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Conserved domains on  [gi|1860023041|ref|WP_175501714|]
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MULTISPECIES: RNase A-like domain-containing protein [Pantoea]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CdiA-CT_Yk_RNaseA-like super family cl39768
C-terminal (CT) domain of the contact-dependent growth inhibition (CDI) system protein CdiA ...
 6-82 8.08e-20

C-terminal (CT) domain of the contact-dependent growth inhibition (CDI) system protein CdiA (CdiA-CT) of Yersinia kristensenii, and similar proteins; CDI toxins are expressed by gram-negative bacteria as part of a mechanism to inhibit the growth of neighboring cells. This model represents the C-terminal (CT) toxin domain of CdiA effector protein from Yersinia kristensenii and similar proteins. CdiA secretion is dependent on the outer membrane protein CdiB. Upon binding to a receptor on the surface of target bacteria, the CDI toxin is delivered via the C-terminal domain. A wide variety of C-terminal toxin domains appear to exist; Yersinia kristensenii CdiA-CT has potent RNase activity in vivo and in vitro. Although CdiA-CT has structural homology with angiogenin and other RNase A paralogs, it does not share sequence similarity with these nucleases and lacks the characteristic disulfide bonds of the superfamily. It binds its cognate immunity protein CdiI which neutralizes toxicity by blocking access to RNA substrates. Y. kristensenii CdiA-CT is the first non-vertebrate protein found to possess the RNase A superfamily fold. Homologs of this toxin are associated with secretion systems in many Gram-negative and Gram-positive bacteria, suggesting that RNase A-like toxins are commonly deployed in inter-bacterial competition.


The actual alignment was detected with superfamily member cd20684:

Pssm-ID: 454353  Cd Length: 112  Bit Score: 76.43  E-value: 8.08e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1860023041   6 RVTSATpfFTRPAAAIQSYLSGNQKGYLTLNYQSSSAIGISVTNGSTSAVQATNAKVVNGRDSSMPDGYKIITGYPT 82
Cdd:cd20684    38 RAISEA--LRANQAKIENWLKGGKGGRLVLDYNFGEPVGRGVSRGSTTVVSVTKVRVVLKRDPYMPKGYYILTAYPT 112
 
Name Accession Description Interval E-value
CdiA-CT_Yk_RNaseA-like cd20684
C-terminal (CT) domain of the contact-dependent growth inhibition (CDI) system protein CdiA ...
 6-82 8.08e-20

C-terminal (CT) domain of the contact-dependent growth inhibition (CDI) system protein CdiA (CdiA-CT) of Yersinia kristensenii, and similar proteins; CDI toxins are expressed by gram-negative bacteria as part of a mechanism to inhibit the growth of neighboring cells. This model represents the C-terminal (CT) toxin domain of CdiA effector protein from Yersinia kristensenii and similar proteins. CdiA secretion is dependent on the outer membrane protein CdiB. Upon binding to a receptor on the surface of target bacteria, the CDI toxin is delivered via the C-terminal domain. A wide variety of C-terminal toxin domains appear to exist; Yersinia kristensenii CdiA-CT has potent RNase activity in vivo and in vitro. Although CdiA-CT has structural homology with angiogenin and other RNase A paralogs, it does not share sequence similarity with these nucleases and lacks the characteristic disulfide bonds of the superfamily. It binds its cognate immunity protein CdiI which neutralizes toxicity by blocking access to RNA substrates. Y. kristensenii CdiA-CT is the first non-vertebrate protein found to possess the RNase A superfamily fold. Homologs of this toxin are associated with secretion systems in many Gram-negative and Gram-positive bacteria, suggesting that RNase A-like toxins are commonly deployed in inter-bacterial competition.


Pssm-ID: 411002  Cd Length: 112  Bit Score: 76.43  E-value: 8.08e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1860023041   6 RVTSATpfFTRPAAAIQSYLSGNQKGYLTLNYQSSSAIGISVTNGSTSAVQATNAKVVNGRDSSMPDGYKIITGYPT 82
Cdd:cd20684    38 RAISEA--LRANQAKIENWLKGGKGGRLVLDYNFGEPVGRGVSRGSTTVVSVTKVRVVLKRDPYMPKGYYILTAYPT 112
RNAse_A_bac pfam18431
Bacterial CdiA-CT RNAse A domain; Contact-dependent growth inhibition (CDI) is an important ...
 18-81 1.17e-11

Bacterial CdiA-CT RNAse A domain; Contact-dependent growth inhibition (CDI) is an important mechanism of inter-bacterial competition found in many Gram-negative pathogens. CDI+ cells express cell-surface CdiA proteins that bind neighboring bacteria and deliver C-terminal toxin domains (CdiA-CT) to inhibit target-cell growth. Structure analysis of CdiA-CT shows that it adopts the same fold (with two beta-sheets forming an overall kidney shape) as angiogenin and other RNase A paralogs, but the toxin does not share sequence similarity with these nucleases and lacks the characteriztic disulfide bonds of the superfamily. Furthermore, structural comparison analysis identified human angiogenin, Rana pipiens protein P-30 (onconase) and mouse pancreatic ribonuclease (RNase 1) as the closest structural homologs of CdiA-CT.


Pssm-ID: 436497  Cd Length: 113  Bit Score: 55.36  E-value: 1.17e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1860023041  18 AAAIQSYLSGNQKGY-LTLNYQSSSAIGISVTNGSTSAVQATNAKVVNGRDSSMPDGYKIITGYP 81
Cdd:pfam18431  49 RARIESWLKGAAGGDrLALDYDFGRVVGRGVTRGSGSPKDMTKVRVVLKYDGDGPKGYRVLTAYP 113
 
Name Accession Description Interval E-value
CdiA-CT_Yk_RNaseA-like cd20684
C-terminal (CT) domain of the contact-dependent growth inhibition (CDI) system protein CdiA ...
 6-82 8.08e-20

C-terminal (CT) domain of the contact-dependent growth inhibition (CDI) system protein CdiA (CdiA-CT) of Yersinia kristensenii, and similar proteins; CDI toxins are expressed by gram-negative bacteria as part of a mechanism to inhibit the growth of neighboring cells. This model represents the C-terminal (CT) toxin domain of CdiA effector protein from Yersinia kristensenii and similar proteins. CdiA secretion is dependent on the outer membrane protein CdiB. Upon binding to a receptor on the surface of target bacteria, the CDI toxin is delivered via the C-terminal domain. A wide variety of C-terminal toxin domains appear to exist; Yersinia kristensenii CdiA-CT has potent RNase activity in vivo and in vitro. Although CdiA-CT has structural homology with angiogenin and other RNase A paralogs, it does not share sequence similarity with these nucleases and lacks the characteristic disulfide bonds of the superfamily. It binds its cognate immunity protein CdiI which neutralizes toxicity by blocking access to RNA substrates. Y. kristensenii CdiA-CT is the first non-vertebrate protein found to possess the RNase A superfamily fold. Homologs of this toxin are associated with secretion systems in many Gram-negative and Gram-positive bacteria, suggesting that RNase A-like toxins are commonly deployed in inter-bacterial competition.


Pssm-ID: 411002  Cd Length: 112  Bit Score: 76.43  E-value: 8.08e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1860023041   6 RVTSATpfFTRPAAAIQSYLSGNQKGYLTLNYQSSSAIGISVTNGSTSAVQATNAKVVNGRDSSMPDGYKIITGYPT 82
Cdd:cd20684    38 RAISEA--LRANQAKIENWLKGGKGGRLVLDYNFGEPVGRGVSRGSTTVVSVTKVRVVLKRDPYMPKGYYILTAYPT 112
RNAse_A_bac pfam18431
Bacterial CdiA-CT RNAse A domain; Contact-dependent growth inhibition (CDI) is an important ...
 18-81 1.17e-11

Bacterial CdiA-CT RNAse A domain; Contact-dependent growth inhibition (CDI) is an important mechanism of inter-bacterial competition found in many Gram-negative pathogens. CDI+ cells express cell-surface CdiA proteins that bind neighboring bacteria and deliver C-terminal toxin domains (CdiA-CT) to inhibit target-cell growth. Structure analysis of CdiA-CT shows that it adopts the same fold (with two beta-sheets forming an overall kidney shape) as angiogenin and other RNase A paralogs, but the toxin does not share sequence similarity with these nucleases and lacks the characteriztic disulfide bonds of the superfamily. Furthermore, structural comparison analysis identified human angiogenin, Rana pipiens protein P-30 (onconase) and mouse pancreatic ribonuclease (RNase 1) as the closest structural homologs of CdiA-CT.


Pssm-ID: 436497  Cd Length: 113  Bit Score: 55.36  E-value: 1.17e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1860023041  18 AAAIQSYLSGNQKGY-LTLNYQSSSAIGISVTNGSTSAVQATNAKVVNGRDSSMPDGYKIITGYP 81
Cdd:pfam18431  49 RARIESWLKGAAGGDrLALDYDFGRVVGRGVTRGSGSPKDMTKVRVVLKYDGDGPKGYRVLTAYP 113
 
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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