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Conserved domains on  [gi|695770883|ref|WP_032693833|]
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MULTISPECIES: molybdopterin-dependent oxidoreductase [Klebsiella]

Protein Classification

COG3915 family protein( domain architecture ID 10008133)

COG3915 family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG3915 COG3915
Uncharacterized conserved protein [Function unknown];
1-165 1.55e-87

Uncharacterized conserved protein [Function unknown];


:

Pssm-ID: 443120  Cd Length: 167  Bit Score: 253.27  E-value: 1.55e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695770883   1 MRLIFAALFCVMVSPSAFAEKLPAPVGKPVLTISGLIANTNEGDTAVFDVAALEKLGMETLVTTTPWYSGKVRFDGISLS 80
Cdd:COG3915    3 LLRLLALLLALLLLPAAAAAALPAPAGPVILTVSGKIGNTNAGGAATFDLAMLEALPQTEITTTTPWTDGVQTFRGVLLR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695770883  81 KLMDLVGAKGKSARVLALNDYTTIVPLDDFHKFPVILALKMNGEYMRIRDKGPLFIVYPYDSSPELQNQIYYSRSAWQVS 160
Cdd:COG3915   83 DLLAAVGAKGTTLRAVALNDYAVEIPISDLEEYGVILAYRMDGKPMSVRDKGPLWLIYPYDDYPELQTEVYYSRSVWQLK 162

                 ....*
gi 695770883 161 KIIIE 165
Cdd:COG3915  163 RIEVE 167
 
Name Accession Description Interval E-value
COG3915 COG3915
Uncharacterized conserved protein [Function unknown];
1-165 1.55e-87

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443120  Cd Length: 167  Bit Score: 253.27  E-value: 1.55e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695770883   1 MRLIFAALFCVMVSPSAFAEKLPAPVGKPVLTISGLIANTNEGDTAVFDVAALEKLGMETLVTTTPWYSGKVRFDGISLS 80
Cdd:COG3915    3 LLRLLALLLALLLLPAAAAAALPAPAGPVILTVSGKIGNTNAGGAATFDLAMLEALPQTEITTTTPWTDGVQTFRGVLLR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695770883  81 KLMDLVGAKGKSARVLALNDYTTIVPLDDFHKFPVILALKMNGEYMRIRDKGPLFIVYPYDSSPELQNQIYYSRSAWQVS 160
Cdd:COG3915   83 DLLAAVGAKGTTLRAVALNDYAVEIPISDLEEYGVILAYRMDGKPMSVRDKGPLWLIYPYDDYPELQTEVYYSRSVWQLK 162

                 ....*
gi 695770883 161 KIIIE 165
Cdd:COG3915  163 RIEVE 167
SO_family_Moco cd00321
Sulfite oxidase (SO) family, molybdopterin binding domain. This molybdopterin cofactor (Moco) ...
31-139 1.40e-10

Sulfite oxidase (SO) family, molybdopterin binding domain. This molybdopterin cofactor (Moco) binding domain is found in a variety of oxidoreductases, main members of this family are nitrate reductase (NR) and sulfite oxidase (SO). SO catalyzes the terminal reaction in the oxidative degradation of the sulfur-containing amino acids cysteine and methionine. Assimilatory NRs catalyze the reduction of nitrate to nitrite which is subsequently converted to NH4+ by nitrite reductase. Common features of all known members of this family 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: 238198 [Multi-domain]  Cd Length: 156  Bit Score: 56.42  E-value: 1.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695770883  31 LTISGLIANTnegdtAVFDVAALEKLGMETLVTT--------TPWYSGKVRFDGISLSKLMDLVGAKGK-------SARV 95
Cdd:cd00321   19 LEVDGLVEKP-----LSLTLDDLKALPQVEVIATlhcvgnrwGGGAVSNAEWTGVPLRDLLEEAGPKPGaryvvfeGADD 93
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 695770883  96 LALNDYTTIVPLDDFHKFPVILALKMNGEYMRIRDKGPLFIVYP 139
Cdd:cd00321   94 PGGDGYTTSLPLEKALDPDVLLAYEMNGEPLPPDHGFPLRLVVP 137
Oxidored_molyb pfam00174
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ...
31-124 2.90e-07

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: 47.50  E-value: 2.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695770883   31 LTISGLIANTnegdtAVFDVAALEKLGMETLVTT----------------TPW---YSGKVRFDGISLSKLMDLVGAKGK 91
Cdd:pfam00174  14 LRVDGLVEKP-----LTLTLDDLKAFPQVTVTATlqcvgnrrkemnrvkgVQWgggAIGNAEWTGVPLRDLLERAGVKPG 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 695770883   92 -------SARVLALNDYTTIVPLDDFHKFPVILALKMNGE 124
Cdd:pfam00174  89 akhvlfeGADTLGDGGYTTSLPLEKALDDDVLLAYEMNGE 128
 
Name Accession Description Interval E-value
COG3915 COG3915
Uncharacterized conserved protein [Function unknown];
1-165 1.55e-87

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443120  Cd Length: 167  Bit Score: 253.27  E-value: 1.55e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695770883   1 MRLIFAALFCVMVSPSAFAEKLPAPVGKPVLTISGLIANTNEGDTAVFDVAALEKLGMETLVTTTPWYSGKVRFDGISLS 80
Cdd:COG3915    3 LLRLLALLLALLLLPAAAAAALPAPAGPVILTVSGKIGNTNAGGAATFDLAMLEALPQTEITTTTPWTDGVQTFRGVLLR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695770883  81 KLMDLVGAKGKSARVLALNDYTTIVPLDDFHKFPVILALKMNGEYMRIRDKGPLFIVYPYDSSPELQNQIYYSRSAWQVS 160
Cdd:COG3915   83 DLLAAVGAKGTTLRAVALNDYAVEIPISDLEEYGVILAYRMDGKPMSVRDKGPLWLIYPYDDYPELQTEVYYSRSVWQLK 162

                 ....*
gi 695770883 161 KIIIE 165
Cdd:COG3915  163 RIEVE 167
MsrP COG2041
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and ...
31-124 5.00e-12

Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and protein-methionine-sulfoxide reductases [Energy production and conversion];


Pssm-ID: 441644 [Multi-domain]  Cd Length: 183  Bit Score: 60.56  E-value: 5.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695770883  31 LTISGLIANTnegdtAVFDVAALEKLGMETLVTT----TPWYSGKVRFDGISLSKLMDLVGAKGKSARVLAL---NDYTT 103
Cdd:COG2041   37 LRVDGLVEKP-----LTLTLDDLLALPLEERIYRlhcvENWSGGVAPWTGVPLRDLLERAGPKPGAKYVLFEsadPGYTE 111
                         90       100
                 ....*....|....*....|.
gi 695770883 104 IVPLDDFHKFPVILALKMNGE 124
Cdd:COG2041  112 SLPLDEALDPDTLLAYGMNGE 132
SO_family_Moco cd00321
Sulfite oxidase (SO) family, molybdopterin binding domain. This molybdopterin cofactor (Moco) ...
31-139 1.40e-10

Sulfite oxidase (SO) family, molybdopterin binding domain. This molybdopterin cofactor (Moco) binding domain is found in a variety of oxidoreductases, main members of this family are nitrate reductase (NR) and sulfite oxidase (SO). SO catalyzes the terminal reaction in the oxidative degradation of the sulfur-containing amino acids cysteine and methionine. Assimilatory NRs catalyze the reduction of nitrate to nitrite which is subsequently converted to NH4+ by nitrite reductase. Common features of all known members of this family 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: 238198 [Multi-domain]  Cd Length: 156  Bit Score: 56.42  E-value: 1.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695770883  31 LTISGLIANTnegdtAVFDVAALEKLGMETLVTT--------TPWYSGKVRFDGISLSKLMDLVGAKGK-------SARV 95
Cdd:cd00321   19 LEVDGLVEKP-----LSLTLDDLKALPQVEVIATlhcvgnrwGGGAVSNAEWTGVPLRDLLEEAGPKPGaryvvfeGADD 93
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 695770883  96 LALNDYTTIVPLDDFHKFPVILALKMNGEYMRIRDKGPLFIVYP 139
Cdd:cd00321   94 PGGDGYTTSLPLEKALDPDVLLAYEMNGEPLPPDHGFPLRLVVP 137
arch_bact_SO_family_Moco cd02109
bacterial and archael members of the sulfite oxidase (SO) family of molybdopterin binding ...
31-139 1.84e-09

bacterial and archael members of the sulfite oxidase (SO) family of molybdopterin binding domains. This molybdopterin cofactor (Moco) binding domain is found in a variety of oxidoreductases, main members of this family are nitrate reductase (NR) and sulfite oxidase (SO). Common features of all known members of this family 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. The specific function of this subgroup is unknown.


Pssm-ID: 239027 [Multi-domain]  Cd Length: 180  Bit Score: 53.79  E-value: 1.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695770883  31 LTISGLIANTnegdtAVFDVAALEKLGMETLVT----TTPWYSGKVRFDGISLSKLMDLVGAKGKSARVLA--LNDYTTI 104
Cdd:cd02109   29 LRVTGLVENP-----LSLTYEDLLALPQTEYTAdfhcVTGWSKLDVVWEGVSLKDLLEAARPDPEATFVMAhsYDGYTTN 103
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 695770883 105 VPLDDFHKFPVILALKMNGEYMRIRDKGPLFIVYP 139
Cdd:cd02109  104 LPLEDLLREDSLLATKMDGEPLPPEHGGPARLVVP 138
Oxidored_molyb pfam00174
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ...
31-124 2.90e-07

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: 47.50  E-value: 2.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695770883   31 LTISGLIANTnegdtAVFDVAALEKLGMETLVTT----------------TPW---YSGKVRFDGISLSKLMDLVGAKGK 91
Cdd:pfam00174  14 LRVDGLVEKP-----LTLTLDDLKAFPQVTVTATlqcvgnrrkemnrvkgVQWgggAIGNAEWTGVPLRDLLERAGVKPG 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 695770883   92 -------SARVLALNDYTTIVPLDDFHKFPVILALKMNGE 124
Cdd:pfam00174  89 akhvlfeGADTLGDGGYTTSLPLEKALDDDVLLAYEMNGE 128
SO_family_Moco_dimer cd02110
Subgroup of sulfite oxidase (SO) family molybdopterin binding domains that contains conserved ...
31-139 5.51e-03

Subgroup of sulfite oxidase (SO) family molybdopterin binding domains that contains conserved dimerization domain. This molybdopterin cofactor (Moco) binding domain is found in a variety of oxidoreductases, main members of this family are nitrate reductase (NR) and sulfite oxidase (SO).


Pssm-ID: 239028 [Multi-domain]  Cd Length: 317  Bit Score: 36.12  E-value: 5.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695770883  31 LTISGLIANTNEgdtavFDVAALEKLGMETLVTT-----------------TPWYSGKV---RFDGISLSKLMDLVGAKG 90
Cdd:cd02110   20 LEIHGLVERPLT-----LTLDDLKRLPSVEVVATlecsgngrggfipvrsgAQWGHGAVgnaRWTGVPLKDLLEEAGVKP 94
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 695770883  91 KSARVLA----------LNDYTTIVPLDDFHKFPVILALKMNGEYMRIRDKGPLFIVYP 139
Cdd:cd02110   95 GAKHVLFegadvppgekAADYTRSVPLSKALDDDALLAYEMNGEPLPPDHGYPLRLVVP 153
 
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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