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Conserved domains on  [gi|505004329|ref|WP_015191431|]
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hemerythrin domain-containing protein [Stanieria cyanosphaera]

Protein Classification

COG5592 family protein( domain architecture ID 10009461)

COG5592 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG5592 COG5592
Hemerythrin domain-containing protein [General function prediction only];
197-343 1.56e-67

Hemerythrin domain-containing protein [General function prediction only];


:

Pssm-ID: 444331 [Multi-domain]  Cd Length: 151  Bit Score: 208.69  E-value: 1.56e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505004329 197 LKIQDIIRMDHQKVNVLIGEIEQSNDNQKIQEYFGQLYQDLLVHSVAEEQVVYPTVRPFYGDEDTQELYDEQAQLREILD 276
Cdd:COG5592    2 MNIQDLIRMDHQKVNTLFEEILQTNDPQKIQEYFGQLYKDLRAHAEAEEEVVYPAVRPFYGEEPTQELYDEQAEMKQLLD 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505004329 277 QMKSLEPDSQEFKDMLQQVKEMVGDHTRQEESTMFSAIKSNCSSQQQQQMATEFKEAKKQLQLEMAG 343
Cdd:COG5592   82 EIKALDPSSPEFKDRIRQLKDLVGDHVRQEESTLFPAIRNNLSPEQQEQLATEFKAAKSKLQDQMAQ 148
 
Name Accession Description Interval E-value
COG5592 COG5592
Hemerythrin domain-containing protein [General function prediction only];
197-343 1.56e-67

Hemerythrin domain-containing protein [General function prediction only];


Pssm-ID: 444331 [Multi-domain]  Cd Length: 151  Bit Score: 208.69  E-value: 1.56e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505004329 197 LKIQDIIRMDHQKVNVLIGEIEQSNDNQKIQEYFGQLYQDLLVHSVAEEQVVYPTVRPFYGDEDTQELYDEQAQLREILD 276
Cdd:COG5592    2 MNIQDLIRMDHQKVNTLFEEILQTNDPQKIQEYFGQLYKDLRAHAEAEEEVVYPAVRPFYGEEPTQELYDEQAEMKQLLD 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505004329 277 QMKSLEPDSQEFKDMLQQVKEMVGDHTRQEESTMFSAIKSNCSSQQQQQMATEFKEAKKQLQLEMAG 343
Cdd:COG5592   82 EIKALDPSSPEFKDRIRQLKDLVGDHVRQEESTLFPAIRNNLSPEQQEQLATEFKAAKSKLQDQMAQ 148
Hemerythrin pfam01814
Hemerythrin HHE cation binding domain; Iteration of the HHE family found it to be related to ...
 199-314 1.63e-09

Hemerythrin HHE cation binding domain; Iteration of the HHE family found it to be related to Hemerythrin. It also demonstrated that what has been described as a single domain in fact consists of two cation binding domains. Members of this family occur all across nature and are involved in a variety of processes. For instance, in Nereis diversicolor Swiss:P80255 binds Cadmium so as to protect the organizm from toxicity. However Hemerythrin is classically described as Oxygen-binding through two attached Fe2+ ions. And the bacterial Swiss:Q7WX96 is a regulator of response to NO, which suggests yet another set-up for its metal ligands. In Staphylococcus aureus P72360 has been noted to be important when the organizm switches to living in environments with low oxygen concentrations; perhaps this protein acts as an oxygen store or scavenger. This domain can bind oxygen (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043)


Pssm-ID: 396400 [Multi-domain]  Cd Length: 128  Bit Score: 55.31  E-value: 1.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505004329  199 IQDIIRMDHQKVNVLIGEIEQSNDN------QKIQEYFGQLYQDLLVHSVAEEQVVYPTVRPFY--GDEDTQELYDEQAQ 270
Cdd:pfam01814   2 IIELLDAEHRRLRELLALLRALADAlgdshlRKLAELLDELVDELEAHHAAEEELLFPALERRSpgGEAPIEVLRKEHDE 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 505004329  271 LREILDQMKSL---EPDSQEFKDMLQQVKEMVGDHTRQEESTMFSAI 314
Cdd:pfam01814  82 IRELLEELEALlkgAEPGAAFAELLEALAEWLREHIAKEEEVLFPLL 128
Hr-like cd12108
Hemerythrin-like domain; Hemerythrin (Hr) like domains have the same four alpha helix bundle ...
 201-311 1.05e-08

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: 52.82  E-value: 1.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505004329 201 DIIRMDHQKVNVLIGEIEQ---------SNDNQKIQEYFGQLYQDLLVHSVAEEQVVYPTVRP-FYGDEDTQELYDEQAQ 270
Cdd:cd12108    1 DLLKLEHRAIRRELGRLARlagalaaggPDDARALAERFRFLATELHHHHTAEEELLFPALRErVPLAAVLDALEAEHAE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 505004329 271 LREILDQMKSL--------EPDSQEFKDMLQQVKEMVGDHTRQEESTMF 311
Cdd:cd12108   81 IDELLARLEALlpallagdAEDAEELAAALEALRTALREHLDEEEEELF 129
 
Name Accession Description Interval E-value
COG5592 COG5592
Hemerythrin domain-containing protein [General function prediction only];
197-343 1.56e-67

Hemerythrin domain-containing protein [General function prediction only];


Pssm-ID: 444331 [Multi-domain]  Cd Length: 151  Bit Score: 208.69  E-value: 1.56e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505004329 197 LKIQDIIRMDHQKVNVLIGEIEQSNDNQKIQEYFGQLYQDLLVHSVAEEQVVYPTVRPFYGDEDTQELYDEQAQLREILD 276
Cdd:COG5592    2 MNIQDLIRMDHQKVNTLFEEILQTNDPQKIQEYFGQLYKDLRAHAEAEEEVVYPAVRPFYGEEPTQELYDEQAEMKQLLD 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505004329 277 QMKSLEPDSQEFKDMLQQVKEMVGDHTRQEESTMFSAIKSNCSSQQQQQMATEFKEAKKQLQLEMAG 343
Cdd:COG5592   82 EIKALDPSSPEFKDRIRQLKDLVGDHVRQEESTLFPAIRNNLSPEQQEQLATEFKAAKSKLQDQMAQ 148
Hemerythrin pfam01814
Hemerythrin HHE cation binding domain; Iteration of the HHE family found it to be related to ...
 199-314 1.63e-09

Hemerythrin HHE cation binding domain; Iteration of the HHE family found it to be related to Hemerythrin. It also demonstrated that what has been described as a single domain in fact consists of two cation binding domains. Members of this family occur all across nature and are involved in a variety of processes. For instance, in Nereis diversicolor Swiss:P80255 binds Cadmium so as to protect the organizm from toxicity. However Hemerythrin is classically described as Oxygen-binding through two attached Fe2+ ions. And the bacterial Swiss:Q7WX96 is a regulator of response to NO, which suggests yet another set-up for its metal ligands. In Staphylococcus aureus P72360 has been noted to be important when the organizm switches to living in environments with low oxygen concentrations; perhaps this protein acts as an oxygen store or scavenger. This domain can bind oxygen (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043)


Pssm-ID: 396400 [Multi-domain]  Cd Length: 128  Bit Score: 55.31  E-value: 1.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505004329  199 IQDIIRMDHQKVNVLIGEIEQSNDN------QKIQEYFGQLYQDLLVHSVAEEQVVYPTVRPFY--GDEDTQELYDEQAQ 270
Cdd:pfam01814   2 IIELLDAEHRRLRELLALLRALADAlgdshlRKLAELLDELVDELEAHHAAEEELLFPALERRSpgGEAPIEVLRKEHDE 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 505004329  271 LREILDQMKSL---EPDSQEFKDMLQQVKEMVGDHTRQEESTMFSAI 314
Cdd:pfam01814  82 IRELLEELEALlkgAEPGAAFAELLEALAEWLREHIAKEEEVLFPLL 128
Hr-like cd12108
Hemerythrin-like domain; Hemerythrin (Hr) like domains have the same four alpha helix bundle ...
 201-311 1.05e-08

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: 52.82  E-value: 1.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505004329 201 DIIRMDHQKVNVLIGEIEQ---------SNDNQKIQEYFGQLYQDLLVHSVAEEQVVYPTVRP-FYGDEDTQELYDEQAQ 270
Cdd:cd12108    1 DLLKLEHRAIRRELGRLARlagalaaggPDDARALAERFRFLATELHHHHTAEEELLFPALRErVPLAAVLDALEAEHAE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 505004329 271 LREILDQMKSL--------EPDSQEFKDMLQQVKEMVGDHTRQEESTMF 311
Cdd:cd12108   81 IDELLARLEALlpallagdAEDAEELAAALEALRTALREHLDEEEEELF 129
 
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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