The domain within your query sequence starts at position 11 and ends at position 216; the E-value for the Heme_oxygenase domain shown below is 7.3e-85.

QDLSEALKEATKEVHIQAENAEFMKNFQKGQVSREGFKLVMASLYHIYTALEEEIERNKQ
NPVYAPLYFPEELHRRAALEQDMAFWYGPHWQEIIPCTPATQHYVKRLHEVGRTHPELLV
AHAYTRYLGDLSGGQVLKKIAQKAMALPSSGEGLAFFTFPNIDSPTKFKQLYRARMNTLE
MTPEVKHRVTEEAKTAFLLNIELFEE

Heme_oxygenase

Heme_oxygenase
PFAM accession number:PF01126
Interpro abstract (IPR016053):

Haem oxygenase ( EC 1.14.99.3 ) (HO) [ (PUBMED:3290025) ] is the microsomal enzyme that, in animals, carries out the oxidation of haem, it cleaves the haem ring at the alpha-methene bridge to form biliverdin and carbon monoxide [ (PUBMED:3032976) ]. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. In mammals there are three isozymes of haem oxygenase: HO-1 to HO-3. The first two isozymes differ in their tissue expression and their inducibility: HO-1 is highly inducible by its substrate haem and by various non-haem substances, while HO-2 is non-inducible. It has been suggested [ (PUBMED:8093563) ] that HO-2 could be implicated in the production of carbon monoxide in the brain where it is said to act as a neurotransmitter. In the genome of the chloroplast of red algae as well as in cyanobacteria, there is a haem oxygenase (gene pbsA) that is the key enzyme in the synthesis of the chromophoric part of the photosynthetic antennae [ (PUBMED:9326680) ]. A haem oxygenase is also present in the bacteria Corynebacterium diphtheriae (gene hmuO), where it is involved in the acquisition of iron from the host haem [ (PUBMED:9006041) ]. There is, in the central section of these enzymes, a well-conserved region centred on a histidine residue.

GO process:heme oxidation (GO:0006788), oxidation-reduction process (GO:0055114)
GO function:heme oxygenase (decyclizing) activity (GO:0004392)

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