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Conserved domains on  [gi|320542283|ref|NP_001188665|]
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sulfiredoxin, isoform B [Drosophila melanogaster]

Protein Classification

sulfiredoxin( domain architecture ID 11611623)

sulfiredoxin reduces and thereby reactivates peroxiredoxins after oxidative inactivation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Srx cd16395
Sulfiredoxin reactivates peroxiredoxins after oxidative inactivation; Sulfiredoxin reduces and ...
 13-104 2.59e-52

Sulfiredoxin reactivates peroxiredoxins after oxidative inactivation; Sulfiredoxin reduces and thereby re-activates 2-cys peroxiredoxins. Peroxiredoxins act as molecular switches, inactivating in response to hyperoxidation from hydrogen peroxide and other free radicals. Sulfiredoxin reactivates Prx-SO(2)(-) via ATP-Mg(2+)-dependent reduction. Arabidopsis sulfiredoxin has been described as a dual function enzyme, having nuclease activity in addition to the sulfiredoxin activity. This protein is similar to ParB N-terminal-like domain of bacterial and plasmid parABS partitioning systems.


:

Pssm-ID: 319253 [Multi-domain]  Cd Length: 90  Bit Score: 158.93  E-value: 2.59e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542283  13 THLVPMSVIQRPIPSVLDEQKVQSLMETIKNETsEDEVPPIDLLWISGsEGGDYYFSFGGCHRFEAYKRLQRPTIKAKLV 92
Cdd:cd16395    1 VHEVPLSVIRRPLPPVLDENKVQSLMETIKGIA-PGLLPPIDVLWVKG-EGGGYYYSFGGCHRYEAHKRLGRETIRCKII 78

                         90
                 ....*....|..
gi 320542283  93 KSTLGDLYHYMG 104
Cdd:cd16395   79 KSTPSDLRVYLG 90
 
Name Accession Description Interval E-value
Srx cd16395
Sulfiredoxin reactivates peroxiredoxins after oxidative inactivation; Sulfiredoxin reduces and ...
 13-104 2.59e-52

Sulfiredoxin reactivates peroxiredoxins after oxidative inactivation; Sulfiredoxin reduces and thereby re-activates 2-cys peroxiredoxins. Peroxiredoxins act as molecular switches, inactivating in response to hyperoxidation from hydrogen peroxide and other free radicals. Sulfiredoxin reactivates Prx-SO(2)(-) via ATP-Mg(2+)-dependent reduction. Arabidopsis sulfiredoxin has been described as a dual function enzyme, having nuclease activity in addition to the sulfiredoxin activity. This protein is similar to ParB N-terminal-like domain of bacterial and plasmid parABS partitioning systems.


Pssm-ID: 319253 [Multi-domain]  Cd Length: 90  Bit Score: 158.93  E-value: 2.59e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542283  13 THLVPMSVIQRPIPSVLDEQKVQSLMETIKNETsEDEVPPIDLLWISGsEGGDYYFSFGGCHRFEAYKRLQRPTIKAKLV 92
Cdd:cd16395    1 VHEVPLSVIRRPLPPVLDENKVQSLMETIKGIA-PGLLPPIDVLWVKG-EGGGYYYSFGGCHRYEAHKRLGRETIRCKII 78

                         90
                 ....*....|..
gi 320542283  93 KSTLGDLYHYMG 104
Cdd:cd16395   79 KSTPSDLRVYLG 90
ParBc pfam02195
ParB/Sulfiredoxin domain; Proteins containing this domain include Escherichia coli plasmid ...
 14-89 3.70e-04

ParB/Sulfiredoxin domain; Proteins containing this domain include Escherichia coli plasmid protein ParB and mammalian Sulfiredoxin-1. ParB is involved in chromosome partition. It localizes to both poles of the predivisional cell following completion of DNA replication. Sulfiredoxin-1 contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in the peroxiredoxins PRDX1, PRDX2, PRDX3 and PRDX4.


Pssm-ID: 426651 [Multi-domain]  Cd Length: 90  Bit Score: 36.49  E-value: 3.70e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 320542283   14 HLVPMSVIqRPI---PSVLDEQKVQSLMETIKnetSEDEVPPIDllwISGSEGGDYYFsFGGCHRFEAYKRLQRPTIKA 89
Cdd:pfam02195   1 EEVPISKL-RPNpdqPRKDSEESLEELAASIK---KRGLLQPII---VRKTPDGRYEI-IAGERRLRAAKLLGLKEVPV 71
 
Name Accession Description Interval E-value
Srx cd16395
Sulfiredoxin reactivates peroxiredoxins after oxidative inactivation; Sulfiredoxin reduces and ...
 13-104 2.59e-52

Sulfiredoxin reactivates peroxiredoxins after oxidative inactivation; Sulfiredoxin reduces and thereby re-activates 2-cys peroxiredoxins. Peroxiredoxins act as molecular switches, inactivating in response to hyperoxidation from hydrogen peroxide and other free radicals. Sulfiredoxin reactivates Prx-SO(2)(-) via ATP-Mg(2+)-dependent reduction. Arabidopsis sulfiredoxin has been described as a dual function enzyme, having nuclease activity in addition to the sulfiredoxin activity. This protein is similar to ParB N-terminal-like domain of bacterial and plasmid parABS partitioning systems.


Pssm-ID: 319253 [Multi-domain]  Cd Length: 90  Bit Score: 158.93  E-value: 2.59e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320542283  13 THLVPMSVIQRPIPSVLDEQKVQSLMETIKNETsEDEVPPIDLLWISGsEGGDYYFSFGGCHRFEAYKRLQRPTIKAKLV 92
Cdd:cd16395    1 VHEVPLSVIRRPLPPVLDENKVQSLMETIKGIA-PGLLPPIDVLWVKG-EGGGYYYSFGGCHRYEAHKRLGRETIRCKII 78

                         90
                 ....*....|..
gi 320542283  93 KSTLGDLYHYMG 104
Cdd:cd16395   79 KSTPSDLRVYLG 90
ParBc pfam02195
ParB/Sulfiredoxin domain; Proteins containing this domain include Escherichia coli plasmid ...
 14-89 3.70e-04

ParB/Sulfiredoxin domain; Proteins containing this domain include Escherichia coli plasmid protein ParB and mammalian Sulfiredoxin-1. ParB is involved in chromosome partition. It localizes to both poles of the predivisional cell following completion of DNA replication. Sulfiredoxin-1 contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in the peroxiredoxins PRDX1, PRDX2, PRDX3 and PRDX4.


Pssm-ID: 426651 [Multi-domain]  Cd Length: 90  Bit Score: 36.49  E-value: 3.70e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 320542283   14 HLVPMSVIqRPI---PSVLDEQKVQSLMETIKnetSEDEVPPIDllwISGSEGGDYYFsFGGCHRFEAYKRLQRPTIKA 89
Cdd:pfam02195   1 EEVPISKL-RPNpdqPRKDSEESLEELAASIK---KRGLLQPII---VRKTPDGRYEI-IAGERRLRAAKLLGLKEVPV 71
 
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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