ID   GLB1_GLYDI              Reviewed;         147 AA.
AC   P02216;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 2.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Globin, major monomeric component;
OS   Glycera dibranchiata (Bloodworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC   Errantia; Phyllodocida; Glyceridae; Glycera.
OX   NCBI_TaxID=6350;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=5063466; DOI=10.1016/s0021-9258(19)45280-0;
RA   Imamura T., Baldwin T.O., Riggs A.;
RT   "The amino acid sequence of the monomeric hemoglobin component from the
RT   bloodworm, Glyat liver.";
RL   J. Biol. Chem. 247:2785-2797(1972).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   PubMed=4855197; DOI=10.1016/s0021-9258(19)42484-8;
RA   Padlan E.A., Love W.E.;
RT   "Three-dimensional structure of hemoglobin from the polychaete annelid,
RT   Glycera dibranchiata, at 2.5-A resolution.";
RL   J. Biol. Chem. 249:4067-4078(1974).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), AND SEQUENCE REVISION.
RX   PubMed=2585515; DOI=10.1016/0022-2836(89)90297-0;
RA   Arents G.A., Love W.E.;
RT   "Glycera dibranchiata hemoglobin. Structure and refinement at 1.5-A
RT   resolution.";
RL   J. Mol. Biol. 210:149-161(1989).
CC   -!- SUBUNIT: Monomer.
CC   -!- MISCELLANEOUS: X-ray crystallographic analysis indicates that the D
CC       helix is absent, Leu-58 replaces the distal His (of myoglobin E7), His-
CC       90 binds covalently to the heme iron, the F helix has several more
CC       residues than in mammalian globins, and Pro-105 (G7) causes a bend in
CC       the G helix.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   PIR; A02538; GGNW1B.
DR   PDB; 1HBG; X-ray; 1.50 A; A=1-147.
DR   PDB; 1JF3; X-ray; 1.40 A; A=1-147.
DR   PDB; 1JL7; X-ray; 1.40 A; A=1-147.
DR   PDB; 2HBG; X-ray; 1.50 A; A=1-147.
DR   PDBsum; 1HBG; -.
DR   PDBsum; 1JF3; -.
DR   PDBsum; 1JL7; -.
DR   PDBsum; 2HBG; -.
DR   AlphaFoldDB; P02216; -.
DR   SMR; P02216; -.
DR   EvolutionaryTrace; P02216; -.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR   GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR   CDD; cd01040; Mb-like; 1.
DR   Gene3D; 1.10.490.10; -; 1.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin-like_sf.
DR   InterPro; IPR012292; Globin/Proto.
DR   InterPro; IPR044399; Mb-like_M.
DR   Pfam; PF00042; Globin; 1.
DR   SUPFAM; SSF46458; SSF46458; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Heme; Iron; Metal-binding;
KW   Oxygen transport; Transport.
FT   CHAIN           1..147
FT                   /note="Globin, major monomeric component"
FT                   /id="PRO_0000052500"
FT   BINDING         90
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   SITE            105
FT                   /note="Causes a bend in the G helix"
FT   CONFLICT        20
FT                   /note="A -> N (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        34
FT                   /note="F -> H (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        54
FT                   /note="G -> A (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        57
FT                   /note="A -> D (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        100
FT                   /note="A -> G (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           4..18
FT                   /evidence="ECO:0007829|PDB:1JF3"
FT   TURN            19..23
FT                   /evidence="ECO:0007829|PDB:1JF3"
FT   HELIX           24..37
FT                   /evidence="ECO:0007829|PDB:1JF3"
FT   HELIX           39..41
FT                   /evidence="ECO:0007829|PDB:1JF3"
FT   TURN            42..46
FT                   /evidence="ECO:0007829|PDB:1JF3"
FT   HELIX           53..71
FT                   /evidence="ECO:0007829|PDB:1JF3"
FT   TURN            72..74
FT                   /evidence="ECO:0007829|PDB:1JF3"
FT   HELIX           76..89
FT                   /evidence="ECO:0007829|PDB:1JF3"
FT   HELIX           90..92
FT                   /evidence="ECO:0007829|PDB:1JF3"
FT   STRAND          94..96
FT                   /evidence="ECO:0007829|PDB:1HBG"
FT   HELIX           100..102
FT                   /evidence="ECO:0007829|PDB:1JF3"
FT   HELIX           103..118
FT                   /evidence="ECO:0007829|PDB:1JF3"
FT   HELIX           119..121
FT                   /evidence="ECO:0007829|PDB:1JF3"
FT   HELIX           124..145
FT                   /evidence="ECO:0007829|PDB:1JF3"
SQ   SEQUENCE   147 AA;  14902 MW;  980558C06D881C43 CRC64;
     GLSAAQRQVI AATWKDIAGA DNGAGVGKDC LIKFLSAHPQ MAAVFGFSGA SDPGVAALGA
     KVLAQIGVAV SHLGDEGKMV AQMKAVGVRH KGYGNKHIKA QYFEPLGASL LSAMEHRIGG
     KMNAAAKDAW AAAYADISGA LISGLQS