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Conserved domains on  [gi|1021312321|ref|NP_001310494|]
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cysteine dioxygenase type 1 isoform 1 [Homo sapiens]

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 ...
 2-189 8.07e-106

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: 301.95  E-value: 8.07e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312321   2 EQTEVLKPRTLADLIRILHQLFAGDEVNVEEVQAIMEAYESDPTEWAMYAKFDQYSrgrglqfvvgggsgggwlwYTRNL 81
Cdd:pfam05995   1 SSPVSASASTPAPLQAQLLDFFRRAAADVQEVASLMEAYESDPTEWAMYAKFDPEG-------------------YTRNL 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312321  82 VDQGNGKFNLMILCWGEGHGSSIHDHTNSHCFLKMLQGNLKETLFAWPDKKSNEMVKKSERVLRENQCAYINDSIGLHRV 161
Cdd:pfam05995  62 VDAGNGKSNLMILCWGPGTGSSWHDHTDSHCFFKTLAGELKETALAWPLKTLELSDGVDRERRLSNGTGYANDRHGLHRV 141

                         170       180
                  ....*....|....*....|....*...
gi 1021312321 162 ENISHTEPAVSLHLYSPPFDTCHAFDQR 189
Cdd:pfam05995 142 ENESHDRHAVSLHLYYPPLPTCRAFDRR 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 ...
 2-189 8.07e-106

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: 301.95  E-value: 8.07e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312321   2 EQTEVLKPRTLADLIRILHQLFAGDEVNVEEVQAIMEAYESDPTEWAMYAKFDQYSrgrglqfvvgggsgggwlwYTRNL 81
Cdd:pfam05995   1 SSPVSASASTPAPLQAQLLDFFRRAAADVQEVASLMEAYESDPTEWAMYAKFDPEG-------------------YTRNL 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312321  82 VDQGNGKFNLMILCWGEGHGSSIHDHTNSHCFLKMLQGNLKETLFAWPDKKSNEMVKKSERVLRENQCAYINDSIGLHRV 161
Cdd:pfam05995  62 VDAGNGKSNLMILCWGPGTGSSWHDHTDSHCFFKTLAGELKETALAWPLKTLELSDGVDRERRLSNGTGYANDRHGLHRV 141

                         170       180
                  ....*....|....*....|....*...
gi 1021312321 162 ENISHTEPAVSLHLYSPPFDTCHAFDQR 189
Cdd:pfam05995 142 ENESHDRHAVSLHLYYPPLPTCRAFDRR 169
cupin_CDO cd10548
cysteine dioxygenase, cupin domain; This family contains cysteine dioxygenase (CDO; EC 1.13.11. ...
 77-180 5.72e-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: 5.72e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312321  77 YTRNLVDQGNGkFNLMILCWGEGHGSSIHDHTNSHCFLKMLQGNLKETLFAWPDKKSNEmvkkSERVLRE--NQCAYIND 154
Cdd:cd10548     1 YTRNLLYRDPD-FELLLLCWPPGQGSPIHDHGGSWCVVKVLEGELTETRYRRPDDGSLS----GEETLEEtpGDVTYINP 75

                          90       100
                  ....*....|....*....|....*.
gi 1021312321 155 SIGLHRVENIShTEPAVSLHLYSPPF 180
Cdd:cd10548    76 DGGIHRVENPS-DEPAVSLHLYSPPL 100
COG5553 COG5553
Predicted metal-dependent enzyme of the double-stranded beta helix superfamily [General ...
 77-191 5.85e-13

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


Pssm-ID: 444296  Cd Length: 179  Bit Score: 64.58  E-value: 5.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312321  77 YTRNLV-DQGNGKFNLMILCWGEGHGSSIHDHTnSHCFLKMLQGNLKETLFAWPDKKsNEMVKKSERVLREnqcayiNDS 155
Cdd:COG5553    60 YARYLLyADPDGRFSVVAFVWGPGQKTPIHDHG-TWGVIGVLRGAEKNTRYRRTDDG-ARLEPGGEVVLGP------GDV 131

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1021312321 156 IGL------HRVENIShTEPAVSLHLYSPPFDTC--HAFDQRTG 191
Cdd:COG5553   132 IALsppgdiHQVENAG-DEPAISLHVYGGNIGRLvrFVFDPETG 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 ...
 2-189 8.07e-106

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: 301.95  E-value: 8.07e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312321   2 EQTEVLKPRTLADLIRILHQLFAGDEVNVEEVQAIMEAYESDPTEWAMYAKFDQYSrgrglqfvvgggsgggwlwYTRNL 81
Cdd:pfam05995   1 SSPVSASASTPAPLQAQLLDFFRRAAADVQEVASLMEAYESDPTEWAMYAKFDPEG-------------------YTRNL 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312321  82 VDQGNGKFNLMILCWGEGHGSSIHDHTNSHCFLKMLQGNLKETLFAWPDKKSNEMVKKSERVLRENQCAYINDSIGLHRV 161
Cdd:pfam05995  62 VDAGNGKSNLMILCWGPGTGSSWHDHTDSHCFFKTLAGELKETALAWPLKTLELSDGVDRERRLSNGTGYANDRHGLHRV 141

                         170       180
                  ....*....|....*....|....*...
gi 1021312321 162 ENISHTEPAVSLHLYSPPFDTCHAFDQR 189
Cdd:pfam05995 142 ENESHDRHAVSLHLYYPPLPTCRAFDRR 169
cupin_CDO cd10548
cysteine dioxygenase, cupin domain; This family contains cysteine dioxygenase (CDO; EC 1.13.11. ...
 77-180 5.72e-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: 5.72e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312321  77 YTRNLVDQGNGkFNLMILCWGEGHGSSIHDHTNSHCFLKMLQGNLKETLFAWPDKKSNEmvkkSERVLRE--NQCAYIND 154
Cdd:cd10548     1 YTRNLLYRDPD-FELLLLCWPPGQGSPIHDHGGSWCVVKVLEGELTETRYRRPDDGSLS----GEETLEEtpGDVTYINP 75

                          90       100
                  ....*....|....*....|....*.
gi 1021312321 155 SIGLHRVENIShTEPAVSLHLYSPPF 180
Cdd:cd10548    76 DGGIHRVENPS-DEPAVSLHLYSPPL 100
COG5553 COG5553
Predicted metal-dependent enzyme of the double-stranded beta helix superfamily [General ...
 77-191 5.85e-13

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


Pssm-ID: 444296  Cd Length: 179  Bit Score: 64.58  E-value: 5.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312321  77 YTRNLV-DQGNGKFNLMILCWGEGHGSSIHDHTnSHCFLKMLQGNLKETLFAWPDKKsNEMVKKSERVLREnqcayiNDS 155
Cdd:COG5553    60 YARYLLyADPDGRFSVVAFVWGPGQKTPIHDHG-TWGVIGVLRGAEKNTRYRRTDDG-ARLEPGGEVVLGP------GDV 131

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1021312321 156 IGL------HRVENIShTEPAVSLHLYSPPFDTC--HAFDQRTG 191
Cdd:COG5553   132 IALsppgdiHQVENAG-DEPAISLHVYGGNIGRLvrFVFDPETG 174
cupin_ADO cd20289
2-aminoethanethiol dioxygenase, cupin domain; This family contains 2-aminoethanethiol ...
 100-181 1.19e-03

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: 37.14  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312321 100 HGSSI--HDHTNSHCFLKMLQGNLKETLFAWPDKKSNEMVKKSERVLR---------ENQCAYINDSIG-LHRVENIshT 167
Cdd:cd20289    12 PGARIplHDHPGMTGLSKVLYGSLRVKSYDWLDDPPEDLPPLKPRLARlvgdavltaSSEPCVLTPTEGnIHEIVAV--E 89

                          90
                  ....*....|....
gi 1021312321 168 EPAVSLHLYSPPFD 181
Cdd:cd20289    90 GPAAFLDILSPPYD 103
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
76-180 2.95e-03

Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 36.27  E-value: 2.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312321  76 WYTRNLVDQGNGKFNLMILCWGEGHGSSIHDHTNSHCFLKMLQGNLKETlfawpdkksnemVKKSERVLRENQCAYINDS 155
Cdd:COG0662    14 WGSYEVLGEGGERLSVKRITVPPGAELSLHVHPHRDEFFYVLEGTGEVT------------IGDEEVELKAGDSVYIPAG 81

                          90       100
                  ....*....|....*....|....*
gi 1021312321 156 IgLHRVENIShTEPAVSLHLYSPPF 180
Cdd:COG0662    82 V-PHRLRNPG-DEPLELLEVQAPAY 104
 
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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