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Conserved domains on  [gi|489009767|ref|WP_002920326|]
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MULTISPECIES: ribosome-associated heat shock protein Hsp15 [Klebsiella]

Protein Classification

ribosome-associated heat shock protein Hsp15( domain architecture ID 10793378)

ribosome-associated heat shock protein Hsp15 is involved in the recycling of free 50S ribosomal subunits that still carry a nascent chain

Gene Symbol:  hslR
Gene Ontology:  GO:0003676|GO:0043023|GO:0034605
PubMed:  10675344|10675343|9867837
SCOP:  4001401

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10348 PRK10348
ribosome-associated heat shock protein Hsp15; Provisional
 1-133 4.72e-88

ribosome-associated heat shock protein Hsp15; Provisional


:

Pssm-ID: 182397  Cd Length: 133  Bit Score: 251.87  E-value: 4.72e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009767   1 MKEKPTETVRLDKWLWAARFYKTRALAREMIEGGKVHYNGQRSKPGKIVELDAMLTLRQGNDERTVRIIGITEQRRPASE 80
Cdd:PRK10348   1 MKEKPAVEVRLDKWLWAARFYKTRALAREMIEGGKVHYNGQRSKPSKIVELNATLTLRQGNDERTVIVKAITEQRRPASE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489009767  81 AVNLYEETAESIEKREKMALARKMNALTMPHPDRRPDKKERRDLMRFKHGESE 133
Cdd:PRK10348  81 AALLYEETAESVEKREKMALARKLNALTMPHPDRRPDKKERRDLLRFKHGDSE 133
 
Name Accession Description Interval E-value
PRK10348 PRK10348
ribosome-associated heat shock protein Hsp15; Provisional
 1-133 4.72e-88

ribosome-associated heat shock protein Hsp15; Provisional


Pssm-ID: 182397  Cd Length: 133  Bit Score: 251.87  E-value: 4.72e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009767   1 MKEKPTETVRLDKWLWAARFYKTRALAREMIEGGKVHYNGQRSKPGKIVELDAMLTLRQGNDERTVRIIGITEQRRPASE 80
Cdd:PRK10348   1 MKEKPAVEVRLDKWLWAARFYKTRALAREMIEGGKVHYNGQRSKPSKIVELNATLTLRQGNDERTVIVKAITEQRRPASE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489009767  81 AVNLYEETAESIEKREKMALARKMNALTMPHPDRRPDKKERRDLMRFKHGESE 133
Cdd:PRK10348  81 AALLYEETAESVEKREKMALARKLNALTMPHPDRRPDKKERRDLLRFKHGDSE 133
HslR COG1188
Ribosomal 50S subunit-recycling heat shock protein, contains S4 domain [Translation, ribosomal ...
 5-129 3.19e-52

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


Pssm-ID: 440801  Cd Length: 120  Bit Score: 160.77  E-value: 3.19e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009767   5 PTETVRLDKWLWAARFYKTRALAREMIEGGKVHYNGQRSKPGKIVELDAMLTLRQGNDERTVRIIGITEQRRPASEAVNL 84
Cdd:COG1188    1 AAERMRLDKWLWAARFFKTRSLAAEACDGGRVRVNGQRAKPSREVKVGDVLTIRQGGRERVVRVLALSERRGPAPEAQLL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489009767  85 YEETAESIEKREKMAlarkmNALTMPHPDRRPDKKERRDLMRFKH 129
Cdd:COG1188   81 YEELTPSPAPREEAA-----AAAPRPRGAGRPTKKDRRELDRFRG 120
S4 cd00165
S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, ...
 9-58 1.17e-10

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: 53.41  E-value: 1.17e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489009767   9 VRLDKWLWAARFYKTRALAREMIEGGKVHYNGQR-SKPGKIVELDAMLTLR 58
Cdd:cd00165    1 MRLDKILARLGLAPSRSEARQLIKHGHVLVNGKVvTKPSYKVKPGDVIEVD 51
S4 smart00363
S4 RNA-binding domain;
9-64 1.62e-10

S4 RNA-binding domain;


Pssm-ID: 214638 [Multi-domain]  Cd Length: 60  Bit Score: 52.98  E-value: 1.62e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 489009767     9 VRLDKWLWAARFYKTRALAREMIEGGKVHYNGQR-SKPGKIVELDAMLTLRQGNDER 64
Cdd:smart00363   1 RRLDKFLARLGLAPSRSQARRLIEQGRVKVNGKKvTKPSYIVKPGDVISVRGKELKR 57
S4 pfam01479
S4 domain; The S4 domain is a small domain consisting of 60-65 amino acid residues that was ...
 9-55 1.11e-09

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: 50.57  E-value: 1.11e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 489009767    9 VRLDKWLWAARFYKTRALAREMIEGGKVHYNGQR-SKPGKIVELDAML 55
Cdd:pfam01479   1 RRLDKVLARLGLASSRSQARQLIEHGRVLVNGKVvKDPSYRVKPGDEI 48
 
Name Accession Description Interval E-value
PRK10348 PRK10348
ribosome-associated heat shock protein Hsp15; Provisional
 1-133 4.72e-88

ribosome-associated heat shock protein Hsp15; Provisional


Pssm-ID: 182397  Cd Length: 133  Bit Score: 251.87  E-value: 4.72e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009767   1 MKEKPTETVRLDKWLWAARFYKTRALAREMIEGGKVHYNGQRSKPGKIVELDAMLTLRQGNDERTVRIIGITEQRRPASE 80
Cdd:PRK10348   1 MKEKPAVEVRLDKWLWAARFYKTRALAREMIEGGKVHYNGQRSKPSKIVELNATLTLRQGNDERTVIVKAITEQRRPASE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489009767  81 AVNLYEETAESIEKREKMALARKMNALTMPHPDRRPDKKERRDLMRFKHGESE 133
Cdd:PRK10348  81 AALLYEETAESVEKREKMALARKLNALTMPHPDRRPDKKERRDLLRFKHGDSE 133
HslR COG1188
Ribosomal 50S subunit-recycling heat shock protein, contains S4 domain [Translation, ribosomal ...
 5-129 3.19e-52

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


Pssm-ID: 440801  Cd Length: 120  Bit Score: 160.77  E-value: 3.19e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009767   5 PTETVRLDKWLWAARFYKTRALAREMIEGGKVHYNGQRSKPGKIVELDAMLTLRQGNDERTVRIIGITEQRRPASEAVNL 84
Cdd:COG1188    1 AAERMRLDKWLWAARFFKTRSLAAEACDGGRVRVNGQRAKPSREVKVGDVLTIRQGGRERVVRVLALSERRGPAPEAQLL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489009767  85 YEETAESIEKREKMAlarkmNALTMPHPDRRPDKKERRDLMRFKH 129
Cdd:COG1188   81 YEELTPSPAPREEAA-----AAAPRPRGAGRPTKKDRRELDRFRG 120
S4 cd00165
S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, ...
 9-58 1.17e-10

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: 53.41  E-value: 1.17e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489009767   9 VRLDKWLWAARFYKTRALAREMIEGGKVHYNGQR-SKPGKIVELDAMLTLR 58
Cdd:cd00165    1 MRLDKILARLGLAPSRSEARQLIKHGHVLVNGKVvTKPSYKVKPGDVIEVD 51
S4 smart00363
S4 RNA-binding domain;
9-64 1.62e-10

S4 RNA-binding domain;


Pssm-ID: 214638 [Multi-domain]  Cd Length: 60  Bit Score: 52.98  E-value: 1.62e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 489009767     9 VRLDKWLWAARFYKTRALAREMIEGGKVHYNGQR-SKPGKIVELDAMLTLRQGNDER 64
Cdd:smart00363   1 RRLDKFLARLGLAPSRSQARRLIEQGRVKVNGKKvTKPSYIVKPGDVISVRGKELKR 57
S4 pfam01479
S4 domain; The S4 domain is a small domain consisting of 60-65 amino acid residues that was ...
 9-55 1.11e-09

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: 50.57  E-value: 1.11e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 489009767    9 VRLDKWLWAARFYKTRALAREMIEGGKVHYNGQR-SKPGKIVELDAML 55
Cdd:pfam01479   1 RRLDKVLARLGLASSRSQARQLIEHGRVLVNGKVvKDPSYRVKPGDEI 48
 
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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