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Conserved domains on  [gi|495388723|ref|WP_008113426|]
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MULTISPECIES: ribosome-associated heat shock protein Hsp15 [unclassified Pseudoalteromonas]

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, ...
 16-138 4.23e-53

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: 164.04  E-value: 4.23e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495388723  16 TLKVRLDKWLWAARFYKTRAIAREMVQGGKVHYNGQRSKASKIVEIGAVIKLAQGVDEKTITVLNILEKRQSAPIAQTMY 95
Cdd:PRK10348   6 AVEVRLDKWLWAARFYKTRALAREMIEGGKVHYNGQRSKPSKIVELNATLTLRQGNDERTVIVKAITEQRRPASEAALLY 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 495388723  96 QESDASIAKREENSIARKNNSFFAPHPDKKPDKKQRRELLKMK 138
Cdd:PRK10348  86 EETAESVEKREKMALARKLNALTMPHPDRRPDKKERRDLLRFK 128
 
Name Accession Description Interval E-value
PRK10348 PRK10348
ribosome-associated heat shock protein Hsp15; Provisional
 16-138 4.23e-53

ribosome-associated heat shock protein Hsp15; Provisional


Pssm-ID: 182397  Cd Length: 133  Bit Score: 164.04  E-value: 4.23e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495388723  16 TLKVRLDKWLWAARFYKTRAIAREMVQGGKVHYNGQRSKASKIVEIGAVIKLAQGVDEKTITVLNILEKRQSAPIAQTMY 95
Cdd:PRK10348   6 AVEVRLDKWLWAARFYKTRALAREMIEGGKVHYNGQRSKPSKIVELNATLTLRQGNDERTVIVKAITEQRRPASEAALLY 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 495388723  96 QESDASIAKREENSIARKNNSFFAPHPDKKPDKKQRRELLKMK 138
Cdd:PRK10348  86 EETAESVEKREKMALARKLNALTMPHPDRRPDKKERRDLLRFK 128
HslR COG1188
Ribosomal 50S subunit-recycling heat shock protein, contains S4 domain [Translation, ribosomal ...
 18-139 1.35e-48

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


Pssm-ID: 440801  Cd Length: 120  Bit Score: 151.91  E-value: 1.35e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495388723  18 KVRLDKWLWAARFYKTRAIAREMVQGGKVHYNGQRSKASKIVEIGAVIKLAQGVDEKTITVLNILEKRQSAPIAQTMYQE 97
Cdd:COG1188    4 RMRLDKWLWAARFFKTRSLAAEACDGGRVRVNGQRAKPSREVKVGDVLTIRQGGRERVVRVLALSERRGPAPEAQLLYEE 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 495388723  98 SDASIAKREENSiarknNSFFAPHPDKKPDKKQRRELLKMKS 139
Cdd:COG1188   84 LTPSPAPREEAA-----AAAPRPRGAGRPTKKDRRELDRFRG 120
S4 cd00165
S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, ...
 19-90 9.73e-11

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: 54.18  E-value: 9.73e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495388723  19 VRLDKWLWAARFYKTRAIAREMVQGGKVHYNGQR-SKASKIVEIGAVIKlaqgVDEKTITVLNILEKRQSAPI 90
Cdd:cd00165    1 MRLDKILARLGLAPSRSEARQLIKHGHVLVNGKVvTKPSYKVKPGDVIE----VDGKSIEEDIVYEDKKLLVV 69
S4 pfam01479
S4 domain; The S4 domain is a small domain consisting of 60-65 amino acid residues that was ...
 19-65 6.75e-10

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: 51.34  E-value: 6.75e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 495388723   19 VRLDKWLWAARFYKTRAIAREMVQGGKVHYNGQR-SKASKIVEIGAVI 65
Cdd:pfam01479   1 RRLDKVLARLGLASSRSQARQLIEHGRVLVNGKVvKDPSYRVKPGDEI 48
S4 smart00363
S4 RNA-binding domain;
19-71 8.28e-09

S4 RNA-binding domain;


Pssm-ID: 214638 [Multi-domain]  Cd Length: 60  Bit Score: 48.74  E-value: 8.28e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 495388723    19 VRLDKWLWAARFYKTRAIAREMVQGGKVHYNGQR-SKASKIVEIGAVIKLAQGV 71
Cdd:smart00363   1 RRLDKFLARLGLAPSRSQARRLIEQGRVKVNGKKvTKPSYIVKPGDVISVRGKE 54
 
Name Accession Description Interval E-value
PRK10348 PRK10348
ribosome-associated heat shock protein Hsp15; Provisional
 16-138 4.23e-53

ribosome-associated heat shock protein Hsp15; Provisional


Pssm-ID: 182397  Cd Length: 133  Bit Score: 164.04  E-value: 4.23e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495388723  16 TLKVRLDKWLWAARFYKTRAIAREMVQGGKVHYNGQRSKASKIVEIGAVIKLAQGVDEKTITVLNILEKRQSAPIAQTMY 95
Cdd:PRK10348   6 AVEVRLDKWLWAARFYKTRALAREMIEGGKVHYNGQRSKPSKIVELNATLTLRQGNDERTVIVKAITEQRRPASEAALLY 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 495388723  96 QESDASIAKREENSIARKNNSFFAPHPDKKPDKKQRRELLKMK 138
Cdd:PRK10348  86 EETAESVEKREKMALARKLNALTMPHPDRRPDKKERRDLLRFK 128
HslR COG1188
Ribosomal 50S subunit-recycling heat shock protein, contains S4 domain [Translation, ribosomal ...
 18-139 1.35e-48

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


Pssm-ID: 440801  Cd Length: 120  Bit Score: 151.91  E-value: 1.35e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495388723  18 KVRLDKWLWAARFYKTRAIAREMVQGGKVHYNGQRSKASKIVEIGAVIKLAQGVDEKTITVLNILEKRQSAPIAQTMYQE 97
Cdd:COG1188    4 RMRLDKWLWAARFFKTRSLAAEACDGGRVRVNGQRAKPSREVKVGDVLTIRQGGRERVVRVLALSERRGPAPEAQLLYEE 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 495388723  98 SDASIAKREENSiarknNSFFAPHPDKKPDKKQRRELLKMKS 139
Cdd:COG1188   84 LTPSPAPREEAA-----AAAPRPRGAGRPTKKDRRELDRFRG 120
S4 cd00165
S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, ...
 19-90 9.73e-11

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: 54.18  E-value: 9.73e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495388723  19 VRLDKWLWAARFYKTRAIAREMVQGGKVHYNGQR-SKASKIVEIGAVIKlaqgVDEKTITVLNILEKRQSAPI 90
Cdd:cd00165    1 MRLDKILARLGLAPSRSEARQLIKHGHVLVNGKVvTKPSYKVKPGDVIE----VDGKSIEEDIVYEDKKLLVV 69
S4 pfam01479
S4 domain; The S4 domain is a small domain consisting of 60-65 amino acid residues that was ...
 19-65 6.75e-10

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: 51.34  E-value: 6.75e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 495388723   19 VRLDKWLWAARFYKTRAIAREMVQGGKVHYNGQR-SKASKIVEIGAVI 65
Cdd:pfam01479   1 RRLDKVLARLGLASSRSQARQLIEHGRVLVNGKVvKDPSYRVKPGDEI 48
S4 smart00363
S4 RNA-binding domain;
19-71 8.28e-09

S4 RNA-binding domain;


Pssm-ID: 214638 [Multi-domain]  Cd Length: 60  Bit Score: 48.74  E-value: 8.28e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 495388723    19 VRLDKWLWAARFYKTRAIAREMVQGGKVHYNGQR-SKASKIVEIGAVIKLAQGV 71
Cdd:smart00363   1 RRLDKFLARLGLAPSRSQARRLIEQGRVKVNGKKvTKPSYIVKPGDVISVRGKE 54
 
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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