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Conserved domains on  [gi|356554181|ref|XP_003545427|]
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exosome complex exonuclease RRP46 homolog [Glycine max]

Protein Classification

exosome complex component RRP46( domain architecture ID 10183533)

exosome complex component RRP46 is a subunit of the eukaryotic exosome and a member of the RNase_PH family, named after the bacterial ribonuclease PH, a 3'-5' exoribonuclease.

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RNase_PH_RRP46 cd11372
RRP46 subunit of eukaryotic exosome; The RRP46 subunit of eukaryotic exosome is a member of ...
 14-221 4.96e-65

RRP46 subunit of eukaryotic exosome; The RRP46 subunit of eukaryotic exosome is a member of the RNase_PH family, named after the bacterial Ribonuclease PH, a 3'-5' exoribonuclease. Structurally all members of this family form hexameric rings (trimers of Rrp41-Rrp45, Rrp46-Rrp43, and Mtr3-Rrp42 dimers). The eukaryotic exosome core is composed of six individually encoded RNase PH-like subunits and three additional proteins (Rrp4, Csl4 and Rrp40) that form a stable cap and contain RNA-binding domains. The RNase PH-like subunits are no longer phosphorolytic enzymes, the exosome directly associates with Rrp44 and Rrp6, hydrolytic exoribonucleases related to bacterial RNase II/R and RNase D. The exosome plays an important role in RNA turnover. It plays a crucial role in the maturation of stable RNA species such as rRNA, snRNA and snoRNA, quality control of mRNA, and the degradation of RNA processing by-products and non-coding transcripts.


:

Pssm-ID: 206777 [Multi-domain]  Cd Length: 199  Bit Score: 200.48  E-value: 4.96e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356554181  14 LRPLacSCSCSILHRSHGSASWAQRETKVLAAVYGPKAGTKKNENPKKASIKVIWKPKTGQIGKVEKEYEMILKRTLESI 93
Cdd:cd11372    1 LRPL--SCELGLLSRADGSARFSQGDTSVLAAVYGPIEVKLRKELPDRATLEVIVRPKSGLPGVKEKLLELLLRSTLEPI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356554181  94 CIRTIYPNTTTLVIVQIVHDDGVLLPCAINAACVALVDARIPLKHLVVAICCSITDSGCIILDPTKDQEEKMKAFINLVF 173
Cdd:cd11372   79 ILLHLHPRTLISVVLQVLQDDGSLLACAINAACLALLDAGVPMKGLFAAVTCAITEDGEIILDPTAEEEKEAKAVATFAF 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 356554181 174 PNtivsvlpegslQEGSEtmahgIMTSITQGAMSgLGGFVACRALSQR 221
Cdd:cd11372  159 DS-----------GEEKN-----LVLSESEGSFT-EEELFACLELAQA 189
 
Name Accession Description Interval E-value
RNase_PH_RRP46 cd11372
RRP46 subunit of eukaryotic exosome; The RRP46 subunit of eukaryotic exosome is a member of ...
 14-221 4.96e-65

RRP46 subunit of eukaryotic exosome; The RRP46 subunit of eukaryotic exosome is a member of the RNase_PH family, named after the bacterial Ribonuclease PH, a 3'-5' exoribonuclease. Structurally all members of this family form hexameric rings (trimers of Rrp41-Rrp45, Rrp46-Rrp43, and Mtr3-Rrp42 dimers). The eukaryotic exosome core is composed of six individually encoded RNase PH-like subunits and three additional proteins (Rrp4, Csl4 and Rrp40) that form a stable cap and contain RNA-binding domains. The RNase PH-like subunits are no longer phosphorolytic enzymes, the exosome directly associates with Rrp44 and Rrp6, hydrolytic exoribonucleases related to bacterial RNase II/R and RNase D. The exosome plays an important role in RNA turnover. It plays a crucial role in the maturation of stable RNA species such as rRNA, snRNA and snoRNA, quality control of mRNA, and the degradation of RNA processing by-products and non-coding transcripts.


Pssm-ID: 206777 [Multi-domain]  Cd Length: 199  Bit Score: 200.48  E-value: 4.96e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356554181  14 LRPLacSCSCSILHRSHGSASWAQRETKVLAAVYGPKAGTKKNENPKKASIKVIWKPKTGQIGKVEKEYEMILKRTLESI 93
Cdd:cd11372    1 LRPL--SCELGLLSRADGSARFSQGDTSVLAAVYGPIEVKLRKELPDRATLEVIVRPKSGLPGVKEKLLELLLRSTLEPI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356554181  94 CIRTIYPNTTTLVIVQIVHDDGVLLPCAINAACVALVDARIPLKHLVVAICCSITDSGCIILDPTKDQEEKMKAFINLVF 173
Cdd:cd11372   79 ILLHLHPRTLISVVLQVLQDDGSLLACAINAACLALLDAGVPMKGLFAAVTCAITEDGEIILDPTAEEEKEAKAVATFAF 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 356554181 174 PNtivsvlpegslQEGSEtmahgIMTSITQGAMSgLGGFVACRALSQR 221
Cdd:cd11372  159 DS-----------GEEKN-----LVLSESEGSFT-EEELFACLELAQA 189
RNase_PH pfam01138
3' exoribonuclease family, domain 1; This family includes 3'-5' exoribonucleases. Ribonuclease ...
 13-135 1.07e-22

3' exoribonuclease family, domain 1; This family includes 3'-5' exoribonucleases. Ribonuclease PH contains a single copy of this domain, and removes nucleotide residues following the -CCA terminus of tRNA. Polyribonucleotide nucleotidyltransferase (PNPase) contains two tandem copies of the domain. PNPase is involved in mRNA degradation in a 3'-5' direction. The exosome is a 3'-5' exoribonuclease complex that is required for 3' processing of the 5.8S rRNA. Three of its five protein components contain a copy of this domain. A hypothetical protein from S. pombe appears to belong to an uncharacterized subfamily. This subfamily is found in both eukaryotes and archaebacteria.


Pssm-ID: 426074 [Multi-domain]  Cd Length: 129  Bit Score: 89.57  E-value: 1.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356554181   13 QLRPLacSCSCSILHRSHGSASWAQRETKVLAAVYGPKaGTKKNENPKKASIKVIWK---------PKTGQIGKVEKEYE 83
Cdd:pfam01138   1 ELRPI--EIETGVLSQADGSALVELGDTKVLATVTGPI-EPKEDRDFAPGRLTVEYElapfasgerPGEGRPSEREIEIS 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 356554181   84 MILKRTLESICIRTIYPNTTTLVIVQIVHDDGVLLPCAINAACVALVDARIP 135
Cdd:pfam01138  78 RLIDRALRPSIPLEGYPRWTIRIDVTVLSSDGSLLDAAINAASLALADAGIP 129
PRK03983 PRK03983
exosome complex exonuclease Rrp41; Provisional
 5-162 3.54e-19

exosome complex exonuclease Rrp41; Provisional


Pssm-ID: 235187 [Multi-domain]  Cd Length: 244  Bit Score: 83.14  E-value: 3.54e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356554181   5 RPDSQTPNQLRPLacSCSCSILHRSHGSASWAQRETKVLAAVYGPK-AGTKKNENPKKASIKVIW-----------KPkt 72
Cdd:PRK03983  15 RLDGRKPDELRPI--KIEVGVLKNADGSAYLEWGNNKIIAAVYGPReMHPRHLQLPDRAVLRVRYnmapfsvderkRP-- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356554181  73 gqiGKVEKEYEM--ILKRTLESICIRTIYPNTTTLVIVQIVHDDGVLLPCAINAACVALVDARIPLKHLVVAICCSITDs 150
Cdd:PRK03983  91 ---GPDRRSIEIskVIREALEPAIMLELFPRTVIDVFIEVLQADAGTRVAGITAASLALADAGIPMRDLVAGCAVGKVD- 166

                        170
                 ....*....|..
gi 356554181 151 GCIILDPTKDQE 162
Cdd:PRK03983 167 GVIVLDLNKEED 178
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
 207-233 3.54e-07

3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440073 [Multi-domain]  Cd Length: 409  Bit Score: 50.09  E-value: 3.54e-07
                         10        20
                 ....*....|....*....|....*..
gi 356554181 207 SGLGGFVACRALSQRNTDPTKASRPWD 233
Cdd:COG0304  195 LGLAGFDALGALSTRNDDPEKASRPFD 221
 
Name Accession Description Interval E-value
RNase_PH_RRP46 cd11372
RRP46 subunit of eukaryotic exosome; The RRP46 subunit of eukaryotic exosome is a member of ...
 14-221 4.96e-65

RRP46 subunit of eukaryotic exosome; The RRP46 subunit of eukaryotic exosome is a member of the RNase_PH family, named after the bacterial Ribonuclease PH, a 3'-5' exoribonuclease. Structurally all members of this family form hexameric rings (trimers of Rrp41-Rrp45, Rrp46-Rrp43, and Mtr3-Rrp42 dimers). The eukaryotic exosome core is composed of six individually encoded RNase PH-like subunits and three additional proteins (Rrp4, Csl4 and Rrp40) that form a stable cap and contain RNA-binding domains. The RNase PH-like subunits are no longer phosphorolytic enzymes, the exosome directly associates with Rrp44 and Rrp6, hydrolytic exoribonucleases related to bacterial RNase II/R and RNase D. The exosome plays an important role in RNA turnover. It plays a crucial role in the maturation of stable RNA species such as rRNA, snRNA and snoRNA, quality control of mRNA, and the degradation of RNA processing by-products and non-coding transcripts.


Pssm-ID: 206777 [Multi-domain]  Cd Length: 199  Bit Score: 200.48  E-value: 4.96e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356554181  14 LRPLacSCSCSILHRSHGSASWAQRETKVLAAVYGPKAGTKKNENPKKASIKVIWKPKTGQIGKVEKEYEMILKRTLESI 93
Cdd:cd11372    1 LRPL--SCELGLLSRADGSARFSQGDTSVLAAVYGPIEVKLRKELPDRATLEVIVRPKSGLPGVKEKLLELLLRSTLEPI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356554181  94 CIRTIYPNTTTLVIVQIVHDDGVLLPCAINAACVALVDARIPLKHLVVAICCSITDSGCIILDPTKDQEEKMKAFINLVF 173
Cdd:cd11372   79 ILLHLHPRTLISVVLQVLQDDGSLLACAINAACLALLDAGVPMKGLFAAVTCAITEDGEIILDPTAEEEKEAKAVATFAF 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 356554181 174 PNtivsvlpegslQEGSEtmahgIMTSITQGAMSgLGGFVACRALSQR 221
Cdd:cd11372  159 DS-----------GEEKN-----LVLSESEGSFT-EEELFACLELAQA 189
RNase_PH cd11358
RNase PH-like 3'-5' exoribonucleases; RNase PH-like 3'-5' exoribonucleases are enzymes that ...
 14-193 1.05e-33

RNase PH-like 3'-5' exoribonucleases; RNase PH-like 3'-5' exoribonucleases are enzymes that catalyze the 3' to 5' processing and decay of RNA substrates. Evolutionarily related members can be fond in prokaryotes, archaea, and eukaryotes. Bacterial ribonuclease PH contains a single copy of this domain, and removes nucleotide residues following the -CCA terminus of tRNA. Polyribonucleotide nucleotidyltransferase (PNPase) contains two tandem copies of the domain and is involved in mRNA degradation in a 3'-5' direction. Archaeal exosomes contain two individually encoded RNase PH-like 3'-5' exoribonucleases and are required for 3' processing of the 5.8S rRNA. The eukaryotic exosome core is composed of six individually encoded RNase PH-like subunits, but it is not a phosphorolytic enzyme per se; it directly associates with Rrp44 and Rrp6, which are hydrolytic exoribonucleases related to bacterial RNase II/R and RNase D. All members of the RNase PH-like family form ring structures by oligomerization of six domains or subunits, except for a total of 3 subunits with tandem repeats in the case of PNPase, with a central channel through which the RNA substrate must pass to gain access to the phosphorolytic active sites.


Pssm-ID: 206766 [Multi-domain]  Cd Length: 218  Bit Score: 120.89  E-value: 1.05e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356554181  14 LRPLACSCScsILHRSHGSASWAQRETKVLAAVYGPKAGTKKNENPKKASIKVIWKPKTGQ--------IGKVEKEYEMI 85
Cdd:cd11358    1 FRPVEIETG--VLNQADGSALVKLGNTKVICAVTGPIVEPDKLERPDKGTLYVNVEISPGAvgerrqgpPGDEEMEISRL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356554181  86 LKRTLESICI---RTIYPNTTTLVIVQIVHDDGVLLPCAINAACVALVDARIPL-------------KHLVVAICCSITD 149
Cdd:cd11358   79 LERTIEASVIldkSTRKPSWVLYVDIQVLSRDGGLLDACWNAAIAALKDAGIPRvfvderspplllmKDLIVAVSVGGIS 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 356554181 150 SGCIILDPTKDQEEKMKAFINLVFPN--TIVSVLPEGSLQEGSETM 193
Cdd:cd11358  159 DGVLLLDPTGEEEELADSTLTVAVDKsgKLCLLSKVGGGSLDTEEI 204
RNase_PH_RRP41 cd11370
RRP41 subunit of eukaryotic exosome; The RRP41 subunit of eukaryotic exosome is a member of ...
 5-182 1.06e-27

RRP41 subunit of eukaryotic exosome; The RRP41 subunit of eukaryotic exosome is a member of the RNase_PH family, named after the bacterial Ribonuclease PH, a 3'-5' exoribonuclease. Structurally all members of this family form hexameric rings (trimers of Rrp41-Rrp45, Rrp46-Rrp43, and Mtr3-Rrp42 dimers). The eukaryotic exosome core is composed of six individually encoded RNase PH-like subunits and three additional proteins (Rrp4, Csl4 and Rrp40) that form a stable cap and contain RNA-binding domains. The RNase PH-like subunits are no longer phosphorolytic enzymes, the exosome directly associates with Rrp44 and Rrp6, hydrolytic exoribonucleases related to bacterial RNase II/R and RNase D. The exosome plays an important role in RNA turnover. It plays a crucial role in the maturation of stable RNA species such as rRNA, snRNA and snoRNA, quality control of mRNA, and the degradation of RNA processing by-products and non-coding transcripts.


Pssm-ID: 206775 [Multi-domain]  Cd Length: 226  Bit Score: 105.32  E-value: 1.06e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356554181   5 RPDSQTPNQLRPLacSCSCSILHRSHGSASWAQRETKVLAAVYGPKAGTKKNE-NPKKASIKV---IWKPKTG---QIGK 77
Cdd:cd11370    3 RLDGRRPNELRRI--RCRIGVFSSADGSAYLEQGNTKVLAAVYGPHEPRNRSQaLHDRAVVNCeysMATFSTGerkRRGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356554181  78 VEK---EYEMILKRTLESICIRTIYPNTTTLVIVQIVHDDGVLLPCAINAACVALVDARIPLKHLVVAICCSITDSgCII 154
Cdd:cd11370   81 GDRrstELSLAIRQTFEAVILTHLYPRSQIDIYVQVLQADGGLLAACINAATLALIDAGIPMKDYVCACSAGYLDS-TPL 159

                        170       180
                 ....*....|....*....|....*...
gi 356554181 155 LDPTKDQEekmkafiNLVFPNTIVSVLP 182
Cdd:cd11370  160 LDLNYLEE-------SGDLPDLTVAVLP 180
RNase_PH pfam01138
3' exoribonuclease family, domain 1; This family includes 3'-5' exoribonucleases. Ribonuclease ...
 13-135 1.07e-22

3' exoribonuclease family, domain 1; This family includes 3'-5' exoribonucleases. Ribonuclease PH contains a single copy of this domain, and removes nucleotide residues following the -CCA terminus of tRNA. Polyribonucleotide nucleotidyltransferase (PNPase) contains two tandem copies of the domain. PNPase is involved in mRNA degradation in a 3'-5' direction. The exosome is a 3'-5' exoribonuclease complex that is required for 3' processing of the 5.8S rRNA. Three of its five protein components contain a copy of this domain. A hypothetical protein from S. pombe appears to belong to an uncharacterized subfamily. This subfamily is found in both eukaryotes and archaebacteria.


Pssm-ID: 426074 [Multi-domain]  Cd Length: 129  Bit Score: 89.57  E-value: 1.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356554181   13 QLRPLacSCSCSILHRSHGSASWAQRETKVLAAVYGPKaGTKKNENPKKASIKVIWK---------PKTGQIGKVEKEYE 83
Cdd:pfam01138   1 ELRPI--EIETGVLSQADGSALVELGDTKVLATVTGPI-EPKEDRDFAPGRLTVEYElapfasgerPGEGRPSEREIEIS 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 356554181   84 MILKRTLESICIRTIYPNTTTLVIVQIVHDDGVLLPCAINAACVALVDARIP 135
Cdd:pfam01138  78 RLIDRALRPSIPLEGYPRWTIRIDVTVLSSDGSLLDAAINAASLALADAGIP 129
RNase_PH_MTR3 cd11371
MTR3 subunit of eukaryotic exosome; The MTR3 subunit of eukaryotic exosome is a member of the ...
 25-200 1.90e-22

MTR3 subunit of eukaryotic exosome; The MTR3 subunit of eukaryotic exosome is a member of the RNase_PH family, named after the bacterial Ribonuclease PH, a 3'-5' exoribonuclease. Structurally all members of this family form hexameric rings (trimers of Rrp41-Rrp45, Rrp46-Rrp43, and Mtr3-Rrp42 dimers). The eukaryotic exosome core is composed of six individually encoded RNase PH-like subunits and three additional proteins (Rrp4, Csl4 and Rrp40) that form a stable cap and contain RNA-binding domains. The RNase PH-like subunits are no longer phosphorolytic enzymes, the exosome directly associates with Rrp44 and Rrp6, hydrolytic exoribonucleases related to bacterial RNase II/R and RNase D. The exosome plays an important role in RNA turnover. It plays a crucial role in the maturation of stable RNA species such as rRNA, snRNA and snoRNA, quality control of mRNA, and the degradation of RNA processing by-products and non-coding transcripts.


Pssm-ID: 206776 [Multi-domain]  Cd Length: 210  Bit Score: 91.09  E-value: 1.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356554181  25 ILHRSHGSASWAQRETKVLAAVYGPKAGTKKNENPKKASIKVIWK--------PKTGQIGKVEKEYEMILKRTLE-SICI 95
Cdd:cd11371   10 VVSQAKGSAYVELGNTKVICSVYGPRPIPGRTEFSDRGRLNCEVKfapfatpgRRRHGQDSEERELSSLLHQALEpAVRL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356554181  96 RTiYPNTTTLVIVQIVHDDGVLLPCAINAACVALVDARIPLKHLVVAICCSItDSGCIILDPTKDQEEKMKAFInlvfpn 175
Cdd:cd11371   90 EK-YPKSQIDVFVTVLESDGSVLAAAITAASLALADAGIEMYDLVTACSAAL-IGDELLLDPTREEEEASSGGV------ 161

                        170       180
                 ....*....|....*....|....*
gi 356554181 176 tIVSVLPegSLQEGSETMAHGIMTS 200
Cdd:cd11371  162 -MLAYMP--SLNQVTQLWQSGEMDV 183
PRK03983 PRK03983
exosome complex exonuclease Rrp41; Provisional
 5-162 3.54e-19

exosome complex exonuclease Rrp41; Provisional


Pssm-ID: 235187 [Multi-domain]  Cd Length: 244  Bit Score: 83.14  E-value: 3.54e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356554181   5 RPDSQTPNQLRPLacSCSCSILHRSHGSASWAQRETKVLAAVYGPK-AGTKKNENPKKASIKVIW-----------KPkt 72
Cdd:PRK03983  15 RLDGRKPDELRPI--KIEVGVLKNADGSAYLEWGNNKIIAAVYGPReMHPRHLQLPDRAVLRVRYnmapfsvderkRP-- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356554181  73 gqiGKVEKEYEM--ILKRTLESICIRTIYPNTTTLVIVQIVHDDGVLLPCAINAACVALVDARIPLKHLVVAICCSITDs 150
Cdd:PRK03983  91 ---GPDRRSIEIskVIREALEPAIMLELFPRTVIDVFIEVLQADAGTRVAGITAASLALADAGIPMRDLVAGCAVGKVD- 166

                        170
                 ....*....|..
gi 356554181 151 GCIILDPTKDQE 162
Cdd:PRK03983 167 GVIVLDLNKEED 178
RNase_PH_archRRP41 cd11366
RRP41 subunit of archaeal exosome; The RRP41 subunit of the archaeal exosome is a member of ...
 13-162 7.35e-17

RRP41 subunit of archaeal exosome; The RRP41 subunit of the archaeal exosome is a member of the RNase_PH family, named after the bacterial Ribonuclease PH, a 3'-5' exoribonuclease. Structurally all members of this family form hexameric rings (trimers of dimers). In archaea, the ring is formed by three Rrp41:Rrp42 dimers. The central chamber within the ring contains three phosphorolytic active sites located in an Rrp41 pocket at the interface between Rrp42 and Rrp41. The ring is capped by three copies of Rrp4 and/or Csl4 which contain putative RNA interaction domains. The archaeal exosome degrades single-stranded RNA (ssRNA) in the 3'-5' direction, but also can catalyze the reverse reaction of adding nucleoside diphosphates to the 3'-end of RNA which has been shown to lead to the formation of poly-A-rich tails on RNA.


Pssm-ID: 206771 [Multi-domain]  Cd Length: 214  Bit Score: 76.22  E-value: 7.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356554181  13 QLRPLacSCSCSILHRSHGSASWAQRETKVLAAVYGPK-AGTKKNENPKKASIKVIWK--P------KTGQIGKVEKEYE 83
Cdd:cd11366    1 ELRPI--KIEVGVLKNADGSAYVEWGNNKIIAAVYGPReVHPRHLQLPDRAVIRVRYNmaPfsvderKRPGPDRREIEIS 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 356554181  84 MILKRTLESICIRTIYPNTTTLVIVQIVHDDGVLLPCAINAACVALVDARIPLKHLVVAICCSITDsGCIILDPTKDQE 162
Cdd:cd11366   79 KVIKEALEPAIILEEFPRTAIDVFVEVLQADAGTRVAGLNAASLALADAGIPMRDLVAACAAGKVD-GKIVLDLNKEED 156
PLN02787 PLN02787
3-oxoacyl-[acyl-carrier-protein] synthase II
 208-234 1.63e-12

3-oxoacyl-[acyl-carrier-protein] synthase II


Pssm-ID: 215421 [Multi-domain]  Cd Length: 540  Bit Score: 66.16  E-value: 1.63e-12
                         10        20
                 ....*....|....*....|....*..
gi 356554181 208 GLGGFVACRALSQRNTDPTKASRPWDI 234
Cdd:PLN02787 326 GLGGFVACRALSQRNDDPTKASRPWDM 352
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
208-233 4.12e-10

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 59.03  E-value: 4.12e-10
                         10        20
                 ....*....|....*....|....*.
gi 356554181 208 GLGGFVACRALSQRNTDPTKASRPWD 233
Cdd:PRK07314 197 GIAGFAAARALSTRNDDPERASRPFD 222
PLN00207 PLN00207
polyribonucleotide nucleotidyltransferase; Provisional
 5-143 2.52e-09

polyribonucleotide nucleotidyltransferase; Provisional


Pssm-ID: 215104 [Multi-domain]  Cd Length: 891  Bit Score: 56.83  E-value: 2.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356554181   5 RPDSQTPNQLRPLacSCSCSILHRSHGSASWAQRETKVLAAV-YGPKAGTKKNEN------PKKASIKVIWKPKT-GQIG 76
Cdd:PLN00207 439 RSDGRTPDEIRPI--NSSCGLLPRAHGSALFTRGETQALAVVtLGDKQMAQRIDNlvdadeVKRFYLQYSFPPSCvGEVG 516

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 356554181  77 KV------EKEYEMILKRTLEsicirTIYPNT-----TTLVIVQIVHDDGVLLPCAINAACVALVDARIPLKHLVVAI 143
Cdd:PLN00207 517 RIgapsrrEIGHGMLAERALE-----PILPSEddfpyTIRVESTITESNGSSSMASVCGGCLALQDAGVPVKCPIAGI 589
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
208-235 7.04e-08

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 52.31  E-value: 7.04e-08
                         10        20
                 ....*....|....*....|....*....
gi 356554181 208 GLGGFVACRALSQR-NTDPTKASRPWDIA 235
Cdd:PRK06333 208 SLAGFAAARALSTRfNDAPEQASRPFDRD 236
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
 207-233 3.54e-07

3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440073 [Multi-domain]  Cd Length: 409  Bit Score: 50.09  E-value: 3.54e-07
                         10        20
                 ....*....|....*....|....*..
gi 356554181 207 SGLGGFVACRALSQRNTDPTKASRPWD 233
Cdd:COG0304  195 LGLAGFDALGALSTRNDDPEKASRPFD 221
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
 208-233 6.95e-07

Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.


Pssm-ID: 238430 [Multi-domain]  Cd Length: 406  Bit Score: 49.07  E-value: 6.95e-07
                         10        20
                 ....*....|....*....|....*.
gi 356554181 208 GLGGFVACRALSQRNTDPTKASRPWD 233
Cdd:cd00834  196 TLAGFAALRALSTRNDDPEKASRPFD 221
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
208-233 2.30e-06

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 47.69  E-value: 2.30e-06
                         10        20
                 ....*....|....*....|....*.
gi 356554181 208 GLGGFVACRALSQRNTDPTKASRPWD 233
Cdd:PRK08722 199 GMAGFGAAKALSTRNDEPQKASRPWD 224
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
 208-233 2.58e-06

3-oxoacyl-(acyl carrier protein) synthase II; Reviewed


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 47.42  E-value: 2.58e-06
                         10        20
                 ....*....|....*....|....*.
gi 356554181 208 GLGGFVACRALSQRNTDPTKASRPWD 233
Cdd:PRK08439 197 GIGGFAAMKALSTRNDDPKKASRPFD 222
 
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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