|
Name |
Accession |
Description |
Interval |
E-value |
| Rph |
COG0689 |
Ribonuclease PH [Translation, ribosomal structure and biogenesis]; |
1-237 |
0e+00 |
|
Ribonuclease PH [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440453 [Multi-domain] Cd Length: 238 Bit Score: 500.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 1 MRPNNRENHQPRQIKITRHYTKHAEGSVLVEFGDTKVLCTATVEDSVPRFLKGQNQGWVTAEYGMLPRSTHSRMQREAAK 80
Cdd:COG0689 1 MRPDGRAPDQLRPVKITRGFTKHAEGSVLIEFGDTKVLCTASVEEGVPPFLKGSGQGWVTAEYGMLPRATHTRNRREAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 81 GKQGGRTMEIQRLIARSLRAMVDLKALGERAITLDCDVIQADGGTRTAAITGAAVALCDAINALIENGTLKTNPIKGLVS 160
Cdd:COG0689 81 GKQSGRTQEIQRLIGRSLRAVVDLKALGERTITIDCDVLQADGGTRTASITGAFVALADALNKLVEKGLLKENPLKDQVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119207624 161 AISVGIVEGNAVCDLEYIEDSAAQTDMNVVMMEDGRMIEVQGTAEGEPFSHEELLTLLDLAKQGCYQIFVAQREALG 237
Cdd:COG0689 161 AVSVGIVDGEPVLDLDYEEDSAAEVDMNVVMTGSGEFVEVQGTAEGAPFSREELDALLDLAEKGIAELIALQKEALG 237
|
|
| rph |
PRK00173 |
ribonuclease PH; Reviewed |
1-237 |
2.61e-178 |
|
ribonuclease PH; Reviewed
Pssm-ID: 178914 Cd Length: 238 Bit Score: 488.46 E-value: 2.61e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 1 MRPNNRENHQPRQIKITRHYTKHAEGSVLVEFGDTKVLCTATVEDSVPRFLKGQNQGWVTAEYGMLPRSTHSRMQREAAK 80
Cdd:PRK00173 1 MRPDGRAADQLRPVTITRNFTKHAEGSVLVEFGDTKVLCTASVEEGVPRFLKGQGQGWVTAEYGMLPRATHTRNDREAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 81 GKQGGRTMEIQRLIARSLRAMVDLKALGERAITLDCDVIQADGGTRTAAITGAAVALCDAINALIENGTLKTNPIKGLVS 160
Cdd:PRK00173 81 GKQGGRTQEIQRLIGRSLRAVVDLKALGERTITIDCDVIQADGGTRTASITGAYVALADALNKLVARGKLKKNPLKDQVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119207624 161 AISVGIVEGNAVCDLEYIEDSAAQTDMNVVMMEDGRMIEVQGTAEGEPFSHEELLTLLDLAKQGCYQIFVAQREALG 237
Cdd:PRK00173 161 AVSVGIVDGEPVLDLDYEEDSAAETDMNVVMTGSGGFVEVQGTAEGAPFSREELDALLDLAEKGIAELVALQKAALA 237
|
|
| RNase_PH_bact |
cd11362 |
Ribonuclease PH; Ribonuclease PH (RNase PH)-like 3'-5' exoribonucleases are enzymes that ... |
10-236 |
4.37e-147 |
|
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: 409.31 E-value: 4.37e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 10 QPRQIKITRHYTKHAEGSVLVEFGDTKVLCTATVEDSVPRFLKGQNQGWVTAEYGMLPRSTHSRMQREAAKGKQGGRTME 89
Cdd:cd11362 1 QLRPISITRGFNKHAEGSVLIEFGDTKVLCTASVEEKVPPFLRGKGKGWVTAEYSMLPRSTHERTQREASKGKQSGRTQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 90 IQRLIARSLRAMVDLKALGERAITLDCDVIQADGGTRTAAITGAAVALCDAINALIENGTLKTNPIKGLVSAISVGIVEG 169
Cdd:cd11362 81 IQRLIGRSLRAAVDLEALGERTITIDCDVLQADGGTRTASITGAYVALADAVDKLVEKGVLEENPLKHFVAAVSVGIVDG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119207624 170 NAVCDLEYIEDSAAQTDMNVVMMEDGRMIEVQGTAEGEPFSHEELLTLLDLAKQGCYQIFVAQREAL 236
Cdd:cd11362 161 EPLLDLDYEEDSAADVDMNVVMTGSGRFVEVQGTGEEAPFSRDELNELLDLAEKGIQELIELQKEAL 227
|
|
| RNasePH |
TIGR01966 |
ribonuclease PH; This bacterial enzyme, ribonuclease PH, performs the final 3'-trimming and ... |
2-237 |
4.92e-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: 404.44 E-value: 4.92e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 2 RPNNRENHQPRQIKITRHYTKHAEGSVLVEFGDTKVLCTATVEDSVPRFLKGQNQGWVTAEYGMLPRSTHSRMQREAAKG 81
Cdd:TIGR01966 1 RPDGRKPDQLRPVSITRDFLKHAEGSVLIEFGNTKVLCTASVEEKVPPFLRGSGEGWITAEYGMLPRATQTRNRRESAKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 82 KQGGRTMEIQRLIARSLRAMVDLKALGERAITLDCDVIQADGGTRTAAITGAAVALCDAINALIENGTLKTNPIKGLVSA 161
Cdd:TIGR01966 81 KQSGRTQEIQRLIGRALRAVVDLEALGERTIWIDCDVIQADGGTRTASITGAFVALADAISKLHKRGILKESPIRDFVAA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119207624 162 ISVGIVEGNAVCDLEYIEDSAAQTDMNVVMMEDGRMIEVQGTAEGEPFSHEELLTLLDLAKQGCYQIFVAQREALG 237
Cdd:TIGR01966 161 VSVGIVDGEPVLDLDYEEDSAADVDMNVVMTGSGGFVEVQGTAEEGPFSRDELNKLLDLAKKGIRELIELQKQALG 236
|
|
| RNase_PH |
pfam01138 |
3' exoribonuclease family, domain 1; This family includes 3'-5' exoribonucleases. Ribonuclease ... |
10-140 |
3.29e-32 |
|
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: 114.23 E-value: 3.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 10 QPRQIKITRHYTKHAEGSVLVEFGDTKVLCTATVEdSVPRFLKGQNQGWVTAEYGMLPRSTHSRMQReaakGKQGGRTME 89
Cdd:pfam01138 1 ELRPIEIETGVLSQADGSALVELGDTKVLATVTGP-IEPKEDRDFAPGRLTVEYELAPFASGERPGE----GRPSEREIE 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2119207624 90 IQRLIARSLRAMVDLKALGERAITLDCDVIQADGGTRTAAITGAAVALCDA 140
Cdd:pfam01138 76 ISRLIDRALRPSIPLEGYPRWTIRIDVTVLSSDGSLLDAAINAASLALADA 126
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Rph |
COG0689 |
Ribonuclease PH [Translation, ribosomal structure and biogenesis]; |
1-237 |
0e+00 |
|
Ribonuclease PH [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440453 [Multi-domain] Cd Length: 238 Bit Score: 500.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 1 MRPNNRENHQPRQIKITRHYTKHAEGSVLVEFGDTKVLCTATVEDSVPRFLKGQNQGWVTAEYGMLPRSTHSRMQREAAK 80
Cdd:COG0689 1 MRPDGRAPDQLRPVKITRGFTKHAEGSVLIEFGDTKVLCTASVEEGVPPFLKGSGQGWVTAEYGMLPRATHTRNRREAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 81 GKQGGRTMEIQRLIARSLRAMVDLKALGERAITLDCDVIQADGGTRTAAITGAAVALCDAINALIENGTLKTNPIKGLVS 160
Cdd:COG0689 81 GKQSGRTQEIQRLIGRSLRAVVDLKALGERTITIDCDVLQADGGTRTASITGAFVALADALNKLVEKGLLKENPLKDQVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119207624 161 AISVGIVEGNAVCDLEYIEDSAAQTDMNVVMMEDGRMIEVQGTAEGEPFSHEELLTLLDLAKQGCYQIFVAQREALG 237
Cdd:COG0689 161 AVSVGIVDGEPVLDLDYEEDSAAEVDMNVVMTGSGEFVEVQGTAEGAPFSREELDALLDLAEKGIAELIALQKEALG 237
|
|
| rph |
PRK00173 |
ribonuclease PH; Reviewed |
1-237 |
2.61e-178 |
|
ribonuclease PH; Reviewed
Pssm-ID: 178914 Cd Length: 238 Bit Score: 488.46 E-value: 2.61e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 1 MRPNNRENHQPRQIKITRHYTKHAEGSVLVEFGDTKVLCTATVEDSVPRFLKGQNQGWVTAEYGMLPRSTHSRMQREAAK 80
Cdd:PRK00173 1 MRPDGRAADQLRPVTITRNFTKHAEGSVLVEFGDTKVLCTASVEEGVPRFLKGQGQGWVTAEYGMLPRATHTRNDREAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 81 GKQGGRTMEIQRLIARSLRAMVDLKALGERAITLDCDVIQADGGTRTAAITGAAVALCDAINALIENGTLKTNPIKGLVS 160
Cdd:PRK00173 81 GKQGGRTQEIQRLIGRSLRAVVDLKALGERTITIDCDVIQADGGTRTASITGAYVALADALNKLVARGKLKKNPLKDQVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119207624 161 AISVGIVEGNAVCDLEYIEDSAAQTDMNVVMMEDGRMIEVQGTAEGEPFSHEELLTLLDLAKQGCYQIFVAQREALG 237
Cdd:PRK00173 161 AVSVGIVDGEPVLDLDYEEDSAAETDMNVVMTGSGGFVEVQGTAEGAPFSREELDALLDLAEKGIAELVALQKAALA 237
|
|
| RNase_PH_bact |
cd11362 |
Ribonuclease PH; Ribonuclease PH (RNase PH)-like 3'-5' exoribonucleases are enzymes that ... |
10-236 |
4.37e-147 |
|
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: 409.31 E-value: 4.37e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 10 QPRQIKITRHYTKHAEGSVLVEFGDTKVLCTATVEDSVPRFLKGQNQGWVTAEYGMLPRSTHSRMQREAAKGKQGGRTME 89
Cdd:cd11362 1 QLRPISITRGFNKHAEGSVLIEFGDTKVLCTASVEEKVPPFLRGKGKGWVTAEYSMLPRSTHERTQREASKGKQSGRTQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 90 IQRLIARSLRAMVDLKALGERAITLDCDVIQADGGTRTAAITGAAVALCDAINALIENGTLKTNPIKGLVSAISVGIVEG 169
Cdd:cd11362 81 IQRLIGRSLRAAVDLEALGERTITIDCDVLQADGGTRTASITGAYVALADAVDKLVEKGVLEENPLKHFVAAVSVGIVDG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119207624 170 NAVCDLEYIEDSAAQTDMNVVMMEDGRMIEVQGTAEGEPFSHEELLTLLDLAKQGCYQIFVAQREAL 236
Cdd:cd11362 161 EPLLDLDYEEDSAADVDMNVVMTGSGRFVEVQGTGEEAPFSRDELNELLDLAEKGIQELIELQKEAL 227
|
|
| RNasePH |
TIGR01966 |
ribonuclease PH; This bacterial enzyme, ribonuclease PH, performs the final 3'-trimming and ... |
2-237 |
4.92e-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: 404.44 E-value: 4.92e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 2 RPNNRENHQPRQIKITRHYTKHAEGSVLVEFGDTKVLCTATVEDSVPRFLKGQNQGWVTAEYGMLPRSTHSRMQREAAKG 81
Cdd:TIGR01966 1 RPDGRKPDQLRPVSITRDFLKHAEGSVLIEFGNTKVLCTASVEEKVPPFLRGSGEGWITAEYGMLPRATQTRNRRESAKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 82 KQGGRTMEIQRLIARSLRAMVDLKALGERAITLDCDVIQADGGTRTAAITGAAVALCDAINALIENGTLKTNPIKGLVSA 161
Cdd:TIGR01966 81 KQSGRTQEIQRLIGRALRAVVDLEALGERTIWIDCDVIQADGGTRTASITGAFVALADAISKLHKRGILKESPIRDFVAA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119207624 162 ISVGIVEGNAVCDLEYIEDSAAQTDMNVVMMEDGRMIEVQGTAEGEPFSHEELLTLLDLAKQGCYQIFVAQREALG 237
Cdd:TIGR01966 161 VSVGIVDGEPVLDLDYEEDSAADVDMNVVMTGSGGFVEVQGTAEEGPFSRDELNKLLDLAKKGIRELIELQKQALG 236
|
|
| RNase_PH |
cd11358 |
RNase PH-like 3'-5' exoribonucleases; RNase PH-like 3'-5' exoribonucleases are enzymes that ... |
12-228 |
5.07e-39 |
|
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: 134.38 E-value: 5.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 12 RQIKITRHYTKHAEGSVLVEFGDTKVLCTATVEDSVPRFLKGQNQGWVTAEYGMLPRSTHSRMQreaakGKQGGRTMEIQ 91
Cdd:cd11358 2 RPVEIETGVLNQADGSALVKLGNTKVICAVTGPIVEPDKLERPDKGTLYVNVEISPGAVGERRQ-----GPPGDEEMEIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 92 RLIARSLRA--MVDLKALG-ERAITLDCDVIQADGGTRTAAITGAAVALCDAI--NALIENGTLKTNPIKGLVSAISVGI 166
Cdd:cd11358 77 RLLERTIEAsvILDKSTRKpSWVLYVDIQVLSRDGGLLDACWNAAIAALKDAGipRVFVDERSPPLLLMKDLIVAVSVGG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119207624 167 VEGNA-VCDLEYIEDSAAQTDMNVVMMEDGRMIEVQGTAEGEPFShEELLTLLDLAKQGCYQI 228
Cdd:cd11358 157 ISDGVlLLDPTGEEEELADSTLTVAVDKSGKLCLLSKVGGGSLDT-EEIKECLELAKKRSLHL 218
|
|
| RNase_PH_archRRP41 |
cd11366 |
RRP41 subunit of archaeal exosome; The RRP41 subunit of the archaeal exosome is a member of ... |
12-236 |
9.17e-38 |
|
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: 131.30 E-value: 9.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 12 RQIKITRHYTKHAEGSVLVEFGDTKVLctATV---EDSVPRFLKGQNQGWVTAEYGMLPRSTHSRMQREAAKgkqggRTM 88
Cdd:cd11366 3 RPIKIEVGVLKNADGSAYVEWGNNKII--AAVygpREVHPRHLQLPDRAVIRVRYNMAPFSVDERKRPGPDR-----REI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 89 EIQRLIARSLRAMVDLKALGERAITLDCDVIQADGGTRTAAITGAAVALCDAinalienGTlktnPIKGLVSAISVGIVE 168
Cdd:cd11366 76 EISKVIKEALEPAIILEEFPRTAIDVFVEVLQADAGTRVAGLNAASLALADA-------GI----PMRDLVAACAAGKVD 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119207624 169 GNAVCDLEYIEDSAAQTDMNVVMMEDGR---MIEVQGTaegepFSHEELLTLLDLAKQGCYQIFVAQREAL 236
Cdd:cd11366 145 GKIVLDLNKEEDNYGEADMPIAMMPNLGeitLLQLDGD-----LTPDEFKQAIELAKKGCKRIYELQKEAL 210
|
|
| PRK03983 |
PRK03983 |
exosome complex exonuclease Rrp41; Provisional |
1-236 |
4.39e-37 |
|
exosome complex exonuclease Rrp41; Provisional
Pssm-ID: 235187 [Multi-domain] Cd Length: 244 Bit Score: 130.14 E-value: 4.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 1 MRPNNRENHQPRQIKITRHYTKHAEGSVLVEFGDTKVLctATV---EDSVPRFLKGQNQGWVTAEYGMLPRSTHSRmqre 77
Cdd:PRK03983 14 LRLDGRKPDELRPIKIEVGVLKNADGSAYLEWGNNKII--AAVygpREMHPRHLQLPDRAVLRVRYNMAPFSVDER---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 78 aakgKQGG---RTMEIQRLIARSLRAMVDLKALGERAITLDCDVIQADGGTRTAAITGAAVALCDAinalienGTlktnP 154
Cdd:PRK03983 88 ----KRPGpdrRSIEISKVIREALEPAIMLELFPRTVIDVFIEVLQADAGTRVAGITAASLALADA-------GI----P 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 155 IKGLVSAISVGIVEGNAVCDLEYIEDSAAQTDMNVVMMEDGRMI---EVQGTaegepFSHEELLTLLDLAKQGCYQIFVA 231
Cdd:PRK03983 153 MRDLVAGCAVGKVDGVIVLDLNKEEDNYGEADMPVAIMPRLGEItllQLDGN-----LTREEFLEALELAKKGIKRIYQL 227
|
....*
gi 2119207624 232 QREAL 236
Cdd:PRK03983 228 QREAL 232
|
|
| RNase_PH |
pfam01138 |
3' exoribonuclease family, domain 1; This family includes 3'-5' exoribonucleases. Ribonuclease ... |
10-140 |
3.29e-32 |
|
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: 114.23 E-value: 3.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 10 QPRQIKITRHYTKHAEGSVLVEFGDTKVLCTATVEdSVPRFLKGQNQGWVTAEYGMLPRSTHSRMQReaakGKQGGRTME 89
Cdd:pfam01138 1 ELRPIEIETGVLSQADGSALVELGDTKVLATVTGP-IEPKEDRDFAPGRLTVEYELAPFASGERPGE----GRPSEREIE 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2119207624 90 IQRLIARSLRAMVDLKALGERAITLDCDVIQADGGTRTAAITGAAVALCDA 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 ... |
2-236 |
8.28e-22 |
|
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: 89.91 E-value: 8.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 2 RPNNRENHQPRQI--KITRHytKHAEGSVLVEFGDTKVLCTAT-VEDSVPRFLKGQNQGWVTAEYGMLPRSTHSRMQRea 78
Cdd:cd11370 3 RLDGRRPNELRRIrcRIGVF--SSADGSAYLEQGNTKVLAAVYgPHEPRNRSQALHDRAVVNCEYSMATFSTGERKRR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 79 akGKQGGRTMEIQRLIARSLRAMVDLKALGERAITLDCDVIQADGGTRTAAITGAAVALCDA-InaliengtlktnPIKG 157
Cdd:cd11370 79 --GKGDRRSTELSLAIRQTFEAVILTHLYPRSQIDIYVQVLQADGGLLAACINAATLALIDAgI------------PMKD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 158 LVSAISVGIVEGNAVCDLEYIEDSAAQTDMNV-VMMEDGRMIEVQGTAEgepFSHEELLTLLDLAKQGCYQIFVAQREAL 236
Cdd:cd11370 145 YVCACSAGYLDSTPLLDLNYLEESGDLPDLTVaVLPKSDKVVLLQMESR---LHLDRLEKVLELAIEGCKVIREIMDEVV 221
|
|
| PRK04282 |
PRK04282 |
exosome complex protein Rrp42; |
2-238 |
9.26e-21 |
|
exosome complex protein Rrp42;
Pssm-ID: 235268 [Multi-domain] Cd Length: 271 Bit Score: 88.01 E-value: 9.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 2 RPNNRENHQPRQIKITRHYTKHAEGSVLVEFGDTKVLCTATVEDSVPrFLKGQNQG--WVTAEygMLPrstHSRMQREAa 79
Cdd:PRK04282 25 RIDGRKLDEYRPIEIETGVIKKAEGSALVKLGNTQVLAGVKLEIGEP-FPDTPNEGvlIVNAE--LLP---LASPTFEP- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 80 kGKQGGRTMEIQRLIARSLR--AMVDLKAL----GERAITL--DCDVIQADGGTRTAAITGAAVALCDAI--NALIENGT 149
Cdd:PRK04282 98 -GPPDENAIELARVVDRGIResKAIDLEKLviepGKKVWVVfiDVYVLDHDGNLLDASMLAAVAALLNTKvpAVEEGEDG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 150 LKTN-------PIKGLVSAISVGIVEGNAVCDLEYIEDSAAQTDMNVVMMEDGRMIEVQGTAEGePFSHEELLTLLDLAK 222
Cdd:PRK04282 177 VVDKlgedfplPVNDKPVTVTFAKIGNYLIVDPTLEEESVMDARITITTDEDGNIVAIQKSGIG-SFTEEEVDKAIDIAL 255
|
250
....*....|....*.
gi 2119207624 223 QGCYQIFVAQREALGI 238
Cdd:PRK04282 256 EKAKELREKLKEALGI 271
|
|
| RNase_PH_archRRP42 |
cd11365 |
RRP42 subunit of archaeal exosome; The RRP42 subunit of the archaeal exosome is a member of ... |
2-229 |
7.50e-18 |
|
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: 79.57 E-value: 7.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 2 RPNNRENHQPRQIKITRHYTKHAEGSVLVEFGDTKVLCTATVEDSVPrFLKGQNQG--WVTAEYgmLPRSThsrmqREAA 79
Cdd:cd11365 17 RIDGRGLDEYRDIEIETGVIPKAEGSALVKLGNTQVLAGVKLEVGEP-FPDTPNEGvlIVNAEL--LPLAS-----PTFE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 80 KGKQGGRTMEIQRLIARSLRA--MVDLKAL----GERAIT--LDCDVIQADGGTRTAAITGAAVALCDA--------INA 143
Cdd:cd11365 89 PGPPDENAIELARVVDRGIREskAIDLEKLviepGKKVWVvfIDIYVLDYDGNLFDASALAAVAALLNTkvpeyevdENE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 144 LIENGTLKTN-PIKGLVSAISVGIVEGNAVCDLEYIEDSAAQTDMNVVMMEDGRMIEVQGTAEGePFSHEELLTLLDLAK 222
Cdd:cd11365 169 VIEVLGEELPlPVNTLPVSVTVAKIGGYIVVDPTLEEELVMDARITITIDEDGNIVALQKGGGG-SFTEDEIDKAIDIAL 247
|
....*..
gi 2119207624 223 QGCYQIF 229
Cdd:cd11365 248 EKAAELR 254
|
|
| RNase_PH_MTR3 |
cd11371 |
MTR3 subunit of eukaryotic exosome; The MTR3 subunit of eukaryotic exosome is a member of the ... |
23-236 |
9.14e-17 |
|
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: 76.07 E-value: 9.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 23 HAEGSVLVEFGDTKVLCtatvedSV--PRFLKGQN----QGWVTAEYGMLPRSTHSRmqreaAKGKQGGRTMEIQRLIAR 96
Cdd:cd11371 13 QAKGSAYVELGNTKVIC------SVygPRPIPGRTefsdRGRLNCEVKFAPFATPGR-----RRHGQDSEERELSSLLHQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 97 SLRAMVDLKALGERAITLDCDVIQADGGTRTAAITGAAVALCDA-InaliengtlktnPIKGLVSAISVGIVEGNAVCDL 175
Cdd:cd11371 82 ALEPAVRLEKYPKSQIDVFVTVLESDGSVLAAAITAASLALADAgI------------EMYDLVTACSAALIGDELLLDP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119207624 176 EYIEDSAAQTDMNVVMMEDGRMIeVQGTAEGEpFSHEELLTLLDLAKQGCYQIFVAQREAL 236
Cdd:cd11371 150 TREEEEASSGGVMLAYMPSLNQV-TQLWQSGE-MDVDQLEEALDLCIDGCNRIHPVVRQAL 208
|
|
| RNase_PH_C |
pfam03725 |
3' exoribonuclease family, domain 2; This family includes 3'-5' exoribonucleases. Ribonuclease ... |
157-224 |
4.95e-12 |
|
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: 59.51 E-value: 4.95e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119207624 157 GLVSAISVGIVEGNAVCDLEYIEDSAAQTDMNVVMMEDGRMIEVQGTAEGePFSHEELLTLLDLAKQG 224
Cdd:pfam03725 1 DPVAAVTVGKIDGQLVVDPTLEEESLSDSDLTVAVAGTGEIVALMKEGGA-GLTEDELLEALELAKEA 67
|
|
| RNase_PH_PNPase_1 |
cd11363 |
Polyribonucleotide nucleotidyltransferase, repeat 1; Polyribonucleotide nucleotidyltransferase ... |
12-234 |
6.38e-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: 6.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 12 RQIKI-TRHYTKHAEGSVLVEFGDTKVLCTATVEDSVPR---FLKgqnqgwVTAEYgmlprsthsrMQREAAKG------ 81
Cdd:cd11363 10 RTLTFeTGKLAKQADGSVVVQYGDTVVLVTAVSSKKPKEgidFFP------LTVDY----------REKLYAAGkipggf 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 82 -KQGGRTME----IQRLIARSLRAMVDLKALGERAITldCDVIQADGG--TRTAAITGAAVALCdainaliengtLKTNP 154
Cdd:cd11363 74 fKREGRPSEkeilTSRLIDRPIRPLFPKGFRNEVQVI--ATVLSVDGVndPDVLAINGASAALS-----------LSDIP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 155 IKGLVSAISVGIVEGNAVC--DLEYIEDSaaqtDMNVVM--MEDG-RMIEvqgtAEGEPFSHEELLTLLDLAKQGCYQIF 229
Cdd:cd11363 141 FNGPVGAVRVGRIDGEFVVnpTREELEES----DLDLVVagTKDAvLMVE----AGAKEVSEEDMLEAIKFGHEAIQQLI 212
|
....*
gi 2119207624 230 VAQRE 234
Cdd:cd11363 213 AAQEE 217
|
|
| RNase_PH_RRP46 |
cd11372 |
RRP46 subunit of eukaryotic exosome; The RRP46 subunit of eukaryotic exosome is a member of ... |
12-229 |
4.86e-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: 51.41 E-value: 4.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 12 RQIKITRHYTKHAEGSVLVEFGDTKVLCTAtvedsvprflkgqnqgwvtaeYGmlPRSThsRMQRE------------AA 79
Cdd:cd11372 2 RPLSCELGLLSRADGSARFSQGDTSVLAAV---------------------YG--PIEV--KLRKElpdratlevivrPK 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 80 KGKQGGRTMEIQRLIARSLRAMVDLKALGERAITLDCDVIQADGGTRTAAITGAAVALCDAinalienGTlktnPIKGLV 159
Cdd:cd11372 57 SGLPGVKEKLLELLLRSTLEPIILLHLHPRTLISVVLQVLQDDGSLLACAINAACLALLDA-------GV----PMKGLF 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 160 SAISVGIVE-GNAVCD--LEYIEDSAA--------QTDMNVVMMEdgrmievqgtAEGePFSHEELLTLLDLAKQGCYQI 228
Cdd:cd11372 126 AAVTCAITEdGEIILDptAEEEKEAKAvatfafdsGEEKNLVLSE----------SEG-SFTEEELFACLELAQAASAAI 194
|
.
gi 2119207624 229 F 229
Cdd:cd11372 195 F 195
|
|
| RNase_PH_RRP45 |
cd11368 |
RRP45 subunit of eukaryotic exosome; The RRP45 subunit of eukaryotic exosome is a member of ... |
2-138 |
6.38e-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: 49.06 E-value: 6.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 2 RPNNRENHQPRQIKIT--RHYtkhaeGSVLVEFGDTKVLCTATVEDSVPR-------FLKgqnqgwVTAEYgmlprSTHS 72
Cdd:cd11368 18 RLDGRGLDEFRPIKITfgLEY-----GCVEVSLGKTRVLAQVSCEIVEPKpdrpnegILF------INVEL-----SPMA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119207624 73 RMQREAakGKQGGRTMEIQRLIARSLR--AMVDLKAL----GER--AITLDCDVIQADGGTRTAAITGAAVALC 138
Cdd:cd11368 82 SPAFEP--GRPSEEEVELSRLLERALRdsRAVDTESLciiaGEKvwSIRVDVHVLNHDGNLIDAASLAAIAALM 153
|
|
| RNase_PH_RRP43 |
cd11369 |
RRP43 subunit of eukaryotic exosome; The RRP43 subunit of eukaryotic exosome is a member of ... |
2-223 |
6.23e-06 |
|
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: 46.01 E-value: 6.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 2 RPNNRENHQPRQIKITRHYTKHAEGSVLVEFGDTKVLCTATVEDSVPRfLKGQNQGWVTAEYGMLPR-STHSRMQR--EA 78
Cdd:cd11369 18 RPDGRELDEFRPTSVNVGSISTADGSALVKLGNTTVLCGIKAEVATPA-ADTPDEGYLVPNVDLPPLcSSKFRPGPpsEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 79 AkgkqggrtMEIQRLIARSLR--AMVDLKAL----GERAITLDCDV--IQADGGTRTAAITGAAVALCD----AINALIE 146
Cdd:cd11369 97 A--------QVLSSFLADILLnsNVLDLEQLcivpGKLAWVLYCDVycLDYDGNLLDAALLALVAALKNlrlpAVTIDEE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 147 NGTLKTNP-------IKGLVSAISVGIVEGNAV-CDLEYIEDSAAQTDMNVVMMEDGRMIEVQGtAEGEPFSHEELLTLL 218
Cdd:cd11369 169 TELVVVNPeerrplnLKNLPVSTTFAVFDDKHLlADPTAEEELLASGLVTVVVDENGELCSVHK-PGGSPLSQAQLQECI 247
|
....*
gi 2119207624 219 DLAKQ 223
Cdd:cd11369 248 ELAKK 252
|
|
| PRK11824 |
PRK11824 |
polynucleotide phosphorylase/polyadenylase; Provisional |
12-234 |
3.95e-04 |
|
polynucleotide phosphorylase/polyadenylase; Provisional
Pssm-ID: 236995 [Multi-domain] Cd Length: 693 Bit Score: 41.19 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 12 RQIKI-TRHYTKHAEGSVLVEFGDTKVLCTATVEDSVPrflKGQNQGWVTAEY-------GMLPRSThsrMQREaakGKQ 83
Cdd:PRK11824 14 RTLTLeTGKLARQANGAVLVRYGDTVVLVTVVASKEPK---EGQDFFPLTVDYeektyaaGKIPGGF---FKRE---GRP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 84 GGRTMEIQRLIARSLR--------------AMVdlkalgeraITLDCDViQADggtrTAAITGAAVALcdAINALiengt 149
Cdd:PRK11824 85 SEKETLTSRLIDRPIRplfpkgfrnevqvvATV---------LSVDPEN-DPD----ILAMIGASAAL--SISGI----- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119207624 150 lktnPIKGLVSAISVGIVEGNAVC--DLEYIEDSA-----AQTDMNVVMMEDGrMIEVqgtaegepfSHEELLTLLDLAK 222
Cdd:PRK11824 144 ----PFNGPIAAVRVGYIDGEFVLnpTVEELEESDldlvvAGTKDAVLMVESE-AKEL---------SEEVMLEAIEFGH 209
|
250
....*....|..
gi 2119207624 223 QGCYQIFVAQRE 234
Cdd:PRK11824 210 EAIQELIDAQEE 221
|
|
| |
