ID   HEMT2_GOLVU             Reviewed;         114 AA.
AC   Q5K471;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 2.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Hemerythrin subunit 2;
DE            Short=Hr 2;
OS   Golfingia vulgaris (Marine worm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Sipuncula; Sipunculidea;
OC   Golfingiida; Golfingiidae; Golfingia.
OX   NCBI_TaxID=210797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2-114.
RA   Vanin S., Negrisolo E., Bailly X., Bubacco L., Beltramini M., Salvato B.;
RT   "Molecular evolution and phylogeny of Sipuculans hemerythrins.";
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Hemerythrin is a respiratory protein in blood cells of
CC       certain marine worms. The oxygen-binding site in each chain contains
CC       two iron atoms (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the hemerythrin family. {ECO:0000305}.
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DR   EMBL; AJ632200; CAG14946.1; -; mRNA.
DR   AlphaFoldDB; Q5K471; -.
DR   SMR; Q5K471; -.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.50; -; 1.
DR   InterPro; IPR002063; Haemerythrin.
DR   InterPro; IPR016131; Haemerythrin_Fe_BS.
DR   InterPro; IPR035938; Hemerythrin-like_sf.
DR   PIRSF; PIRSF002033; Hemerythrin; 1.
DR   PRINTS; PR00186; HEMERYTHRIN.
DR   SUPFAM; SSF47188; SSF47188; 1.
DR   TIGRFAMs; TIGR00058; Hemerythrin; 1.
DR   PROSITE; PS00550; HEMERYTHRINS; 1.
PE   3: Inferred from homology;
KW   Iron; Metal-binding; Oxygen transport; Transport.
FT   CHAIN           1..114
FT                   /note="Hemerythrin subunit 2"
FT                   /id="PRO_0000343353"
FT   BINDING         26
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P02244"
FT   BINDING         55
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P02244"
FT   BINDING         59
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P02244"
FT   BINDING         59
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P02244"
FT   BINDING         74
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P02244"
FT   BINDING         78
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P02244"
FT   BINDING         102
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P02244"
FT   BINDING         107
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P02244"
FT   BINDING         107
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P02244"
SQ   SEQUENCE   114 AA;  13443 MW;  AF46D8515FA596E5 CRC64;
     MGFPIPDPYV WDPSFRIFYS IIDDEHKTLF NGIFHLGHDD SADNLAELRR CTGKHFLNEQ
     VLMQDSQYAG YAEHVRAHDG FIHQLDNWHG DVKWAKNWLV NHIKTIDFKY KGKI