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Conserved domains on  [gi|518359905|ref|WP_019530112|]
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cold shock domain-containing protein CspD [Dasania marina]

Protein Classification

S1 domain-containing protein( domain architecture ID 237)

S1 domain-containing protein may bind RNA

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
S1_like super family cl09927
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
1-68 1.81e-36

S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of RNA-associated proteins. Originally identified in S1 ribosomal protein. This superfamily also contains the Cold Shock Domain (CSD), which is a homolog of the S1 domain. Both domains are members of the Oligonucleotide/oligosaccharide Binding (OB) fold.


The actual alignment was detected with superfamily member TIGR02381:

Pssm-ID: 471952  Cd Length: 68  Bit Score: 117.26  E-value: 1.81e-36
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518359905   1 MYTGMVKWFNNAKGYGFILSEEGGGDIFAHYSAIDMDGYKTLKAGQSVTFETEQGPKGLHATQIQAVA 68
Cdd:TIGR02381  1 MAIGIVKWFNNAKGFGFICPEGVDGDIFAHYSTIQMDGYRTLKAGQKVQFEVVQGPKGAHATHIVPIE 68
 
Name Accession Description Interval E-value
cspD TIGR02381
cold shock domain protein CspD; This model represents what appears to be a phylogenetically ...
1-68 1.81e-36

cold shock domain protein CspD; This model represents what appears to be a phylogenetically distinct clade, containing E. coli CspD (SP|P24245) and related proteobacterial proteins within the larger family of cold shock domain proteins described by pfam00313. The gene symbol cspD may have been used idependently for other subfamilies of cold shock domain proteins, such as for B. subtilis CspD. These proteins typically are shorter than 70 amino acids. In E. coli, CspD is a stress response protein induced in stationary phase. This homodimer binds single-stranded DNA and appears to inhibit DNA replication. [DNA metabolism, DNA replication, recombination, and repair, Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 131434  Cd Length: 68  Bit Score: 117.26  E-value: 1.81e-36
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518359905   1 MYTGMVKWFNNAKGYGFILSEEGGGDIFAHYSAIDMDGYKTLKAGQSVTFETEQGPKGLHATQIQAVA 68
Cdd:TIGR02381  1 MAIGIVKWFNNAKGFGFICPEGVDGDIFAHYSTIQMDGYRTLKAGQKVQFEVVQGPKGAHATHIVPIE 68
CspC COG1278
Cold shock protein, CspA family [Transcription];
1-67 2.29e-35

Cold shock protein, CspA family [Transcription];


Pssm-ID: 440889  Cd Length: 67  Bit Score: 114.52  E-value: 2.29e-35
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518359905  1 MYTGMVKWFNNAKGYGFILSEEGGGDIFAHYSAIDMDGYKTLKAGQSVTFETEQGPKGLHATQIQAV 67
Cdd:COG1278   1 MATGTVKWFNAEKGFGFITPDDGGEDVFVHISALQRSGFRTLREGQRVEFEVEQGDKGPQAVNVRVL 67
CSP_CDS cd04458
Cold-Shock Protein (CSP) contains an S1-like cold-shock domain (CSD) that is found in ...
2-65 9.51e-32

Cold-Shock Protein (CSP) contains an S1-like cold-shock domain (CSD) that is found in eukaryotes, prokaryotes, and archaea. CSP's include the major cold-shock proteins CspA and CspB in bacteria and the eukaryotic gene regulatory factor Y-box protein. CSP expression is up-regulated by an abrupt drop in growth temperature. CSP's are also expressed under normal condition at lower level. The function of cold-shock proteins is not fully understood. They preferentially bind poly-pyrimidine region of single-stranded RNA and DNA. CSP's are thought to bind mRNA and regulate ribosomal translation, mRNA degradation, and the rate of transcription termination. The human Y-box protein, which contains a CSD, regulates transcription and translation of genes that contain the Y-box sequence in their promoters. This specific ssDNA-binding properties of CSD are required for the binding of Y-box protein to the promoter's Y-box sequence, thereby regulating transcription.


Pssm-ID: 239905  Cd Length: 65  Bit Score: 105.35  E-value: 9.51e-32
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518359905  2 YTGMVKWFNNAKGYGFILSEEGGGDIFAHYSAIDMDGYKTLKAGQSVTFETEQGPKGLHATQIQ 65
Cdd:cd04458   1 VTGTVKWFDDEKGFGFITPDDGGEDVFVHISALEGDGFRSLEEGDRVEFELEEGDKGPQAVNVR 64
PRK09937 PRK09937
cold shock-like protein CspD;
1-67 1.33e-29

cold shock-like protein CspD;


Pssm-ID: 77494  Cd Length: 74  Bit Score: 100.19  E-value: 1.33e-29
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518359905  1 MYTGMVKWFNNAKGYGFILSEEGGGDIFAHYSAIDMDGYKTLKAGQSVTFETEQGPKGLHATQIQAV 67
Cdd:PRK09937  1 MEKGTVKWFNNAKGFGFICPEGGGEDIFAHYSTIQMDGYRTLKAGQSVQFDVHQGPKGNHASVIVPV 67
CSD pfam00313
'Cold-shock' DNA-binding domain;
3-67 5.78e-29

'Cold-shock' DNA-binding domain;


Pssm-ID: 278729  Cd Length: 66  Bit Score: 98.47  E-value: 5.78e-29
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518359905   3 TGMVKWFNNAKGYGFILSEEGGGDIFAHYSAIDMDGYKTLKAGQSVTFETEQGPKGLHATQIQAV 67
Cdd:pfam00313  2 TGTVKWFNAKKGFGFITPEDGDKDVFVHFSAIQGDGFRSLQEGQKVEFEVVEGTKGPQAANVTKP 66
CSP smart00357
Cold shock protein domain; RNA-binding domain that functions as a RNA-chaperone in bacteria ...
3-67 8.47e-16

Cold shock protein domain; RNA-binding domain that functions as a RNA-chaperone in bacteria and is involved in regulating translation in eukaryotes. Contains sub-family of RNA-binding domains in the Rho transcription termination factor.


Pssm-ID: 214633 [Multi-domain]  Cd Length: 64  Bit Score: 64.93  E-value: 8.47e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518359905    3 TGMVKWFNnaKGYGFILSEEGGGDIFAHYSAIDMdGYKTLKAGQSVTFETE--QGPKGLHATQIQAV 67
Cdd:smart00357  1 TGVVKWFN--KGFGFIRPDDGGKDVFVHPSQIQG-GLKSLREGDEVEFKVVspEGGEKPEAENVVKL 64
 
Name Accession Description Interval E-value
cspD TIGR02381
cold shock domain protein CspD; This model represents what appears to be a phylogenetically ...
1-68 1.81e-36

cold shock domain protein CspD; This model represents what appears to be a phylogenetically distinct clade, containing E. coli CspD (SP|P24245) and related proteobacterial proteins within the larger family of cold shock domain proteins described by pfam00313. The gene symbol cspD may have been used idependently for other subfamilies of cold shock domain proteins, such as for B. subtilis CspD. These proteins typically are shorter than 70 amino acids. In E. coli, CspD is a stress response protein induced in stationary phase. This homodimer binds single-stranded DNA and appears to inhibit DNA replication. [DNA metabolism, DNA replication, recombination, and repair, Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 131434  Cd Length: 68  Bit Score: 117.26  E-value: 1.81e-36
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518359905   1 MYTGMVKWFNNAKGYGFILSEEGGGDIFAHYSAIDMDGYKTLKAGQSVTFETEQGPKGLHATQIQAVA 68
Cdd:TIGR02381  1 MAIGIVKWFNNAKGFGFICPEGVDGDIFAHYSTIQMDGYRTLKAGQKVQFEVVQGPKGAHATHIVPIE 68
CspC COG1278
Cold shock protein, CspA family [Transcription];
1-67 2.29e-35

Cold shock protein, CspA family [Transcription];


Pssm-ID: 440889  Cd Length: 67  Bit Score: 114.52  E-value: 2.29e-35
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518359905  1 MYTGMVKWFNNAKGYGFILSEEGGGDIFAHYSAIDMDGYKTLKAGQSVTFETEQGPKGLHATQIQAV 67
Cdd:COG1278   1 MATGTVKWFNAEKGFGFITPDDGGEDVFVHISALQRSGFRTLREGQRVEFEVEQGDKGPQAVNVRVL 67
CSP_CDS cd04458
Cold-Shock Protein (CSP) contains an S1-like cold-shock domain (CSD) that is found in ...
2-65 9.51e-32

Cold-Shock Protein (CSP) contains an S1-like cold-shock domain (CSD) that is found in eukaryotes, prokaryotes, and archaea. CSP's include the major cold-shock proteins CspA and CspB in bacteria and the eukaryotic gene regulatory factor Y-box protein. CSP expression is up-regulated by an abrupt drop in growth temperature. CSP's are also expressed under normal condition at lower level. The function of cold-shock proteins is not fully understood. They preferentially bind poly-pyrimidine region of single-stranded RNA and DNA. CSP's are thought to bind mRNA and regulate ribosomal translation, mRNA degradation, and the rate of transcription termination. The human Y-box protein, which contains a CSD, regulates transcription and translation of genes that contain the Y-box sequence in their promoters. This specific ssDNA-binding properties of CSD are required for the binding of Y-box protein to the promoter's Y-box sequence, thereby regulating transcription.


Pssm-ID: 239905  Cd Length: 65  Bit Score: 105.35  E-value: 9.51e-32
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518359905  2 YTGMVKWFNNAKGYGFILSEEGGGDIFAHYSAIDMDGYKTLKAGQSVTFETEQGPKGLHATQIQ 65
Cdd:cd04458   1 VTGTVKWFDDEKGFGFITPDDGGEDVFVHISALEGDGFRSLEEGDRVEFELEEGDKGPQAVNVR 64
PRK09937 PRK09937
cold shock-like protein CspD;
1-67 1.33e-29

cold shock-like protein CspD;


Pssm-ID: 77494  Cd Length: 74  Bit Score: 100.19  E-value: 1.33e-29
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518359905  1 MYTGMVKWFNNAKGYGFILSEEGGGDIFAHYSAIDMDGYKTLKAGQSVTFETEQGPKGLHATQIQAV 67
Cdd:PRK09937  1 MEKGTVKWFNNAKGFGFICPEGGGEDIFAHYSTIQMDGYRTLKAGQSVQFDVHQGPKGNHASVIVPV 67
CSD pfam00313
'Cold-shock' DNA-binding domain;
3-67 5.78e-29

'Cold-shock' DNA-binding domain;


Pssm-ID: 278729  Cd Length: 66  Bit Score: 98.47  E-value: 5.78e-29
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518359905   3 TGMVKWFNNAKGYGFILSEEGGGDIFAHYSAIDMDGYKTLKAGQSVTFETEQGPKGLHATQIQAV 67
Cdd:pfam00313  2 TGTVKWFNAKKGFGFITPEDGDKDVFVHFSAIQGDGFRSLQEGQKVEFEVVEGTKGPQAANVTKP 66
PRK14998 PRK14998
cold shock-like protein CspD; Provisional
1-64 1.92e-28

cold shock-like protein CspD; Provisional


Pssm-ID: 184960  Cd Length: 73  Bit Score: 97.43  E-value: 1.92e-28
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518359905  1 MYTGMVKWFNNAKGYGFILSEEGGGDIFAHYSAIDMDGYKTLKAGQSVTFETEQGPKGLHATQI 64
Cdd:PRK14998  1 METGTVKWFNNAKGFGFICPEGGGEDIFAHYSTIQMDGYRTLKAGQSVRFDVHQGPKGNHASVI 64
cspE PRK09507
cold shock-like protein CspE;
4-67 2.17e-20

cold shock-like protein CspE;


Pssm-ID: 169931  Cd Length: 69  Bit Score: 76.62  E-value: 2.17e-20
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518359905  4 GMVKWFNNAKGYGFILSEEGGGDIFAHYSAIDMDGYKTLKAGQSVTFETEQGPKGLHATQIQAV 67
Cdd:PRK09507  6 GNVKWFNESKGFGFITPEDGSKDVFVHFSAIQTNGFKTLAEGQRVEFEITNGAKGPSAANVIAL 69
PRK10354 PRK10354
RNA chaperone/antiterminator CspA;
3-67 2.86e-20

RNA chaperone/antiterminator CspA;


Pssm-ID: 182402  Cd Length: 70  Bit Score: 76.55  E-value: 2.86e-20
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518359905  3 TGMVKWFNNAKGYGFILSEEGGGDIFAHYSAIDMDGYKTLKAGQSVTFETEQGPKGLHATQIQAV 67
Cdd:PRK10354  6 TGIVKWFNADKGFGFITPDDGSKDVFVHFSAIQNDGYKSLDEGQKVSFTIESGAKGPAAGNVTSL 70
PRK09890 PRK09890
cold shock protein CspG; Provisional
3-64 6.55e-17

cold shock protein CspG; Provisional


Pssm-ID: 77467  Cd Length: 70  Bit Score: 67.87  E-value: 6.55e-17
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518359905  3 TGMVKWFNNAKGYGFILSEEGGGDIFAHYSAIDMDGYKTLKAGQSVTFETEQGPKGLHATQI 64
Cdd:PRK09890  6 TGLVKWFNADKGFGFITPDDGSKDVFVHFTAIQSNEFRTLNENQKVEFSIEQGQRGPAAANV 67
PRK10943 PRK10943
cold shock-like protein CspC; Provisional
4-67 3.52e-16

cold shock-like protein CspC; Provisional


Pssm-ID: 170841  Cd Length: 69  Bit Score: 66.25  E-value: 3.52e-16
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518359905  4 GMVKWFNNAKGYGFILSEEGGGDIFAHYSAIDMDGYKTLKAGQSVTFETEQGPKGLHATQIQAV 67
Cdd:PRK10943  6 GQVKWFNESKGFGFITPADGSKDVFVHFSAIQGNGFKTLAEGQNVEFEIQDGQKGPAAVNVTAI 69
CSP smart00357
Cold shock protein domain; RNA-binding domain that functions as a RNA-chaperone in bacteria ...
3-67 8.47e-16

Cold shock protein domain; RNA-binding domain that functions as a RNA-chaperone in bacteria and is involved in regulating translation in eukaryotes. Contains sub-family of RNA-binding domains in the Rho transcription termination factor.


Pssm-ID: 214633 [Multi-domain]  Cd Length: 64  Bit Score: 64.93  E-value: 8.47e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518359905    3 TGMVKWFNnaKGYGFILSEEGGGDIFAHYSAIDMdGYKTLKAGQSVTFETE--QGPKGLHATQIQAV 67
Cdd:smart00357  1 TGVVKWFN--KGFGFIRPDDGGKDVFVHPSQIQG-GLKSLREGDEVEFKVVspEGGEKPEAENVVKL 64
PRK15463 PRK15463
cold shock-like protein CspF; Provisional
3-64 9.94e-05

cold shock-like protein CspF; Provisional


Pssm-ID: 185360  Cd Length: 70  Bit Score: 36.80  E-value: 9.94e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518359905  3 TGMVKWFNNAKGYGFILSEEGGGDIFAHYSAIDMDGYKTLKAGQSVTFETEQGPKGLHATQI 64
Cdd:PRK15463  6 TGIVKTFDGKSGKGLITPSDGRKDVQVHISALNLRDAEELTTGLRVEFCRINGLRGPTAANV 67
 
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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