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Conserved domains on  [gi|17402904|ref|NP_478126|]
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exosome complex component MTR3 [Homo sapiens]

Protein Classification

exosome complex component MTR3( domain architecture ID 10183529)

exosome complex component MTR3 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_MTR3 cd11371
MTR3 subunit of eukaryotic exosome; The MTR3 subunit of eukaryotic exosome is a member of the ...
 36-260 5.32e-72

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: 219.74  E-value: 5.32e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402904  36 LRPVYARAGLLSQAKGSAYLEAGGTKVLCAVSGPRQAEGGERGGGpagaggeapaalRGRLLCDFRRAPFAGRRRRAPPG 115
Cdd:cd11371   1 IRPIFLKTGVVSQAKGSAYVELGNTKVICSVYGPRPIPGRTEFSD------------RGRLNCEVKFAPFATPGRRRHGQ 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402904 116 GCEERELALALQEALEPAVRLGRYPRAQLEVSALLLEDGGSALAAALTAAALALADAGVEMYDLVVGCGLSLAPGpapTW 195
Cdd:cd11371  69 DSEERELSSLLHQALEPAVRLEKYPKSQIDVFVTVLESDGSVLAAAITAASLALADAGIEMYDLVTACSAALIGD---EL 145

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17402904 196 LLDPTRLEEERAAAGLTVALMPVLNQVAgLLGSGEGGLTESWAEAVRLGLEGCQRLYPVLQQSLV 260
Cdd:cd11371 146 LLDPTREEEEASSGGVMLAYMPSLNQVT-QLWQSGEMDVDQLEEALDLCIDGCNRIHPVVRQALL 209
 
Name Accession Description Interval E-value
RNase_PH_MTR3 cd11371
MTR3 subunit of eukaryotic exosome; The MTR3 subunit of eukaryotic exosome is a member of the ...
 36-260 5.32e-72

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: 219.74  E-value: 5.32e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402904  36 LRPVYARAGLLSQAKGSAYLEAGGTKVLCAVSGPRQAEGGERGGGpagaggeapaalRGRLLCDFRRAPFAGRRRRAPPG 115
Cdd:cd11371   1 IRPIFLKTGVVSQAKGSAYVELGNTKVICSVYGPRPIPGRTEFSD------------RGRLNCEVKFAPFATPGRRRHGQ 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402904 116 GCEERELALALQEALEPAVRLGRYPRAQLEVSALLLEDGGSALAAALTAAALALADAGVEMYDLVVGCGLSLAPGpapTW 195
Cdd:cd11371  69 DSEERELSSLLHQALEPAVRLEKYPKSQIDVFVTVLESDGSVLAAAITAASLALADAGIEMYDLVTACSAALIGD---EL 145

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17402904 196 LLDPTRLEEERAAAGLTVALMPVLNQVAgLLGSGEGGLTESWAEAVRLGLEGCQRLYPVLQQSLV 260
Cdd:cd11371 146 LLDPTREEEEASSGGVMLAYMPSLNQVT-QLWQSGEMDVDQLEEALDLCIDGCNRIHPVVRQALL 209
PRK03983 PRK03983
exosome complex exonuclease Rrp41; Provisional
 13-252 3.39e-27

exosome complex exonuclease Rrp41; Provisional


Pssm-ID: 235187 [Multi-domain]  Cd Length: 244  Bit Score: 105.49  E-value: 3.39e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402904   13 ESQPPQLYAADEEEAPGtRDPTRLRPVYARAGLLSQAKGSAYLEAGGTKVLCAVSGPRQAEGGERGGGPagaggeapaal 92
Cdd:PRK03983   2 QVEPPKLILEDGLRLDG-RKPDELRPIKIEVGVLKNADGSAYLEWGNNKIIAAVYGPREMHPRHLQLPD----------- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402904   93 RGRLLCDFRRAPFAGRRRRAPPGGCEERELALALQEALEPAVRLGRYPRAQLEVSALLLEDGGSALAAALTAAALALADA 172
Cdd:PRK03983  70 RAVLRVRYNMAPFSVDERKRPGPDRRSIEISKVIREALEPAIMLELFPRTVIDVFIEVLQADAGTRVAGITAASLALADA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402904  173 GVEMYDLVVGCGLSLAPGpapTWLLDPTRLEEERAAAGLTVALMPVLNQVAGLLGSGEGGLtESWAEAVRLGLEGCQRLY 252
Cdd:PRK03983 150 GIPMRDLVAGCAVGKVDG---VIVLDLNKEEDNYGEADMPVAIMPRLGEITLLQLDGNLTR-EEFLEALELAKKGIKRIY 225
RNase_PH pfam01138
3' exoribonuclease family, domain 1; This family includes 3'-5' exoribonucleases. Ribonuclease ...
 36-175 1.37e-18

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: 79.56  E-value: 1.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402904    36 LRPVYARAGLLSQAKGSAYLEAGGTKVLCAVSGPRqaeggergggpagAGGEAPAALRGRLLCDFRRAPFA-GRRRRAPP 114
Cdd:pfam01138   2 LRPIEIETGVLSQADGSALVELGDTKVLATVTGPI-------------EPKEDRDFAPGRLTVEYELAPFAsGERPGEGR 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17402904   115 GGCEERELALALQEALEPAVRLGRYPRAQLEVSALLLEDGGSALAAALTAAALALADAGVE 175
Cdd:pfam01138  69 PSEREIEISRLIDRALRPSIPLEGYPRWTIRIDVTVLSSDGSLLDAAINAASLALADAGIP 129
Rph COG0689
Ribonuclease PH [Translation, ribosomal structure and biogenesis];
31-67 2.82e-03

Ribonuclease PH [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440453 [Multi-domain]  Cd Length: 238  Bit Score: 38.09  E-value: 2.82e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 17402904  31 RDPTRLRPVYARAGLLSQAKGSAYLEAGGTKVLCAVS 67
Cdd:COG0689   6 RAPDQLRPVKITRGFTKHAEGSVLIEFGDTKVLCTAS 42
 
Name Accession Description Interval E-value
RNase_PH_MTR3 cd11371
MTR3 subunit of eukaryotic exosome; The MTR3 subunit of eukaryotic exosome is a member of the ...
 36-260 5.32e-72

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: 219.74  E-value: 5.32e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402904  36 LRPVYARAGLLSQAKGSAYLEAGGTKVLCAVSGPRQAEGGERGGGpagaggeapaalRGRLLCDFRRAPFAGRRRRAPPG 115
Cdd:cd11371   1 IRPIFLKTGVVSQAKGSAYVELGNTKVICSVYGPRPIPGRTEFSD------------RGRLNCEVKFAPFATPGRRRHGQ 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402904 116 GCEERELALALQEALEPAVRLGRYPRAQLEVSALLLEDGGSALAAALTAAALALADAGVEMYDLVVGCGLSLAPGpapTW 195
Cdd:cd11371  69 DSEERELSSLLHQALEPAVRLEKYPKSQIDVFVTVLESDGSVLAAAITAASLALADAGIEMYDLVTACSAALIGD---EL 145

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17402904 196 LLDPTRLEEERAAAGLTVALMPVLNQVAgLLGSGEGGLTESWAEAVRLGLEGCQRLYPVLQQSLV 260
Cdd:cd11371 146 LLDPTREEEEASSGGVMLAYMPSLNQVT-QLWQSGEMDVDQLEEALDLCIDGCNRIHPVVRQALL 209
RNase_PH cd11358
RNase PH-like 3'-5' exoribonucleases; RNase PH-like 3'-5' exoribonucleases are enzymes that ...
 36-251 1.00e-37

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: 132.07  E-value: 1.00e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402904  36 LRPVYARAGLLSQAKGSAYLEAGGTKVLCAVSGPRQAEGGERGGGpagaggeapaalRGRLLCDFRRAPFAGRRRRAPPG 115
Cdd:cd11358   1 FRPVEIETGVLNQADGSALVKLGNTKVICAVTGPIVEPDKLERPD------------KGTLYVNVEISPGAVGERRQGPP 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402904 116 GCEERELALALQEALEPAVRL---GRYPRAQLEVSALLLEDGGSALAAAL-------------TAAALALADAGVEMYDL 179
Cdd:cd11358  69 GDEEMEISRLLERTIEASVILdksTRKPSWVLYVDIQVLSRDGGLLDACWnaaiaalkdagipRVFVDERSPPLLLMKDL 148

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17402904 180 VVGCGLSLAPGpaPTWLLDPTRLEEERAAAGLTVALMPVLNQVAGLLGSGEGGLTESWAEAVRLGLEGCQRL 251
Cdd:cd11358 149 IVAVSVGGISD--GVLLLDPTGEEEELADSTLTVAVDKSGKLCLLSKVGGGSLDTEEIKECLELAKKRSLHL 218
PRK03983 PRK03983
exosome complex exonuclease Rrp41; Provisional
 13-252 3.39e-27

exosome complex exonuclease Rrp41; Provisional


Pssm-ID: 235187 [Multi-domain]  Cd Length: 244  Bit Score: 105.49  E-value: 3.39e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402904   13 ESQPPQLYAADEEEAPGtRDPTRLRPVYARAGLLSQAKGSAYLEAGGTKVLCAVSGPRQAEGGERGGGPagaggeapaal 92
Cdd:PRK03983   2 QVEPPKLILEDGLRLDG-RKPDELRPIKIEVGVLKNADGSAYLEWGNNKIIAAVYGPREMHPRHLQLPD----------- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402904   93 RGRLLCDFRRAPFAGRRRRAPPGGCEERELALALQEALEPAVRLGRYPRAQLEVSALLLEDGGSALAAALTAAALALADA 172
Cdd:PRK03983  70 RAVLRVRYNMAPFSVDERKRPGPDRRSIEISKVIREALEPAIMLELFPRTVIDVFIEVLQADAGTRVAGITAASLALADA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402904  173 GVEMYDLVVGCGLSLAPGpapTWLLDPTRLEEERAAAGLTVALMPVLNQVAGLLGSGEGGLtESWAEAVRLGLEGCQRLY 252
Cdd:PRK03983 150 GIPMRDLVAGCAVGKVDG---VIVLDLNKEEDNYGEADMPVAIMPRLGEITLLQLDGNLTR-EEFLEALELAKKGIKRIY 225
RNase_PH_archRRP41 cd11366
RRP41 subunit of archaeal exosome; The RRP41 subunit of the archaeal exosome is a member of ...
 36-259 4.11e-27

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: 104.34  E-value: 4.11e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402904  36 LRPVYARAGLLSQAKGSAYLEAGGTKVLCAVSGPRQAEGGERGGGPagaggeapaalRGRLLCDFRRAPFAGRRRRAPPG 115
Cdd:cd11366   2 LRPIKIEVGVLKNADGSAYVEWGNNKIIAAVYGPREVHPRHLQLPD-----------RAVIRVRYNMAPFSVDERKRPGP 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402904 116 GCEERELALALQEALEPAVRLGRYPRAQLEVSALLLEDGGSALAAALTAAALALADAGVEMYDLVVGCGLSLAPGpapTW 195
Cdd:cd11366  71 DRREIEISKVIKEALEPAIILEEFPRTAIDVFVEVLQADAGTRVAGLNAASLALADAGIPMRDLVAACAAGKVDG---KI 147

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17402904 196 LLDPTRLEEERAAAGLTVALMPVLNQVAgLLGSGEGGLTESWAEAVRLGLEGCQRLYPVLQQSL 259
Cdd:cd11366 148 VLDLNKEEDNYGEADMPIAMMPNLGEIT-LLQLDGDLTPDEFKQAIELAKKGCKRIYELQKEAL 210
RNase_PH_RRP41 cd11370
RRP41 subunit of eukaryotic exosome; The RRP41 subunit of eukaryotic exosome is a member of ...
 31-257 6.75e-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: 104.16  E-value: 6.75e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402904  31 RDPTRLRPVYARAGLLSQAKGSAYLEAGGTKVLCAVSGPRQAEGGERGGGPagaggeapaalRGRLLCDFRRAPFAGRRR 110
Cdd:cd11370   7 RRPNELRRIRCRIGVFSSADGSAYLEQGNTKVLAAVYGPHEPRNRSQALHD-----------RAVVNCEYSMATFSTGER 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402904 111 RAPPGGceER---ELALALQEALEPAVRLGRYPRAQLEVSALLLEDGGSALAAALTAAALALADAGVEMYDLVVGCGLSL 187
Cdd:cd11370  76 KRRGKG--DRrstELSLAIRQTFEAVILTHLYPRSQIDIYVQVLQADGGLLAACINAATLALIDAGIPMKDYVCACSAGY 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402904 188 APGpapTWLLDPTRLEEERAAAGLTVALMPVLNQVAGLLGSGEGGLtESWAEAVRLGLEGCQRLYPVLQQ 257
Cdd:cd11370 154 LDS---TPLLDLNYLEESGDLPDLTVAVLPKSDKVVLLQMESRLHL-DRLEKVLELAIEGCKVIREIMDE 219
RNase_PH pfam01138
3' exoribonuclease family, domain 1; This family includes 3'-5' exoribonucleases. Ribonuclease ...
 36-175 1.37e-18

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: 79.56  E-value: 1.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402904    36 LRPVYARAGLLSQAKGSAYLEAGGTKVLCAVSGPRqaeggergggpagAGGEAPAALRGRLLCDFRRAPFA-GRRRRAPP 114
Cdd:pfam01138   2 LRPIEIETGVLSQADGSALVELGDTKVLATVTGPI-------------EPKEDRDFAPGRLTVEYELAPFAsGERPGEGR 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17402904   115 GGCEERELALALQEALEPAVRLGRYPRAQLEVSALLLEDGGSALAAALTAAALALADAGVE 175
Cdd:pfam01138  69 PSEREIEISRLIDRALRPSIPLEGYPRWTIRIDVTVLSSDGSLLDAAINAASLALADAGIP 129
RNase_PH_RRP46 cd11372
RRP46 subunit of eukaryotic exosome; The RRP46 subunit of eukaryotic exosome is a member of ...
 36-216 2.91e-17

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: 77.60  E-value: 2.91e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402904  36 LRPVYARAGLLSQAKGSAYLEAGGTKVLCAVSGPRQAEGGERGGGpagaggeapaalRGRLLCDFRRApfAGrrrrapPG 115
Cdd:cd11372   1 LRPLSCELGLLSRADGSARFSQGDTSVLAAVYGPIEVKLRKELPD------------RATLEVIVRPK--SG------LP 60

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402904 116 GCEERELALALQEALEPAVRLGRYPRAQLEVSALLLEDGGSALAAALTAAALALADAGVEMYDLVVGCGLSLAPGpaPTW 195
Cdd:cd11372  61 GVKEKLLELLLRSTLEPIILLHLHPRTLISVVLQVLQDDGSLLACAINAACLALLDAGVPMKGLFAAVTCAITED--GEI 138

                       170       180
                ....*....|....*....|.
gi 17402904 196 LLDPTRLEEERAAAGLTVALM 216
Cdd:cd11372 139 ILDPTAEEEKEAKAVATFAFD 159
Rph COG0689
Ribonuclease PH [Translation, ribosomal structure and biogenesis];
31-67 2.82e-03

Ribonuclease PH [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440453 [Multi-domain]  Cd Length: 238  Bit Score: 38.09  E-value: 2.82e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 17402904  31 RDPTRLRPVYARAGLLSQAKGSAYLEAGGTKVLCAVS 67
Cdd:COG0689   6 RAPDQLRPVKITRGFTKHAEGSVLIEFGDTKVLCTAS 42
 
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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