|
Name |
Accession |
Description |
Interval |
E-value |
| Rph |
COG0689 |
Ribonuclease PH [Translation, ribosomal structure and biogenesis]; |
1-238 |
1.80e-180 |
|
Ribonuclease PH [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440453 [Multi-domain] Cd Length: 238 Bit Score: 494.55 E-value: 1.80e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 1 MRVDGRAHDQLRPVTITRNYIKHAEGSCLIEVGDTKVICTATLEDRVPPFMRGGGKGWITAEYSMLPRATATRNARESSK 80
Cdd:COG0689 1 MRPDGRAPDQLRPVKITRGFTKHAEGSVLIEFGDTKVLCTASVEEGVPPFLKGSGQGWVTAEYGMLPRATHTRNRREAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 81 GKVGGRTMEIQRLIGRALRSVVSLEAMGERTIWLDCDVIQADGGTRTASITGAYVAMVDAMQKLVDSGTWKQLPLNDFLA 160
Cdd:COG0689 81 GKQSGRTQEIQRLIGRSLRAVVDLKALGERTITIDCDVLQADGGTRTASITGAFVALADALNKLVEKGLLKENPLKDQVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1851129091 161 ATSVGVVGEEAVLDLNYKEDSTAIVDMNVVMTGKGKFVELQGTGEDAPFSPEQLQEMIALAKVGIDNLINSQKEALAD 238
Cdd:COG0689 161 AVSVGIVDGEPVLDLDYEEDSAAEVDMNVVMTGSGEFVEVQGTAEGAPFSREELDALLDLAEKGIAELIALQKEALGE 238
|
|
| rph |
PRK00173 |
ribonuclease PH; Reviewed |
1-238 |
6.37e-170 |
|
ribonuclease PH; Reviewed
Pssm-ID: 178914 Cd Length: 238 Bit Score: 468.05 E-value: 6.37e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 1 MRVDGRAHDQLRPVTITRNYIKHAEGSCLIEVGDTKVICTATLEDRVPPFMRGGGKGWITAEYSMLPRATATRNARESSK 80
Cdd:PRK00173 1 MRPDGRAADQLRPVTITRNFTKHAEGSVLVEFGDTKVLCTASVEEGVPRFLKGQGQGWVTAEYGMLPRATHTRNDREAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 81 GKVGGRTMEIQRLIGRALRSVVSLEAMGERTIWLDCDVIQADGGTRTASITGAYVAMVDAMQKLVDSGTWKQLPLNDFLA 160
Cdd:PRK00173 81 GKQGGRTQEIQRLIGRSLRAVVDLKALGERTITIDCDVIQADGGTRTASITGAYVALADALNKLVARGKLKKNPLKDQVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1851129091 161 ATSVGVVGEEAVLDLNYKEDSTAIVDMNVVMTGKGKFVELQGTGEDAPFSPEQLQEMIALAKVGIDNLINSQKEALAD 238
Cdd:PRK00173 161 AVSVGIVDGEPVLDLDYEEDSAAETDMNVVMTGSGGFVEVQGTAEGAPFSREELDALLDLAEKGIAELVALQKAALAD 238
|
|
| RNase_PH_bact |
cd11362 |
Ribonuclease PH; Ribonuclease PH (RNase PH)-like 3'-5' exoribonucleases are enzymes that ... |
10-236 |
4.75e-149 |
|
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: 414.70 E-value: 4.75e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 10 QLRPVTITRNYIKHAEGSCLIEVGDTKVICTATLEDRVPPFMRGGGKGWITAEYSMLPRATATRNARESSKGKVGGRTME 89
Cdd:cd11362 1 QLRPISITRGFNKHAEGSVLIEFGDTKVLCTASVEEKVPPFLRGKGKGWVTAEYSMLPRSTHERTQREASKGKQSGRTQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 90 IQRLIGRALRSVVSLEAMGERTIWLDCDVIQADGGTRTASITGAYVAMVDAMQKLVDSGTWKQLPLNDFLAATSVGVVGE 169
Cdd:cd11362 81 IQRLIGRSLRAAVDLEALGERTITIDCDVLQADGGTRTASITGAYVALADAVDKLVEKGVLEENPLKHFVAAVSVGIVDG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1851129091 170 EAVLDLNYKEDSTAIVDMNVVMTGKGKFVELQGTGEDAPFSPEQLQEMIALAKVGIDNLINSQKEAL 236
Cdd:cd11362 161 EPLLDLDYEEDSAADVDMNVVMTGSGRFVEVQGTGEEAPFSRDELNELLDLAEKGIQELIELQKEAL 227
|
|
| RNasePH |
TIGR01966 |
ribonuclease PH; This bacterial enzyme, ribonuclease PH, performs the final 3'-trimming and ... |
2-237 |
7.60e-147 |
|
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: 409.83 E-value: 7.60e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 2 RVDGRAHDQLRPVTITRNYIKHAEGSCLIEVGDTKVICTATLEDRVPPFMRGGGKGWITAEYSMLPRATATRNARESSKG 81
Cdd:TIGR01966 1 RPDGRKPDQLRPVSITRDFLKHAEGSVLIEFGNTKVLCTASVEEKVPPFLRGSGEGWITAEYGMLPRATQTRNRRESAKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 82 KVGGRTMEIQRLIGRALRSVVSLEAMGERTIWLDCDVIQADGGTRTASITGAYVAMVDAMQKLVDSGTWKQLPLNDFLAA 161
Cdd:TIGR01966 81 KQSGRTQEIQRLIGRALRAVVDLEALGERTIWIDCDVIQADGGTRTASITGAFVALADAISKLHKRGILKESPIRDFVAA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1851129091 162 TSVGVVGEEAVLDLNYKEDSTAIVDMNVVMTGKGKFVELQGTGEDAPFSPEQLQEMIALAKVGIDNLINSQKEALA 237
Cdd:TIGR01966 161 VSVGIVDGEPVLDLDYEEDSAADVDMNVVMTGSGGFVEVQGTAEEGPFSRDELNKLLDLAKKGIRELIELQKQALG 236
|
|
| RNase_PH |
pfam01138 |
3' exoribonuclease family, domain 1; This family includes 3'-5' exoribonucleases. Ribonuclease ... |
10-140 |
6.71e-36 |
|
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: 124.24 E-value: 6.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 10 QLRPVTITRNYIKHAEGSCLIEVGDTKVICTATLEdRVPPFMRGGGKGWITAEYSMLPRATATRNAResskGKVGGRTME 89
Cdd:pfam01138 1 ELRPIEIETGVLSQADGSALVELGDTKVLATVTGP-IEPKEDRDFAPGRLTVEYELAPFASGERPGE----GRPSEREIE 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1851129091 90 IQRLIGRALRSVVSLEAMGERTIWLDCDVIQADGGTRTASITGAYVAMVDA 140
Cdd:pfam01138 76 ISRLIDRALRPSIPLEGYPRWTIRIDVTVLSSDGSLLDAAINAASLALADA 126
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Rph |
COG0689 |
Ribonuclease PH [Translation, ribosomal structure and biogenesis]; |
1-238 |
1.80e-180 |
|
Ribonuclease PH [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440453 [Multi-domain] Cd Length: 238 Bit Score: 494.55 E-value: 1.80e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 1 MRVDGRAHDQLRPVTITRNYIKHAEGSCLIEVGDTKVICTATLEDRVPPFMRGGGKGWITAEYSMLPRATATRNARESSK 80
Cdd:COG0689 1 MRPDGRAPDQLRPVKITRGFTKHAEGSVLIEFGDTKVLCTASVEEGVPPFLKGSGQGWVTAEYGMLPRATHTRNRREAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 81 GKVGGRTMEIQRLIGRALRSVVSLEAMGERTIWLDCDVIQADGGTRTASITGAYVAMVDAMQKLVDSGTWKQLPLNDFLA 160
Cdd:COG0689 81 GKQSGRTQEIQRLIGRSLRAVVDLKALGERTITIDCDVLQADGGTRTASITGAFVALADALNKLVEKGLLKENPLKDQVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1851129091 161 ATSVGVVGEEAVLDLNYKEDSTAIVDMNVVMTGKGKFVELQGTGEDAPFSPEQLQEMIALAKVGIDNLINSQKEALAD 238
Cdd:COG0689 161 AVSVGIVDGEPVLDLDYEEDSAAEVDMNVVMTGSGEFVEVQGTAEGAPFSREELDALLDLAEKGIAELIALQKEALGE 238
|
|
| rph |
PRK00173 |
ribonuclease PH; Reviewed |
1-238 |
6.37e-170 |
|
ribonuclease PH; Reviewed
Pssm-ID: 178914 Cd Length: 238 Bit Score: 468.05 E-value: 6.37e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 1 MRVDGRAHDQLRPVTITRNYIKHAEGSCLIEVGDTKVICTATLEDRVPPFMRGGGKGWITAEYSMLPRATATRNARESSK 80
Cdd:PRK00173 1 MRPDGRAADQLRPVTITRNFTKHAEGSVLVEFGDTKVLCTASVEEGVPRFLKGQGQGWVTAEYGMLPRATHTRNDREAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 81 GKVGGRTMEIQRLIGRALRSVVSLEAMGERTIWLDCDVIQADGGTRTASITGAYVAMVDAMQKLVDSGTWKQLPLNDFLA 160
Cdd:PRK00173 81 GKQGGRTQEIQRLIGRSLRAVVDLKALGERTITIDCDVIQADGGTRTASITGAYVALADALNKLVARGKLKKNPLKDQVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1851129091 161 ATSVGVVGEEAVLDLNYKEDSTAIVDMNVVMTGKGKFVELQGTGEDAPFSPEQLQEMIALAKVGIDNLINSQKEALAD 238
Cdd:PRK00173 161 AVSVGIVDGEPVLDLDYEEDSAAETDMNVVMTGSGGFVEVQGTAEGAPFSREELDALLDLAEKGIAELVALQKAALAD 238
|
|
| RNase_PH_bact |
cd11362 |
Ribonuclease PH; Ribonuclease PH (RNase PH)-like 3'-5' exoribonucleases are enzymes that ... |
10-236 |
4.75e-149 |
|
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: 414.70 E-value: 4.75e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 10 QLRPVTITRNYIKHAEGSCLIEVGDTKVICTATLEDRVPPFMRGGGKGWITAEYSMLPRATATRNARESSKGKVGGRTME 89
Cdd:cd11362 1 QLRPISITRGFNKHAEGSVLIEFGDTKVLCTASVEEKVPPFLRGKGKGWVTAEYSMLPRSTHERTQREASKGKQSGRTQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 90 IQRLIGRALRSVVSLEAMGERTIWLDCDVIQADGGTRTASITGAYVAMVDAMQKLVDSGTWKQLPLNDFLAATSVGVVGE 169
Cdd:cd11362 81 IQRLIGRSLRAAVDLEALGERTITIDCDVLQADGGTRTASITGAYVALADAVDKLVEKGVLEENPLKHFVAAVSVGIVDG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1851129091 170 EAVLDLNYKEDSTAIVDMNVVMTGKGKFVELQGTGEDAPFSPEQLQEMIALAKVGIDNLINSQKEAL 236
Cdd:cd11362 161 EPLLDLDYEEDSAADVDMNVVMTGSGRFVEVQGTGEEAPFSRDELNELLDLAEKGIQELIELQKEAL 227
|
|
| RNasePH |
TIGR01966 |
ribonuclease PH; This bacterial enzyme, ribonuclease PH, performs the final 3'-trimming and ... |
2-237 |
7.60e-147 |
|
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: 409.83 E-value: 7.60e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 2 RVDGRAHDQLRPVTITRNYIKHAEGSCLIEVGDTKVICTATLEDRVPPFMRGGGKGWITAEYSMLPRATATRNARESSKG 81
Cdd:TIGR01966 1 RPDGRKPDQLRPVSITRDFLKHAEGSVLIEFGNTKVLCTASVEEKVPPFLRGSGEGWITAEYGMLPRATQTRNRRESAKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 82 KVGGRTMEIQRLIGRALRSVVSLEAMGERTIWLDCDVIQADGGTRTASITGAYVAMVDAMQKLVDSGTWKQLPLNDFLAA 161
Cdd:TIGR01966 81 KQSGRTQEIQRLIGRALRAVVDLEALGERTIWIDCDVIQADGGTRTASITGAFVALADAISKLHKRGILKESPIRDFVAA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1851129091 162 TSVGVVGEEAVLDLNYKEDSTAIVDMNVVMTGKGKFVELQGTGEDAPFSPEQLQEMIALAKVGIDNLINSQKEALA 237
Cdd:TIGR01966 161 VSVGIVDGEPVLDLDYEEDSAADVDMNVVMTGSGGFVEVQGTAEEGPFSRDELNKLLDLAKKGIRELIELQKQALG 236
|
|
| RNase_PH |
cd11358 |
RNase PH-like 3'-5' exoribonucleases; RNase PH-like 3'-5' exoribonucleases are enzymes that ... |
11-228 |
1.76e-45 |
|
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: 151.71 E-value: 1.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 11 LRPVTITRNYIKHAEGSCLIEVGDTKVICTATLEDRVPPFMRGGGKGWITAEYSMLPRATatrnaRESSKGKVGGRTMEI 90
Cdd:cd11358 1 FRPVEIETGVLNQADGSALVKLGNTKVICAVTGPIVEPDKLERPDKGTLYVNVEISPGAV-----GERRQGPPGDEEMEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 91 QRLIGRALRSVVSLEAMGE---RTIWLDCDVIQADGGTRTASITGAYVAMVDAMQKLV--DSGTWKQLPLNDFLAATSVG 165
Cdd:cd11358 76 SRLLERTIEASVILDKSTRkpsWVLYVDIQVLSRDGGLLDACWNAAIAALKDAGIPRVfvDERSPPLLLMKDLIVAVSVG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1851129091 166 VV-GEEAVLDLNYKEDSTAIVDMNVVMTGKGKFVELQGTGEDAPFsPEQLQEMIALAKVGIDNL 228
Cdd:cd11358 156 GIsDGVLLLDPTGEEEELADSTLTVAVDKSGKLCLLSKVGGGSLD-TEEIKECLELAKKRSLHL 218
|
|
| PRK03983 |
PRK03983 |
exosome complex exonuclease Rrp41; Provisional |
1-248 |
9.11e-43 |
|
exosome complex exonuclease Rrp41; Provisional
Pssm-ID: 235187 [Multi-domain] Cd Length: 244 Bit Score: 145.55 E-value: 9.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 1 MRVDGRAHDQLRPVTITRNYIKHAEGSCLIEVGDTKVIcTATLEDRV--PPFMRGGGKGWITAEYSMLPRATATRNARES 78
Cdd:PRK03983 14 LRLDGRKPDELRPIKIEVGVLKNADGSAYLEWGNNKII-AAVYGPREmhPRHLQLPDRAVLRVRYNMAPFSVDERKRPGP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 79 SKgkvggRTMEIQRLIGRALRSVVSLEAMGERTIWLDCDVIQADGGTRTASITGAYVAMVDAmqklvdsgtwkQLPLNDF 158
Cdd:PRK03983 93 DR-----RSIEISKVIREALEPAIMLELFPRTVIDVFIEVLQADAGTRVAGITAASLALADA-----------GIPMRDL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 159 LAATSVGVVGEEAVLDLNYKEDSTAIVDMNV-VMTGKGKFVELQgtgEDAPFSPEQLQEMIALAKVGIDNLINSQKEALA 237
Cdd:PRK03983 157 VAGCAVGKVDGVIVLDLNKEEDNYGEADMPVaIMPRLGEITLLQ---LDGNLTREEFLEALELAKKGIKRIYQLQREALK 233
|
250
....*....|.
gi 1851129091 238 DVTLSFAQSVA 248
Cdd:PRK03983 234 SKYGEIAEEGE 244
|
|
| RNase_PH_archRRP41 |
cd11366 |
RRP41 subunit of archaeal exosome; The RRP41 subunit of the archaeal exosome is a member of ... |
10-238 |
1.93e-37 |
|
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: 130.92 E-value: 1.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 10 QLRPVTITRNYIKHAEGSCLIEVGDTKVICTATL-EDRVPPFMRGGGKGWITAEYSMLPRATATRNARESSKgkvggRTM 88
Cdd:cd11366 1 ELRPIKIEVGVLKNADGSAYVEWGNNKIIAAVYGpREVHPRHLQLPDRAVIRVRYNMAPFSVDERKRPGPDR-----REI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 89 EIQRLIGRALRSVVSLEAMGERTIWLDCDVIQADGGTRTASITGAYVAMVDAmqklvdsgtwkQLPLNDFLAATSVGVVG 168
Cdd:cd11366 76 EISKVIKEALEPAIILEEFPRTAIDVFVEVLQADAGTRVAGLNAASLALADA-----------GIPMRDLVAACAAGKVD 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1851129091 169 EEAVLDLNYKEDSTAIVDMNVVMT-GKGKFVELQgtgEDAPFSPEQLQEMIALAKVGIDNLINSQKEALAD 238
Cdd:cd11366 145 GKIVLDLNKEEDNYGEADMPIAMMpNLGEITLLQ---LDGDLTPDEFKQAIELAKKGCKRIYELQKEALKR 212
|
|
| RNase_PH |
pfam01138 |
3' exoribonuclease family, domain 1; This family includes 3'-5' exoribonucleases. Ribonuclease ... |
10-140 |
6.71e-36 |
|
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: 124.24 E-value: 6.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 10 QLRPVTITRNYIKHAEGSCLIEVGDTKVICTATLEdRVPPFMRGGGKGWITAEYSMLPRATATRNAResskGKVGGRTME 89
Cdd:pfam01138 1 ELRPIEIETGVLSQADGSALVELGDTKVLATVTGP-IEPKEDRDFAPGRLTVEYELAPFASGERPGE----GRPSEREIE 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1851129091 90 IQRLIGRALRSVVSLEAMGERTIWLDCDVIQADGGTRTASITGAYVAMVDA 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 ... |
2-224 |
6.06e-28 |
|
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: 106.47 E-value: 6.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 2 RVDGRAHDQLRPVTITRNYIKHAEGSCLIEVGDTKVICTAT--LEDRVPPfMRGGGKGWITAEYSMLPRATATRNARess 79
Cdd:cd11370 3 RLDGRRPNELRRIRCRIGVFSSADGSAYLEQGNTKVLAAVYgpHEPRNRS-QALHDRAVVNCEYSMATFSTGERKRR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 80 kGKVGGRTMEIQRLIGRALRSVVSLEAMGERTIWLDCDVIQADGGTRTASITGAYVAMVDAmqklvdsGtwkqLPLNDFL 159
Cdd:cd11370 79 -GKGDRRSTELSLAIRQTFEAVILTHLYPRSQIDIYVQVLQADGGLLAACINAATLALIDA-------G----IPMKDYV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1851129091 160 AATSVGVVGEEAVLDLNYKEDSTAIVDMNV-VMTGKGKFVELQGtgeDAPFSPEQLQEMIALAKVG 224
Cdd:cd11370 147 CACSAGYLDSTPLLDLNYLEESGDLPDLTVaVLPKSDKVVLLQM---ESRLHLDRLEKVLELAIEG 209
|
|
| PRK04282 |
PRK04282 |
exosome complex protein Rrp42; |
2-237 |
1.75e-25 |
|
exosome complex protein Rrp42;
Pssm-ID: 235268 [Multi-domain] Cd Length: 271 Bit Score: 101.11 E-value: 1.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 2 RVDGRAHDQLRPVTITRNYIKHAEGSCLIEVGDTKVICTATLEDrVPPFMRGGGKGWITAEYSMLPRATATRNAresskG 81
Cdd:PRK04282 25 RIDGRKLDEYRPIEIETGVIKKAEGSALVKLGNTQVLAGVKLEI-GEPFPDTPNEGVLIVNAELLPLASPTFEP-----G 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 82 KVGGRTMEIQRLIGRALRS--VVSLEAM----GE--RTIWLDCDVIQADGGTRTASITGAYVAMVDAM---------QKL 144
Cdd:PRK04282 99 PPDENAIELARVVDRGIREskAIDLEKLviepGKkvWVVFIDVYVLDHDGNLLDASMLAAVAALLNTKvpaveegedGVV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 145 VDSGTWKQLPLNDFLAATSVGVVGEEAVLDLNYKEDSTAIVDMNVVMTGKGKFVELQGTGEdAPFSPEQLQEMIALAKVG 224
Cdd:PRK04282 179 DKLGEDFPLPVNDKPVTVTFAKIGNYLIVDPTLEEESVMDARITITTDEDGNIVAIQKSGI-GSFTEEEVDKAIDIALEK 257
|
250
....*....|...
gi 1851129091 225 IDNLINSQKEALA 237
Cdd:PRK04282 258 AKELREKLKEALG 270
|
|
| RNase_PH_archRRP42 |
cd11365 |
RRP42 subunit of archaeal exosome; The RRP42 subunit of the archaeal exosome is a member of ... |
2-221 |
1.88e-22 |
|
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: 92.67 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 2 RVDGRAHDQLRPVTITRNYIKHAEGSCLIEVGDTKVICTATLEDRVpPFMRGGGKGWITAEYSMLPRATATrnaRESskG 81
Cdd:cd11365 17 RIDGRGLDEYRDIEIETGVIPKAEGSALVKLGNTQVLAGVKLEVGE-PFPDTPNEGVLIVNAELLPLASPT---FEP--G 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 82 KVGGRTMEIQRLIGRALRS--VVSLEAM----GER--TIWLDCDVIQADGGTRTASITGAYVAMVDAM---------QKL 144
Cdd:cd11365 91 PPDENAIELARVVDRGIREskAIDLEKLviepGKKvwVVFIDIYVLDYDGNLFDASALAAVAALLNTKvpeyevdenEVI 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1851129091 145 VDSGTWKQLPLNDFLAATSVGVVGEEAVLDLNYKEDSTAIVDMNVVMTGKGKFVELQgTGEDAPFSPEQLQEMIALA 221
Cdd:cd11365 171 EVLGEELPLPVNTLPVSVTVAKIGGYIVVDPTLEEELVMDARITITIDEDGNIVALQ-KGGGGSFTEDEIDKAIDIA 246
|
|
| RNase_PH_C |
pfam03725 |
3' exoribonuclease family, domain 2; This family includes 3'-5' exoribonucleases. Ribonuclease ... |
157-224 |
6.26e-14 |
|
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: 64.91 E-value: 6.26e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1851129091 157 DFLAATSVGVVGEEAVLDLNYKEDSTAIVDMNVVMTGKGKFVELQGTGEdAPFSPEQLQEMIALAKVG 224
Cdd:pfam03725 1 DPVAAVTVGKIDGQLVVDPTLEEESLSDSDLTVAVAGTGEIVALMKEGG-AGLTEDELLEALELAKEA 67
|
|
| RNase_PH_MTR3 |
cd11371 |
MTR3 subunit of eukaryotic exosome; The MTR3 subunit of eukaryotic exosome is a member of the ... |
21-238 |
4.70e-13 |
|
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: 66.05 E-value: 4.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 21 IKHAEGSCLIEVGDTKVICTATLEDRVPPFMRGGGKGWITAEYSMLPRATATRnaRESSKgkvGGRTMEIQRLIGRALRS 100
Cdd:cd11371 11 VSQAKGSAYVELGNTKVICSVYGPRPIPGRTEFSDRGRLNCEVKFAPFATPGR--RRHGQ---DSEERELSSLLHQALEP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 101 VVSLEAMGERTIWLDCDVIQADGGTRTASITGAYVAmvdamqkLVDSGtwkqLPLNDFLAATSVGVVGEEAVLDLNYKED 180
Cdd:cd11371 86 AVRLEKYPKSQIDVFVTVLESDGSVLAAAITAASLA-------LADAG----IEMYDLVTACSAALIGDELLLDPTREEE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1851129091 181 STAIVDMNV-VMTGKGKFVELQGTGEdapFSPEQLQEMIALAKVGIDNLINSQKEALAD 238
Cdd:cd11371 155 EASSGGVMLaYMPSLNQVTQLWQSGE---MDVDQLEEALDLCIDGCNRIHPVVRQALLE 210
|
|
| RNase_PH_RRP43 |
cd11369 |
RRP43 subunit of eukaryotic exosome; The RRP43 subunit of eukaryotic exosome is a member of ... |
2-223 |
5.07e-13 |
|
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: 66.81 E-value: 5.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 2 RVDGRAHDQLRPVTITRNYIKHAEGSCLIEVGDTKVICTATLEDRVPPFMRgGGKGWITAEYSMLPRAtatrnareSSKG 81
Cdd:cd11369 18 RPDGRELDEFRPTSVNVGSISTADGSALVKLGNTTVLCGIKAEVATPAADT-PDEGYLVPNVDLPPLC--------SSKF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 82 KVGGRTMEIQRL---IGRALRS--VVSLEAM---GERTIW-LDCDV--IQADGGTRTASItgayVAMVDAMQKL------ 144
Cdd:cd11369 89 RPGPPSEEAQVLssfLADILLNsnVLDLEQLcivPGKLAWvLYCDVycLDYDGNLLDAAL----LALVAALKNLrlpavt 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 145 ---------VDSGTWKQLPLNDFLAATSVGVVGEEAVL-DLNYKEDSTAIVDMNVVMTGKGKFVELQGTGeDAPFSPEQL 214
Cdd:cd11369 165 ideetelvvVNPEERRPLNLKNLPVSTTFAVFDDKHLLaDPTAEEELLASGLVTVVVDENGELCSVHKPG-GSPLSQAQL 243
|
....*....
gi 1851129091 215 QEMIALAKV 223
Cdd:cd11369 244 QECIELAKK 252
|
|
| RNase_PH_RRP42 |
cd11367 |
RRP42 subunit of eukaryotic exosome; The RRP42 subunit of eukaryotic exosome is a member of ... |
1-237 |
8.25e-08 |
|
RRP42 subunit of eukaryotic exosome; The RRP42 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: 206772 [Multi-domain] Cd Length: 272 Bit Score: 51.83 E-value: 8.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 1 MRVDGRAHDQLRPVTITRNYIKHAEGSCLIEVGDTKVICTATLEDRVPPFMRgGGKGWITAEYSMLPRATATRNARessk 80
Cdd:cd11367 18 IRNDGRSRLDYRPIELETGVLSNTNGSARVRLGNTDVLVGVKAEVGSPDPET-PNKGRLEFFVDCSPNASPEFEGR---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 81 gkvGG--RTMEIQRLIGRALRSVVSLEA-----MGERTIW---LDCDVIQADGGTRTASITGAYVAM-------VDAMQk 143
Cdd:cd11367 93 ---GGeeLATELSSALERALKSGSAIDLsklciVPGKQCWvlyVDVLVLESGGNLLDAISIAVKAALfntripkVEVSE- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 144 lVDSGT-----------WKQLPLNDFLAATSVGVVGEEAVLDLNYKEDSTAIVDMNVVMTGKGKFVELQGTGEDApFSPE 212
Cdd:cd11367 169 -DDEGTkeielsddpydVKRLDVSNVPLIVTLSKIGNRHIVDATAEEEACSSARLLVAVNAKGRICGVQKSGGGS-LEPE 246
|
250 260
....*....|....*....|....*
gi 1851129091 213 QLQEMIALAKVGIDNLINSQKEALA 237
Cdd:cd11367 247 SIIEMIETAKEVGKKLNAALDKALK 271
|
|
| RNase_PH_RRP45 |
cd11368 |
RRP45 subunit of eukaryotic exosome; The RRP45 subunit of eukaryotic exosome is a member of ... |
2-123 |
2.02e-07 |
|
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: 50.60 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 2 RVDGRAHDQLRPVTIT--RNYikhaeGSCLIEVGDTKVIC--TATLedrVPPFMRGGGKG--WITAEYS-MLPRATATRN 74
Cdd:cd11368 18 RLDGRGLDEFRPIKITfgLEY-----GCVEVSLGKTRVLAqvSCEI---VEPKPDRPNEGilFINVELSpMASPAFEPGR 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1851129091 75 ARESSkgkvggrtMEIQRLIGRALRS--VVSLEAM----GERtIW---LDCDVIQADG 123
Cdd:cd11368 90 PSEEE--------VELSRLLERALRDsrAVDTESLciiaGEK-VWsirVDVHVLNHDG 138
|
|
| RNase_PH_RRP46 |
cd11372 |
RRP46 subunit of eukaryotic exosome; The RRP46 subunit of eukaryotic exosome is a member of ... |
11-222 |
1.33e-06 |
|
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: 47.56 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 11 LRPVTITRNYIKHAEGSCLIEVGDTKVICTATledrvppfmrggGKGWITAEYSMLPRATATRNAR-ESSKGKVGGRTME 89
Cdd:cd11372 1 LRPLSCELGLLSRADGSARFSQGDTSVLAAVY------------GPIEVKLRKELPDRATLEVIVRpKSGLPGVKEKLLE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851129091 90 iqRLIGRALRSVVSLEAMGERTIWLDCDVIQADGGTRTASITGAYVAmvdamqkLVDSGtwkqLPLNDFLAATSVGVVGE 169
Cdd:cd11372 69 --LLLRSTLEPIILLHLHPRTLISVVLQVLQDDGSLLACAINAACLA-------LLDAG----VPMKGLFAAVTCAITED 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1851129091 170 EAVL---DLNYKEDSTAIVdmNVVM--TGKGKFVELQGTGedaPFSPEQLQEMIALAK 222
Cdd:cd11372 136 GEIIldpTAEEEKEAKAVA--TFAFdsGEEKNLVLSESEG---SFTEEELFACLELAQ 188
|
|
| PRK11824 |
PRK11824 |
polynucleotide phosphorylase/polyadenylase; Provisional |
2-43 |
6.76e-05 |
|
polynucleotide phosphorylase/polyadenylase; Provisional
Pssm-ID: 236995 [Multi-domain] Cd Length: 693 Bit Score: 43.50 E-value: 6.76e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1851129091 2 RVDGRAHDQLRPVTITRNYIKHAEGSCLIEVGDTKVICTATL 43
Cdd:PRK11824 315 RIDGRKLDEIRPISIEVGVLPRTHGSALFTRGETQALVVATL 356
|
|
| |
