRCKFGQVDELKRQHKH--TGNVAVL--EQDGRHIYNLVTKERSH 235
Cdd:cd02901   1 KITYVKGDLFACPETKSLAHCCNCDGVMGKGIALQFKKKPGRVEELRAQCKKklLGGVAVLkrDGVKRYIYYLITKKSYG 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 28574784 236 EKCTYAALYYALLAMREHMREHGVTKLAIPRLGCGIDRLDWLRVRSLLDLVFAED 290
Cdd:cd02901  81 PKPTYEALRSSLEELREHCRENGVTSVAMPRIGCGLDGLDWEEVEPILKEVFDDR 135
Macro_Poa1p-like cd02901
macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse ...
 5-135 5.83e-47

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: 155.49  E-value: 5.83e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574784   5 KIVESKLDIFHAPQTHSLAHAVeSSFTAERGTLAWQFALIYGDVDELRQRSVSR--GNCAVLEHNA--RFIYYLVTKSSL 80
Cdd:cd02901   1 KITYVKGDLFACPETKSLAHCC-NCDGVMGKGIALQFKKKPGRVEELRAQCKKKllGGVAVLKRDGvkRYIYYLITKKSY 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 28574784  81 YEASTYGDVQAALICMREHMRNHEITKVAMPRICCGNDGLEWKHVKRLVQQTFSQ 135
Cdd:cd02901  80 GPKPTYEALRSSLEELREHCRENGVTSVAMPRIGCGLDGLDWEEVEPILKEVFDD 134
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 161-283 4.14e-07

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: 48.46  E-value: 4.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574784    161 ITEARGNlFSAPENYALVHSVSADFAMCAGINLQFRCKFGQV---DELKRQHKH---TGNVAVLE---QDGRHIYNLVTK 231
Cdd:smart00506   2 LKVVKGD-ITKPRADAIVNAANSDGAHGGGVAGAIARAAGKAlskEEVRKLAGGecpVGTAVVTEggnLPAKYVIHAVGP 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28574784    232 ERSheKCTYAALYYALLAMREHMR---EHGVTKLAIPRLGCGIDRLDWLRVRSLL 283
Cdd:smart00506  81 RAS--GHSKEGFELLENAYRNCLElaiELGITSVALPLIGTGIYGVPKDRSAQAL 133
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 22-128 2.69e-06

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: 46.14  E-value: 2.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574784     22 LAHAVESSFTAERGtLAWQFALIYG------DVDELRQRSVSRGNCAVLEHN---ARFIYYLVT-KSSLYEASTYGDVQA 91
Cdd:smart00506  17 IVNAANSDGAHGGG-VAGAIARAAGkalskeEVRKLAGGECPVGTAVVTEGGnlpAKYVIHAVGpRASGHSKEGFELLEN 95

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 28574784     92 ALI-CMREHMRNHeITKVAMPRICCGNDGLEWKHVKRL 128
Cdd:smart00506  96 AYRnCLELAIELG-ITSVALPLIGTGIYGVPKDRSAQA 132
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 161-280 1.31e-04

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: 42.09  E-value: 1.31e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574784 161 ITEARGNLFSApENYALVHSVSADFAMCAGINLQFRCKFGQ--VDELKRQHKH----TGNVAV-----LeqDGRHIYNLV 229
Cdd:COG2110   1 IEIVQGDITEL-DVDAIVNAANSSLLGGGGVAGAIHRAAGPelLEECRRLCKQggcpTGEAVItpagnL--PAKYVIHTV 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574784 230 TK--------ERSH-EKCTYAalyyallaMREHMREHGVTKLAIPRLGCGIDRLDWLRVR 280
Cdd:COG2110  78 GPvwrgggpsEEELlASCYRN--------SLELAEELGIRSIAFPAIGTGVGGFPWEEAA 129
PHA03033 PHA03033
hypothetical protein; Provisional
 161-229 5.06e-04

hypothetical protein; Provisional


Pssm-ID: 165330  Cd Length: 142  Bit Score: 39.96  E-value: 5.06e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574784  161 ITEARGNLFSAPENYALVHSVSADFAMCAGINLQF-RCKFGQVDELKRQHKHTGNVAVLEQDGRHIYNLV 229
Cdd:PHA03033   6 INENIWDFLSDDDNINIISFISADFILCKDDCFIYiKKKYNSIKELKKQKKKKGEVAYIYKNNKYIIYII 75
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 67-149 5.89e-03

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: 37.08  E-value: 5.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574784  67 NARFIYYLVTK-SSLYEASTYGDVQAALICMREHMRNHEITKVAMPRICCGNDGLEWKHVKRLVQQTFS----QSEYPIE 141
Cdd:COG2110  69 PAKYVIHTVGPvWRGGGPSEEELLASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRdfleEHPSLEE 148


                ....*...
gi 28574784 142 ILICEHED 149
Cdd:COG2110 149 VRFVLFDE 156
 
Name Accession Description Interval E-value
Macro_Poa1p-like cd02901
macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse ...
 160-290 4.22e-47

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: 155.87  E-value: 4.22e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574784 160 QITEARGNLFSAPENYALVHSVSADFAMCAGINLQFRCKFGQVDELKRQHKH--TGNVAVL--EQDGRHIYNLVTKERSH 235
Cdd:cd02901   1 KITYVKGDLFACPETKSLAHCCNCDGVMGKGIALQFKKKPGRVEELRAQCKKklLGGVAVLkrDGVKRYIYYLITKKSYG 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 28574784 236 EKCTYAALYYALLAMREHMREHGVTKLAIPRLGCGIDRLDWLRVRSLLDLVFAED 290
Cdd:cd02901  81 PKPTYEALRSSLEELREHCRENGVTSVAMPRIGCGLDGLDWEEVEPILKEVFDDR 135
Macro_Poa1p-like cd02901
macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse ...
 5-135 5.83e-47

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: 155.49  E-value: 5.83e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574784   5 KIVESKLDIFHAPQTHSLAHAVeSSFTAERGTLAWQFALIYGDVDELRQRSVSR--GNCAVLEHNA--RFIYYLVTKSSL 80
Cdd:cd02901   1 KITYVKGDLFACPETKSLAHCC-NCDGVMGKGIALQFKKKPGRVEELRAQCKKKllGGVAVLKRDGvkRYIYYLITKKSY 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 28574784  81 YEASTYGDVQAALICMREHMRNHEITKVAMPRICCGNDGLEWKHVKRLVQQTFSQ 135
Cdd:cd02901  80 GPKPTYEALRSSLEELREHCRENGVTSVAMPRIGCGLDGLDWEEVEPILKEVFDD 134
Macro_SF cd02749
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 175-276 3.11e-07

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: 48.55  E-value: 3.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574784 175 YALVHSVSADFAMCAGINLQFRCKFGQVDE------LKRQHKHTGNVAVLEQDG---RHIYNLVTKERSHEKCTYAALYY 245
Cdd:cd02749   1 DAIVNPANNDLYLGGGVAKAISKKAGGDLQeeceerKKNGYLKVGEVAVTKGGNlpaRYIIHVVGPVASSKKKTYEPLKK 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 28574784 246 ALLAMREHMREHGVTKLAIPRLGCGIDRLDW 276
Cdd:cd02749  81 CVKNCLSLADEKGLKSVAFPAIGTGIAGFPP 111
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 161-283 4.14e-07

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: 48.46  E-value: 4.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574784    161 ITEARGNlFSAPENYALVHSVSADFAMCAGINLQFRCKFGQV---DELKRQHKH---TGNVAVLE---QDGRHIYNLVTK 231
Cdd:smart00506   2 LKVVKGD-ITKPRADAIVNAANSDGAHGGGVAGAIARAAGKAlskEEVRKLAGGecpVGTAVVTEggnLPAKYVIHAVGP 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28574784    232 ERSheKCTYAALYYALLAMREHMR---EHGVTKLAIPRLGCGIDRLDWLRVRSLL 283
Cdd:smart00506  81 RAS--GHSKEGFELLENAYRNCLElaiELGITSVALPLIGTGIYGVPKDRSAQAL 133
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 22-128 2.69e-06

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: 46.14  E-value: 2.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574784     22 LAHAVESSFTAERGtLAWQFALIYG------DVDELRQRSVSRGNCAVLEHN---ARFIYYLVT-KSSLYEASTYGDVQA 91
Cdd:smart00506  17 IVNAANSDGAHGGG-VAGAIARAAGkalskeEVRKLAGGECPVGTAVVTEGGnlpAKYVIHAVGpRASGHSKEGFELLEN 95

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 28574784     92 ALI-CMREHMRNHeITKVAMPRICCGNDGLEWKHVKRL 128
Cdd:smart00506  96 AYRnCLELAIELG-ITSVALPLIGTGIYGVPKDRSAQA 132
Macro_SF cd02749
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 38-122 6.34e-05

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: 42.00  E-value: 6.34e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574784  38 AWQFALIYGDVDELRqrSVSRGNCAvlehnARFIYYLVTKSSLYEASTYGDVQAALICMREHMRNHEITKVAMPRICCGN 117
Cdd:cd02749  34 EERKKNGYLKVGEVA--VTKGGNLP-----ARYIIHVVGPVASSKKKTYEPLKKCVKNCLSLADEKGLKSVAFPAIGTGI 106


                ....*
gi 28574784 118 DGLEW 122
Cdd:cd02749 107 AGFPP 111
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 161-280 1.31e-04

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: 42.09  E-value: 1.31e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574784 161 ITEARGNLFSApENYALVHSVSADFAMCAGINLQFRCKFGQ--VDELKRQHKH----TGNVAV-----LeqDGRHIYNLV 229
Cdd:COG2110   1 IEIVQGDITEL-DVDAIVNAANSSLLGGGGVAGAIHRAAGPelLEECRRLCKQggcpTGEAVItpagnL--PAKYVIHTV 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574784 230 TK--------ERSH-EKCTYAalyyallaMREHMREHGVTKLAIPRLGCGIDRLDWLRVR 280
Cdd:COG2110  78 GPvwrgggpsEEELlASCYRN--------SLELAEELGIRSIAFPAIGTGVGGFPWEEAA 129
PHA03033 PHA03033
hypothetical protein; Provisional
 161-229 5.06e-04

hypothetical protein; Provisional


Pssm-ID: 165330  Cd Length: 142  Bit Score: 39.96  E-value: 5.06e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574784  161 ITEARGNLFSAPENYALVHSVSADFAMCAGINLQF-RCKFGQVDELKRQHKHTGNVAVLEQDGRHIYNLV 229
Cdd:PHA03033   6 INENIWDFLSDDDNINIISFISADFILCKDDCFIYiKKKYNSIKELKKQKKKKGEVAYIYKNNKYIIYII 75
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 67-149 5.89e-03

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: 37.08  E-value: 5.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574784  67 NARFIYYLVTK-SSLYEASTYGDVQAALICMREHMRNHEITKVAMPRICCGNDGLEWKHVKRLVQQTFS----QSEYPIE 141
Cdd:COG2110  69 PAKYVIHTVGPvWRGGGPSEEELLASCYRNSLELAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLRdfleEHPSLEE 148


                ....*...
gi 28574784 142 ILICEHED 149
Cdd:COG2110 149 VRFVLFDE 156
 
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