MULTISPECIES: hemerythrin domain-containing protein [Citrobacter]
hemerythrin domain-containing protein( domain architecture ID 10485355)
hemerythrin domain-containing protein adopts a four alpha helix bundle fold and may bind cations
List of domain hits
Name | Accession | Description | Interval | E-value | |||
Hemerythrin | pfam01814 | Hemerythrin HHE cation binding domain; Iteration of the HHE family found it to be related to ... |
3-133 | 7.84e-08 | |||
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: 47.60 E-value: 7.84e-08
|
|||||||
Name | Accession | Description | Interval | E-value | |||
Hemerythrin | pfam01814 | Hemerythrin HHE cation binding domain; Iteration of the HHE family found it to be related to ... |
3-133 | 7.84e-08 | |||
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: 47.60 E-value: 7.84e-08
|
|||||||
Name | Accession | Description | Interval | E-value | |||
Hemerythrin | pfam01814 | Hemerythrin HHE cation binding domain; Iteration of the HHE family found it to be related to ... |
3-133 | 7.84e-08 | |||
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: 47.60 E-value: 7.84e-08
|
|||||||
Blast search parameters | ||||
|