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Conserved domains on  [gi|1463288392|emb|SVJ61011|]
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oxidoreductase [Klebsiella pneumoniae]

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 1.81e-89

Uncharacterized conserved protein [Function unknown];


:

Pssm-ID: 443120  Cd Length: 167  Bit Score: 258.28  E-value: 1.81e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463288392   1 MRLLLAVLFCSVMLPSAYAEKLPAPTGKPVLTISGKIGNMNVGDKAVFDLAMLEKLGMKTIETTTPWYTGKVRFDGIPLN 80
Cdd:COG3915     3 LLRLLALLLALLLLPAAAAAALPAPAGPVILTVSGKIGNTNAGGAATFDLAMLEALPQTEITTTTPWTDGVQTFRGVLLR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463288392  81 KLMDLVGAKGTSARVLALNDYTTIIPIDDFYKFPVIMALKMNGQYMRIRDKGPLFIVYPYDSSAELQNQIYYSRSAWQVS 160
Cdd:COG3915    83 DLLAAVGAKGTTLRAVALNDYAVEIPISDLEEYGVILAYRMDGKPMSVRDKGPLWLIYPYDDYPELQTEVYYSRSVWQLK 162


                  ....*
gi 1463288392 161 KMIIE 165
Cdd:COG3915   163 RIEVE 167
 
Name Accession Description Interval E-value
COG3915 COG3915
Uncharacterized conserved protein [Function unknown];
1-165 1.81e-89

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443120  Cd Length: 167  Bit Score: 258.28  E-value: 1.81e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463288392   1 MRLLLAVLFCSVMLPSAYAEKLPAPTGKPVLTISGKIGNMNVGDKAVFDLAMLEKLGMKTIETTTPWYTGKVRFDGIPLN 80
Cdd:COG3915     3 LLRLLALLLALLLLPAAAAAALPAPAGPVILTVSGKIGNTNAGGAATFDLAMLEALPQTEITTTTPWTDGVQTFRGVLLR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463288392  81 KLMDLVGAKGTSARVLALNDYTTIIPIDDFYKFPVIMALKMNGQYMRIRDKGPLFIVYPYDSSAELQNQIYYSRSAWQVS 160
Cdd:COG3915    83 DLLAAVGAKGTTLRAVALNDYAVEIPISDLEEYGVILAYRMDGKPMSVRDKGPLWLIYPYDDYPELQTEVYYSRSVWQLK 162


                  ....*
gi 1463288392 161 KMIIE 165
Cdd:COG3915   163 RIEVE 167
arch_bact_SO_family_Moco cd02109
bacterial and archael members of the sulfite oxidase (SO) family of molybdopterin binding ...
 65-139 6.49e-08

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: 49.55  E-value: 6.49e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1463288392  65 TPWYTGKVRFDGIPLNKLMDLVGAKGTSARVLA--LNDYTTIIPIDDFYKFPVIMALKMNGQYMRIRDKGPLFIVYP 139
Cdd:cd02109    62 TGWSKLDVVWEGVSLKDLLEAARPDPEATFVMAhsYDGYTTNLPLEDLLREDSLLATKMDGEPLPPEHGGPARLVVP 138
Oxidored_molyb pfam00174
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ...
 31-124 8.05e-05

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: 40.95  E-value: 8.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463288392  31 LTISGkignmNVGDKAVFDLAMLEKLGMKTIETT----------------TPW---YTGKVRFDGIPLNKLMDLVGAKG- 90
Cdd:pfam00174  14 LRVDG-----LVEKPLTLTLDDLKAFPQVTVTATlqcvgnrrkemnrvkgVQWgggAIGNAEWTGVPLRDLLERAGVKPg 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1463288392  91 ------TSARVLALNDYTTIIPIDDFYKFPVIMALKMNGQ 124
Cdd:pfam00174  89 akhvlfEGADTLGDGGYTTSLPLEKALDDDVLLAYEMNGE 128
 
Name Accession Description Interval E-value
COG3915 COG3915
Uncharacterized conserved protein [Function unknown];
1-165 1.81e-89

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443120  Cd Length: 167  Bit Score: 258.28  E-value: 1.81e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463288392   1 MRLLLAVLFCSVMLPSAYAEKLPAPTGKPVLTISGKIGNMNVGDKAVFDLAMLEKLGMKTIETTTPWYTGKVRFDGIPLN 80
Cdd:COG3915     3 LLRLLALLLALLLLPAAAAAALPAPAGPVILTVSGKIGNTNAGGAATFDLAMLEALPQTEITTTTPWTDGVQTFRGVLLR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463288392  81 KLMDLVGAKGTSARVLALNDYTTIIPIDDFYKFPVIMALKMNGQYMRIRDKGPLFIVYPYDSSAELQNQIYYSRSAWQVS 160
Cdd:COG3915    83 DLLAAVGAKGTTLRAVALNDYAVEIPISDLEEYGVILAYRMDGKPMSVRDKGPLWLIYPYDDYPELQTEVYYSRSVWQLK 162


                  ....*
gi 1463288392 161 KMIIE 165
Cdd:COG3915   163 RIEVE 167
MsrP COG2041
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and ...
 31-124 1.19e-08

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: 51.70  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463288392  31 LTISGkignmNVGDKAVFDLAMLEKLGMKTIETT----TPWYTGKVRFDGIPLNKLMDLVGAKgTSARVLAL----NDYT 102
Cdd:COG2041    37 LRVDG-----LVEKPLTLTLDDLLALPLEERIYRlhcvENWSGGVAPWTGVPLRDLLERAGPK-PGAKYVLFesadPGYT 110

                          90       100
                  ....*....|....*....|..
gi 1463288392 103 TIIPIDDFYKFPVIMALKMNGQ 124
Cdd:COG2041   111 ESLPLDEALDPDTLLAYGMNGE 132
arch_bact_SO_family_Moco cd02109
bacterial and archael members of the sulfite oxidase (SO) family of molybdopterin binding ...
 65-139 6.49e-08

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: 49.55  E-value: 6.49e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1463288392  65 TPWYTGKVRFDGIPLNKLMDLVGAKGTSARVLA--LNDYTTIIPIDDFYKFPVIMALKMNGQYMRIRDKGPLFIVYP 139
Cdd:cd02109    62 TGWSKLDVVWEGVSLKDLLEAARPDPEATFVMAhsYDGYTTNLPLEDLLREDSLLATKMDGEPLPPEHGGPARLVVP 138
SO_family_Moco cd00321
Sulfite oxidase (SO) family, molybdopterin binding domain. This molybdopterin cofactor (Moco) ...
 31-139 7.47e-07

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: 46.41  E-value: 7.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463288392  31 LTISGkignmNVGDKAVFDLAMLEKLGMKTIETT--------TPWYTGKVRFDGIPLNKLMDLVGAKG-------TSARV 95
Cdd:cd00321    19 LEVDG-----LVEKPLSLTLDDLKALPQVEVIATlhcvgnrwGGGAVSNAEWTGVPLRDLLEEAGPKPgaryvvfEGADD 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1463288392  96 LALNDYTTIIPIDDFYKFPVIMALKMNGQYMRIRDKGPLFIVYP 139
Cdd:cd00321    94 PGGDGYTTSLPLEKALDPDVLLAYEMNGEPLPPDHGFPLRLVVP 137
Oxidored_molyb pfam00174
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ...
 31-124 8.05e-05

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: 40.95  E-value: 8.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463288392  31 LTISGkignmNVGDKAVFDLAMLEKLGMKTIETT----------------TPW---YTGKVRFDGIPLNKLMDLVGAKG- 90
Cdd:pfam00174  14 LRVDG-----LVEKPLTLTLDDLKAFPQVTVTATlqcvgnrrkemnrvkgVQWgggAIGNAEWTGVPLRDLLERAGVKPg 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1463288392  91 ------TSARVLALNDYTTIIPIDDFYKFPVIMALKMNGQ 124
Cdd:pfam00174  89 akhvlfEGADTLGDGGYTTSLPLEKALDDDVLLAYEMNGE 128
 
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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