|
Name |
Accession |
Description |
Interval |
E-value |
| Rph |
COG0689 |
Ribonuclease PH [Translation, ribosomal structure and biogenesis]; |
1-238 |
0e+00 |
|
Ribonuclease PH [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440453 [Multi-domain] Cd Length: 238 Bit Score: 499.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 1 MRPNDRAVDQIRPIKITRNYTAYAEGSVLVEFGNTKVLCNATVEENVPRWLKGQGKGWVTAEYGMLPRATHTRNRREAAS 80
Cdd:COG0689 1 MRPDGRAPDQLRPVKITRGFTKHAEGSVLIEFGDTKVLCTASVEEGVPPFLKGSGQGWVTAEYGMLPRATHTRNRREAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 81 GKQGGRTMEIQRLIARSLRAVVDLKVMGEIMITVDCDVIQADGGTRTASISGASVAMADAINSLLASGKLKKNPMKGHVA 160
Cdd:COG0689 81 GKQSGRTQEIQRLIGRSLRAVVDLKALGERTITIDCDVLQADGGTRTASITGAFVALADALNKLVEKGLLKENPLKDQVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490873725 161 AVSVGIVGAQALCDLEYVEDSAADTDMNVVMTEDGKMIEIQGTAEGEPFSHEELMQLLALANKGITDIVEAQKAALAD 238
Cdd:COG0689 161 AVSVGIVDGEPVLDLDYEEDSAAEVDMNVVMTGSGEFVEVQGTAEGAPFSREELDALLDLAEKGIAELIALQKEALGE 238
|
|
| rph |
PRK00173 |
ribonuclease PH; Reviewed |
1-238 |
5.80e-178 |
|
ribonuclease PH; Reviewed
Pssm-ID: 178914 Cd Length: 238 Bit Score: 487.69 E-value: 5.80e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 1 MRPNDRAVDQIRPIKITRNYTAYAEGSVLVEFGNTKVLCNATVEENVPRWLKGQGKGWVTAEYGMLPRATHTRNRREAAS 80
Cdd:PRK00173 1 MRPDGRAADQLRPVTITRNFTKHAEGSVLVEFGDTKVLCTASVEEGVPRFLKGQGQGWVTAEYGMLPRATHTRNDREAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 81 GKQGGRTMEIQRLIARSLRAVVDLKVMGEIMITVDCDVIQADGGTRTASISGASVAMADAINSLLASGKLKKNPMKGHVA 160
Cdd:PRK00173 81 GKQGGRTQEIQRLIGRSLRAVVDLKALGERTITIDCDVIQADGGTRTASITGAYVALADALNKLVARGKLKKNPLKDQVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490873725 161 AVSVGIVGAQALCDLEYVEDSAADTDMNVVMTEDGKMIEIQGTAEGEPFSHEELMQLLALANKGITDIVEAQKAALAD 238
Cdd:PRK00173 161 AVSVGIVDGEPVLDLDYEEDSAAETDMNVVMTGSGGFVEVQGTAEGAPFSREELDALLDLAEKGIAELVALQKAALAD 238
|
|
| RNasePH |
TIGR01966 |
ribonuclease PH; This bacterial enzyme, ribonuclease PH, performs the final 3'-trimming and ... |
2-237 |
3.32e-145 |
|
ribonuclease PH; This bacterial enzyme, ribonuclease PH, performs the final 3'-trimming and modification of tRNA precursors. This model is restricted absolutely to bacteria. Related families outside the model include proteins described as probable exosome complex exonucleases (rRNA processing) and polyribonucleotide nucleotidyltransferases (mRNA degradation). The most divergent member within the family is RNase PH from Deinococcus radiodurans. [Transcription, RNA processing]
Pssm-ID: 131021 Cd Length: 236 Bit Score: 404.82 E-value: 3.32e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 2 RPNDRAVDQIRPIKITRNYTAYAEGSVLVEFGNTKVLCNATVEENVPRWLKGQGKGWVTAEYGMLPRATHTRNRREAASG 81
Cdd:TIGR01966 1 RPDGRKPDQLRPVSITRDFLKHAEGSVLIEFGNTKVLCTASVEEKVPPFLRGSGEGWITAEYGMLPRATQTRNRRESAKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 82 KQGGRTMEIQRLIARSLRAVVDLKVMGEIMITVDCDVIQADGGTRTASISGASVAMADAINSLLASGKLKKNPMKGHVAA 161
Cdd:TIGR01966 81 KQSGRTQEIQRLIGRALRAVVDLEALGERTIWIDCDVIQADGGTRTASITGAFVALADAISKLHKRGILKESPIRDFVAA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490873725 162 VSVGIVGAQALCDLEYVEDSAADTDMNVVMTEDGKMIEIQGTAEGEPFSHEELMQLLALANKGITDIVEAQKAALA 237
Cdd:TIGR01966 161 VSVGIVDGEPVLDLDYEEDSAADVDMNVVMTGSGGFVEVQGTAEEGPFSRDELNKLLDLAKKGIRELIELQKQALG 236
|
|
| RNase_PH_bact |
cd11362 |
Ribonuclease PH; Ribonuclease PH (RNase PH)-like 3'-5' exoribonucleases are enzymes that ... |
10-236 |
8.72e-145 |
|
Ribonuclease PH; Ribonuclease PH (RNase PH)-like 3'-5' exoribonucleases are enzymes that catalyze the 3' to 5' processing and decay of RNA substrates. Structurally all members of this family form hexameric rings (trimers of dimers). Bacterial RNase PH forms a homohexameric ring, and removes nucleotide residues following the -CCA terminus of tRNA.
Pssm-ID: 206767 [Multi-domain] Cd Length: 227 Bit Score: 403.53 E-value: 8.72e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 10 QIRPIKITRNYTAYAEGSVLVEFGNTKVLCNATVEENVPRWLKGQGKGWVTAEYGMLPRATHTRNRREAASGKQGGRTME 89
Cdd:cd11362 1 QLRPISITRGFNKHAEGSVLIEFGDTKVLCTASVEEKVPPFLRGKGKGWVTAEYSMLPRSTHERTQREASKGKQSGRTQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 90 IQRLIARSLRAVVDLKVMGEIMITVDCDVIQADGGTRTASISGASVAMADAINSLLASGKLKKNPMKGHVAAVSVGIVGA 169
Cdd:cd11362 81 IQRLIGRSLRAAVDLEALGERTITIDCDVLQADGGTRTASITGAYVALADAVDKLVEKGVLEENPLKHFVAAVSVGIVDG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490873725 170 QALCDLEYVEDSAADTDMNVVMTEDGKMIEIQGTAEGEPFSHEELMQLLALANKGITDIVEAQKAAL 236
Cdd:cd11362 161 EPLLDLDYEEDSAADVDMNVVMTGSGRFVEVQGTGEEAPFSRDELNELLDLAEKGIQELIELQKEAL 227
|
|
| RNase_PH |
pfam01138 |
3' exoribonuclease family, domain 1; This family includes 3'-5' exoribonucleases. Ribonuclease ... |
10-140 |
9.96e-33 |
|
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: 115.38 E-value: 9.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 10 QIRPIKITRNYTAYAEGSVLVEFGNTKVLCNATVEEnVPRWLKGQGKGWVTAEYGMLPRATHTRNRReaasGKQGGRTME 89
Cdd:pfam01138 1 ELRPIEIETGVLSQADGSALVELGDTKVLATVTGPI-EPKEDRDFAPGRLTVEYELAPFASGERPGE----GRPSEREIE 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 490873725 90 IQRLIARSLRAVVDLKVMGEIMITVDCDVIQADGGTRTASISGASVAMADA 140
Cdd:pfam01138 76 ISRLIDRALRPSIPLEGYPRWTIRIDVTVLSSDGSLLDAAINAASLALADA 126
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Rph |
COG0689 |
Ribonuclease PH [Translation, ribosomal structure and biogenesis]; |
1-238 |
0e+00 |
|
Ribonuclease PH [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440453 [Multi-domain] Cd Length: 238 Bit Score: 499.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 1 MRPNDRAVDQIRPIKITRNYTAYAEGSVLVEFGNTKVLCNATVEENVPRWLKGQGKGWVTAEYGMLPRATHTRNRREAAS 80
Cdd:COG0689 1 MRPDGRAPDQLRPVKITRGFTKHAEGSVLIEFGDTKVLCTASVEEGVPPFLKGSGQGWVTAEYGMLPRATHTRNRREAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 81 GKQGGRTMEIQRLIARSLRAVVDLKVMGEIMITVDCDVIQADGGTRTASISGASVAMADAINSLLASGKLKKNPMKGHVA 160
Cdd:COG0689 81 GKQSGRTQEIQRLIGRSLRAVVDLKALGERTITIDCDVLQADGGTRTASITGAFVALADALNKLVEKGLLKENPLKDQVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490873725 161 AVSVGIVGAQALCDLEYVEDSAADTDMNVVMTEDGKMIEIQGTAEGEPFSHEELMQLLALANKGITDIVEAQKAALAD 238
Cdd:COG0689 161 AVSVGIVDGEPVLDLDYEEDSAAEVDMNVVMTGSGEFVEVQGTAEGAPFSREELDALLDLAEKGIAELIALQKEALGE 238
|
|
| rph |
PRK00173 |
ribonuclease PH; Reviewed |
1-238 |
5.80e-178 |
|
ribonuclease PH; Reviewed
Pssm-ID: 178914 Cd Length: 238 Bit Score: 487.69 E-value: 5.80e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 1 MRPNDRAVDQIRPIKITRNYTAYAEGSVLVEFGNTKVLCNATVEENVPRWLKGQGKGWVTAEYGMLPRATHTRNRREAAS 80
Cdd:PRK00173 1 MRPDGRAADQLRPVTITRNFTKHAEGSVLVEFGDTKVLCTASVEEGVPRFLKGQGQGWVTAEYGMLPRATHTRNDREAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 81 GKQGGRTMEIQRLIARSLRAVVDLKVMGEIMITVDCDVIQADGGTRTASISGASVAMADAINSLLASGKLKKNPMKGHVA 160
Cdd:PRK00173 81 GKQGGRTQEIQRLIGRSLRAVVDLKALGERTITIDCDVIQADGGTRTASITGAYVALADALNKLVARGKLKKNPLKDQVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490873725 161 AVSVGIVGAQALCDLEYVEDSAADTDMNVVMTEDGKMIEIQGTAEGEPFSHEELMQLLALANKGITDIVEAQKAALAD 238
Cdd:PRK00173 161 AVSVGIVDGEPVLDLDYEEDSAAETDMNVVMTGSGGFVEVQGTAEGAPFSREELDALLDLAEKGIAELVALQKAALAD 238
|
|
| RNasePH |
TIGR01966 |
ribonuclease PH; This bacterial enzyme, ribonuclease PH, performs the final 3'-trimming and ... |
2-237 |
3.32e-145 |
|
ribonuclease PH; This bacterial enzyme, ribonuclease PH, performs the final 3'-trimming and modification of tRNA precursors. This model is restricted absolutely to bacteria. Related families outside the model include proteins described as probable exosome complex exonucleases (rRNA processing) and polyribonucleotide nucleotidyltransferases (mRNA degradation). The most divergent member within the family is RNase PH from Deinococcus radiodurans. [Transcription, RNA processing]
Pssm-ID: 131021 Cd Length: 236 Bit Score: 404.82 E-value: 3.32e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 2 RPNDRAVDQIRPIKITRNYTAYAEGSVLVEFGNTKVLCNATVEENVPRWLKGQGKGWVTAEYGMLPRATHTRNRREAASG 81
Cdd:TIGR01966 1 RPDGRKPDQLRPVSITRDFLKHAEGSVLIEFGNTKVLCTASVEEKVPPFLRGSGEGWITAEYGMLPRATQTRNRRESAKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 82 KQGGRTMEIQRLIARSLRAVVDLKVMGEIMITVDCDVIQADGGTRTASISGASVAMADAINSLLASGKLKKNPMKGHVAA 161
Cdd:TIGR01966 81 KQSGRTQEIQRLIGRALRAVVDLEALGERTIWIDCDVIQADGGTRTASITGAFVALADAISKLHKRGILKESPIRDFVAA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490873725 162 VSVGIVGAQALCDLEYVEDSAADTDMNVVMTEDGKMIEIQGTAEGEPFSHEELMQLLALANKGITDIVEAQKAALA 237
Cdd:TIGR01966 161 VSVGIVDGEPVLDLDYEEDSAADVDMNVVMTGSGGFVEVQGTAEEGPFSRDELNKLLDLAKKGIRELIELQKQALG 236
|
|
| RNase_PH_bact |
cd11362 |
Ribonuclease PH; Ribonuclease PH (RNase PH)-like 3'-5' exoribonucleases are enzymes that ... |
10-236 |
8.72e-145 |
|
Ribonuclease PH; Ribonuclease PH (RNase PH)-like 3'-5' exoribonucleases are enzymes that catalyze the 3' to 5' processing and decay of RNA substrates. Structurally all members of this family form hexameric rings (trimers of dimers). Bacterial RNase PH forms a homohexameric ring, and removes nucleotide residues following the -CCA terminus of tRNA.
Pssm-ID: 206767 [Multi-domain] Cd Length: 227 Bit Score: 403.53 E-value: 8.72e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 10 QIRPIKITRNYTAYAEGSVLVEFGNTKVLCNATVEENVPRWLKGQGKGWVTAEYGMLPRATHTRNRREAASGKQGGRTME 89
Cdd:cd11362 1 QLRPISITRGFNKHAEGSVLIEFGDTKVLCTASVEEKVPPFLRGKGKGWVTAEYSMLPRSTHERTQREASKGKQSGRTQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 90 IQRLIARSLRAVVDLKVMGEIMITVDCDVIQADGGTRTASISGASVAMADAINSLLASGKLKKNPMKGHVAAVSVGIVGA 169
Cdd:cd11362 81 IQRLIGRSLRAAVDLEALGERTITIDCDVLQADGGTRTASITGAYVALADAVDKLVEKGVLEENPLKHFVAAVSVGIVDG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490873725 170 QALCDLEYVEDSAADTDMNVVMTEDGKMIEIQGTAEGEPFSHEELMQLLALANKGITDIVEAQKAAL 236
Cdd:cd11362 161 EPLLDLDYEEDSAADVDMNVVMTGSGRFVEVQGTGEEAPFSRDELNELLDLAEKGIQELIELQKEAL 227
|
|
| RNase_PH |
cd11358 |
RNase PH-like 3'-5' exoribonucleases; RNase PH-like 3'-5' exoribonucleases are enzymes that ... |
11-228 |
1.10e-42 |
|
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: 144.01 E-value: 1.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 11 IRPIKITRNYTAYAEGSVLVEFGNTKVLCNATVEENVPRWLKGQGKGWVTAEYGMLPRATHTRNRreaasGKQGGRTMEI 90
Cdd:cd11358 1 FRPVEIETGVLNQADGSALVKLGNTKVICAVTGPIVEPDKLERPDKGTLYVNVEISPGAVGERRQ-----GPPGDEEMEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 91 QRLIARSLRAVVDLKVMGEI---MITVDCDVIQADGGTRTASISGASVAMADAI--NSLLASGKLKKNPMKGHVAAVSVG 165
Cdd:cd11358 76 SRLLERTIEASVILDKSTRKpswVLYVDIQVLSRDGGLLDACWNAAIAALKDAGipRVFVDERSPPLLLMKDLIVAVSVG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490873725 166 IVGA-QALCDLEYVEDSAADTDMNVVMTEDGKMIEIQGTAEGEPFShEELMQLLALANKGITDI 228
Cdd:cd11358 156 GISDgVLLLDPTGEEEELADSTLTVAVDKSGKLCLLSKVGGGSLDT-EEIKECLELAKKRSLHL 218
|
|
| PRK03983 |
PRK03983 |
exosome complex exonuclease Rrp41; Provisional |
1-236 |
7.23e-36 |
|
exosome complex exonuclease Rrp41; Provisional
Pssm-ID: 235187 [Multi-domain] Cd Length: 244 Bit Score: 127.06 E-value: 7.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 1 MRPNDRAVDQIRPIKITRNYTAYAEGSVLVEFGNTKVLcnATV---EENVPRWLKGQGKGWVTAEYGMLPRATHTRNR-- 75
Cdd:PRK03983 14 LRLDGRKPDELRPIKIEVGVLKNADGSAYLEWGNNKII--AAVygpREMHPRHLQLPDRAVLRVRYNMAPFSVDERKRpg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 76 --ReaasgkqggRTMEIQRLIARSLRAVVDLKVMGEIMITVDCDVIQADGGTRTASISGASVAMADA-Insllasgklkk 152
Cdd:PRK03983 92 pdR---------RSIEISKVIREALEPAIMLELFPRTVIDVFIEVLQADAGTRVAGITAASLALADAgI----------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 153 nPMKGHVAAVSVGIVGAQALCDLEYVEDSAADTDMNVVMTEDGKMI---EIQGTaegepFSHEELMQLLALANKGITDIV 229
Cdd:PRK03983 152 -PMRDLVAGCAVGKVDGVIVLDLNKEEDNYGEADMPVAIMPRLGEItllQLDGN-----LTREEFLEALELAKKGIKRIY 225
|
....*..
gi 490873725 230 EAQKAAL 236
Cdd:PRK03983 226 QLQREAL 232
|
|
| RNase_PH_archRRP41 |
cd11366 |
RRP41 subunit of archaeal exosome; The RRP41 subunit of the archaeal exosome is a member of ... |
10-238 |
7.72e-36 |
|
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: 126.29 E-value: 7.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 10 QIRPIKITRNYTAYAEGSVLVEFGNTKVLcnATV---EENVPRWLKGQGKGWVTAEYGMLPRATHTRnRREAASGkqggR 86
Cdd:cd11366 1 ELRPIKIEVGVLKNADGSAYVEWGNNKII--AAVygpREVHPRHLQLPDRAVIRVRYNMAPFSVDER-KRPGPDR----R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 87 TMEIQRLIARSLRAVVDLKVMGEIMITVDCDVIQADGGTRTASISGASVAMADA-InsllasgklkknPMKGHVAAVSVG 165
Cdd:cd11366 74 EIEISKVIKEALEPAIILEEFPRTAIDVFVEVLQADAGTRVAGLNAASLALADAgI------------PMRDLVAACAAG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490873725 166 IVGAQALCDLEYVEDSAADTDMNVVMTEDGK---MIEIQGTaegepFSHEELMQLLALANKGITDIVEAQKAALAD 238
Cdd:cd11366 142 KVDGKIVLDLNKEEDNYGEADMPIAMMPNLGeitLLQLDGD-----LTPDEFKQAIELAKKGCKRIYELQKEALKR 212
|
|
| RNase_PH |
pfam01138 |
3' exoribonuclease family, domain 1; This family includes 3'-5' exoribonucleases. Ribonuclease ... |
10-140 |
9.96e-33 |
|
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: 115.38 E-value: 9.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 10 QIRPIKITRNYTAYAEGSVLVEFGNTKVLCNATVEEnVPRWLKGQGKGWVTAEYGMLPRATHTRNRReaasGKQGGRTME 89
Cdd:pfam01138 1 ELRPIEIETGVLSQADGSALVELGDTKVLATVTGPI-EPKEDRDFAPGRLTVEYELAPFASGERPGE----GRPSEREIE 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 490873725 90 IQRLIARSLRAVVDLKVMGEIMITVDCDVIQADGGTRTASISGASVAMADA 140
Cdd:pfam01138 76 ISRLIDRALRPSIPLEGYPRWTIRIDVTVLSSDGSLLDAAINAASLALADA 126
|
|
| RNase_PH_RRP41 |
cd11370 |
RRP41 subunit of eukaryotic exosome; The RRP41 subunit of eukaryotic exosome is a member of ... |
24-236 |
7.20e-25 |
|
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: 98.00 E-value: 7.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 24 AEGSVLVEFGNTKVLCnaTV---EENVPRWLKGQGKGWVTAEYGMLPRATHTRNRReaasGKQGGRTMEIQRLIARSLRA 100
Cdd:cd11370 25 ADGSAYLEQGNTKVLA--AVygpHEPRNRSQALHDRAVVNCEYSMATFSTGERKRR----GKGDRRSTELSLAIRQTFEA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 101 VVDLKVMGEIMITVDCDVIQADGGTRTASISGASVAMADA-InsllasgklkknPMKGHVAAVSVGIVGAQALCDLEYVE 179
Cdd:cd11370 99 VILTHLYPRSQIDIYVQVLQADGGLLAACINAATLALIDAgI------------PMKDYVCACSAGYLDSTPLLDLNYLE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490873725 180 DSAADTDMNV-VMTEDGKMIEIQGTAEgepFSHEELMQLLALANKGITDIVEAQKAAL 236
Cdd:cd11370 167 ESGDLPDLTVaVLPKSDKVVLLQMESR---LHLDRLEKVLELAIEGCKVIREIMDEVV 221
|
|
| PRK04282 |
PRK04282 |
exosome complex protein Rrp42; |
2-237 |
2.13e-22 |
|
exosome complex protein Rrp42;
Pssm-ID: 235268 [Multi-domain] Cd Length: 271 Bit Score: 92.25 E-value: 2.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 2 RPNDRAVDQIRPIKITRNYTAYAEGSVLVEFGNTKVLCNATVEENVP-RWLKGQGKGWVTAEygMLPRATHTrnrREAas 80
Cdd:PRK04282 25 RIDGRKLDEYRPIEIETGVIKKAEGSALVKLGNTQVLAGVKLEIGEPfPDTPNEGVLIVNAE--LLPLASPT---FEP-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 81 GKQGGRTMEIQRLIARSLR--AVVDLKVM----GEI--MITVDCDVIQADGGTRTASISGASVAMADAI---------NS 143
Cdd:PRK04282 98 GPPDENAIELARVVDRGIResKAIDLEKLviepGKKvwVVFIDVYVLDHDGNLLDASMLAAVAALLNTKvpaveegedGV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 144 LLASGKLKKNPMKGHVAAVSVGIVGAQALCDLEYVEDSAADTDMNVVMTEDGKMIEIQGTAEGePFSHEELMQLLALANK 223
Cdd:PRK04282 178 VDKLGEDFPLPVNDKPVTVTFAKIGNYLIVDPTLEEESVMDARITITTDEDGNIVAIQKSGIG-SFTEEEVDKAIDIALE 256
|
250
....*....|....
gi 490873725 224 GITDIVEAQKAALA 237
Cdd:PRK04282 257 KAKELREKLKEALG 270
|
|
| RNase_PH_archRRP42 |
cd11365 |
RRP42 subunit of archaeal exosome; The RRP42 subunit of the archaeal exosome is a member of ... |
2-231 |
1.87e-17 |
|
RRP42 subunit of archaeal exosome; The RRP42 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. It is required for 3' processing of the 5.8S rRNA.
Pssm-ID: 206770 [Multi-domain] Cd Length: 256 Bit Score: 78.80 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 2 RPNDRAVDQIRPIKITRNYTAYAEGSVLVEFGNTKVLCNATVE-----ENVPrwlkGQGKGWVTAEYgmLPRAThtrnrR 76
Cdd:cd11365 17 RIDGRGLDEYRDIEIETGVIPKAEGSALVKLGNTQVLAGVKLEvgepfPDTP----NEGVLIVNAEL--LPLAS-----P 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 77 EAASGKQGGRTMEIQRLIARSLRA--VVDLK----VMGE--IMITVDCDVIQADGGTRTASISGASVAMADA-------- 140
Cdd:cd11365 86 TFEPGPPDENAIELARVVDRGIREskAIDLEklviEPGKkvWVVFIDIYVLDYDGNLFDASALAAVAALLNTkvpeyevd 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 141 -INSLLASGKLKKNPMKGHVAAVSVGIVGAQALCDLEYVEDSAADTDMNVVMTEDGKMIEIQGTAEGePFSHEELMQLLA 219
Cdd:cd11365 166 eNEVIEVLGEELPLPVNTLPVSVTVAKIGGYIVVDPTLEEELVMDARITITIDEDGNIVALQKGGGG-SFTEDEIDKAID 244
|
250
....*....|..
gi 490873725 220 LANKGITDIVEA 231
Cdd:cd11365 245 IALEKAAELREK 256
|
|
| RNase_PH_MTR3 |
cd11371 |
MTR3 subunit of eukaryotic exosome; The MTR3 subunit of eukaryotic exosome is a member of the ... |
24-238 |
1.32e-14 |
|
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: 69.90 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 24 AEGSVLVEFGNTKVLCNATVEENVPRWLKGQGKGWVTAEYGMLPRATHTRNRReaasgKQGGRTMEIQRLIARSLRAVVD 103
Cdd:cd11371 14 AKGSAYVELGNTKVICSVYGPRPIPGRTEFSDRGRLNCEVKFAPFATPGRRRH-----GQDSEERELSSLLHQALEPAVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 104 LKVMGEIMITVDCDVIQADGGTRTASISGASVAMADA-InsllasgklkknPMKGHVAAVSVGIVGAQALCDLEYVEDSA 182
Cdd:cd11371 89 LEKYPKSQIDVFVTVLESDGSVLAAAITAASLALADAgI------------EMYDLVTACSAALIGDELLLDPTREEEEA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490873725 183 ADTDMNV-VMTEDGKMIEIqgTAEGEpFSHEELMQLLALANKGITDIVEAQKAALAD 238
Cdd:cd11371 157 SSGGVMLaYMPSLNQVTQL--WQSGE-MDVDQLEEALDLCIDGCNRIHPVVRQALLE 210
|
|
| RNase_PH_C |
pfam03725 |
3' exoribonuclease family, domain 2; This family includes 3'-5' exoribonucleases. Ribonuclease ... |
159-224 |
3.09e-11 |
|
3' exoribonuclease family, domain 2; 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, Swiss:P46948 Swiss:Q12277 and Swiss:P25359 contain a copy of this domain. Swiss:Q10205, a hypothetical protein from S. pombe appears to belong to an uncharacterized subfamily. This subfamily is found in both eukaryotes and archaebacteria.
Pssm-ID: 427466 [Multi-domain] Cd Length: 67 Bit Score: 57.20 E-value: 3.09e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490873725 159 VAAVSVGIVGAQALCDLEYVEDSAADTDMNVVMTEDGKMIEIQGTAEGePFSHEELMQLLALANKG 224
Cdd:pfam03725 3 VAAVTVGKIDGQLVVDPTLEEESLSDSDLTVAVAGTGEIVALMKEGGA-GLTEDELLEALELAKEA 67
|
|
| RNase_PH_PNPase_1 |
cd11363 |
Polyribonucleotide nucleotidyltransferase, repeat 1; Polyribonucleotide nucleotidyltransferase ... |
24-237 |
5.52e-09 |
|
Polyribonucleotide nucleotidyltransferase, repeat 1; Polyribonucleotide nucleotidyltransferase (PNPase) 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. In the case of PNPase the complex is a trimer, since each monomer contains two tandem copies of the domain. PNPase is involved in mRNA degradation in a 3'-5' direction and in quality control of ribosomal RNA precursors. It is part of the RNA degradosome complex and binds to the scaffolding domain of the endoribonuclease RNase E.
Pssm-ID: 206768 [Multi-domain] Cd Length: 229 Bit Score: 54.45 E-value: 5.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 24 AEGSVLVEFGNTKVLCNATVEENVPrwlKGQGKGWVTAEY-------GMLPratHTRNRREaasGKQGGRTMEIQRLIAR 96
Cdd:cd11363 23 ADGSVVVQYGDTVVLVTAVSSKKPK---EGIDFFPLTVDYreklyaaGKIP---GGFFKRE---GRPSEKEILTSRLIDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 97 SLRAVVDLKVMGEIMITvdCDVIQADGG--TRTASISGASVAMAdainsllasgkLKKNPMKGHVAAVSVGIVGAQALCD 174
Cdd:cd11363 94 PIRPLFPKGFRNEVQVI--ATVLSVDGVndPDVLAINGASAALS-----------LSDIPFNGPVGAVRVGRIDGEFVVN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490873725 175 LEYVEDSAADTDMNVVMTEDG-KMIEiqgtAEGEPFSHEELMQLLALANKGITDIVEAQKAALA 237
Cdd:cd11363 161 PTREELEESDLDLVVAGTKDAvLMVE----AGAKEVSEEDMLEAIKFGHEAIQQLIAAQEELAA 220
|
|
| RNase_PH_RRP46 |
cd11372 |
RRP46 subunit of eukaryotic exosome; The RRP46 subunit of eukaryotic exosome is a member of ... |
11-230 |
1.12e-08 |
|
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: 53.34 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 11 IRPIKITRNYTAYAEGSVLVEFGNTKVLCNATveenvprwlkgqGKGWVTAEYGMLPRATHTRNRReAASGKQGGRTMEI 90
Cdd:cd11372 1 LRPLSCELGLLSRADGSARFSQGDTSVLAAVY------------GPIEVKLRKELPDRATLEVIVR-PKSGLPGVKEKLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 91 QRLIARSLRAVVDLKVMGEIMITVDCDVIQADGGTRTASISGASVAMADA-InsllasgklkknPMKGHVAAVSVGIVG- 168
Cdd:cd11372 68 ELLLRSTLEPIILLHLHPRTLISVVLQVLQDDGSLLACAINAACLALLDAgV------------PMKGLFAAVTCAITEd 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490873725 169 ------------AQALCDLEYVEDSAADTdmNVVMTEdgkmieiqgtAEGePFSHEELMQLLALANKGITDIVE 230
Cdd:cd11372 136 geiildptaeeeKEAKAVATFAFDSGEEK--NLVLSE----------SEG-SFTEEELFACLELAQAASAAIFD 196
|
|
| RNase_PH_PNPase_2 |
cd11364 |
Polyribonucleotide nucleotidyltransferase, repeat 2; Polyribonucleotide nucleotidyltransferase ... |
10-237 |
1.19e-08 |
|
Polyribonucleotide nucleotidyltransferase, repeat 2; Polyribonucleotide nucleotidyltransferase (PNPase) 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. In the case of PNPase the complex is a trimer, since each monomer contains two tandem copies of the domain. PNPase is involved in mRNA degradation in a 3'-5' direction and in quality control of ribosomal RNA precursors, with the second repeat containing the active site. PNPase is part of the RNA degradosome complex and binds to the scaffolding domain of the endoribonuclease RNase E.
Pssm-ID: 206769 [Multi-domain] Cd Length: 223 Bit Score: 53.70 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 10 QIRPIKITRNYTAYAEGSVLVEFGNTKVLCNATV----EENVPRWLKGQGKGWVTAEYGMLPRAT-HTR-----NRREAA 79
Cdd:cd11364 1 EIRPISCEVGLLPRTHGSALFTRGETQVLCTVTLgtleDAQKIDSLGGEKSKRFMLHYNFPPYSVgETGrvggpGRREIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 80 SGkqggrtmeiqRLIARSLRAVVDLKVMGEIMITVDCDVIQADGGTRTASISGASVAMADAinsllasGKlkknPMKGHV 159
Cdd:cd11364 81 HG----------ALAERALLPVLPSPEDFPYTIRVVSEVLESNGSSSMASVCGGSLALMDA-------GV----PIKAPV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 160 AAVSVGIVGAQA-----LCDLEYVEDSAADTDMNVVMTEDG----KM-IEIQGtaegepFSHEELMQLLALANKGITDIV 229
Cdd:cd11364 140 AGIAMGLITEGIddyrvLTDILGLEDHLGDMDFKVAGTRDGitalQMdIKIPG------ITLEIMREALQQAKEGRLHIL 213
|
....*...
gi 490873725 230 EAQKAALA 237
Cdd:cd11364 214 DIMEKAIS 221
|
|
| PLN00207 |
PLN00207 |
polyribonucleotide nucleotidyltransferase; Provisional |
2-195 |
3.26e-07 |
|
polyribonucleotide nucleotidyltransferase; Provisional
Pssm-ID: 215104 [Multi-domain] Cd Length: 891 Bit Score: 50.66 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 2 RPNDRAVDQIRPIKITRNYTAYAEGSVLVEFGNTKVLCNATVEEnvpRWLKGQGKGWVTAE--------YGMLPRATHTR 73
Cdd:PLN00207 439 RSDGRTPDEIRPINSSCGLLPRAHGSALFTRGETQALAVVTLGD---KQMAQRIDNLVDADevkrfylqYSFPPSCVGEV 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 74 NRREAASGKQGGRTMeiqrLIARSLRAVVDLKVMGEIMITVDCDVIQADGGTRTASISGASVAMADAinsllasgklkKN 153
Cdd:PLN00207 516 GRIGAPSRREIGHGM----LAERALEPILPSEDDFPYTIRVESTITESNGSSSMASVCGGCLALQDA-----------GV 580
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490873725 154 PMKGHVAAVSVGIV----------GAQALCDLEYVEDSAADTDMNVVMTEDG 195
Cdd:PLN00207 581 PVKCPIAGIAMGMVldteefggdgSPLILSDITGSEDASGDMDFKVAGNEDG 632
|
|
| RNase_PH_RRP45 |
cd11368 |
RRP45 subunit of eukaryotic exosome; The RRP45 subunit of eukaryotic exosome is a member of ... |
2-230 |
2.20e-06 |
|
RRP45 subunit of eukaryotic exosome; The RRP45 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: 206773 [Multi-domain] Cd Length: 259 Bit Score: 47.14 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 2 RPNDRAVDQIRPIKIT--RNYtayaeGSVLVEFGNTKVLCNATVEENVPRWLKG-QGKGWVTAEYGMLPRATHtrnrrea 78
Cdd:cd11368 18 RLDGRGLDEFRPIKITfgLEY-----GCVEVSLGKTRVLAQVSCEIVEPKPDRPnEGILFINVELSPMASPAF------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 79 ASGKQGGRTMEIQRLIARSLR--AVVDLK----VMGEI--MITVDCDVIQADGGtrtaSISGASVAmadAINSLLA---- 146
Cdd:cd11368 86 EPGRPSEEEVELSRLLERALRdsRAVDTEslciIAGEKvwSIRVDVHVLNHDGN----LIDAASLA---AIAALMHfrrp 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 147 -----SGKLKKNPMKGHVA----------AVSVGIV--GAQALCDLEYVEDSAADTDMNVVMTEDGKMIEIQgTAEGEPF 209
Cdd:cd11368 159 dvtvdGEEVTVHSPEEREPvplsihhipiCVTFAFFddGEIVVVDPTLLEEAVADGSLTVALNKHREICALS-KSGGAPL 237
|
250 260
....*....|....*....|.
gi 490873725 210 SHEELMQLLALANKGITDIVE 230
Cdd:cd11368 238 SPSQILRCVKIAAAKAKELTE 258
|
|
| RNase_PH_RRP43 |
cd11369 |
RRP43 subunit of eukaryotic exosome; The RRP43 subunit of eukaryotic exosome is a member of ... |
2-223 |
9.16e-05 |
|
RRP43 subunit of eukaryotic exosome; The RRP43 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: 206774 [Multi-domain] Cd Length: 261 Bit Score: 42.54 E-value: 9.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 2 RPNDRAVDQIRPIKITRNYTAYAEGSVLVEFGNTKVLCNATVE-----ENVPRwlkgqgKGWVTAEYGMLPR-ATHTRnr 75
Cdd:cd11369 18 RPDGRELDEFRPTSVNVGSISTADGSALVKLGNTTVLCGIKAEvatpaADTPD------EGYLVPNVDLPPLcSSKFR-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 76 reaaSGKQGGRTMEIQRLIARSLR--AVVDLK----VMGEIMITVDCDV--IQADGGTRTASISGASVAMAD----AINS 143
Cdd:cd11369 90 ----PGPPSEEAQVLSSFLADILLnsNVLDLEqlciVPGKLAWVLYCDVycLDYDGNLLDAALLALVAALKNlrlpAVTI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490873725 144 LLASGKLKKNP-------MKGHVAAVSVGIVGAQA-LCDLEYVEDSAADTDMNVVMTEDGKMIEIQGtAEGEPFSHEELM 215
Cdd:cd11369 166 DEETELVVVNPeerrplnLKNLPVSTTFAVFDDKHlLADPTAEEELLASGLVTVVVDENGELCSVHK-PGGSPLSQAQLQ 244
|
....*...
gi 490873725 216 QLLALANK 223
Cdd:cd11369 245 ECIELAKK 252
|
|
| |
