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Conserved domains on  [gi|2462600126|ref|XP_054207403|]
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cysteine dioxygenase type 1 isoform X1 [Homo sapiens]

Protein Classification

cupin domain-containing protein( domain architecture ID 1562428)

cupin domain-containing protein, part of a functionally diverse superfamily with the active site generally located at the center of a conserved domain forming a beta-barrel fold

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cupin_RmlC-like super family cl40423
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 56-168 3.07e-76

RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase)-like cupins. RmlC is a dTDP-sugar isomerase involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria. Cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin ('cupa' is the Latin term for small barrel). The active site of members of this superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. The different functional classes in this superfamily include single domain bacterial isomerases and epimerases involved in the modification of cell wall carbohydrates, two domain bicupins such as the desiccation-tolerant seed storage globulins, and multidomain nuclear transcription factors involved in legume root nodulation.


The actual alignment was detected with superfamily member pfam05995:

Pssm-ID: 477354  Cd Length: 169  Bit Score: 226.07  E-value: 3.07e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600126  56 YTRNLVDQGNGKFNLMILCWGEGHGSSIHDHTNSHCFLKMLQGNLKETLFAWPDKKSNEMVKKSERVLRENQCAYINDSI 135
Cdd:pfam05995  57 YTRNLVDAGNGKSNLMILCWGPGTGSSWHDHTDSHCFFKTLAGELKETALAWPLKTLELSDGVDRERRLSNGTGYANDRH 136

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2462600126 136 GLHRVENISHTEPAVSLHLYSPPFDTCHAFDQR 168
Cdd:pfam05995 137 GLHRVENESHDRHAVSLHLYYPPLPTCRAFDRR 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 ...
 56-168 3.07e-76

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: 226.07  E-value: 3.07e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600126  56 YTRNLVDQGNGKFNLMILCWGEGHGSSIHDHTNSHCFLKMLQGNLKETLFAWPDKKSNEMVKKSERVLRENQCAYINDSI 135
Cdd:pfam05995  57 YTRNLVDAGNGKSNLMILCWGPGTGSSWHDHTDSHCFFKTLAGELKETALAWPLKTLELSDGVDRERRLSNGTGYANDRH 136

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2462600126 136 GLHRVENISHTEPAVSLHLYSPPFDTCHAFDQR 168
Cdd:pfam05995 137 GLHRVENESHDRHAVSLHLYYPPLPTCRAFDRR 169
cupin_CDO cd10548
cysteine dioxygenase, cupin domain; This family contains cysteine dioxygenase (CDO; EC 1.13.11. ...
 56-159 1.40e-42

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: 138.20  E-value: 1.40e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600126  56 YTRNLVDQGNGkFNLMILCWGEGHGSSIHDHTNSHCFLKMLQGNLKETLFAWPDKKSNEmvkkSERVLRE--NQCAYIND 133
Cdd:cd10548     1 YTRNLLYRDPD-FELLLLCWPPGQGSPIHDHGGSWCVVKVLEGELTETRYRRPDDGSLS----GEETLEEtpGDVTYINP 75

                          90       100
                  ....*....|....*....|....*.
gi 2462600126 134 SIGLHRVENIShTEPAVSLHLYSPPF 159
Cdd:cd10548    76 DGGIHRVENPS-DEPAVSLHLYSPPL 100
COG5553 COG5553
Predicted metal-dependent enzyme of the double-stranded beta helix superfamily [General ...
 56-170 3.88e-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: 3.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600126  56 YTRNLV-DQGNGKFNLMILCWGEGHGSSIHDHTnSHCFLKMLQGNLKETLFAWPDKKsNEMVKKSERVLREnqcayiNDS 134
Cdd:COG5553    60 YARYLLyADPDGRFSVVAFVWGPGQKTPIHDHG-TWGVIGVLRGAEKNTRYRRTDDG-ARLEPGGEVVLGP------GDV 131

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462600126 135 IGL------HRVENIShTEPAVSLHLYSPPFDTC--HAFDQRTG 170
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 ...
 56-168 3.07e-76

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: 226.07  E-value: 3.07e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600126  56 YTRNLVDQGNGKFNLMILCWGEGHGSSIHDHTNSHCFLKMLQGNLKETLFAWPDKKSNEMVKKSERVLRENQCAYINDSI 135
Cdd:pfam05995  57 YTRNLVDAGNGKSNLMILCWGPGTGSSWHDHTDSHCFFKTLAGELKETALAWPLKTLELSDGVDRERRLSNGTGYANDRH 136

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2462600126 136 GLHRVENISHTEPAVSLHLYSPPFDTCHAFDQR 168
Cdd:pfam05995 137 GLHRVENESHDRHAVSLHLYYPPLPTCRAFDRR 169
cupin_CDO cd10548
cysteine dioxygenase, cupin domain; This family contains cysteine dioxygenase (CDO; EC 1.13.11. ...
 56-159 1.40e-42

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: 138.20  E-value: 1.40e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600126  56 YTRNLVDQGNGkFNLMILCWGEGHGSSIHDHTNSHCFLKMLQGNLKETLFAWPDKKSNEmvkkSERVLRE--NQCAYIND 133
Cdd:cd10548     1 YTRNLLYRDPD-FELLLLCWPPGQGSPIHDHGGSWCVVKVLEGELTETRYRRPDDGSLS----GEETLEEtpGDVTYINP 75

                          90       100
                  ....*....|....*....|....*.
gi 2462600126 134 SIGLHRVENIShTEPAVSLHLYSPPF 159
Cdd:cd10548    76 DGGIHRVENPS-DEPAVSLHLYSPPL 100
COG5553 COG5553
Predicted metal-dependent enzyme of the double-stranded beta helix superfamily [General ...
 56-170 3.88e-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: 3.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600126  56 YTRNLV-DQGNGKFNLMILCWGEGHGSSIHDHTnSHCFLKMLQGNLKETLFAWPDKKsNEMVKKSERVLREnqcayiNDS 134
Cdd:COG5553    60 YARYLLyADPDGRFSVVAFVWGPGQKTPIHDHG-TWGVIGVLRGAEKNTRYRRTDDG-ARLEPGGEVVLGP------GDV 131

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462600126 135 IGL------HRVENIShTEPAVSLHLYSPPFDTC--HAFDQRTG 170
Cdd:COG5553   132 IALsppgdiHQVENAG-DEPAISLHVYGGNIGRLvrFVFDPETG 174
cupin_ADO cd20289
2-aminoethanethiol dioxygenase, cupin domain; This family contains 2-aminoethanethiol ...
 79-160 1.12e-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: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600126  79 HGSSI--HDHTNSHCFLKMLQGNLKETLFAWPDKKSNEMVKKSERVLR---------ENQCAYINDSIG-LHRVENIshT 146
Cdd:cd20289    12 PGARIplHDHPGMTGLSKVLYGSLRVKSYDWLDDPPEDLPPLKPRLARlvgdavltaSSEPCVLTPTEGnIHEIVAV--E 89

                          90
                  ....*....|....
gi 2462600126 147 EPAVSLHLYSPPFD 160
Cdd:cd20289    90 GPAAFLDILSPPYD 103
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
55-159 2.28e-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: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462600126  55 WYTRNLVDQGNGKFNLMILCWGEGHGSSIHDHTNSHCFLKMLQGNLKETlfawpdkksnemVKKSERVLRENQCAYINDS 134
Cdd:COG0662    14 WGSYEVLGEGGERLSVKRITVPPGAELSLHVHPHRDEFFYVLEGTGEVT------------IGDEEVELKAGDSVYIPAG 81

                          90       100
                  ....*....|....*....|....*
gi 2462600126 135 IgLHRVENIShTEPAVSLHLYSPPF 159
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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