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Conserved domains on  [gi|1131173046|ref|XP_019829227|]
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PREDICTED: exosome complex component RRP41 [Bos indicus]

Protein Classification

RRP41/SKI6 family exosome complex component( domain architecture ID 10183526)

RRP41/SKI6 family exosome complex component is a non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RNase_PH_RRP41 cd11370
RRP41 subunit of eukaryotic exosome; The RRP41 subunit of eukaryotic exosome is a member of ...
 11-237 1.27e-136

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: 383.05  E-value: 1.27e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131173046  11 GYRVDGRRAGELRKIQARMGVFAQADGSAYIEQGNTKALAVVYGPHEIRGSRArALPDRALVNCQYSSATFSTGERKRRP 90
Cdd:cd11370     1 GLRLDGRRPNELRRIRCRIGVFSSADGSAYLEQGNTKVLAAVYGPHEPRNRSQ-ALHDRAVVNCEYSMATFSTGERKRRG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131173046  91 HGDRKSCEMGLQLRQTFEAAILTQLHPRSQIDIYVQVLQADGGTYAACVNAATLAVLDAGIPMRDFVCACSAGFVDGTAL 170
Cdd:cd11370    80 KGDRRSTELSLAIRQTFEAVILTHLYPRSQIDIYVQVLQADGGLLAACINAATLALIDAGIPMKDYVCACSAGYLDSTPL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1131173046 171 ADLSHVEEAAGGPQLALALLPASGQIALLEMDARLHEDHLEQVLEAAARASRDVHTVLDRVVRQHVQ 237
Cdd:cd11370   160 LDLNYLEESGDLPDLTVAVLPKSDKVVLLQMESRLHLDRLEKVLELAIEGCKVIREIMDEVVREHTK 226
 
Name Accession Description Interval E-value
RNase_PH_RRP41 cd11370
RRP41 subunit of eukaryotic exosome; The RRP41 subunit of eukaryotic exosome is a member of ...
 11-237 1.27e-136

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: 383.05  E-value: 1.27e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131173046  11 GYRVDGRRAGELRKIQARMGVFAQADGSAYIEQGNTKALAVVYGPHEIRGSRArALPDRALVNCQYSSATFSTGERKRRP 90
Cdd:cd11370     1 GLRLDGRRPNELRRIRCRIGVFSSADGSAYLEQGNTKVLAAVYGPHEPRNRSQ-ALHDRAVVNCEYSMATFSTGERKRRG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131173046  91 HGDRKSCEMGLQLRQTFEAAILTQLHPRSQIDIYVQVLQADGGTYAACVNAATLAVLDAGIPMRDFVCACSAGFVDGTAL 170
Cdd:cd11370    80 KGDRRSTELSLAIRQTFEAVILTHLYPRSQIDIYVQVLQADGGLLAACINAATLALIDAGIPMKDYVCACSAGYLDSTPL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1131173046 171 ADLSHVEEAAGGPQLALALLPASGQIALLEMDARLHEDHLEQVLEAAARASRDVHTVLDRVVRQHVQ 237
Cdd:cd11370   160 LDLNYLEESGDLPDLTVAVLPKSDKVVLLQMESRLHLDRLEKVLELAIEGCKVIREIMDEVVREHTK 226
PRK03983 PRK03983
exosome complex exonuclease Rrp41; Provisional
 1-225 1.47e-76

exosome complex exonuclease Rrp41; Provisional


Pssm-ID: 235187 [Multi-domain]  Cd Length: 244  Bit Score: 231.45  E-value: 1.47e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131173046   1 MAGLELLSDQGYRVDGRRAGELRKIQARMGVFAQADGSAYIEQGNTKALAVVYGPHEIRgSRARALPDRALVNCQYSSAT 80
Cdd:PRK03983    3 VEPPKLILEDGLRLDGRKPDELRPIKIEVGVLKNADGSAYLEWGNNKIIAAVYGPREMH-PRHLQLPDRAVLRVRYNMAP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131173046  81 FSTGERKRrPHGDRKSCEMGLQLRQTFEAAILTQLHPRSQIDIYVQVLQADGGTYAACVNAATLAVLDAGIPMRDFVCAC 160
Cdd:PRK03983   82 FSVDERKR-PGPDRRSIEISKVIREALEPAIMLELFPRTVIDVFIEVLQADAGTRVAGITAASLALADAGIPMRDLVAGC 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1131173046 161 SAGFVDGTALADLSHVEEAAGGPQLALALLPASGQIALLEMDARLHEDHLEQVLEAAARASRDVH 225
Cdd:PRK03983  161 AVGKVDGVIVLDLNKEEDNYGEADMPVAIMPRLGEITLLQLDGNLTREEFLEALELAKKGIKRIY 225
RNase_PH pfam01138
3' exoribonuclease family, domain 1; This family includes 3'-5' exoribonucleases. Ribonuclease ...
 21-152 9.42e-40

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: 133.87  E-value: 9.42e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131173046  21 ELRKIQARMGVFAQADGSAYIEQGNTKALAVVYGPHEIRGSRARAlpdRALVNCQYSSATFSTGERKRRPHGDRKSCEMG 100
Cdd:pfam01138   1 ELRPIEIETGVLSQADGSALVELGDTKVLATVTGPIEPKEDRDFA---PGRLTVEYELAPFASGERPGEGRPSEREIEIS 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1131173046 101 LQLRQTFEAAILTQLHPRSQIDIYVQVLQADGGTYAACVNAATLAVLDAGIP 152
Cdd:pfam01138  78 RLIDRALRPSIPLEGYPRWTIRIDVTVLSSDGSLLDAAINAASLALADAGIP 129
Rph COG0689
Ribonuclease PH [Translation, ribosomal structure and biogenesis];
13-177 1.37e-13

Ribonuclease PH [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440453 [Multi-domain]  Cd Length: 238  Bit Score: 67.75  E-value: 1.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131173046  13 RVDGRRAGELRKIQARMGVFAQADGSAYIEQGNTKALA-------VvygPHEIRGSRaralpdRALVNCQYSSATFSTGE 85
Cdd:COG0689     2 RPDGRAPDQLRPVKITRGFTKHAEGSVLIEFGDTKVLCtasveegV---PPFLKGSG------QGWVTAEYGMLPRATHT 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131173046  86 RKRRPHGDRK----SCE----MGLQLRqtfeAAI-LTQLHPRsQIDIYVQVLQADGGTYAACVNAATLAVLDA------- 149
Cdd:COG0689    73 RNRREAARGKqsgrTQEiqrlIGRSLR----AVVdLKALGER-TITIDCDVLQADGGTRTASITGAFVALADAlnklvek 147

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1131173046 150 ----GIPMRDFVCACSAGFVDGTALADLSHVE 177
Cdd:COG0689   148 gllkENPLKDQVAAVSVGIVDGEPVLDLDYEE 179
 
Name Accession Description Interval E-value
RNase_PH_RRP41 cd11370
RRP41 subunit of eukaryotic exosome; The RRP41 subunit of eukaryotic exosome is a member of ...
 11-237 1.27e-136

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: 383.05  E-value: 1.27e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131173046  11 GYRVDGRRAGELRKIQARMGVFAQADGSAYIEQGNTKALAVVYGPHEIRGSRArALPDRALVNCQYSSATFSTGERKRRP 90
Cdd:cd11370     1 GLRLDGRRPNELRRIRCRIGVFSSADGSAYLEQGNTKVLAAVYGPHEPRNRSQ-ALHDRAVVNCEYSMATFSTGERKRRG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131173046  91 HGDRKSCEMGLQLRQTFEAAILTQLHPRSQIDIYVQVLQADGGTYAACVNAATLAVLDAGIPMRDFVCACSAGFVDGTAL 170
Cdd:cd11370    80 KGDRRSTELSLAIRQTFEAVILTHLYPRSQIDIYVQVLQADGGLLAACINAATLALIDAGIPMKDYVCACSAGYLDSTPL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1131173046 171 ADLSHVEEAAGGPQLALALLPASGQIALLEMDARLHEDHLEQVLEAAARASRDVHTVLDRVVRQHVQ 237
Cdd:cd11370   160 LDLNYLEESGDLPDLTVAVLPKSDKVVLLQMESRLHLDRLEKVLELAIEGCKVIREIMDEVVREHTK 226
PRK03983 PRK03983
exosome complex exonuclease Rrp41; Provisional
 1-225 1.47e-76

exosome complex exonuclease Rrp41; Provisional


Pssm-ID: 235187 [Multi-domain]  Cd Length: 244  Bit Score: 231.45  E-value: 1.47e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131173046   1 MAGLELLSDQGYRVDGRRAGELRKIQARMGVFAQADGSAYIEQGNTKALAVVYGPHEIRgSRARALPDRALVNCQYSSAT 80
Cdd:PRK03983    3 VEPPKLILEDGLRLDGRKPDELRPIKIEVGVLKNADGSAYLEWGNNKIIAAVYGPREMH-PRHLQLPDRAVLRVRYNMAP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131173046  81 FSTGERKRrPHGDRKSCEMGLQLRQTFEAAILTQLHPRSQIDIYVQVLQADGGTYAACVNAATLAVLDAGIPMRDFVCAC 160
Cdd:PRK03983   82 FSVDERKR-PGPDRRSIEISKVIREALEPAIMLELFPRTVIDVFIEVLQADAGTRVAGITAASLALADAGIPMRDLVAGC 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1131173046 161 SAGFVDGTALADLSHVEEAAGGPQLALALLPASGQIALLEMDARLHEDHLEQVLEAAARASRDVH 225
Cdd:PRK03983  161 AVGKVDGVIVLDLNKEEDNYGEADMPVAIMPRLGEITLLQLDGNLTREEFLEALELAKKGIKRIY 225
RNase_PH_archRRP41 cd11366
RRP41 subunit of archaeal exosome; The RRP41 subunit of the archaeal exosome is a member of ...
 21-227 6.53e-71

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: 216.05  E-value: 6.53e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131173046  21 ELRKIQARMGVFAQADGSAYIEQGNTKALAVVYGPHEIRgSRARALPDRALVNCQYSSATFSTGERKRrPHGDRKSCEMG 100
Cdd:cd11366     1 ELRPIKIEVGVLKNADGSAYVEWGNNKIIAAVYGPREVH-PRHLQLPDRAVIRVRYNMAPFSVDERKR-PGPDRREIEIS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131173046 101 LQLRQTFEAAILTQLHPRSQIDIYVQVLQADGGTYAACVNAATLAVLDAGIPMRDFVCACSAGFVDGTALADLSHVEEAA 180
Cdd:cd11366    79 KVIKEALEPAIILEEFPRTAIDVFVEVLQADAGTRVAGLNAASLALADAGIPMRDLVAACAAGKVDGKIVLDLNKEEDNY 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1131173046 181 GGPQLALALLPASGQIALLEMDARLHEDHLEQVLEAAARASRDVHTV 227
Cdd:cd11366   159 GEADMPIAMMPNLGEITLLQLDGDLTPDEFKQAIELAKKGCKRIYEL 205
RNase_PH_MTR3 cd11371
MTR3 subunit of eukaryotic exosome; The MTR3 subunit of eukaryotic exosome is a member of the ...
 22-228 4.02e-57

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: 180.84  E-value: 4.02e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131173046  22 LRKIQARMGVFAQADGSAYIEQGNTKALAVVYGPHEIRGSRARAlpDRALVNCQYSSATFSTgeRKRRPHG-DRKSCEMG 100
Cdd:cd11371     1 IRPIFLKTGVVSQAKGSAYVELGNTKVICSVYGPRPIPGRTEFS--DRGRLNCEVKFAPFAT--PGRRRHGqDSEERELS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131173046 101 LQLRQTFEAAILTQLHPRSQIDIYVQVLQADGGTYAACVNAATLAVLDAGIPMRDFVCACSAGFVDGTALADLSHVEEAA 180
Cdd:cd11371    77 SLLHQALEPAVRLEKYPKSQIDVFVTVLESDGSVLAAAITAASLALADAGIEMYDLVTACSAALIGDELLLDPTREEEEA 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1131173046 181 GGPQLALALLPASGQIALLEMDARLHEDHLEQVLEAAARASRDVHTVL 228
Cdd:cd11371   157 SSGGVMLAYMPSLNQVTQLWQSGEMDVDQLEEALDLCIDGCNRIHPVV 204
RNase_PH cd11358
RNase PH-like 3'-5' exoribonucleases; RNase PH-like 3'-5' exoribonucleases are enzymes that ...
 22-224 2.03e-56

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: 179.44  E-value: 2.03e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131173046  22 LRKIQARMGVFAQADGSAYIEQGNTKALAVVYGPHEIRGSRARalPDRALVNCQYSSATFSTGERkRRPHGDRKSCEMGL 101
Cdd:cd11358     1 FRPVEIETGVLNQADGSALVKLGNTKVICAVTGPIVEPDKLER--PDKGTLYVNVEISPGAVGER-RQGPPGDEEMEISR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131173046 102 QLRQTFEAAILTQL---HPRSQIDIYVQVLQADGGTYAACVNAATLAVLDAGIP-------------MRDFVCACSAGFV 165
Cdd:cd11358    78 LLERTIEASVILDKstrKPSWVLYVDIQVLSRDGGLLDACWNAAIAALKDAGIPrvfvderspplllMKDLIVAVSVGGI 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131173046 166 -DGTALADLSHVEEAAGGPQLALALLPaSGQIALLEMDARLHED--HLEQVLEAAARASRDV 224
Cdd:cd11358   158 sDGVLLLDPTGEEEELADSTLTVAVDK-SGKLCLLSKVGGGSLDteEIKECLELAKKRSLHL 218
RNase_PH_RRP46 cd11372
RRP46 subunit of eukaryotic exosome; The RRP46 subunit of eukaryotic exosome is a member of ...
 22-226 3.63e-44

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: 147.33  E-value: 3.63e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131173046  22 LRKIQARMGVFAQADGSAYIEQGNTKALAVVYGPHEIRgsRARALPDRALVNCQYSSATFSTGERKRrphgdrkscEMGL 101
Cdd:cd11372     1 LRPLSCELGLLSRADGSARFSQGDTSVLAAVYGPIEVK--LRKELPDRATLEVIVRPKSGLPGVKEK---------LLEL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131173046 102 QLRQTFEAAILTQLHPRSQIDIYVQVLQADGGTYAACVNAATLAVLDAGIPMRDFVCACSAGFV-DGTALADLSHVEEAA 180
Cdd:cd11372    70 LLRSTLEPIILLHLHPRTLISVVLQVLQDDGSLLACAINAACLALLDAGVPMKGLFAAVTCAITeDGEIILDPTAEEEKE 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1131173046 181 GgpqLALAL--LPASGQIALLEMDAR--LHEDHLEQVLEAAARASRDVHT 226
Cdd:cd11372   150 A---KAVATfaFDSGEEKNLVLSESEgsFTEEELFACLELAQAASAAIFD 196
RNase_PH pfam01138
3' exoribonuclease family, domain 1; This family includes 3'-5' exoribonucleases. Ribonuclease ...
 21-152 9.42e-40

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: 133.87  E-value: 9.42e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131173046  21 ELRKIQARMGVFAQADGSAYIEQGNTKALAVVYGPHEIRGSRARAlpdRALVNCQYSSATFSTGERKRRPHGDRKSCEMG 100
Cdd:pfam01138   1 ELRPIEIETGVLSQADGSALVELGDTKVLATVTGPIEPKEDRDFA---PGRLTVEYELAPFASGERPGEGRPSEREIEIS 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1131173046 101 LQLRQTFEAAILTQLHPRSQIDIYVQVLQADGGTYAACVNAATLAVLDAGIP 152
Cdd:pfam01138  78 RLIDRALRPSIPLEGYPRWTIRIDVTVLSSDGSLLDAAINAASLALADAGIP 129
Rph COG0689
Ribonuclease PH [Translation, ribosomal structure and biogenesis];
13-177 1.37e-13

Ribonuclease PH [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440453 [Multi-domain]  Cd Length: 238  Bit Score: 67.75  E-value: 1.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131173046  13 RVDGRRAGELRKIQARMGVFAQADGSAYIEQGNTKALA-------VvygPHEIRGSRaralpdRALVNCQYSSATFSTGE 85
Cdd:COG0689     2 RPDGRAPDQLRPVKITRGFTKHAEGSVLIEFGDTKVLCtasveegV---PPFLKGSG------QGWVTAEYGMLPRATHT 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131173046  86 RKRRPHGDRK----SCE----MGLQLRqtfeAAI-LTQLHPRsQIDIYVQVLQADGGTYAACVNAATLAVLDA------- 149
Cdd:COG0689    73 RNRREAARGKqsgrTQEiqrlIGRSLR----AVVdLKALGER-TITIDCDVLQADGGTRTASITGAFVALADAlnklvek 147

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1131173046 150 ----GIPMRDFVCACSAGFVDGTALADLSHVE 177
Cdd:COG0689   148 gllkENPLKDQVAAVSVGIVDGEPVLDLDYEE 179
RNase_PH_bact cd11362
Ribonuclease PH; Ribonuclease PH (RNase PH)-like 3'-5' exoribonucleases are enzymes that ...
 21-180 2.16e-13

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: 67.25  E-value: 2.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131173046  21 ELRKIQARMGVFAQADGSAYIEQGNTKALAVVYG----PHEIRGSRaralpdRALVNCQYSSATFSTGERKRRPHGDRK- 95
Cdd:cd11362     1 QLRPISITRGFNKHAEGSVLIEFGDTKVLCTASVeekvPPFLRGKG------KGWVTAEYSMLPRSTHERTQREASKGKq 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131173046  96 ---SCE----MGLQLRqtfeAAI-LTQLHPRsQIDIYVQVLQADGGTYAACVNAATLAVLDA-----------GIPMRDF 156
Cdd:cd11362    75 sgrTQEiqrlIGRSLR----AAVdLEALGER-TITIDCDVLQADGGTRTASITGAYVALADAvdklvekgvleENPLKHF 149

                         170       180
                  ....*....|....*....|....
gi 1131173046 157 VCACSAGFVDGTALADLSHVEEAA 180
Cdd:cd11362   150 VAAVSVGIVDGEPLLDLDYEEDSA 173
RNase_PH_C pfam03725
3' exoribonuclease family, domain 2; This family includes 3'-5' exoribonucleases. Ribonuclease ...
 155-220 2.99e-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: 60.28  E-value: 2.99e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1131173046 155 DFVCACSAGFVDGTALADLSHVEEAAGGPQLALALLPASGQIALLEMD-ARLHEDHLEQVLEAAARA 220
Cdd:pfam03725   1 DPVAAVTVGKIDGQLVVDPTLEEESLSDSDLTVAVAGTGEIVALMKEGgAGLTEDELLEALELAKEA 67
rph PRK00173
ribonuclease PH; Reviewed
 13-180 1.07e-11

ribonuclease PH; Reviewed


Pssm-ID: 178914  Cd Length: 238  Bit Score: 62.43  E-value: 1.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131173046  13 RVDGRRAGELRKIQARMGVFAQADGSAYIEQGNTKAL---AVVYG-PHEIRGSRaralpdRALVNCQYSSATFSTGERKR 88
Cdd:PRK00173    2 RPDGRAADQLRPVTITRNFTKHAEGSVLVEFGDTKVLctaSVEEGvPRFLKGQG------QGWVTAEYGMLPRATHTRND 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131173046  89 RPHGDRK----SCEM----GLQLRqtfeAAI-LTQLHPRsQIDIYVQVLQADGGTYAACVNAATLAVLDA---------- 149
Cdd:PRK00173   76 REAAKGKqggrTQEIqrliGRSLR----AVVdLKALGER-TITIDCDVIQADGGTRTASITGAYVALADAlnklvargkl 150

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1131173046 150 -GIPMRDFVCACSAGFVDGTALADLSHVEEAA 180
Cdd:PRK00173  151 kKNPLKDQVAAVSVGIVDGEPVLDLDYEEDSA 182
PLN00207 PLN00207
polyribonucleotide nucleotidyltransferase; Provisional
 11-223 9.50e-11

polyribonucleotide nucleotidyltransferase; Provisional


Pssm-ID: 215104 [Multi-domain]  Cd Length: 891  Bit Score: 61.45  E-value: 9.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131173046  11 GYRVDGRRAGELRKIQARMGVFAQADGSAYIEQGNTKALAVVygpheIRGSRARALPDRALVNC--------QYSSATFS 82
Cdd:PLN00207  437 GKRSDGRTPDEIRPINSSCGLLPRAHGSALFTRGETQALAVV-----TLGDKQMAQRIDNLVDAdevkrfylQYSFPPSC 511

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131173046  83 TGERKRRPHGDRKSCEMGLQLRQTFEAAILTQLHPRSQIDIYVQVLQADGGTYAACVNAATLAVLDAGIPMRDFVCACSA 162
Cdd:PLN00207  512 VGEVGRIGAPSRREIGHGMLAERALEPILPSEDDFPYTIRVESTITESNGSSSMASVCGGCLALQDAGVPVKCPIAGIAM 591

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131173046 163 GFV--------DGTA--LADLSHVEEAAGGPQLALAllPASGQIALLEMDARLHEDHLEqVLEAAARASRD 223
Cdd:PLN00207  592 GMVldteefggDGSPliLSDITGSEDASGDMDFKVA--GNEDGITAFQMDIKVGGITLP-IMERALLQAKD 659
RNase_PH_archRRP42 cd11365
RRP42 subunit of archaeal exosome; The RRP42 subunit of the archaeal exosome is a member of ...
 4-225 1.60e-07

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: 50.68  E-value: 1.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131173046   4 LELLSdQGYRVDGRRAGELRKIQARMGVFAQADGSAYIEQGNTKALAVVygpheiRGSRARALPDRA-----LVNCQYS- 77
Cdd:cd11365     9 LSLLE-KGKRIDGRGLDEYRDIEIETGVIPKAEGSALVKLGNTQVLAGV------KLEVGEPFPDTPnegvlIVNAELLp 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131173046  78 --SATFSTGERkrrphgDRKSCEMG----LQLRQTfEAAILTQL--HPRSQ-----IDIYvqVLQADGGTYAACVNAATL 144
Cdd:cd11365    82 laSPTFEPGPP------DENAIELArvvdRGIRES-KAIDLEKLviEPGKKvwvvfIDIY--VLDYDGNLFDASALAAVA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131173046 145 AVLDAGIP--------------------MRDFVCACSAGFVDGTALADLSHVEEAAGGPQLALAlLPASGQIALL---EM 201
Cdd:cd11365   153 ALLNTKVPeyevdenevievlgeelplpVNTLPVSVTVAKIGGYIVVDPTLEEELVMDARITIT-IDEDGNIVALqkgGG 231

                         250       260
                  ....*....|....*....|....
gi 1131173046 202 DArLHEDHLEQVLEAAARASRDVH 225
Cdd:cd11365   232 GS-FTEDEIDKAIDIALEKAAELR 254
Rrp42 COG2123
Exosome complex RNA-binding protein Rrp42, RNase PH superfamily [Intracellular trafficking, ...
 4-52 1.54e-06

Exosome complex RNA-binding protein Rrp42, RNase PH superfamily [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441726 [Multi-domain]  Cd Length: 264  Bit Score: 47.87  E-value: 1.54e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1131173046   4 LELLSdQGYRVDGRRAGELRKIQARMGVFAQADGSAYIEQGNTKALAVV 52
Cdd:COG2123    15 LSLLK-KGKRIDGRGLDEYRPIEIETGVIEKAEGSALVKLGNTQVLAGV 62
PRK04282 PRK04282
exosome complex protein Rrp42;
4-52 3.00e-06

exosome complex protein Rrp42;


Pssm-ID: 235268 [Multi-domain]  Cd Length: 271  Bit Score: 47.18  E-value: 3.00e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1131173046   4 LELLSdQGYRVDGRRAGELRKIQARMGVFAQADGSAYIEQGNTKALAVV 52
Cdd:PRK04282   17 LSLLK-KGKRIDGRKLDEYRPIEIETGVIKKAEGSALVKLGNTQVLAGV 64
RNase_PH_PNPase_2 cd11364
Polyribonucleotide nucleotidyltransferase, repeat 2; Polyribonucleotide nucleotidyltransferase ...
 21-165 7.61e-06

Polyribonucleotide nucleotidyltransferase, repeat 2; Polyribonucleotide nucleotidyltransferase (PNPase) is a member of the RNase_PH family, named after the bacterial Ribonuclease PH, a 3'-5' exoribonuclease. Structurally, all members of this family form hexameric rings. In the case of PNPase the complex is a trimer, since each monomer contains two tandem copies of the domain. PNPase is involved in mRNA degradation in a 3'-5' direction and in quality control of ribosomal RNA precursors, with the second repeat containing the active site. PNPase is part of the RNA degradosome complex and binds to the scaffolding domain of the endoribonuclease RNase E.


Pssm-ID: 206769 [Multi-domain]  Cd Length: 223  Bit Score: 45.62  E-value: 7.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131173046  21 ELRKIQARMGVFAQADGSAYIEQGNTKALAVV-YGPHEiRGSRARALPD----RALVncQYSSATFSTGERKR-RPHGDR 94
Cdd:cd11364     1 EIRPISCEVGLLPRTHGSALFTRGETQVLCTVtLGTLE-DAQKIDSLGGekskRFML--HYNFPPYSVGETGRvGGPGRR 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1131173046  95 kscEMG---LQlrqtfEAAILTQLHPRSQ----IDIYVQVLQADGGTYAACVNAATLAVLDAGIPMRDFVCACSAGFV 165
Cdd:cd11364    78 ---EIGhgaLA-----ERALLPVLPSPEDfpytIRVVSEVLESNGSSSMASVCGGSLALMDAGVPIKAPVAGIAMGLI 147
RNase_PH_RRP45 cd11368
RRP45 subunit of eukaryotic exosome; The RRP45 subunit of eukaryotic exosome is a member of ...
 10-52 3.62e-05

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: 43.67  E-value: 3.62e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1131173046  10 QGYRVDGRRAGELRKIQARmgvFAQADGSAYIEQGNTKALAVV 52
Cdd:cd11368    15 EGLRLDGRGLDEFRPIKIT---FGLEYGCVEVSLGKTRVLAQV 54
RNase_PH_RRP43 cd11369
RRP43 subunit of eukaryotic exosome; The RRP43 subunit of eukaryotic exosome is a member of ...
 9-50 5.30e-04

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: 40.23  E-value: 5.30e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1131173046   9 DQGYRVDGRRAGELRKIQARMGVFAQADGSAYIEQGNTKALA 50
Cdd:cd11369    14 AENVRPDGRELDEFRPTSVNVGSISTADGSALVKLGNTTVLC 55
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
 9-52 2.94e-03

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 38.49  E-value: 2.94e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1131173046   9 DQGYRVDGRRAGELRKIQARMGVFAQADGSAYIEQGNTKALAVV 52
Cdd:PRK11824  311 EEGIRIDGRKLDEIRPISIEVGVLPRTHGSALFTRGETQALVVA 354
RNase_PH_RRP42 cd11367
RRP42 subunit of eukaryotic exosome; The RRP42 subunit of eukaryotic exosome is a member of ...
 10-152 4.74e-03

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: 37.58  E-value: 4.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131173046  10 QGYRVDGRRAGELRKIQARMGVFAQADGSAYIEQGNTKALAVVYGphEIrGSRARALPDRALVNCQYS-SATFSTGERKR 88
Cdd:cd11367    16 QNIRNDGRSRLDYRPIELETGVLSNTNGSARVRLGNTDVLVGVKA--EV-GSPDPETPNKGRLEFFVDcSPNASPEFEGR 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131173046  89 rpHGDRKSCEMGLQLRQTFEAAIL-----TQLHPRSQI-DIYVQ--VLQADGGTYAACVNAATLAVLDAGIP 152
Cdd:cd11367    93 --GGEELATELSSALERALKSGSAidlskLCIVPGKQCwVLYVDvlVLESGGNLLDAISIAVKAALFNTRIP 162
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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