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Conserved domains on  [gi|149064195|gb|EDM14398|]
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cysteine dioxygenase 1, cytosolic, isoform CRA_d [Rattus norvegicus]

Protein Classification

similar to cysteine dioxygenase( domain architecture ID 10532333)

protein similar to cysteine dioxygenase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CDO_I pfam05995
Cysteine dioxygenase type I; Cysteine dioxygenase type I (EC:1.13.11.20) converts cysteine to ...
 2-170 1.94e-105

Cysteine dioxygenase type I; Cysteine dioxygenase type I (EC:1.13.11.20) converts cysteine to cysteinesulphinic acid and is the rate-limiting step in sulphate production.


:

Pssm-ID: 428713  Cd Length: 169  Bit Score: 300.02  E-value: 1.94e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064195    2 ERTELLKPRTLADLIRILHELFAGDEVNVEEVQAVLEAYESNPAEWALYAKFDQYRYTRNLVDQGNGKFNLMILCWGEGH 81
Cdd:pfam05995   1 SSPVSASASTPAPLQAQLLDFFRRAAADVQEVASLMEAYESDPTEWAMYAKFDPEGYTRNLVDAGNGKSNLMILCWGPGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064195   82 GSSIHDHTDSHCFLKLLQGNLKETLFDWPDKKSNEMIKKSERTLRENQCAYINDSIGLHRVENVSHTEPAVSLHLYSPPF 161
Cdd:pfam05995  81 GSSWHDHTDSHCFFKTLAGELKETALAWPLKTLELSDGVDRERRLSNGTGYANDRHGLHRVENESHDRHAVSLHLYYPPL 160


                  ....*....
gi 149064195  162 DTCHAFDQR 170
Cdd:pfam05995 161 PTCRAFDRR 169
 
Name Accession Description Interval E-value
CDO_I pfam05995
Cysteine dioxygenase type I; Cysteine dioxygenase type I (EC:1.13.11.20) converts cysteine to ...
 2-170 1.94e-105

Cysteine dioxygenase type I; Cysteine dioxygenase type I (EC:1.13.11.20) converts cysteine to cysteinesulphinic acid and is the rate-limiting step in sulphate production.


Pssm-ID: 428713  Cd Length: 169  Bit Score: 300.02  E-value: 1.94e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064195    2 ERTELLKPRTLADLIRILHELFAGDEVNVEEVQAVLEAYESNPAEWALYAKFDQYRYTRNLVDQGNGKFNLMILCWGEGH 81
Cdd:pfam05995   1 SSPVSASASTPAPLQAQLLDFFRRAAADVQEVASLMEAYESDPTEWAMYAKFDPEGYTRNLVDAGNGKSNLMILCWGPGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064195   82 GSSIHDHTDSHCFLKLLQGNLKETLFDWPDKKSNEMIKKSERTLRENQCAYINDSIGLHRVENVSHTEPAVSLHLYSPPF 161
Cdd:pfam05995  81 GSSWHDHTDSHCFFKTLAGELKETALAWPLKTLELSDGVDRERRLSNGTGYANDRHGLHRVENESHDRHAVSLHLYYPPL 160


                  ....*....
gi 149064195  162 DTCHAFDQR 170
Cdd:pfam05995 161 PTCRAFDRR 169
cupin_CDO cd10548
cysteine dioxygenase, cupin domain; This family contains cysteine dioxygenase (CDO; EC 1.13.11. ...
 58-161 2.57e-43

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: 140.13  E-value: 2.57e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064195  58 YTRNLVDQGNGkFNLMILCWGEGHGSSIHDHTDSHCFLKLLQGNLKETLFDWPDKKSNEmikkSERTLRE--NQCAYIND 135
Cdd:cd10548    1 YTRNLLYRDPD-FELLLLCWPPGQGSPIHDHGGSWCVVKVLEGELTETRYRRPDDGSLS----GEETLEEtpGDVTYINP 75

                         90       100
                 ....*....|....*....|....*.
gi 149064195 136 SIGLHRVENVShTEPAVSLHLYSPPF 161
Cdd:cd10548   76 DGGIHRVENPS-DEPAVSLHLYSPPL 100
COG5553 COG5553
Predicted metal-dependent enzyme of the double-stranded beta helix superfamily [General ...
 4-172 2.24e-14

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


Pssm-ID: 444296  Cd Length: 179  Bit Score: 68.05  E-value: 2.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064195   4 TELLKPRTLADLI---RILHELFAGDEVNVEEVQAVLEAYESNPaEWaLYAKFDQY---RYTRNLV-DQGNGKFNLMILC 76
Cdd:COG5553    2 TTQRRPPRLRRFIaalRALVDRGPDEREILAAVRPLLRRLVASD-DW-LPAEFAEPdpdRYARYLLyADPDGRFSVVAFV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064195  77 WGEGHGSSIHDHTdSHCFLKLLQGNLKETLFDWPDKKsNEMIKKSERTLREnqcayiNDSIGL------HRVENVShTEP 150
Cdd:COG5553   80 WGPGQKTPIHDHG-TWGVIGVLRGAEKNTRYRRTDDG-ARLEPGGEVVLGP------GDVIALsppgdiHQVENAG-DEP 150

                        170       180
                 ....*....|....*....|....
gi 149064195 151 AVSLHLYSPPFDTC--HAFDQRTG 172
Cdd:COG5553  151 AISLHVYGGNIGRLvrFVFDPETG 174
 
Name Accession Description Interval E-value
CDO_I pfam05995
Cysteine dioxygenase type I; Cysteine dioxygenase type I (EC:1.13.11.20) converts cysteine to ...
 2-170 1.94e-105

Cysteine dioxygenase type I; Cysteine dioxygenase type I (EC:1.13.11.20) converts cysteine to cysteinesulphinic acid and is the rate-limiting step in sulphate production.


Pssm-ID: 428713  Cd Length: 169  Bit Score: 300.02  E-value: 1.94e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064195    2 ERTELLKPRTLADLIRILHELFAGDEVNVEEVQAVLEAYESNPAEWALYAKFDQYRYTRNLVDQGNGKFNLMILCWGEGH 81
Cdd:pfam05995   1 SSPVSASASTPAPLQAQLLDFFRRAAADVQEVASLMEAYESDPTEWAMYAKFDPEGYTRNLVDAGNGKSNLMILCWGPGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064195   82 GSSIHDHTDSHCFLKLLQGNLKETLFDWPDKKSNEMIKKSERTLRENQCAYINDSIGLHRVENVSHTEPAVSLHLYSPPF 161
Cdd:pfam05995  81 GSSWHDHTDSHCFFKTLAGELKETALAWPLKTLELSDGVDRERRLSNGTGYANDRHGLHRVENESHDRHAVSLHLYYPPL 160


                  ....*....
gi 149064195  162 DTCHAFDQR 170
Cdd:pfam05995 161 PTCRAFDRR 169
cupin_CDO cd10548
cysteine dioxygenase, cupin domain; This family contains cysteine dioxygenase (CDO; EC 1.13.11. ...
 58-161 2.57e-43

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: 140.13  E-value: 2.57e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064195  58 YTRNLVDQGNGkFNLMILCWGEGHGSSIHDHTDSHCFLKLLQGNLKETLFDWPDKKSNEmikkSERTLRE--NQCAYIND 135
Cdd:cd10548    1 YTRNLLYRDPD-FELLLLCWPPGQGSPIHDHGGSWCVVKVLEGELTETRYRRPDDGSLS----GEETLEEtpGDVTYINP 75

                         90       100
                 ....*....|....*....|....*.
gi 149064195 136 SIGLHRVENVShTEPAVSLHLYSPPF 161
Cdd:cd10548   76 DGGIHRVENPS-DEPAVSLHLYSPPL 100
COG5553 COG5553
Predicted metal-dependent enzyme of the double-stranded beta helix superfamily [General ...
 4-172 2.24e-14

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


Pssm-ID: 444296  Cd Length: 179  Bit Score: 68.05  E-value: 2.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064195   4 TELLKPRTLADLI---RILHELFAGDEVNVEEVQAVLEAYESNPaEWaLYAKFDQY---RYTRNLV-DQGNGKFNLMILC 76
Cdd:COG5553    2 TTQRRPPRLRRFIaalRALVDRGPDEREILAAVRPLLRRLVASD-DW-LPAEFAEPdpdRYARYLLyADPDGRFSVVAFV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064195  77 WGEGHGSSIHDHTdSHCFLKLLQGNLKETLFDWPDKKsNEMIKKSERTLREnqcayiNDSIGL------HRVENVShTEP 150
Cdd:COG5553   80 WGPGQKTPIHDHG-TWGVIGVLRGAEKNTRYRRTDDG-ARLEPGGEVVLGP------GDVIALsppgdiHQVENAG-DEP 150

                        170       180
                 ....*....|....*....|....
gi 149064195 151 AVSLHLYSPPFDTC--HAFDQRTG 172
Cdd:COG5553  151 AISLHVYGGNIGRLvrFVFDPETG 174
cupin_ADO cd20289
2-aminoethanethiol dioxygenase, cupin domain; This family contains 2-aminoethanethiol ...
 81-162 8.64e-05

2-aminoethanethiol dioxygenase, cupin domain; This family contains 2-aminoethanethiol dioxygenase (also known as cysteamine dioxygenase, persulfurase or ADO; EC 1.13.11.19), which catalyzes the addition of two oxygen atoms to free cysteamine (2-aminoethanethiol) to form hypotaurine that subsequently oxidizes to taurine. 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: 380423  Cd Length: 103  Bit Score: 40.23  E-value: 8.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064195  81 HGSSI--HDHTDSHCFLKLLQGNLKETLFDWPDKKSNEMIKKSERTLR---------ENQCAYINDSIG-LHRVENVshT 148
Cdd:cd20289   12 PGARIplHDHPGMTGLSKVLYGSLRVKSYDWLDDPPEDLPPLKPRLARlvgdavltaSSEPCVLTPTEGnIHEIVAV--E 89

                         90
                 ....*....|....
gi 149064195 149 EPAVSLHLYSPPFD 162
Cdd:cd20289   90 GPAAFLDILSPPYD 103
PCO_ADO pfam07847
PCO_ADO; This entry includes cysteine oxidases (PCOs) from plants and 2-aminoethanethiol ...
 82-168 6.19e-03

PCO_ADO; This entry includes cysteine oxidases (PCOs) from plants and 2-aminoethanethiol dioxygenases (ADOs) from animals.


Pssm-ID: 462286  Cd Length: 201  Bit Score: 36.15  E-value: 6.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064195   82 GSSI--HDHTDSHCFLKLLQGNLKETLFDWPDK---------KSNEMIKKSERTLREnQCA----YINDSIGLHRVENVs 146
Cdd:pfam07847  54 GAVIplHDHPGMTVFSKLLYGSVHIKSYDWVDPpvdspgqgrPLRLAKLVSDGEFTA-PSDtsvlYPTEGGNLHEITAI- 131

                          90       100
                  ....*....|....*....|..
gi 149064195  147 hTEPAVSLHLYSPPFDTCHAFD 168
Cdd:pfam07847 132 -TGPCAFLDILAPPYSEDPGRD 152
 
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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