The domain within your query sequence starts at position 355 and ends at position 697; the E-value for the TR_FER domain shown below is 3.26e-179.

VKWCAVGQQERTKCDQWSAVSGGALACATEETPEDCIAATMKGEADAMSLDGGFAYVAGH
CGLVPVLAENYLSTHSSGRLGSKCVNAPLEGYYVVAVVKKSDVGITWKSLQGKKSCHTAV
GTSEGWNVPMGLIYNQTGSCKFDAFFSRSCAPGSDPDSPLCALCVGGNNPAHMCAANNAE
GYHGSSGALRCLVEKGDVAFMKHPTVLQNTDGKNPEPWAKGLKHEDFELLCLDGTRKPVT
EAQSCHLARVPNRAVFSRKDKADFVRRILFNQQELFGRNGFEYMMFQMFESSAKDLLFSD
DTECLSNLQNKTTYKTYLGPQYLTLMDNFRQCLSSELLDACTF

TR_FER

Transferrin
TR_FER
SMART accession number:SM00094
Description: -
Interpro abstract (IPR001156):

Transferrins are eukaryotic iron-binding glycoproteins that control the level of free iron in biological fluids [ (PUBMED:3032619) ]. Evidence suggests that members of the TF family arose from the duplication and fusion of two homologous domains, with each duplicated domain binding one iron atom. Members of the family include blood serotransferrin (siderophilin); milk lactotransferrin (lactoferrin); egg white ovotransferrin (conalbumin); and membrane-associated melanotransferrin. Family members that do not bind iron have also been discovered, including inhibitor of carbonic anhydrase (ICA), which strongly binds to and inhibits certain isoforms of carbonic anhydrase [ (PUBMED:20572014) ].

This entry represents the transferrin-like domain, which can be further divided into two subdomains that form a cleft inside of which the iron atom is bound in iron-transporting transferrin [ (PUBMED:2585506) ]. The iron-coordinating residues consist of an aspartic acid, two tyrosines and a histidine, as well as an arginine that coordinates a requisite anion. In addition to iron and anion liganding residues, the transferrin-like domain contains conserved cysteine residues involved in disulphide bond formation.

Family alignment:
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There are 4096 TR_FER domains in 2538 proteins in SMART's nrdb database.

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