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Conserved domains on  [gi|488142378|ref|WP_002213586|]
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BrnA antitoxin family protein [Neisseria meningitidis]

Protein Classification

BrnA antitoxin family protein( domain architecture ID 10007504)

BrnA antitoxin family protein similar to type II toxin-antitoxin system antitoxin BrnA that neutralizes the toxin BrnT

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG3514 COG3514
Uncharacterized conserved protein, DUF4415 family [Function unknown];
10-97 7.23e-21

Uncharacterized conserved protein, DUF4415 family [Function unknown];


:

Pssm-ID: 442736  Cd Length: 91  Bit Score: 78.93  E-value: 7.23e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488142378  10 DGEVRELAAEDFALARPIAEalpEDLAQVlfshqkqleeKGVMQKRNTGKTPKQLVTIRLSADVVEKFRAGGKGWQTRIN 89
Cdd:COG3514   17 DEEITAAAAIDPSDAPELTD---EFFARA----------RKRRRGRPKAAPPKVQVTIRLDPDVLEWFKATGPGWQTRIN 83


                 ....*...
gi 488142378  90 EVLRQYVA 97
Cdd:COG3514   84 AALRDYLK 91
 
Name Accession Description Interval E-value
COG3514 COG3514
Uncharacterized conserved protein, DUF4415 family [Function unknown];
10-97 7.23e-21

Uncharacterized conserved protein, DUF4415 family [Function unknown];


Pssm-ID: 442736  Cd Length: 91  Bit Score: 78.93  E-value: 7.23e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488142378  10 DGEVRELAAEDFALARPIAEalpEDLAQVlfshqkqleeKGVMQKRNTGKTPKQLVTIRLSADVVEKFRAGGKGWQTRIN 89
Cdd:COG3514   17 DEEITAAAAIDPSDAPELTD---EFFARA----------RKRRRGRPKAAPPKVQVTIRLDPDVLEWFKATGPGWQTRIN 83


                 ....*...
gi 488142378  90 EVLRQYVA 97
Cdd:COG3514   84 AALRDYLK 91
BrnA_antitoxin pfam14384
BrnA antitoxin of type II toxin-antitoxin system; BrnA is family of antitoxins that ...
 12-96 7.82e-20

BrnA antitoxin of type II toxin-antitoxin system; BrnA is family of antitoxins that neutralizes the toxin BrnT, pfam04365. It consists of 3 alpha-helices and a C-terminal ribbon-helix-helix DNA binding domain. As in other toxin-antitoxin systems, BrnA negatively autoregulates the brnTA operon and has higher affinity for the DNA operator when complexed with BrnT. It dimerizes with two molecules of its toxin BrnT.


Pssm-ID: 433924  Cd Length: 67  Bit Score: 75.79  E-value: 7.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488142378   12 EVREL-AAEDFALARPIAEALPedlaqvlfshqkqleeKGVMQKRntgKTPKQLVTIRLSADVVEKFRAGGKGWQTRINE 90
Cdd:pfam14384   1 DAPELtDEQWLARARPAKEALP----------------RGRPRRP---LPPKKAVTIRLDADVLEAFKATGKGWQTRMNA 61


                  ....*.
gi 488142378   91 VLRQYV 96
Cdd:pfam14384  62 ALREAL 67
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 1-40 4.31e-03

2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 dihydrozybenzoate dehydrogenase shares the characteristics of the classical SDRs. This subgroup includes Escherichai coli EntA which catalyzes the NAD+-dependent oxidation of 2,3-dihydro-2,3-dihydroxybenzoate to 2,3-dihydroxybenzoate during biosynthesis of the siderophore Enterobactin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187592 [Multi-domain]  Cd Length: 244  Bit Score: 34.75  E-value: 4.31e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 488142378   1 MQRQSLTNADGEVRELA--AEDFALARPIAE-ALPEDLAQ-VLF 40
Cdd:cd05331  177 MQRTLWHDEDGAAQVIAgvPEQFRLGIPLGKiAQPADIANaVLF 220
 
Name Accession Description Interval E-value
COG3514 COG3514
Uncharacterized conserved protein, DUF4415 family [Function unknown];
10-97 7.23e-21

Uncharacterized conserved protein, DUF4415 family [Function unknown];


Pssm-ID: 442736  Cd Length: 91  Bit Score: 78.93  E-value: 7.23e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488142378  10 DGEVRELAAEDFALARPIAEalpEDLAQVlfshqkqleeKGVMQKRNTGKTPKQLVTIRLSADVVEKFRAGGKGWQTRIN 89
Cdd:COG3514   17 DEEITAAAAIDPSDAPELTD---EFFARA----------RKRRRGRPKAAPPKVQVTIRLDPDVLEWFKATGPGWQTRIN 83


                 ....*...
gi 488142378  90 EVLRQYVA 97
Cdd:COG3514   84 AALRDYLK 91
BrnA_antitoxin pfam14384
BrnA antitoxin of type II toxin-antitoxin system; BrnA is family of antitoxins that ...
 12-96 7.82e-20

BrnA antitoxin of type II toxin-antitoxin system; BrnA is family of antitoxins that neutralizes the toxin BrnT, pfam04365. It consists of 3 alpha-helices and a C-terminal ribbon-helix-helix DNA binding domain. As in other toxin-antitoxin systems, BrnA negatively autoregulates the brnTA operon and has higher affinity for the DNA operator when complexed with BrnT. It dimerizes with two molecules of its toxin BrnT.


Pssm-ID: 433924  Cd Length: 67  Bit Score: 75.79  E-value: 7.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488142378   12 EVREL-AAEDFALARPIAEALPedlaqvlfshqkqleeKGVMQKRntgKTPKQLVTIRLSADVVEKFRAGGKGWQTRINE 90
Cdd:pfam14384   1 DAPELtDEQWLARARPAKEALP----------------RGRPRRP---LPPKKAVTIRLDADVLEAFKATGKGWQTRMNA 61


                  ....*.
gi 488142378   91 VLRQYV 96
Cdd:pfam14384  62 ALREAL 67
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 1-40 4.31e-03

2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 dihydrozybenzoate dehydrogenase shares the characteristics of the classical SDRs. This subgroup includes Escherichai coli EntA which catalyzes the NAD+-dependent oxidation of 2,3-dihydro-2,3-dihydroxybenzoate to 2,3-dihydroxybenzoate during biosynthesis of the siderophore Enterobactin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187592 [Multi-domain]  Cd Length: 244  Bit Score: 34.75  E-value: 4.31e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 488142378   1 MQRQSLTNADGEVRELA--AEDFALARPIAE-ALPEDLAQ-VLF 40
Cdd:cd05331  177 MQRTLWHDEDGAAQVIAgvPEQFRLGIPLGKiAQPADIANaVLF 220
 
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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