NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|727185204|ref|WP_033647255|]
View 

MULTISPECIES: diiron oxygenase [Serratia]

Protein Classification

ferritin family protein( domain architecture ID 38)

ferritin family protein similar to rubrerythrin, a non-heme di-iron that is involved in oxidative stress defense as a peroxide scavenger in a wide range of organisms

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Ferritin_like super family cl00264
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 35-228 2.35e-08

Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, diiron-carboxylate proteins participate in a range of functions including iron regulation, mono-oxygenation, and reactive radical production. These proteins are characterized by the fact that they catalyze dioxygen-dependent oxidation-hydroxylation reactions within diiron centers; one exception is manganese catalase, which catalyzes peroxide-dependent oxidation-reduction within a dimanganese center. Diiron-carboxylate proteins are further characterized by the presence of duplicate metal ligands, glutamates and histidines (ExxH) and two additional glutamates within a four-helix bundle. Outside of these conserved residues there is little obvious homology. Members include bacterioferritin, ferritin, rubrerythrin, aromatic and alkene monooxygenase hydroxylases (AAMH), ribonucleotide reductase R2 (RNRR2), acyl-ACP-desaturases (Acyl_ACP_Desat), manganese (Mn) catalases, demethoxyubiquinone hydroxylases (DMQH), DNA protecting proteins (DPS), and ubiquinol oxidases (AOX), and the aerobic cyclase system, Fe-containing subunit (ACSF).


The actual alignment was detected with superfamily member pfam11583:

Pssm-ID: 469698  Cd Length: 279  Bit Score: 54.14  E-value: 2.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185204   35 FFPLERLPLCLHPRVAALGEQAlryiQVQTLYHylnGIANIeldiindssyklykNAVGVDFplEMRL------------ 102
Cdd:pfam11583  39 DLPPELDPLYGTPLWERLPEEQ----RIELGRW---EWANY--------------AKVGIWF--ESILiqgllryaypld 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185204  103 -------DALTVVVDESYHALVALDLINQVEQMtsiapLPMPKDTEASYALAQSLAmgdERLRELLRLVCVSLSEQALTT 175
Cdd:pfam11583  96 pgspefqYALTEIADECRHTLMFAEAVNRIGDV-----PGMYRPRRRLRPLGRLLP---TWARGLVFFAGVLVGEEPIDH 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 727185204  176 DLIDVINNEDIFPTFYLVMKDHVADEGRHARFSQQVLSHIWRHSDAATKQALQ 228
Cdd:pfam11583 168 YQRELMRDEEVQPLVRRVMRIHVAEEARHISFAREELRRRVPRLGRAERAYLR 220
 
Name Accession Description Interval E-value
AurF pfam11583
P-aminobenzoate N-oxygenase AurF; This family is a metalloenzyme which is involved in the ...
 35-228 2.35e-08

P-aminobenzoate N-oxygenase AurF; This family is a metalloenzyme which is involved in the biosynthesis of antibiotic aureothin by catalysing the formation of p-nitrobenzoic acid from p-aminobenzoic acid. AurF is a non-heme di-iron monooxygenase which creates nitroarenes via the sequential oxidation of aminoarenes.


Pssm-ID: 431946  Cd Length: 279  Bit Score: 54.14  E-value: 2.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185204   35 FFPLERLPLCLHPRVAALGEQAlryiQVQTLYHylnGIANIeldiindssyklykNAVGVDFplEMRL------------ 102
Cdd:pfam11583  39 DLPPELDPLYGTPLWERLPEEQ----RIELGRW---EWANY--------------AKVGIWF--ESILiqgllryaypld 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185204  103 -------DALTVVVDESYHALVALDLINQVEQMtsiapLPMPKDTEASYALAQSLAmgdERLRELLRLVCVSLSEQALTT 175
Cdd:pfam11583  96 pgspefqYALTEIADECRHTLMFAEAVNRIGDV-----PGMYRPRRRLRPLGRLLP---TWARGLVFFAGVLVGEEPIDH 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 727185204  176 DLIDVINNEDIFPTFYLVMKDHVADEGRHARFSQQVLSHIWRHSDAATKQALQ 228
Cdd:pfam11583 168 YQRELMRDEEVQPLVRRVMRIHVAEEARHISFAREELRRRVPRLGRAERAYLR 220
 
Name Accession Description Interval E-value
AurF pfam11583
P-aminobenzoate N-oxygenase AurF; This family is a metalloenzyme which is involved in the ...
 35-228 2.35e-08

P-aminobenzoate N-oxygenase AurF; This family is a metalloenzyme which is involved in the biosynthesis of antibiotic aureothin by catalysing the formation of p-nitrobenzoic acid from p-aminobenzoic acid. AurF is a non-heme di-iron monooxygenase which creates nitroarenes via the sequential oxidation of aminoarenes.


Pssm-ID: 431946  Cd Length: 279  Bit Score: 54.14  E-value: 2.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185204   35 FFPLERLPLCLHPRVAALGEQAlryiQVQTLYHylnGIANIeldiindssyklykNAVGVDFplEMRL------------ 102
Cdd:pfam11583  39 DLPPELDPLYGTPLWERLPEEQ----RIELGRW---EWANY--------------AKVGIWF--ESILiqgllryaypld 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185204  103 -------DALTVVVDESYHALVALDLINQVEQMtsiapLPMPKDTEASYALAQSLAmgdERLRELLRLVCVSLSEQALTT 175
Cdd:pfam11583  96 pgspefqYALTEIADECRHTLMFAEAVNRIGDV-----PGMYRPRRRLRPLGRLLP---TWARGLVFFAGVLVGEEPIDH 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 727185204  176 DLIDVINNEDIFPTFYLVMKDHVADEGRHARFSQQVLSHIWRHSDAATKQALQ 228
Cdd:pfam11583 168 YQRELMRDEEVQPLVRRVMRIHVAEEARHISFAREELRRRVPRLGRAERAYLR 220
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH