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Conserved domains on  [gi|1002298433|ref|XP_015612636|]
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CRM-domain containing factor CFM3, chloroplastic/mitochondrial [Oryza sativa Japonica Group]

Protein Classification

YhbY family RNA-binding protein( domain architecture ID 10488007)

YhbY family RNA-binding protein similar to ribosome assembly RNA-binding protein YhbY that adopts a fold resembling that of the C-terminal domain of translation initiation factor 3 (IF3C), which binds to 16S rRNA in the 30S ribosome

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CRS1_YhbY pfam01985
CRS1 / YhbY (CRM) domain; Escherichia coli YhbY is associated with pre-50S ribosomal subunits, ...
 341-424 7.79e-22

CRS1 / YhbY (CRM) domain; Escherichia coli YhbY is associated with pre-50S ribosomal subunits, which implies a function in ribosome assembly. GFP fused to a single-domain CRM protein from maize localizes to the nucleolus, suggesting that an analogous activity may have been retained in plants. A CRM domain containing protein in plant chloroplasts has been shown to function in group I and II intron splicing. In vitro experiments with an isolated maize CRM domain have shown it to have RNA binding activity. These and other results suggest that the CRM domain evolved in the context of ribosome function prior to the divergence of Archaea and Bacteria, that this function has been maintained in extant prokaryotes, and that the domain was recruited to serve as an RNA binding module during the evolution of plant genomes. YhbY has a fold similar to that of the C-terminal domain of translation initiation factor 3 (IF3C), which binds to 16S rRNA in the 30S ribosome.


:

Pssm-ID: 460405  Cd Length: 84  Bit Score: 90.15  E-value: 7.79e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298433 341 IPEHELRRLRDVALRMKERMRVGPGGVTQLIVESIHQKWRVEEVVKLRFEGPPSLNMKRTHDILEERTGGIVIWRSGRSV 420
Cdd:pfam01985   1 LTSKERRYLRKLAHHLKPIVQIGKNGVTEGVVEEIHEALEARELIKVKVLKNCREDRKEIAEELAEKTGAEVVQVIGRTI 80


                  ....
gi 1002298433 421 VLYR 424
Cdd:pfam01985  81 VLYR 84
CRS1_YhbY smart01103
Escherichia coli YhbY is associated with pre-50S ribosomal subunits, which implies a function ...
 752-838 1.04e-21

Escherichia coli YhbY is associated with pre-50S ribosomal subunits, which implies a function in ribosome assembly; GFP fused to a single-domain CRM protein from maize localises to the nucleolus, suggesting that an analogous activity may have been retained in plants. A CRM domain containing protein in plant chloroplasts has been shown to function in group I and II intron splicing. In vitro experiments with an isolated maize CRM domain have shown it to have RNA binding activity. These and other results suggest that the CRM domain evolved in the context of ribosome function prior to the divergence of Archaea and Bacteria, that this function has been maintained in extant prokaryotes, and that the domain was recruited to serve as an RNA binding module during the evolution of plant genomes. YhbY has a fold similar to that of the C-terminal domain of translation initiation factor 3 (IF3C), which binds to 16S rRNA in the 30S ribosome.


:

Pssm-ID: 198171  Cd Length: 84  Bit Score: 89.83  E-value: 1.04e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298433  752 TDEERFLLRRIGLKMKAFLMLGRREVFDGTVQNMHLHWKHRELVKVLVKGKSFPQVKHIAISLEAESGGVLISVdkttKG 831
Cdd:smart01103   2 TGKQKRYLRSLAHHLKPVVQIGKNGLTEGVLEEIDEALEKHELIKVKVLGNDREDRKEIAEELAEETGAELVQV----IG 77


                   ....*..
gi 1002298433  832 YAIILYR 838
Cdd:smart01103  78 KTIVLYR 84
CRS1_YhbY pfam01985
CRS1 / YhbY (CRM) domain; Escherichia coli YhbY is associated with pre-50S ribosomal subunits, ...
 538-622 8.74e-18

CRS1 / YhbY (CRM) domain; Escherichia coli YhbY is associated with pre-50S ribosomal subunits, which implies a function in ribosome assembly. GFP fused to a single-domain CRM protein from maize localizes to the nucleolus, suggesting that an analogous activity may have been retained in plants. A CRM domain containing protein in plant chloroplasts has been shown to function in group I and II intron splicing. In vitro experiments with an isolated maize CRM domain have shown it to have RNA binding activity. These and other results suggest that the CRM domain evolved in the context of ribosome function prior to the divergence of Archaea and Bacteria, that this function has been maintained in extant prokaryotes, and that the domain was recruited to serve as an RNA binding module during the evolution of plant genomes. YhbY has a fold similar to that of the C-terminal domain of translation initiation factor 3 (IF3C), which binds to 16S rRNA in the 30S ribosome.


:

Pssm-ID: 460405  Cd Length: 84  Bit Score: 78.98  E-value: 8.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298433 538 LRNKEMTALRRLARQTAPHFALGRNREHQGLATAIVKLWEKSSIAKIAIKRGVPNTCnDRMAEEIRKLTGGVLLSRNKEY 617
Cdd:pfam01985   1 LTSKERRYLRKLAHHLKPIVQIGKNGVTEGVVEEIHEALEARELIKVKVLKNCREDR-KEIAEELAEKTGAEVVQVIGRT 79


                  ....*
gi 1002298433 618 IVFYR 622
Cdd:pfam01985  80 IVLYR 84
 
Name Accession Description Interval E-value
CRS1_YhbY pfam01985
CRS1 / YhbY (CRM) domain; Escherichia coli YhbY is associated with pre-50S ribosomal subunits, ...
 341-424 7.79e-22

CRS1 / YhbY (CRM) domain; Escherichia coli YhbY is associated with pre-50S ribosomal subunits, which implies a function in ribosome assembly. GFP fused to a single-domain CRM protein from maize localizes to the nucleolus, suggesting that an analogous activity may have been retained in plants. A CRM domain containing protein in plant chloroplasts has been shown to function in group I and II intron splicing. In vitro experiments with an isolated maize CRM domain have shown it to have RNA binding activity. These and other results suggest that the CRM domain evolved in the context of ribosome function prior to the divergence of Archaea and Bacteria, that this function has been maintained in extant prokaryotes, and that the domain was recruited to serve as an RNA binding module during the evolution of plant genomes. YhbY has a fold similar to that of the C-terminal domain of translation initiation factor 3 (IF3C), which binds to 16S rRNA in the 30S ribosome.


Pssm-ID: 460405  Cd Length: 84  Bit Score: 90.15  E-value: 7.79e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298433 341 IPEHELRRLRDVALRMKERMRVGPGGVTQLIVESIHQKWRVEEVVKLRFEGPPSLNMKRTHDILEERTGGIVIWRSGRSV 420
Cdd:pfam01985   1 LTSKERRYLRKLAHHLKPIVQIGKNGVTEGVVEEIHEALEARELIKVKVLKNCREDRKEIAEELAEKTGAEVVQVIGRTI 80


                  ....
gi 1002298433 421 VLYR 424
Cdd:pfam01985  81 VLYR 84
CRS1_YhbY smart01103
Escherichia coli YhbY is associated with pre-50S ribosomal subunits, which implies a function ...
 752-838 1.04e-21

Escherichia coli YhbY is associated with pre-50S ribosomal subunits, which implies a function in ribosome assembly; GFP fused to a single-domain CRM protein from maize localises to the nucleolus, suggesting that an analogous activity may have been retained in plants. A CRM domain containing protein in plant chloroplasts has been shown to function in group I and II intron splicing. In vitro experiments with an isolated maize CRM domain have shown it to have RNA binding activity. These and other results suggest that the CRM domain evolved in the context of ribosome function prior to the divergence of Archaea and Bacteria, that this function has been maintained in extant prokaryotes, and that the domain was recruited to serve as an RNA binding module during the evolution of plant genomes. YhbY has a fold similar to that of the C-terminal domain of translation initiation factor 3 (IF3C), which binds to 16S rRNA in the 30S ribosome.


Pssm-ID: 198171  Cd Length: 84  Bit Score: 89.83  E-value: 1.04e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298433  752 TDEERFLLRRIGLKMKAFLMLGRREVFDGTVQNMHLHWKHRELVKVLVKGKSFPQVKHIAISLEAESGGVLISVdkttKG 831
Cdd:smart01103   2 TGKQKRYLRSLAHHLKPVVQIGKNGLTEGVLEEIDEALEKHELIKVKVLGNDREDRKEIAEELAEETGAELVQV----IG 77


                   ....*..
gi 1002298433  832 YAIILYR 838
Cdd:smart01103  78 KTIVLYR 84
CRS1_YhbY pfam01985
CRS1 / YhbY (CRM) domain; Escherichia coli YhbY is associated with pre-50S ribosomal subunits, ...
 752-838 1.26e-21

CRS1 / YhbY (CRM) domain; Escherichia coli YhbY is associated with pre-50S ribosomal subunits, which implies a function in ribosome assembly. GFP fused to a single-domain CRM protein from maize localizes to the nucleolus, suggesting that an analogous activity may have been retained in plants. A CRM domain containing protein in plant chloroplasts has been shown to function in group I and II intron splicing. In vitro experiments with an isolated maize CRM domain have shown it to have RNA binding activity. These and other results suggest that the CRM domain evolved in the context of ribosome function prior to the divergence of Archaea and Bacteria, that this function has been maintained in extant prokaryotes, and that the domain was recruited to serve as an RNA binding module during the evolution of plant genomes. YhbY has a fold similar to that of the C-terminal domain of translation initiation factor 3 (IF3C), which binds to 16S rRNA in the 30S ribosome.


Pssm-ID: 460405  Cd Length: 84  Bit Score: 89.77  E-value: 1.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298433 752 TDEERFLLRRIGLKMKAFLMLGRREVFDGTVQNMHLHWKHRELVKVLVKGKSFPQVKHIAISLEAESGGVLISVdkttKG 831
Cdd:pfam01985   2 TSKERRYLRKLAHHLKPIVQIGKNGVTEGVVEEIHEALEARELIKVKVLKNCREDRKEIAEELAEKTGAEVVQV----IG 77


                  ....*..
gi 1002298433 832 YAIILYR 838
Cdd:pfam01985  78 RTIVLYR 84
CRS1_YhbY smart01103
Escherichia coli YhbY is associated with pre-50S ribosomal subunits, which implies a function ...
 341-424 3.33e-19

Escherichia coli YhbY is associated with pre-50S ribosomal subunits, which implies a function in ribosome assembly; GFP fused to a single-domain CRM protein from maize localises to the nucleolus, suggesting that an analogous activity may have been retained in plants. A CRM domain containing protein in plant chloroplasts has been shown to function in group I and II intron splicing. In vitro experiments with an isolated maize CRM domain have shown it to have RNA binding activity. These and other results suggest that the CRM domain evolved in the context of ribosome function prior to the divergence of Archaea and Bacteria, that this function has been maintained in extant prokaryotes, and that the domain was recruited to serve as an RNA binding module during the evolution of plant genomes. YhbY has a fold similar to that of the C-terminal domain of translation initiation factor 3 (IF3C), which binds to 16S rRNA in the 30S ribosome.


Pssm-ID: 198171  Cd Length: 84  Bit Score: 82.90  E-value: 3.33e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298433  341 IPEHELRRLRDVALRMKERMRVGPGGVTQLIVESIHQKWRVEEVVKLRFEGPPSLNMKRTHDILEERTGGIVIWRSGRSV 420
Cdd:smart01103   1 LTGKQKRYLRSLAHHLKPVVQIGKNGLTEGVLEEIDEALEKHELIKVKVLGNDREDRKEIAEELAEETGAELVQVIGKTI 80


                   ....
gi 1002298433  421 VLYR 424
Cdd:smart01103  81 VLYR 84
CRS1_YhbY pfam01985
CRS1 / YhbY (CRM) domain; Escherichia coli YhbY is associated with pre-50S ribosomal subunits, ...
 538-622 8.74e-18

CRS1 / YhbY (CRM) domain; Escherichia coli YhbY is associated with pre-50S ribosomal subunits, which implies a function in ribosome assembly. GFP fused to a single-domain CRM protein from maize localizes to the nucleolus, suggesting that an analogous activity may have been retained in plants. A CRM domain containing protein in plant chloroplasts has been shown to function in group I and II intron splicing. In vitro experiments with an isolated maize CRM domain have shown it to have RNA binding activity. These and other results suggest that the CRM domain evolved in the context of ribosome function prior to the divergence of Archaea and Bacteria, that this function has been maintained in extant prokaryotes, and that the domain was recruited to serve as an RNA binding module during the evolution of plant genomes. YhbY has a fold similar to that of the C-terminal domain of translation initiation factor 3 (IF3C), which binds to 16S rRNA in the 30S ribosome.


Pssm-ID: 460405  Cd Length: 84  Bit Score: 78.98  E-value: 8.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298433 538 LRNKEMTALRRLARQTAPHFALGRNREHQGLATAIVKLWEKSSIAKIAIKRGVPNTCnDRMAEEIRKLTGGVLLSRNKEY 617
Cdd:pfam01985   1 LTSKERRYLRKLAHHLKPIVQIGKNGVTEGVVEEIHEALEARELIKVKVLKNCREDR-KEIAEELAEKTGAEVVQVIGRT 79


                  ....*
gi 1002298433 618 IVFYR 622
Cdd:pfam01985  80 IVLYR 84
CRS1_YhbY smart01103
Escherichia coli YhbY is associated with pre-50S ribosomal subunits, which implies a function ...
 538-622 2.85e-17

Escherichia coli YhbY is associated with pre-50S ribosomal subunits, which implies a function in ribosome assembly; GFP fused to a single-domain CRM protein from maize localises to the nucleolus, suggesting that an analogous activity may have been retained in plants. A CRM domain containing protein in plant chloroplasts has been shown to function in group I and II intron splicing. In vitro experiments with an isolated maize CRM domain have shown it to have RNA binding activity. These and other results suggest that the CRM domain evolved in the context of ribosome function prior to the divergence of Archaea and Bacteria, that this function has been maintained in extant prokaryotes, and that the domain was recruited to serve as an RNA binding module during the evolution of plant genomes. YhbY has a fold similar to that of the C-terminal domain of translation initiation factor 3 (IF3C), which binds to 16S rRNA in the 30S ribosome.


Pssm-ID: 198171  Cd Length: 84  Bit Score: 77.50  E-value: 2.85e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298433  538 LRNKEMTALRRLARQTAPHFALGRNREHQGLATAIVKLWEKSSIAKIAIKrGVPNTCNDRMAEEIRKLTGGVLLSRNKEY 617
Cdd:smart01103   1 LTGKQKRYLRSLAHHLKPVVQIGKNGLTEGVLEEIDEALEKHELIKVKVL-GNDREDRKEIAEELAEETGAELVQVIGKT 79


                   ....*
gi 1002298433  618 IVFYR 622
Cdd:smart01103  80 IVLYR 84
 
Name Accession Description Interval E-value
CRS1_YhbY pfam01985
CRS1 / YhbY (CRM) domain; Escherichia coli YhbY is associated with pre-50S ribosomal subunits, ...
 341-424 7.79e-22

CRS1 / YhbY (CRM) domain; Escherichia coli YhbY is associated with pre-50S ribosomal subunits, which implies a function in ribosome assembly. GFP fused to a single-domain CRM protein from maize localizes to the nucleolus, suggesting that an analogous activity may have been retained in plants. A CRM domain containing protein in plant chloroplasts has been shown to function in group I and II intron splicing. In vitro experiments with an isolated maize CRM domain have shown it to have RNA binding activity. These and other results suggest that the CRM domain evolved in the context of ribosome function prior to the divergence of Archaea and Bacteria, that this function has been maintained in extant prokaryotes, and that the domain was recruited to serve as an RNA binding module during the evolution of plant genomes. YhbY has a fold similar to that of the C-terminal domain of translation initiation factor 3 (IF3C), which binds to 16S rRNA in the 30S ribosome.


Pssm-ID: 460405  Cd Length: 84  Bit Score: 90.15  E-value: 7.79e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298433 341 IPEHELRRLRDVALRMKERMRVGPGGVTQLIVESIHQKWRVEEVVKLRFEGPPSLNMKRTHDILEERTGGIVIWRSGRSV 420
Cdd:pfam01985   1 LTSKERRYLRKLAHHLKPIVQIGKNGVTEGVVEEIHEALEARELIKVKVLKNCREDRKEIAEELAEKTGAEVVQVIGRTI 80


                  ....
gi 1002298433 421 VLYR 424
Cdd:pfam01985  81 VLYR 84
CRS1_YhbY smart01103
Escherichia coli YhbY is associated with pre-50S ribosomal subunits, which implies a function ...
 752-838 1.04e-21

Escherichia coli YhbY is associated with pre-50S ribosomal subunits, which implies a function in ribosome assembly; GFP fused to a single-domain CRM protein from maize localises to the nucleolus, suggesting that an analogous activity may have been retained in plants. A CRM domain containing protein in plant chloroplasts has been shown to function in group I and II intron splicing. In vitro experiments with an isolated maize CRM domain have shown it to have RNA binding activity. These and other results suggest that the CRM domain evolved in the context of ribosome function prior to the divergence of Archaea and Bacteria, that this function has been maintained in extant prokaryotes, and that the domain was recruited to serve as an RNA binding module during the evolution of plant genomes. YhbY has a fold similar to that of the C-terminal domain of translation initiation factor 3 (IF3C), which binds to 16S rRNA in the 30S ribosome.


Pssm-ID: 198171  Cd Length: 84  Bit Score: 89.83  E-value: 1.04e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298433  752 TDEERFLLRRIGLKMKAFLMLGRREVFDGTVQNMHLHWKHRELVKVLVKGKSFPQVKHIAISLEAESGGVLISVdkttKG 831
Cdd:smart01103   2 TGKQKRYLRSLAHHLKPVVQIGKNGLTEGVLEEIDEALEKHELIKVKVLGNDREDRKEIAEELAEETGAELVQV----IG 77


                   ....*..
gi 1002298433  832 YAIILYR 838
Cdd:smart01103  78 KTIVLYR 84
CRS1_YhbY pfam01985
CRS1 / YhbY (CRM) domain; Escherichia coli YhbY is associated with pre-50S ribosomal subunits, ...
 752-838 1.26e-21

CRS1 / YhbY (CRM) domain; Escherichia coli YhbY is associated with pre-50S ribosomal subunits, which implies a function in ribosome assembly. GFP fused to a single-domain CRM protein from maize localizes to the nucleolus, suggesting that an analogous activity may have been retained in plants. A CRM domain containing protein in plant chloroplasts has been shown to function in group I and II intron splicing. In vitro experiments with an isolated maize CRM domain have shown it to have RNA binding activity. These and other results suggest that the CRM domain evolved in the context of ribosome function prior to the divergence of Archaea and Bacteria, that this function has been maintained in extant prokaryotes, and that the domain was recruited to serve as an RNA binding module during the evolution of plant genomes. YhbY has a fold similar to that of the C-terminal domain of translation initiation factor 3 (IF3C), which binds to 16S rRNA in the 30S ribosome.


Pssm-ID: 460405  Cd Length: 84  Bit Score: 89.77  E-value: 1.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298433 752 TDEERFLLRRIGLKMKAFLMLGRREVFDGTVQNMHLHWKHRELVKVLVKGKSFPQVKHIAISLEAESGGVLISVdkttKG 831
Cdd:pfam01985   2 TSKERRYLRKLAHHLKPIVQIGKNGVTEGVVEEIHEALEARELIKVKVLKNCREDRKEIAEELAEKTGAEVVQV----IG 77


                  ....*..
gi 1002298433 832 YAIILYR 838
Cdd:pfam01985  78 RTIVLYR 84
CRS1_YhbY smart01103
Escherichia coli YhbY is associated with pre-50S ribosomal subunits, which implies a function ...
 341-424 3.33e-19

Escherichia coli YhbY is associated with pre-50S ribosomal subunits, which implies a function in ribosome assembly; GFP fused to a single-domain CRM protein from maize localises to the nucleolus, suggesting that an analogous activity may have been retained in plants. A CRM domain containing protein in plant chloroplasts has been shown to function in group I and II intron splicing. In vitro experiments with an isolated maize CRM domain have shown it to have RNA binding activity. These and other results suggest that the CRM domain evolved in the context of ribosome function prior to the divergence of Archaea and Bacteria, that this function has been maintained in extant prokaryotes, and that the domain was recruited to serve as an RNA binding module during the evolution of plant genomes. YhbY has a fold similar to that of the C-terminal domain of translation initiation factor 3 (IF3C), which binds to 16S rRNA in the 30S ribosome.


Pssm-ID: 198171  Cd Length: 84  Bit Score: 82.90  E-value: 3.33e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298433  341 IPEHELRRLRDVALRMKERMRVGPGGVTQLIVESIHQKWRVEEVVKLRFEGPPSLNMKRTHDILEERTGGIVIWRSGRSV 420
Cdd:smart01103   1 LTGKQKRYLRSLAHHLKPVVQIGKNGLTEGVLEEIDEALEKHELIKVKVLGNDREDRKEIAEELAEETGAELVQVIGKTI 80


                   ....
gi 1002298433  421 VLYR 424
Cdd:smart01103  81 VLYR 84
CRS1_YhbY pfam01985
CRS1 / YhbY (CRM) domain; Escherichia coli YhbY is associated with pre-50S ribosomal subunits, ...
 538-622 8.74e-18

CRS1 / YhbY (CRM) domain; Escherichia coli YhbY is associated with pre-50S ribosomal subunits, which implies a function in ribosome assembly. GFP fused to a single-domain CRM protein from maize localizes to the nucleolus, suggesting that an analogous activity may have been retained in plants. A CRM domain containing protein in plant chloroplasts has been shown to function in group I and II intron splicing. In vitro experiments with an isolated maize CRM domain have shown it to have RNA binding activity. These and other results suggest that the CRM domain evolved in the context of ribosome function prior to the divergence of Archaea and Bacteria, that this function has been maintained in extant prokaryotes, and that the domain was recruited to serve as an RNA binding module during the evolution of plant genomes. YhbY has a fold similar to that of the C-terminal domain of translation initiation factor 3 (IF3C), which binds to 16S rRNA in the 30S ribosome.


Pssm-ID: 460405  Cd Length: 84  Bit Score: 78.98  E-value: 8.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298433 538 LRNKEMTALRRLARQTAPHFALGRNREHQGLATAIVKLWEKSSIAKIAIKRGVPNTCnDRMAEEIRKLTGGVLLSRNKEY 617
Cdd:pfam01985   1 LTSKERRYLRKLAHHLKPIVQIGKNGVTEGVVEEIHEALEARELIKVKVLKNCREDR-KEIAEELAEKTGAEVVQVIGRT 79


                  ....*
gi 1002298433 618 IVFYR 622
Cdd:pfam01985  80 IVLYR 84
CRS1_YhbY smart01103
Escherichia coli YhbY is associated with pre-50S ribosomal subunits, which implies a function ...
 538-622 2.85e-17

Escherichia coli YhbY is associated with pre-50S ribosomal subunits, which implies a function in ribosome assembly; GFP fused to a single-domain CRM protein from maize localises to the nucleolus, suggesting that an analogous activity may have been retained in plants. A CRM domain containing protein in plant chloroplasts has been shown to function in group I and II intron splicing. In vitro experiments with an isolated maize CRM domain have shown it to have RNA binding activity. These and other results suggest that the CRM domain evolved in the context of ribosome function prior to the divergence of Archaea and Bacteria, that this function has been maintained in extant prokaryotes, and that the domain was recruited to serve as an RNA binding module during the evolution of plant genomes. YhbY has a fold similar to that of the C-terminal domain of translation initiation factor 3 (IF3C), which binds to 16S rRNA in the 30S ribosome.


Pssm-ID: 198171  Cd Length: 84  Bit Score: 77.50  E-value: 2.85e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298433  538 LRNKEMTALRRLARQTAPHFALGRNREHQGLATAIVKLWEKSSIAKIAIKrGVPNTCNDRMAEEIRKLTGGVLLSRNKEY 617
Cdd:smart01103   1 LTGKQKRYLRSLAHHLKPVVQIGKNGLTEGVLEEIDEALEKHELIKVKVL-GNDREDRKEIAEELAEETGAELVQVIGKT 79


                   ....*
gi 1002298433  618 IVFYR 622
Cdd:smart01103  80 IVLYR 84
 
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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