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Conserved domains on  [gi|17569245|ref|NP_510208|]
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Uncharacterized protein CELE_R04D3.2 [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DOMON_like super family cl14783
Domon-like ligand-binding domains; DOMON-like domains can be found in all three kindgoms of ...
22-189 1.38e-11

Domon-like ligand-binding domains; DOMON-like domains can be found in all three kindgoms of life and are a diverse group of ligand binding domains that have been shown to interact with sugars and hemes. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases.


The actual alignment was detected with superfamily member cd09628:

Pssm-ID: 472705  Cd Length: 169  Bit Score: 62.45  E-value: 1.38e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569245  22 DCSRENSCFGEPYGCSPNAGCNSLFQFdTDHNLHLYI--RNFTDMNGYAAFAVNRRPD-EIIEYLVCLPHQGQRLRA-HA 97
Cdd:cd09628   6 GCGKTKGCFGLPVGCDPSKDCNFLVTY-RVDGDSVEFelSGKTVDDGYVAVGFSDDKKmGDDDVVECVRDAGGRVEVrHS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569245  98 ELGGTVL------VTEQNLTGVVESLGNNDFRCTFATSELPSnfeqeqllfiskgtfvdsliihDGIQLFNLNDDEYSV- 170
Cdd:cd09628  85 YNPGTGNtqgsieLESENVSRDGAEYSDGVIYCRFLRNVVPT----------------------VQGNRFDLNSGSYLLf 142
                       170       180
                ....*....|....*....|
gi 17569245 171 -DGPEEVFATPSIHYIGSPI 189
Cdd:cd09628 143 aAGSASSTGSVQYHSIGSVS 162
 
Name Accession Description Interval E-value
DOMON_SDR_2_like cd09628
DOMON domain of stromal cell-derived receptor 2 (ferric chelate reductase 1) and related ...
22-189 1.38e-11

DOMON domain of stromal cell-derived receptor 2 (ferric chelate reductase 1) and related proteins; Stromal cell-derived receptor 2 (or ferric chelate reductase 1) reduces Fe(3+) to Fe(2+) ahead of iron transport from the endosome to the cytoplasm. This transmembrane protein is a member of the cytochrome b561 family and contains a DOMON domain which may bind to heme or another ligand. DOMON-like domains can be found in all three kindgoms of life and are a diverse group of ligand binding domains that have been shown to interact with sugars and hemes. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases.


Pssm-ID: 187686  Cd Length: 169  Bit Score: 62.45  E-value: 1.38e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569245  22 DCSRENSCFGEPYGCSPNAGCNSLFQFdTDHNLHLYI--RNFTDMNGYAAFAVNRRPD-EIIEYLVCLPHQGQRLRA-HA 97
Cdd:cd09628   6 GCGKTKGCFGLPVGCDPSKDCNFLVTY-RVDGDSVEFelSGKTVDDGYVAVGFSDDKKmGDDDVVECVRDAGGRVEVrHS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569245  98 ELGGTVL------VTEQNLTGVVESLGNNDFRCTFATSELPSnfeqeqllfiskgtfvdsliihDGIQLFNLNDDEYSV- 170
Cdd:cd09628  85 YNPGTGNtqgsieLESENVSRDGAEYSDGVIYCRFLRNVVPT----------------------VQGNRFDLNSGSYLLf 142
                       170       180
                ....*....|....*....|
gi 17569245 171 -DGPEEVFATPSIHYIGSPI 189
Cdd:cd09628 143 aAGSASSTGSVQYHSIGSVS 162
 
Name Accession Description Interval E-value
DOMON_SDR_2_like cd09628
DOMON domain of stromal cell-derived receptor 2 (ferric chelate reductase 1) and related ...
22-189 1.38e-11

DOMON domain of stromal cell-derived receptor 2 (ferric chelate reductase 1) and related proteins; Stromal cell-derived receptor 2 (or ferric chelate reductase 1) reduces Fe(3+) to Fe(2+) ahead of iron transport from the endosome to the cytoplasm. This transmembrane protein is a member of the cytochrome b561 family and contains a DOMON domain which may bind to heme or another ligand. DOMON-like domains can be found in all three kindgoms of life and are a diverse group of ligand binding domains that have been shown to interact with sugars and hemes. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases.


Pssm-ID: 187686  Cd Length: 169  Bit Score: 62.45  E-value: 1.38e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569245  22 DCSRENSCFGEPYGCSPNAGCNSLFQFdTDHNLHLYI--RNFTDMNGYAAFAVNRRPD-EIIEYLVCLPHQGQRLRA-HA 97
Cdd:cd09628   6 GCGKTKGCFGLPVGCDPSKDCNFLVTY-RVDGDSVEFelSGKTVDDGYVAVGFSDDKKmGDDDVVECVRDAGGRVEVrHS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569245  98 ELGGTVL------VTEQNLTGVVESLGNNDFRCTFATSELPSnfeqeqllfiskgtfvdsliihDGIQLFNLNDDEYSV- 170
Cdd:cd09628  85 YNPGTGNtqgsieLESENVSRDGAEYSDGVIYCRFLRNVVPT----------------------VQGNRFDLNSGSYLLf 142
                       170       180
                ....*....|....*....|
gi 17569245 171 -DGPEEVFATPSIHYIGSPI 189
Cdd:cd09628 143 aAGSASSTGSVQYHSIGSVS 162
 
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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