The domain within your query sequence starts at position 8 and ends at position 67; the E-value for the HRG domain shown below is 5.3e-11.



PFAM accession number:PF16954
Interpro abstract (IPR026218):

Haems are metalloporphyrins that serve as prosthetic groups for a variety of biological processes, including respiration, gas sensing, xenobiotic detoxification, cell differentiation, circadian clock control, metabolic reprogramming and microRNA processing. Haem is usually synthesised by a multistep biosynthetic pathway. The cellular pathways and molecules that mediate intracellular haem trafficking are still largely unknown [(PUBMED:18418376)].

Caenorhabditis elegans and related helminths are natural haem auxotrophs that acquire environmental haem for incorporation into haemoproteins. In C.elegans, it has been shown that HRG-1 proteins are essential for haem homeostasis. In worms, depletion of hrg-1, or its paralogue hrg-4, results in the disruption of organismal haem sensing, and an abnormal response to haem analogues [(PUBMED:18418376)].

HRG-1 and HRG-4 are transmembrane (TM) proteins that reside in distinct intracellular compartments. Transient knockdown of hrg-1 in zebrafish leads to hydrocephalus, yolk tube malformations and profound defects in erythropoiesis-phenotypes that are fully rescued by worm HRG-1. Human and worm proteins have been shown to co-localise, and bind and transport haem, thus establishing an evolutionarily conserved function for HRG-1 [(PUBMED:18418376)].

Sequence analysis of HRG-1 has identified 4 predicted TM domains, and a conserved tyrosine and acidic-di-leucine-based sorting signal in the cytoplasmic C terminus. In addition, residues that could potentially either directly bind haem (H90 in TM2) or interact with the haem side chains (FARKY) are situated in the C-terminal tail [(PUBMED:18418376)].

GO process:heme transport (GO:0015886)
GO function:heme transporter activity (GO:0015232)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry HRG