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Conserved domains on  [gi|501460830|ref|WP_012484275|]
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hemerythrin domain-containing protein [Rhizobium phaseoli]

Protein Classification

hemerythrin domain-containing protein; hemerythrin family protein( domain architecture ID 10186786)

hemerythrin domain-containing protein adopts a four alpha helix bundle fold and may bind cations| hemerythrin family protein similar to bacteriohemerythrin, an oxygen-binding protein that may be involved in a storage mechanism or for delivery to oxygen-requiring enzymes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Hr_FBXL5 cd12109
Hemerythrin-like domain of FBXL5-like proteins; Human FBXL5 (F-box and leucine-rich repeat ...
 16-172 4.53e-58

Hemerythrin-like domain of FBXL5-like proteins; Human FBXL5 (F-box and leucine-rich repeat protein 5) protein plays a role in cellular iron homeostasis. It is part of an E3 ubiquitin ligase complex that targets the iron regulatory protein IRP2 for proteasomal degradation. The FBXL5's stability is regulated by iron concentration, with its iron- and oxygen-binding hemerythrin domain acting as a ligand-dependent regulatory switch.


:

Pssm-ID: 213984  Cd Length: 158  Bit Score: 180.95  E-value: 4.53e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501460830  16 RYDIYGAIHKGLRKAGCDLLGRLGTADFQNVEETVFLIGDLRHYLMLAASHVTHEDDNIHTALADKGVSTV-TLDEQHDD 94
Cdd:cd12109    1 RVDVYGFIHKALRALLFDLLQKLGRTDFSDPQDLAALLESLRRLLQEFKAHEQHENEFIHPLLEKRLPGLSaAVANEHSD 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501460830  95 HRTAFRELEELVVAWERAWPLNKAACGRKLYLAFAAYLADDFAHMHEEEAVTGPLLWRNFDDQEIFGIEMRIIGSLPP 172
Cdd:cd12109   81 HDLSIMLLLELLGALRTAPEAERPAAGRQLYRALAAFVADNLPHMHEEETVFQPLLWEYFSDEELKAIKKAVIASHPP 158
 
Name Accession Description Interval E-value
Hr_FBXL5 cd12109
Hemerythrin-like domain of FBXL5-like proteins; Human FBXL5 (F-box and leucine-rich repeat ...
 16-172 4.53e-58

Hemerythrin-like domain of FBXL5-like proteins; Human FBXL5 (F-box and leucine-rich repeat protein 5) protein plays a role in cellular iron homeostasis. It is part of an E3 ubiquitin ligase complex that targets the iron regulatory protein IRP2 for proteasomal degradation. The FBXL5's stability is regulated by iron concentration, with its iron- and oxygen-binding hemerythrin domain acting as a ligand-dependent regulatory switch.


Pssm-ID: 213984  Cd Length: 158  Bit Score: 180.95  E-value: 4.53e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501460830  16 RYDIYGAIHKGLRKAGCDLLGRLGTADFQNVEETVFLIGDLRHYLMLAASHVTHEDDNIHTALADKGVSTV-TLDEQHDD 94
Cdd:cd12109    1 RVDVYGFIHKALRALLFDLLQKLGRTDFSDPQDLAALLESLRRLLQEFKAHEQHENEFIHPLLEKRLPGLSaAVANEHSD 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501460830  95 HRTAFRELEELVVAWERAWPLNKAACGRKLYLAFAAYLADDFAHMHEEEAVTGPLLWRNFDDQEIFGIEMRIIGSLPP 172
Cdd:cd12109   81 HDLSIMLLLELLGALRTAPEAERPAAGRQLYRALAAFVADNLPHMHEEETVFQPLLWEYFSDEELKAIKKAVIASHPP 158
 
Name Accession Description Interval E-value
Hr_FBXL5 cd12109
Hemerythrin-like domain of FBXL5-like proteins; Human FBXL5 (F-box and leucine-rich repeat ...
 16-172 4.53e-58

Hemerythrin-like domain of FBXL5-like proteins; Human FBXL5 (F-box and leucine-rich repeat protein 5) protein plays a role in cellular iron homeostasis. It is part of an E3 ubiquitin ligase complex that targets the iron regulatory protein IRP2 for proteasomal degradation. The FBXL5's stability is regulated by iron concentration, with its iron- and oxygen-binding hemerythrin domain acting as a ligand-dependent regulatory switch.


Pssm-ID: 213984  Cd Length: 158  Bit Score: 180.95  E-value: 4.53e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501460830  16 RYDIYGAIHKGLRKAGCDLLGRLGTADFQNVEETVFLIGDLRHYLMLAASHVTHEDDNIHTALADKGVSTV-TLDEQHDD 94
Cdd:cd12109    1 RVDVYGFIHKALRALLFDLLQKLGRTDFSDPQDLAALLESLRRLLQEFKAHEQHENEFIHPLLEKRLPGLSaAVANEHSD 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501460830  95 HRTAFRELEELVVAWERAWPLNKAACGRKLYLAFAAYLADDFAHMHEEEAVTGPLLWRNFDDQEIFGIEMRIIGSLPP 172
Cdd:cd12109   81 HDLSIMLLLELLGALRTAPEAERPAAGRQLYRALAAFVADNLPHMHEEETVFQPLLWEYFSDEELKAIKKAVIASHPP 158
Hr-like cd12108
Hemerythrin-like domain; Hemerythrin (Hr) like domains have the same four alpha helix bundle ...
 18-145 2.34e-04

Hemerythrin-like domain; Hemerythrin (Hr) like domains have the same four alpha helix bundle and a similar, but slightly different active site structure than hemerythrin. They are non-heme diiron binding proteins mainly found in bacteria and eukaryotes. Like Hr, they may be involved in oxygen transport or like human FBXL5 (F-box and leucine-rich repeat protein 5), a member of this group, play a role in cellular iron homeostasis.


Pssm-ID: 213983 [Multi-domain]  Cd Length: 130  Bit Score: 39.72  E-value: 2.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501460830  18 DIYGAIHKGLRKAGCDLLGRLGTADFQNVEETVFLIGDLRHYLMLAASHVTHEDDNIHTALADKGVSTVTLDEQHDDHRT 97
Cdd:cd12108    1 DLLKLEHRAIRRELGRLARLAGALAAGGPDDARALAERFRFLATELHHHHTAEEELLFPALRERVPLAAVLDALEAEHAE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 501460830  98 A---FRELEELVVAWERAwplnKAACGRKLYLAFAAYLADDFAHMHEEEAV 145
Cdd:cd12108   81 IdelLARLEALLPALLAG----DAEDAEELAAALEALRTALREHLDEEEEE 127
 
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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