|
Name |
Accession |
Description |
Interval |
E-value |
| Rph |
COG0689 |
Ribonuclease PH [Translation, ribosomal structure and biogenesis]; |
7-243 |
0e+00 |
|
Ribonuclease PH [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440453 [Multi-domain] Cd Length: 238 Bit Score: 511.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 7 RPSGRPADQLREVRLTRHYTKHAEGSVLVEFGDTKVICTASVVERVPEFLRDRGQGWLTAEYGMLPRATHTRSDREAARG 86
Cdd:COG0689 2 RPDGRAPDQLRPVKITRGFTKHAEGSVLIEFGDTKVLCTASVEEGVPPFLKGSGQGWVTAEYGMLPRATHTRNRREAARG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 87 KQTGRTQEIQRLIGRALRAVVDLEQLGARTIHIDCDVIQADGGTRTASITGAFVAVQDAVAKLIAAGKLASSPITDSVAA 166
Cdd:COG0689 82 KQSGRTQEIQRLIGRSLRAVVDLKALGERTITIDCDVLQADGGTRTASITGAFVALADALNKLVEKGLLKENPLKDQVAA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503462289 167 ISVGVYQGTPVLDLDYAEDSRCDTDMNVVMTGKGGLVEVQGTAEGVPFTRDEMNALLDLAQKGIGELIALQKAALGD 243
Cdd:COG0689 162 VSVGIVDGEPVLDLDYEEDSAAEVDMNVVMTGSGEFVEVQGTAEGAPFSREELDALLDLAEKGIAELIALQKEALGE 238
|
|
| rph |
PRK00173 |
ribonuclease PH; Reviewed |
6-243 |
1.06e-180 |
|
ribonuclease PH; Reviewed
Pssm-ID: 178914 Cd Length: 238 Bit Score: 494.63 E-value: 1.06e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 6 SRPSGRPADQLREVRLTRHYTKHAEGSVLVEFGDTKVICTASVVERVPEFLRDRGQGWLTAEYGMLPRATHTRSDREAAR 85
Cdd:PRK00173 1 MRPDGRAADQLRPVTITRNFTKHAEGSVLVEFGDTKVLCTASVEEGVPRFLKGQGQGWVTAEYGMLPRATHTRNDREAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 86 GKQTGRTQEIQRLIGRALRAVVDLEQLGARTIHIDCDVIQADGGTRTASITGAFVAVQDAVAKLIAAGKLASSPITDSVA 165
Cdd:PRK00173 81 GKQGGRTQEIQRLIGRSLRAVVDLKALGERTITIDCDVIQADGGTRTASITGAYVALADALNKLVARGKLKKNPLKDQVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503462289 166 AISVGVYQGTPVLDLDYAEDSRCDTDMNVVMTGKGGLVEVQGTAEGVPFTRDEMNALLDLAQKGIGELIALQKAALGD 243
Cdd:PRK00173 161 AVSVGIVDGEPVLDLDYEEDSAAETDMNVVMTGSGGFVEVQGTAEGAPFSREELDALLDLAEKGIAELVALQKAALAD 238
|
|
| RNasePH |
TIGR01966 |
ribonuclease PH; This bacterial enzyme, ribonuclease PH, performs the final 3'-trimming and ... |
7-242 |
8.72e-154 |
|
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: 426.78 E-value: 8.72e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 7 RPSGRPADQLREVRLTRHYTKHAEGSVLVEFGDTKVICTASVVERVPEFLRDRGQGWLTAEYGMLPRATHTRSDREAARG 86
Cdd:TIGR01966 1 RPDGRKPDQLRPVSITRDFLKHAEGSVLIEFGNTKVLCTASVEEKVPPFLRGSGEGWITAEYGMLPRATQTRNRRESAKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 87 KQTGRTQEIQRLIGRALRAVVDLEQLGARTIHIDCDVIQADGGTRTASITGAFVAVQDAVAKLIAAGKLASSPITDSVAA 166
Cdd:TIGR01966 81 KQSGRTQEIQRLIGRALRAVVDLEALGERTIWIDCDVIQADGGTRTASITGAFVALADAISKLHKRGILKESPIRDFVAA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503462289 167 ISVGVYQGTPVLDLDYAEDSRCDTDMNVVMTGKGGLVEVQGTAEGVPFTRDEMNALLDLAQKGIGELIALQKAALG 242
Cdd:TIGR01966 161 VSVGIVDGEPVLDLDYEEDSAADVDMNVVMTGSGGFVEVQGTAEEGPFSRDELNKLLDLAKKGIRELIELQKQALG 236
|
|
| RNase_PH_bact |
cd11362 |
Ribonuclease PH; Ribonuclease PH (RNase PH)-like 3'-5' exoribonucleases are enzymes that ... |
15-241 |
1.48e-148 |
|
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: 413.16 E-value: 1.48e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 15 QLREVRLTRHYTKHAEGSVLVEFGDTKVICTASVVERVPEFLRDRGQGWLTAEYGMLPRATHTRSDREAARGKQTGRTQE 94
Cdd:cd11362 1 QLRPISITRGFNKHAEGSVLIEFGDTKVLCTASVEEKVPPFLRGKGKGWVTAEYSMLPRSTHERTQREASKGKQSGRTQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 95 IQRLIGRALRAVVDLEQLGARTIHIDCDVIQADGGTRTASITGAFVAVQDAVAKLIAAGKLASSPITDSVAAISVGVYQG 174
Cdd:cd11362 81 IQRLIGRSLRAAVDLEALGERTITIDCDVLQADGGTRTASITGAYVALADAVDKLVEKGVLEENPLKHFVAAVSVGIVDG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503462289 175 TPVLDLDYAEDSRCDTDMNVVMTGKGGLVEVQGTAEGVPFTRDEMNALLDLAQKGIGELIALQKAAL 241
Cdd:cd11362 161 EPLLDLDYEEDSAADVDMNVVMTGSGRFVEVQGTGEEAPFSRDELNELLDLAEKGIQELIELQKEAL 227
|
|
| RNase_PH |
pfam01138 |
3' exoribonuclease family, domain 1; This family includes 3'-5' exoribonucleases. Ribonuclease ... |
15-145 |
6.43e-35 |
|
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: 121.16 E-value: 6.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 15 QLREVRLTRHYTKHAEGSVLVEFGDTKVICTASVvERVPEFLRDRGQGWLTAEYGMLPRATHTRSDReaarGKQTGRTQE 94
Cdd:pfam01138 1 ELRPIEIETGVLSQADGSALVELGDTKVLATVTG-PIEPKEDRDFAPGRLTVEYELAPFASGERPGE----GRPSEREIE 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 503462289 95 IQRLIGRALRAVVDLEQLGARTIHIDCDVIQADGGTRTASITGAFVAVQDA 145
Cdd:pfam01138 76 ISRLIDRALRPSIPLEGYPRWTIRIDVTVLSSDGSLLDAAINAASLALADA 126
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Rph |
COG0689 |
Ribonuclease PH [Translation, ribosomal structure and biogenesis]; |
7-243 |
0e+00 |
|
Ribonuclease PH [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440453 [Multi-domain] Cd Length: 238 Bit Score: 511.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 7 RPSGRPADQLREVRLTRHYTKHAEGSVLVEFGDTKVICTASVVERVPEFLRDRGQGWLTAEYGMLPRATHTRSDREAARG 86
Cdd:COG0689 2 RPDGRAPDQLRPVKITRGFTKHAEGSVLIEFGDTKVLCTASVEEGVPPFLKGSGQGWVTAEYGMLPRATHTRNRREAARG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 87 KQTGRTQEIQRLIGRALRAVVDLEQLGARTIHIDCDVIQADGGTRTASITGAFVAVQDAVAKLIAAGKLASSPITDSVAA 166
Cdd:COG0689 82 KQSGRTQEIQRLIGRSLRAVVDLKALGERTITIDCDVLQADGGTRTASITGAFVALADALNKLVEKGLLKENPLKDQVAA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503462289 167 ISVGVYQGTPVLDLDYAEDSRCDTDMNVVMTGKGGLVEVQGTAEGVPFTRDEMNALLDLAQKGIGELIALQKAALGD 243
Cdd:COG0689 162 VSVGIVDGEPVLDLDYEEDSAAEVDMNVVMTGSGEFVEVQGTAEGAPFSREELDALLDLAEKGIAELIALQKEALGE 238
|
|
| rph |
PRK00173 |
ribonuclease PH; Reviewed |
6-243 |
1.06e-180 |
|
ribonuclease PH; Reviewed
Pssm-ID: 178914 Cd Length: 238 Bit Score: 494.63 E-value: 1.06e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 6 SRPSGRPADQLREVRLTRHYTKHAEGSVLVEFGDTKVICTASVVERVPEFLRDRGQGWLTAEYGMLPRATHTRSDREAAR 85
Cdd:PRK00173 1 MRPDGRAADQLRPVTITRNFTKHAEGSVLVEFGDTKVLCTASVEEGVPRFLKGQGQGWVTAEYGMLPRATHTRNDREAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 86 GKQTGRTQEIQRLIGRALRAVVDLEQLGARTIHIDCDVIQADGGTRTASITGAFVAVQDAVAKLIAAGKLASSPITDSVA 165
Cdd:PRK00173 81 GKQGGRTQEIQRLIGRSLRAVVDLKALGERTITIDCDVIQADGGTRTASITGAYVALADALNKLVARGKLKKNPLKDQVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503462289 166 AISVGVYQGTPVLDLDYAEDSRCDTDMNVVMTGKGGLVEVQGTAEGVPFTRDEMNALLDLAQKGIGELIALQKAALGD 243
Cdd:PRK00173 161 AVSVGIVDGEPVLDLDYEEDSAAETDMNVVMTGSGGFVEVQGTAEGAPFSREELDALLDLAEKGIAELVALQKAALAD 238
|
|
| RNasePH |
TIGR01966 |
ribonuclease PH; This bacterial enzyme, ribonuclease PH, performs the final 3'-trimming and ... |
7-242 |
8.72e-154 |
|
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: 426.78 E-value: 8.72e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 7 RPSGRPADQLREVRLTRHYTKHAEGSVLVEFGDTKVICTASVVERVPEFLRDRGQGWLTAEYGMLPRATHTRSDREAARG 86
Cdd:TIGR01966 1 RPDGRKPDQLRPVSITRDFLKHAEGSVLIEFGNTKVLCTASVEEKVPPFLRGSGEGWITAEYGMLPRATQTRNRRESAKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 87 KQTGRTQEIQRLIGRALRAVVDLEQLGARTIHIDCDVIQADGGTRTASITGAFVAVQDAVAKLIAAGKLASSPITDSVAA 166
Cdd:TIGR01966 81 KQSGRTQEIQRLIGRALRAVVDLEALGERTIWIDCDVIQADGGTRTASITGAFVALADAISKLHKRGILKESPIRDFVAA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503462289 167 ISVGVYQGTPVLDLDYAEDSRCDTDMNVVMTGKGGLVEVQGTAEGVPFTRDEMNALLDLAQKGIGELIALQKAALG 242
Cdd:TIGR01966 161 VSVGIVDGEPVLDLDYEEDSAADVDMNVVMTGSGGFVEVQGTAEEGPFSRDELNKLLDLAKKGIRELIELQKQALG 236
|
|
| RNase_PH_bact |
cd11362 |
Ribonuclease PH; Ribonuclease PH (RNase PH)-like 3'-5' exoribonucleases are enzymes that ... |
15-241 |
1.48e-148 |
|
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: 413.16 E-value: 1.48e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 15 QLREVRLTRHYTKHAEGSVLVEFGDTKVICTASVVERVPEFLRDRGQGWLTAEYGMLPRATHTRSDREAARGKQTGRTQE 94
Cdd:cd11362 1 QLRPISITRGFNKHAEGSVLIEFGDTKVLCTASVEEKVPPFLRGKGKGWVTAEYSMLPRSTHERTQREASKGKQSGRTQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 95 IQRLIGRALRAVVDLEQLGARTIHIDCDVIQADGGTRTASITGAFVAVQDAVAKLIAAGKLASSPITDSVAAISVGVYQG 174
Cdd:cd11362 81 IQRLIGRSLRAAVDLEALGERTITIDCDVLQADGGTRTASITGAYVALADAVDKLVEKGVLEENPLKHFVAAVSVGIVDG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503462289 175 TPVLDLDYAEDSRCDTDMNVVMTGKGGLVEVQGTAEGVPFTRDEMNALLDLAQKGIGELIALQKAAL 241
Cdd:cd11362 161 EPLLDLDYEEDSAADVDMNVVMTGSGRFVEVQGTGEEAPFSRDELNELLDLAEKGIQELIELQKEAL 227
|
|
| RNase_PH_archRRP41 |
cd11366 |
RRP41 subunit of archaeal exosome; The RRP41 subunit of the archaeal exosome is a member of ... |
15-241 |
4.60e-35 |
|
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: 124.37 E-value: 4.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 15 QLREVRLTRHYTKHAEGSVLVEFGDTKVIctASVV---ERVPEFLRDRGQGWLTAEYGMLPRATHTRsdreaARGKQTGR 91
Cdd:cd11366 1 ELRPIKIEVGVLKNADGSAYVEWGNNKII--AAVYgprEVHPRHLQLPDRAVIRVRYNMAPFSVDER-----KRPGPDRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 92 TQEIQRLIGRALRAVVDLEQLGARTIHIDCDVIQADGGTRTASITGAFVAVQDavakliaagklASSPITDSVAAISVGV 171
Cdd:cd11366 74 EIEISKVIKEALEPAIILEEFPRTAIDVFVEVLQADAGTRVAGLNAASLALAD-----------AGIPMRDLVAACAAGK 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503462289 172 YQGTPVLDLDYAEDSRCDTDMNVVMTGKGG---LVEVQGTaegvpFTRDEMNALLDLAQKGIGELIALQKAAL 241
Cdd:cd11366 143 VDGKIVLDLNKEEDNYGEADMPIAMMPNLGeitLLQLDGD-----LTPDEFKQAIELAKKGCKRIYELQKEAL 210
|
|
| PRK03983 |
PRK03983 |
exosome complex exonuclease Rrp41; Provisional |
1-241 |
5.30e-35 |
|
exosome complex exonuclease Rrp41; Provisional
Pssm-ID: 235187 [Multi-domain] Cd Length: 244 Bit Score: 125.13 E-value: 5.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 1 MTNSSSRPSGRPADQLREVRLTRHYTKHAEGSVLVEFGDTKVIctASVV---ERVPEFLRDRGQGWLTAEYGMLPRATHT 77
Cdd:PRK03983 9 ILEDGLRLDGRKPDELRPIKIEVGVLKNADGSAYLEWGNNKII--AAVYgprEMHPRHLQLPDRAVLRVRYNMAPFSVDE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 78 RSDREAARgkqtgRTQEIQRLIGRALRAVVDLEQLGARTIHIDCDVIQADGGTRTASITGAFVAVQDavakliaagklAS 157
Cdd:PRK03983 87 RKRPGPDR-----RSIEISKVIREALEPAIMLELFPRTVIDVFIEVLQADAGTRVAGITAASLALAD-----------AG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 158 SPITDSVAAISVGVYQGTPVLDLDYAEDSRCDTDMNVVMTGKGG---LVEVQGTaegvpFTRDEMNALLDLAQKGIGELI 234
Cdd:PRK03983 151 IPMRDLVAGCAVGKVDGVIVLDLNKEEDNYGEADMPVAIMPRLGeitLLQLDGN-----LTREEFLEALELAKKGIKRIY 225
|
....*..
gi 503462289 235 ALQKAAL 241
Cdd:PRK03983 226 QLQREAL 232
|
|
| RNase_PH |
pfam01138 |
3' exoribonuclease family, domain 1; This family includes 3'-5' exoribonucleases. Ribonuclease ... |
15-145 |
6.43e-35 |
|
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: 121.16 E-value: 6.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 15 QLREVRLTRHYTKHAEGSVLVEFGDTKVICTASVvERVPEFLRDRGQGWLTAEYGMLPRATHTRSDReaarGKQTGRTQE 94
Cdd:pfam01138 1 ELRPIEIETGVLSQADGSALVELGDTKVLATVTG-PIEPKEDRDFAPGRLTVEYELAPFASGERPGE----GRPSEREIE 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 503462289 95 IQRLIGRALRAVVDLEQLGARTIHIDCDVIQADGGTRTASITGAFVAVQDA 145
Cdd:pfam01138 76 ISRLIDRALRPSIPLEGYPRWTIRIDVTVLSSDGSLLDAAINAASLALADA 126
|
|
| RNase_PH |
cd11358 |
RNase PH-like 3'-5' exoribonucleases; RNase PH-like 3'-5' exoribonucleases are enzymes that ... |
16-233 |
1.17e-34 |
|
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: 123.21 E-value: 1.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 16 LREVRLTRHYTKHAEGSVLVEFGDTKVICTASVVERVPEFLRDRGQGWLTAEYGMLPRATHTRSdreaaRGKQTGRTQEI 95
Cdd:cd11358 1 FRPVEIETGVLNQADGSALVKLGNTKVICAVTGPIVEPDKLERPDKGTLYVNVEISPGAVGERR-----QGPPGDEEMEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 96 QRLIGRALRAVV--DLEQLGAR-TIHIDCDVIQADGGTRTASITGAFVAVQDAVAKLIAAGKLASSP--ITDSVAAISVG 170
Cdd:cd11358 76 SRLLERTIEASVilDKSTRKPSwVLYVDIQVLSRDGGLLDACWNAAIAALKDAGIPRVFVDERSPPLllMKDLIVAVSVG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503462289 171 VYQ-GTPVLDLDYAEDSRCDTDMNVVMTGKGGLVEVQGTAEGVPFTrDEMNALLDLAQKGIGEL 233
Cdd:cd11358 156 GISdGVLLLDPTGEEEELADSTLTVAVDKSGKLCLLSKVGGGSLDT-EEIKECLELAKKRSLHL 218
|
|
| RNase_PH_RRP41 |
cd11370 |
RRP41 subunit of eukaryotic exosome; The RRP41 subunit of eukaryotic exosome is a member of ... |
7-186 |
5.56e-21 |
|
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: 87.60 E-value: 5.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 7 RPSGRPADQLREV--RLTRHytKHAEGSVLVEFGDTKVICtaSV-----VERVPEFLRDRGQgwLTAEYGMLPRATHTRS 79
Cdd:cd11370 3 RLDGRRPNELRRIrcRIGVF--SSADGSAYLEQGNTKVLA--AVygphePRNRSQALHDRAV--VNCEYSMATFSTGERK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 80 dreaARGKQTGRTQEIQRLIGRALRAVVDLEQLGARTIHIDCDVIQADGGTRTASITGAFVAvqdavakLIAAGklasSP 159
Cdd:cd11370 77 ----RRGKGDRRSTELSLAIRQTFEAVILTHLYPRSQIDIYVQVLQADGGLLAACINAATLA-------LIDAG----IP 141
|
170 180
....*....|....*....|....*..
gi 503462289 160 ITDSVAAISVGVYQGTPVLDLDYAEDS 186
Cdd:cd11370 142 MKDYVCACSAGYLDSTPLLDLNYLEES 168
|
|
| PRK04282 |
PRK04282 |
exosome complex protein Rrp42; |
7-242 |
7.87e-21 |
|
exosome complex protein Rrp42;
Pssm-ID: 235268 [Multi-domain] Cd Length: 271 Bit Score: 88.39 E-value: 7.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 7 RPSGRPADQLREVRLTRHYTKHAEGSVLVEFGDTKVICTASVVERVPeFLRDRGQGWLTAEYGMLPRATHTrsdREAarG 86
Cdd:PRK04282 25 RIDGRKLDEYRPIEIETGVIKKAEGSALVKLGNTQVLAGVKLEIGEP-FPDTPNEGVLIVNAELLPLASPT---FEP--G 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 87 KQTGRTQEIQRLIGRALR--AVVDLEQL------GARTIHIDCDVIQADGGTRTASITGAFVA---------VQDAVAKL 149
Cdd:PRK04282 99 PPDENAIELARVVDRGIResKAIDLEKLviepgkKVWVVFIDVYVLDHDGNLLDASMLAAVAAllntkvpavEEGEDGVV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 150 IAAGKLASSPITDSVAAISVGVYQGTPVLDLDYAEDSRCDTDMNVVMTGKGGLVEVQGTAEGvPFTRDEMNALLDLAQKG 229
Cdd:PRK04282 179 DKLGEDFPLPVNDKPVTVTFAKIGNYLIVDPTLEEESVMDARITITTDEDGNIVAIQKSGIG-SFTEEEVDKAIDIALEK 257
|
250
....*....|...
gi 503462289 230 IGELIALQKAALG 242
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 ... |
7-234 |
3.52e-16 |
|
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: 75.33 E-value: 3.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 7 RPSGRPADQLREVRLTRHYTKHAEGSVLVEFGDTKVICTASVVERVPefLRDRG-QGWLTAEYGMLPRATHTRS----DR 81
Cdd:cd11365 17 RIDGRGLDEYRDIEIETGVIPKAEGSALVKLGNTQVLAGVKLEVGEP--FPDTPnEGVLIVNAELLPLASPTFEpgppDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 82 EAArgkqtgrtqEIQRLIGRALRA--VVDLEQL------GARTIHIDCDVIQADGGTRTASITGAFVAVQDAV------- 146
Cdd:cd11365 95 NAI---------ELARVVDRGIREskAIDLEKLviepgkKVWVVFIDIYVLDYDGNLFDASALAAVAALLNTKvpeyevd 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 147 --AKLIAAGKLASSPITDSVAAISVGVYQGTPVLDLDYAEDSRCDTDMNVVMTGKGGLVEVQGTAEGvPFTRDEMNALLD 224
Cdd:cd11365 166 enEVIEVLGEELPLPVNTLPVSVTVAKIGGYIVVDPTLEEELVMDARITITIDEDGNIVALQKGGGG-SFTEDEIDKAID 244
|
250
....*....|
gi 503462289 225 LAQKGIGELI 234
Cdd:cd11365 245 IALEKAAELR 254
|
|
| RNase_PH_MTR3 |
cd11371 |
MTR3 subunit of eukaryotic exosome; The MTR3 subunit of eukaryotic exosome is a member of the ... |
28-241 |
2.20e-15 |
|
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: 72.21 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 28 HAEGSVLVEFGDTKVICtaSV-----VERVPEFlRDRGQgwLTAEYGMLPRATHTRSDReaargKQTGRTQEIQRLIGRA 102
Cdd:cd11371 13 QAKGSAYVELGNTKVIC--SVygprpIPGRTEF-SDRGR--LNCEVKFAPFATPGRRRH-----GQDSEERELSSLLHQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 103 LRAVVDLEQLGARTIHIDCDVIQADGGTRTASITGAFVAVQDavakliaagklASSPITDSVAAISVGVYQGTPVLDLDY 182
Cdd:cd11371 83 LEPAVRLEKYPKSQIDVFVTVLESDGSVLAAAITAASLALAD-----------AGIEMYDLVTACSAALIGDELLLDPTR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503462289 183 AEDSRCDTDMNV-VMTGKGGLVEV--QGTAEGvpftrDEMNALLDLAQKGIGELIALQKAAL 241
Cdd:cd11371 152 EEEEASSGGVMLaYMPSLNQVTQLwqSGEMDV-----DQLEEALDLCIDGCNRIHPVVRQAL 208
|
|
| RNase_PH_C |
pfam03725 |
3' exoribonuclease family, domain 2; This family includes 3'-5' exoribonucleases. Ribonuclease ... |
162-229 |
1.42e-13 |
|
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: 63.75 E-value: 1.42e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503462289 162 DSVAAISVGVYQGTPVLDLDYAEDSRCDTDMNVVMTGKGGLVEVQGTAEGvPFTRDEMNALLDLAQKG 229
Cdd:pfam03725 1 DPVAAVTVGKIDGQLVVDPTLEEESLSDSDLTVAVAGTGEIVALMKEGGA-GLTEDELLEALELAKEA 67
|
|
| RNase_PH_PNPase_1 |
cd11363 |
Polyribonucleotide nucleotidyltransferase, repeat 1; Polyribonucleotide nucleotidyltransferase ... |
17-238 |
1.01e-08 |
|
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: 54.06 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 17 REVRL-TRHYTKHAEGSVLVEFGDTKVICTASVVERVPE---FLRdrgqgwLTAEY-------GMLPrATHTRsdREaar 85
Cdd:cd11363 10 RTLTFeTGKLAKQADGSVVVQYGDTVVLVTAVSSKKPKEgidFFP------LTVDYreklyaaGKIP-GGFFK--RE--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 86 GKQTgrTQEI--QRLIGRALRAVVDlEQLGARTiHIDCDVIQADGG--TRTASITGAFVAVqdAVAKLiaagklassPIT 161
Cdd:cd11363 78 GRPS--EKEIltSRLIDRPIRPLFP-KGFRNEV-QVIATVLSVDGVndPDVLAINGASAAL--SLSDI---------PFN 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503462289 162 DSVAAISVGVYQGTPVLDLDYAEDSRCDTDMnVVMTGKGGLVEVQGTAEGVPftRDEMNALLDLAQKGIGELIALQK 238
Cdd:cd11363 143 GPVGAVRVGRIDGEFVVNPTREELEESDLDL-VVAGTKDAVLMVEAGAKEVS--EEDMLEAIKFGHEAIQQLIAAQE 216
|
|
| RNase_PH_RRP43 |
cd11369 |
RRP43 subunit of eukaryotic exosome; The RRP43 subunit of eukaryotic exosome is a member of ... |
7-236 |
7.61e-08 |
|
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: 51.79 E-value: 7.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 7 RPSGRPADQLREVRLTRHYTKHAEGSVLVEFGDTKVIC-----TASVVERVPEflrdrgQGWLTAEYGMLPR-ATHTRSD 80
Cdd:cd11369 18 RPDGRELDEFRPTSVNVGSISTADGSALVKLGNTTVLCgikaeVATPAADTPD------EGYLVPNVDLPPLcSSKFRPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 81 R--EAArgkQTGrTQEIQRLIGRAlrAVVDLEQL------GARTIHIDCDVIQADGGTRTASITGAFVAVQDA---VAKL 149
Cdd:cd11369 92 PpsEEA---QVL-SSFLADILLNS--NVLDLEQLcivpgkLAWVLYCDVYCLDYDGNLLDAALLALVAALKNLrlpAVTI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 150 IAAGKLASSPITDSVA--------AISVGVYQGTPVL-DLDYAEDSRCDTDMNVVMTGKGGLVEVQGtAEGVPFTRDEMN 220
Cdd:cd11369 166 DEETELVVVNPEERRPlnlknlpvSTTFAVFDDKHLLaDPTAEEELLASGLVTVVVDENGELCSVHK-PGGSPLSQAQLQ 244
|
250
....*....|....*.
gi 503462289 221 ALLDLAQKGIGELIAL 236
Cdd:cd11369 245 ECIELAKKRAKELQKL 260
|
|
| RNase_PH_RRP46 |
cd11372 |
RRP46 subunit of eukaryotic exosome; The RRP46 subunit of eukaryotic exosome is a member of ... |
16-238 |
1.09e-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: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 16 LREVRLTRHYTKHAEGSVLVEFGDTKVICTAsvvervpeflrdrgqgwltaeYG----MLPRATHTRSDRE----AARGK 87
Cdd:cd11372 1 LRPLSCELGLLSRADGSARFSQGDTSVLAAV---------------------YGpievKLRKELPDRATLEvivrPKSGL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 88 QTGRTQEIQRLIGRALRAVVDLEQLGARTIHIDCDVIQADGGTRTASITGAFVAVQDavakliaagklASSPITDSVAAI 167
Cdd:cd11372 60 PGVKEKLLELLLRSTLEPIILLHLHPRTLISVVLQVLQDDGSLLACAINAACLALLD-----------AGVPMKGLFAAV 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503462289 168 SVGV-YQGTPVLDLDYAEDSRCDTDMNVVMTGKGG----LVEVQGTaegvpFTRDEMNALLDLAQKGIGELIALQK 238
Cdd:cd11372 129 TCAItEDGEIILDPTAEEEKEAKAVATFAFDSGEEknlvLSESEGS-----FTEEELFACLELAQAASAAIFDFYR 199
|
|
| RNase_PH_RRP45 |
cd11368 |
RRP45 subunit of eukaryotic exosome; The RRP45 subunit of eukaryotic exosome is a member of ... |
7-236 |
2.52e-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: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 7 RPSGRPADQLREVRLT--RHYtkhaeGSVLVEFGDTKVIC--TASVVERVPeflrDRG-QGWLT--AEYG-MLPRATHTR 78
Cdd:cd11368 18 RLDGRGLDEFRPIKITfgLEY-----GCVEVSLGKTRVLAqvSCEIVEPKP----DRPnEGILFinVELSpMASPAFEPG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 79 SDREAARgkqtgrtqEIQRLIGRALR--AVVDLEQL----GAR--TIHIDCDVIQADGGTR----TASITG--AF----V 140
Cdd:cd11368 89 RPSEEEV--------ELSRLLERALRdsRAVDTESLciiaGEKvwSIRVDVHVLNHDGNLIdaasLAAIAAlmHFrrpdV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 141 AVQDAVAKLIAAGKLAssPITDSV----AAISVGVYQGTP--VLDLDYAEDSRCDTDMNVVMTGKGGLVEVQgTAEGVPF 214
Cdd:cd11368 161 TVDGEEVTVHSPEERE--PVPLSIhhipICVTFAFFDDGEivVVDPTLLEEAVADGSLTVALNKHREICALS-KSGGAPL 237
|
250 260
....*....|....*....|..
gi 503462289 215 TRDEMNALLDLAQKGIGELIAL 236
Cdd:cd11368 238 SPSQILRCVKIAAAKAKELTEL 259
|
|
| PLN00207 |
PLN00207 |
polyribonucleotide nucleotidyltransferase; Provisional |
97-200 |
5.04e-05 |
|
polyribonucleotide nucleotidyltransferase; Provisional
Pssm-ID: 215104 [Multi-domain] Cd Length: 891 Bit Score: 44.11 E-value: 5.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503462289 97 RLIGRALRAVVDLEQLGARTIHIDCDVIQADGGTRTASITGAFVAVQDavakliaagklASSPITDSVAAISVGVY---- 172
Cdd:PLN00207 530 MLAERALEPILPSEDDFPYTIRVESTITESNGSSSMASVCGGCLALQD-----------AGVPVKCPIAGIAMGMVldte 598
|
90 100 110
....*....|....*....|....*....|....
gi 503462289 173 ----QGTPVL--DLDYAEDSRCDTDMNVVMTGKG 200
Cdd:PLN00207 599 efggDGSPLIlsDITGSEDASGDMDFKVAGNEDG 632
|
|
| |
