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Conserved domains on  [gi|1002274519|ref|XP_015641574|]
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sulfite oxidase [Oryza sativa Japonica Group]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN00177 super family cl30134
sulfite oxidase; Provisional
 7-65 6.09e-17

sulfite oxidase; Provisional


The actual alignment was detected with superfamily member PLN00177:

Pssm-ID: 177772 [Multi-domain]  Cd Length: 393  Bit Score: 72.96  E-value: 6.09e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002274519   7 SYYVTIGTLIDRPAKLSLDDIKRGSGPSTMSLPLC---RRTEISKSRKVRGITWDICALGNG 65
Cdd:PLN00177   64 RYSVTITGLIENPRKLSMKDIRKLPKYNVTATLQCagnRRTAMSKVRKVRGVGWDVSAIGNA 125
 
Name Accession Description Interval E-value
PLN00177 PLN00177
sulfite oxidase; Provisional
 7-65 6.09e-17

sulfite oxidase; Provisional


Pssm-ID: 177772 [Multi-domain]  Cd Length: 393  Bit Score: 72.96  E-value: 6.09e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002274519   7 SYYVTIGTLIDRPAKLSLDDIKRGSGPSTMSLPLC---RRTEISKSRKVRGITWDICALGNG 65
Cdd:PLN00177   64 RYSVTITGLIENPRKLSMKDIRKLPKYNVTATLQCagnRRTAMSKVRKVRGVGWDVSAIGNA 125
eukary_SO_Moco cd02111
molybdopterin binding domain of sulfite oxidase (SO). SO catalyzes the terminal reaction in ...
 6-64 6.25e-07

molybdopterin binding domain of sulfite oxidase (SO). SO catalyzes the terminal reaction in the oxidative degradation of the sulfur-containing amino acids cysteine and methionine. Common features of all known members of the sulfite oxidase (SO) family of molybdopterin binding domains are that they contain one single pterin cofactor and part of the coordination of the metal (Mo) is a cysteine ligand of the protein and that they catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate.


Pssm-ID: 239029 [Multi-domain]  Cd Length: 365  Bit Score: 44.69  E-value: 6.25e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002274519   6 ASYYVTIGTLIDRPAKLSLDDIKRGSGPSTMSLPL-C---RRTEISKSRKVRGITWDICALGN 64
Cdd:cd02111    44 DTYSLEVEGPDGTTLSLSLEDLKSLFPKHEVTATLqCagnRRSEMTKVKKVKGLQWGDGAISN 106
Oxidored_molyb pfam00174
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ...
 6-64 1.19e-03

Oxidoreductase molybdopterin binding domain; This domain is found in a variety of oxidoreductases. This domain binds to a molybdopterin cofactor. Xanthine dehydrogenases, that also bind molybdopterin, have essentially no similarity.


Pssm-ID: 459699 [Multi-domain]  Cd Length: 168  Bit Score: 35.17  E-value: 1.19e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002274519   6 ASYYVTIGTLIDRPAKLSLDDIKRgsgpstmsLPL--------C---RRTEIsksRKVRGITWDICALGN 64
Cdd:pfam00174  10 DTWRLRVDGLVEKPLTLTLDDLKA--------FPQvtvtatlqCvgnRRKEM---NRVKGVQWGGGAIGN 68
 
Name Accession Description Interval E-value
PLN00177 PLN00177
sulfite oxidase; Provisional
 7-65 6.09e-17

sulfite oxidase; Provisional


Pssm-ID: 177772 [Multi-domain]  Cd Length: 393  Bit Score: 72.96  E-value: 6.09e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002274519   7 SYYVTIGTLIDRPAKLSLDDIKRGSGPSTMSLPLC---RRTEISKSRKVRGITWDICALGNG 65
Cdd:PLN00177   64 RYSVTITGLIENPRKLSMKDIRKLPKYNVTATLQCagnRRTAMSKVRKVRGVGWDVSAIGNA 125
eukary_SO_Moco cd02111
molybdopterin binding domain of sulfite oxidase (SO). SO catalyzes the terminal reaction in ...
 6-64 6.25e-07

molybdopterin binding domain of sulfite oxidase (SO). SO catalyzes the terminal reaction in the oxidative degradation of the sulfur-containing amino acids cysteine and methionine. Common features of all known members of the sulfite oxidase (SO) family of molybdopterin binding domains are that they contain one single pterin cofactor and part of the coordination of the metal (Mo) is a cysteine ligand of the protein and that they catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate.


Pssm-ID: 239029 [Multi-domain]  Cd Length: 365  Bit Score: 44.69  E-value: 6.25e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002274519   6 ASYYVTIGTLIDRPAKLSLDDIKRGSGPSTMSLPL-C---RRTEISKSRKVRGITWDICALGN 64
Cdd:cd02111    44 DTYSLEVEGPDGTTLSLSLEDLKSLFPKHEVTATLqCagnRRSEMTKVKKVKGLQWGDGAISN 106
Oxidored_molyb pfam00174
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ...
 6-64 1.19e-03

Oxidoreductase molybdopterin binding domain; This domain is found in a variety of oxidoreductases. This domain binds to a molybdopterin cofactor. Xanthine dehydrogenases, that also bind molybdopterin, have essentially no similarity.


Pssm-ID: 459699 [Multi-domain]  Cd Length: 168  Bit Score: 35.17  E-value: 1.19e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002274519   6 ASYYVTIGTLIDRPAKLSLDDIKRgsgpstmsLPL--------C---RRTEIsksRKVRGITWDICALGN 64
Cdd:pfam00174  10 DTWRLRVDGLVEKPLTLTLDDLKA--------FPQvtvtatlqCvgnRRKEM---NRVKGVQWGGGAIGN 68
 
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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