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Conserved domains on  [gi|1876456491|ref|WP_180344218|]
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ribosome-associated heat shock protein Hsp15 [Aeromonas allosaccharophila]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
S4 super family cl09940
S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, ...
 6-130 9.00e-51

S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, charged residues that define a likely RNA-binding site; Found in stress proteins, ribosomal proteins and tRNA synthetases; This may imply a hitherto unrecognized functional similarity between these three protein classes.


The actual alignment was detected with superfamily member PRK10348:

Pssm-ID: 447867  Cd Length: 133  Bit Score: 157.50  E-value: 9.00e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1876456491   6 ESALEVRLDKWLWAARFYKARSVARDQIDGGKVHYNGQRSKPGKQVEVGALIRFWQGQDEREVRVLALSEQRKSAPLAQQ 85
Cdd:PRK10348    4 KPAVEVRLDKWLWAARFYKTRALAREMIEGGKVHYNGQRSKPSKIVELNATLTLRQGNDERTVIVKAITEQRRPASEAAL 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1876456491  86 LYEETAESLKKRAKNSEARRFNSQFAPSPERRPDKQERRQLLKVK 130
Cdd:PRK10348   84 LYEETAESVEKREKMALARKLNALTMPHPDRRPDKKERRDLLRFK 128
 
Name Accession Description Interval E-value
PRK10348 PRK10348
ribosome-associated heat shock protein Hsp15; Provisional
 6-130 9.00e-51

ribosome-associated heat shock protein Hsp15; Provisional


Pssm-ID: 182397  Cd Length: 133  Bit Score: 157.50  E-value: 9.00e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1876456491   6 ESALEVRLDKWLWAARFYKARSVARDQIDGGKVHYNGQRSKPGKQVEVGALIRFWQGQDEREVRVLALSEQRKSAPLAQQ 85
Cdd:PRK10348    4 KPAVEVRLDKWLWAARFYKTRALAREMIEGGKVHYNGQRSKPSKIVELNATLTLRQGNDERTVIVKAITEQRRPASEAAL 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1876456491  86 LYEETAESLKKRAKNSEARRFNSQFAPSPERRPDKQERRQLLKVK 130
Cdd:PRK10348   84 LYEETAESVEKREKMALARKLNALTMPHPDRRPDKKERRDLLRFK 128
HslR COG1188
Ribosomal 50S subunit-recycling heat shock protein, contains S4 domain [Translation, ribosomal ...
 11-131 1.77e-47

Ribosomal 50S subunit-recycling heat shock protein, contains S4 domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440801  Cd Length: 120  Bit Score: 148.83  E-value: 1.77e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1876456491  11 VRLDKWLWAARFYKARSVARDQIDGGKVHYNGQRSKPGKQVEVGALIRFWQGQDEREVRVLALSEQRKSAPLAQQLYEET 90
Cdd:COG1188     5 MRLDKWLWAARFFKTRSLAAEACDGGRVRVNGQRAKPSREVKVGDVLTIRQGGRERVVRVLALSERRGPAPEAQLLYEEL 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1876456491  91 AESLKKRAKNSEArrfnsQFAPSPERRPDKQERRQLLKVKQ 131
Cdd:COG1188    85 TPSPAPREEAAAA-----APRPRGAGRPTKKDRRELDRFRG 120
S4 cd00165
S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, ...
 11-82 9.93e-09

S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, charged residues that define a likely RNA-binding site; Found in stress proteins, ribosomal proteins and tRNA synthetases; This may imply a hitherto unrecognized functional similarity between these three protein classes.


Pssm-ID: 238095 [Multi-domain]  Cd Length: 70  Bit Score: 48.40  E-value: 9.93e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1876456491  11 VRLDKWLWAARFYKARSVARDQIDGGKVHYNGQR-SKPGKQVEVGALIRFwqgqDEREVRVLALSEQRKSAPL 82
Cdd:cd00165     1 MRLDKILARLGLAPSRSEARQLIKHGHVLVNGKVvTKPSYKVKPGDVIEV----DGKSIEEDIVYEDKKLLVV 69
S4 pfam01479
S4 domain; The S4 domain is a small domain consisting of 60-65 amino acid residues that was ...
 11-57 2.14e-08

S4 domain; The S4 domain is a small domain consisting of 60-65 amino acid residues that was detected in the bacterial ribosomal protein S4, eukaryotic ribosomal S9, two families of pseudouridine synthases, a novel family of predicted RNA methylases, a yeast protein containing a pseudouridine synthetase and a deaminase domain, bacterial tyrosyl-tRNA synthetases, and a number of uncharacterized, small proteins that may be involved in translation regulation. The S4 domain probably mediates binding to RNA.


Pssm-ID: 396182 [Multi-domain]  Cd Length: 48  Bit Score: 47.10  E-value: 2.14e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1876456491  11 VRLDKWLWAARFYKARSVARDQIDGGKVHYNGQR-SKPGKQVEVGALI 57
Cdd:pfam01479   1 RRLDKVLARLGLASSRSQARQLIEHGRVLVNGKVvKDPSYRVKPGDEI 48
S4 smart00363
S4 RNA-binding domain;
11-66 1.51e-07

S4 RNA-binding domain;


Pssm-ID: 214638 [Multi-domain]  Cd Length: 60  Bit Score: 45.28  E-value: 1.51e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1876456491   11 VRLDKWLWAARFYKARSVARDQIDGGKVHYNGQR-SKPGKQVEVGALIRFWQGQDER 66
Cdd:smart00363   1 RRLDKFLARLGLAPSRSQARRLIEQGRVKVNGKKvTKPSYIVKPGDVISVRGKELKR 57
 
Name Accession Description Interval E-value
PRK10348 PRK10348
ribosome-associated heat shock protein Hsp15; Provisional
 6-130 9.00e-51

ribosome-associated heat shock protein Hsp15; Provisional


Pssm-ID: 182397  Cd Length: 133  Bit Score: 157.50  E-value: 9.00e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1876456491   6 ESALEVRLDKWLWAARFYKARSVARDQIDGGKVHYNGQRSKPGKQVEVGALIRFWQGQDEREVRVLALSEQRKSAPLAQQ 85
Cdd:PRK10348    4 KPAVEVRLDKWLWAARFYKTRALAREMIEGGKVHYNGQRSKPSKIVELNATLTLRQGNDERTVIVKAITEQRRPASEAAL 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1876456491  86 LYEETAESLKKRAKNSEARRFNSQFAPSPERRPDKQERRQLLKVK 130
Cdd:PRK10348   84 LYEETAESVEKREKMALARKLNALTMPHPDRRPDKKERRDLLRFK 128
HslR COG1188
Ribosomal 50S subunit-recycling heat shock protein, contains S4 domain [Translation, ribosomal ...
 11-131 1.77e-47

Ribosomal 50S subunit-recycling heat shock protein, contains S4 domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440801  Cd Length: 120  Bit Score: 148.83  E-value: 1.77e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1876456491  11 VRLDKWLWAARFYKARSVARDQIDGGKVHYNGQRSKPGKQVEVGALIRFWQGQDEREVRVLALSEQRKSAPLAQQLYEET 90
Cdd:COG1188     5 MRLDKWLWAARFFKTRSLAAEACDGGRVRVNGQRAKPSREVKVGDVLTIRQGGRERVVRVLALSERRGPAPEAQLLYEEL 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1876456491  91 AESLKKRAKNSEArrfnsQFAPSPERRPDKQERRQLLKVKQ 131
Cdd:COG1188    85 TPSPAPREEAAAA-----APRPRGAGRPTKKDRRELDRFRG 120
S4 cd00165
S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, ...
 11-82 9.93e-09

S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, charged residues that define a likely RNA-binding site; Found in stress proteins, ribosomal proteins and tRNA synthetases; This may imply a hitherto unrecognized functional similarity between these three protein classes.


Pssm-ID: 238095 [Multi-domain]  Cd Length: 70  Bit Score: 48.40  E-value: 9.93e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1876456491  11 VRLDKWLWAARFYKARSVARDQIDGGKVHYNGQR-SKPGKQVEVGALIRFwqgqDEREVRVLALSEQRKSAPL 82
Cdd:cd00165     1 MRLDKILARLGLAPSRSEARQLIKHGHVLVNGKVvTKPSYKVKPGDVIEV----DGKSIEEDIVYEDKKLLVV 69
S4 pfam01479
S4 domain; The S4 domain is a small domain consisting of 60-65 amino acid residues that was ...
 11-57 2.14e-08

S4 domain; The S4 domain is a small domain consisting of 60-65 amino acid residues that was detected in the bacterial ribosomal protein S4, eukaryotic ribosomal S9, two families of pseudouridine synthases, a novel family of predicted RNA methylases, a yeast protein containing a pseudouridine synthetase and a deaminase domain, bacterial tyrosyl-tRNA synthetases, and a number of uncharacterized, small proteins that may be involved in translation regulation. The S4 domain probably mediates binding to RNA.


Pssm-ID: 396182 [Multi-domain]  Cd Length: 48  Bit Score: 47.10  E-value: 2.14e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1876456491  11 VRLDKWLWAARFYKARSVARDQIDGGKVHYNGQR-SKPGKQVEVGALI 57
Cdd:pfam01479   1 RRLDKVLARLGLASSRSQARQLIEHGRVLVNGKVvKDPSYRVKPGDEI 48
S4 smart00363
S4 RNA-binding domain;
11-66 1.51e-07

S4 RNA-binding domain;


Pssm-ID: 214638 [Multi-domain]  Cd Length: 60  Bit Score: 45.28  E-value: 1.51e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1876456491   11 VRLDKWLWAARFYKARSVARDQIDGGKVHYNGQR-SKPGKQVEVGALIRFWQGQDER 66
Cdd:smart00363   1 RRLDKFLARLGLAPSRSQARRLIEQGRVKVNGKKvTKPSYIVKPGDVISVRGKELKR 57
 
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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