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Conserved domains on  [gi|446877182|ref|WP_000954438|]
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MULTISPECIES: cysteine dioxygenase family protein [Bacillus]

Protein Classification

COG5553 family protein( domain architecture ID 10009427)

COG5553 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG5553 COG5553
Predicted metal-dependent enzyme of the double-stranded beta helix superfamily [General ...
 1-179 6.07e-37

Predicted metal-dependent enzyme of the double-stranded beta helix superfamily [General function prediction only];


:

Pssm-ID: 444296  Cd Length: 179  Bit Score: 126.21  E-value: 6.07e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446877182   1 MLTCNGSKSFQKFIKGVTDLMENGLFEEEIVCGIEKLLEELLEKKTWLPLDKQKANLTQYARHLLYEDPLKRFEVLALVW 80
Cdd:COG5553    1 MTTQRRPPRLRRFIAALRALVDRGPDEREILAAVRPLLRRLVASDDWLPAEFAEPDPDRYARYLLYADPDGRFSVVAFVW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446877182  81 KDGQSTPLHDHdGTWGVEGVFSGRIMVQNFiqtkQLGNSLVYLTHTGNLYLGEGETDKVIPPADCHILEISTNESVITIH 160
Cdd:COG5553   81 GPGQKTPIHDH-GTWGVIGVLRGAEKNTRY----RRTDDGARLEPGGEVVLGPGDVIALSPPGDIHQVENAGDEPAISLH 155

                        170
                 ....*....|....*....
gi 446877182 161 VYGKRLEKFKVYIPTEEKN 179
Cdd:COG5553  156 VYGGNIGRLVRFVFDPETG 174
 
Name Accession Description Interval E-value
COG5553 COG5553
Predicted metal-dependent enzyme of the double-stranded beta helix superfamily [General ...
 1-179 6.07e-37

Predicted metal-dependent enzyme of the double-stranded beta helix superfamily [General function prediction only];


Pssm-ID: 444296  Cd Length: 179  Bit Score: 126.21  E-value: 6.07e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446877182   1 MLTCNGSKSFQKFIKGVTDLMENGLFEEEIVCGIEKLLEELLEKKTWLPLDKQKANLTQYARHLLYEDPLKRFEVLALVW 80
Cdd:COG5553    1 MTTQRRPPRLRRFIAALRALVDRGPDEREILAAVRPLLRRLVASDDWLPAEFAEPDPDRYARYLLYADPDGRFSVVAFVW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446877182  81 KDGQSTPLHDHdGTWGVEGVFSGRIMVQNFiqtkQLGNSLVYLTHTGNLYLGEGETDKVIPPADCHILEISTNESVITIH 160
Cdd:COG5553   81 GPGQKTPIHDH-GTWGVIGVLRGAEKNTRY----RRTDDGARLEPGGEVVLGPGDVIALSPPGDIHQVENAGDEPAISLH 155

                        170
                 ....*....|....*....
gi 446877182 161 VYGKRLEKFKVYIPTEEKN 179
Cdd:COG5553  156 VYGGNIGRLVRFVFDPETG 174
cupin_CDO cd10548
cysteine dioxygenase, cupin domain; This family contains cysteine dioxygenase (CDO; EC 1.13.11. ...
 60-166 5.67e-27

cysteine dioxygenase, cupin domain; This family contains cysteine dioxygenase (CDO; EC 1.13.11.20), which catalyzes the conversion of cysteine to cysteine sulfinic acid, the first step in the biosynthesis of essential oxidized cysteine metabolites such as sulfate, hypotaurine, and taurine. CDO also plays an important role in the regulation of intracellular cysteine levels in mammals; CDO expression is altered in cancer cells, and abnormal or deficient CDO activity has been linked to Parkinson's disease, Alzheimer's disease, and rheumatoid arthritis. CDO is an iron-dependent thiol dioxygenase that uses molecular oxygen to oxidize the sulfhydryl group of cysteine to generate cysteine sulfinic acid. The CDO active site contains an amino acid-derived cofactor. These enzymes are found in prokaryotes as well as eukaryotes and belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380416 [Multi-domain]  Cd Length: 100  Bit Score: 98.14  E-value: 5.67e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446877182  60 YARHLLYEDPlkRFEVLALVWKDGQSTPLHDHDGTWGVEGVFSGRIMVQNFIQTKQLGnslvyLTHTGNLYLGEGETDKV 139
Cdd:cd10548    1 YTRNLLYRDP--DFELLLLCWPPGQGSPIHDHGGSWCVVKVLEGELTETRYRRPDDGS-----LSGEETLEETPGDVTYI 73

                         90       100
                 ....*....|....*....|....*..
gi 446877182 140 IPPADCHILEISTNESVITIHVYGKRL 166
Cdd:cd10548   74 NPDGGIHRVENPSDEPAVSLHLYSPPL 100
 
Name Accession Description Interval E-value
COG5553 COG5553
Predicted metal-dependent enzyme of the double-stranded beta helix superfamily [General ...
 1-179 6.07e-37

Predicted metal-dependent enzyme of the double-stranded beta helix superfamily [General function prediction only];


Pssm-ID: 444296  Cd Length: 179  Bit Score: 126.21  E-value: 6.07e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446877182   1 MLTCNGSKSFQKFIKGVTDLMENGLFEEEIVCGIEKLLEELLEKKTWLPLDKQKANLTQYARHLLYEDPLKRFEVLALVW 80
Cdd:COG5553    1 MTTQRRPPRLRRFIAALRALVDRGPDEREILAAVRPLLRRLVASDDWLPAEFAEPDPDRYARYLLYADPDGRFSVVAFVW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446877182  81 KDGQSTPLHDHdGTWGVEGVFSGRIMVQNFiqtkQLGNSLVYLTHTGNLYLGEGETDKVIPPADCHILEISTNESVITIH 160
Cdd:COG5553   81 GPGQKTPIHDH-GTWGVIGVLRGAEKNTRY----RRTDDGARLEPGGEVVLGPGDVIALSPPGDIHQVENAGDEPAISLH 155

                        170
                 ....*....|....*....
gi 446877182 161 VYGKRLEKFKVYIPTEEKN 179
Cdd:COG5553  156 VYGGNIGRLVRFVFDPETG 174
cupin_CDO cd10548
cysteine dioxygenase, cupin domain; This family contains cysteine dioxygenase (CDO; EC 1.13.11. ...
 60-166 5.67e-27

cysteine dioxygenase, cupin domain; This family contains cysteine dioxygenase (CDO; EC 1.13.11.20), which catalyzes the conversion of cysteine to cysteine sulfinic acid, the first step in the biosynthesis of essential oxidized cysteine metabolites such as sulfate, hypotaurine, and taurine. CDO also plays an important role in the regulation of intracellular cysteine levels in mammals; CDO expression is altered in cancer cells, and abnormal or deficient CDO activity has been linked to Parkinson's disease, Alzheimer's disease, and rheumatoid arthritis. CDO is an iron-dependent thiol dioxygenase that uses molecular oxygen to oxidize the sulfhydryl group of cysteine to generate cysteine sulfinic acid. The CDO active site contains an amino acid-derived cofactor. These enzymes are found in prokaryotes as well as eukaryotes and belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380416 [Multi-domain]  Cd Length: 100  Bit Score: 98.14  E-value: 5.67e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446877182  60 YARHLLYEDPlkRFEVLALVWKDGQSTPLHDHDGTWGVEGVFSGRIMVQNFIQTKQLGnslvyLTHTGNLYLGEGETDKV 139
Cdd:cd10548    1 YTRNLLYRDP--DFELLLLCWPPGQGSPIHDHGGSWCVVKVLEGELTETRYRRPDDGS-----LSGEETLEETPGDVTYI 73

                         90       100
                 ....*....|....*....|....*..
gi 446877182 140 IPPADCHILEISTNESVITIHVYGKRL 166
Cdd:cd10548   74 NPDGGIHRVENPSDEPAVSLHLYSPPL 100
 
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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