HEMTB_SIPNU
ID HEMTB_SIPNU Reviewed; 119 AA.
AC Q5K474;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Hemerythrin subunit B;
DE Short=Hr B;
OS Sipunculus nudus (Marine worm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Sipuncula; Sipunculidea;
OC Golfingiida; Sipunculidae; Sipunculus.
OX NCBI_TaxID=6446;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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; AJ632197; CAG14943.1; -; mRNA.
DR AlphaFoldDB; Q5K474; -.
DR SMR; Q5K474; -.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR CDD; cd12107; Hemerythrin; 1.
DR Gene3D; 1.20.120.50; -; 1.
DR InterPro; IPR002063; Haemerythrin.
DR InterPro; IPR016131; Haemerythrin_Fe_BS.
DR InterPro; IPR035938; Hemerythrin-like_sf.
DR InterPro; IPR012827; Hemerythrin_metal-bd.
DR PIRSF; PIRSF002033; Hemerythrin; 1.
DR PRINTS; PR00186; HEMERYTHRIN.
DR SUPFAM; SSF47188; SSF47188; 1.
DR TIGRFAMs; TIGR02481; hemeryth_dom; 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..119
FT /note="Hemerythrin subunit B"
FT /id="PRO_0000343357"
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 107
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 112
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 112
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02244"
SQ SEQUENCE 119 AA; 14064 MW; 18DC71E3F87BABCB CRC64;
MPFPVPDPFV WDTSFQVFYF KLDDQHRAIF ETLFNSTNDN TPGNLQLFYI VTANHFEEEE
GWMVSASYGG YDAHKKLHEE FLAKVRSFSA PVSKENLFYA KDWLVQHIKT IDFKYKQLL
