ID A0EH17_PARTE Unreviewed; 121 AA.
AC A0EH17;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE RecName: Full=Group 1 truncated hemoglobin {ECO:0000256|PIRNR:PIRNR002030};
GN ORFNames=GSPATT00026932001 {ECO:0000313|EMBL:CAK94608.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK94608.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK94608.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK94608.1,
RC ECO:0000313|Proteomes:UP000000600};
RX PubMed=17086204; DOI=10.1038/nature05230;
RG Genoscope;
RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA Cohen J., Wincker P.;
RT "Global trends of whole-genome duplications revealed by the ciliate
RT Paramecium tetraurelia.";
RL Nature 444:171-178(2006).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|PIRSR:PIRSR002030-1};
CC Note=Binds 1 heme group per subunit. {ECO:0000256|PIRSR:PIRSR002030-1};
CC -!- SIMILARITY: Belongs to the truncated hemoglobin family. Group I
CC subfamily. {ECO:0000256|ARBA:ARBA00009660,
CC ECO:0000256|PIRNR:PIRNR002030}.
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DR EMBL; CT868678; CAK94608.1; -; Genomic_DNA.
DR RefSeq; XP_001461981.1; XM_001461944.1.
DR AlphaFoldDB; A0EH17; -.
DR STRING; 5888.A0EH17; -.
DR EnsemblProtists; CAK94608; CAK94608; GSPATT00026932001.
DR GeneID; 5047766; -.
DR KEGG; ptm:GSPATT00026932001; -.
DR eggNOG; ENOG502SC6F; Eukaryota.
DR HOGENOM; CLU_103526_2_1_1; -.
DR InParanoid; A0EH17; -.
DR OMA; HQTQFIS; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR CDD; cd00454; TrHb1_N; 1.
DR Gene3D; 1.10.490.10; Globins; 1.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR019795; Globin_bac-like_CS.
DR InterPro; IPR001486; Hemoglobin_trunc.
DR InterPro; IPR016339; Hemoglobin_trunc_I.
DR Pfam; PF01152; Bac_globin; 1.
DR PIRSF; PIRSF002030; Globin_Protozoa/Cyanobacteria; 1.
DR SUPFAM; SSF46458; Globin-like; 1.
DR PROSITE; PS01213; GLOBIN_FAM_2; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|PIRNR:PIRNR002030, ECO:0000256|PIRSR:PIRSR002030-1};
KW Iron {ECO:0000256|PIRNR:PIRNR002030, ECO:0000256|PIRSR:PIRSR002030-1};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR002030,
KW ECO:0000256|PIRSR:PIRSR002030-1};
KW Oxygen transport {ECO:0000256|PIRNR:PIRNR002030};
KW Reference proteome {ECO:0000313|Proteomes:UP000000600};
KW Transport {ECO:0000256|PIRNR:PIRNR002030}.
FT BINDING 72
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="proximal binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR002030-1"
SQ SEQUENCE 121 AA; 13149 MW; F5A91BBE0E038838 CRC64;
MQNKTVFDKL GGQANIDAAV VKFYEKVLSD PSVSHYFKNT DMKKQTENQQ KFLTMAFGGP
NNYKGRDMKA GHAGLGITTV AFNTIVKHLG DTLKEMGVPA DVIAEAAAVA ETTRADIVEI
K
//
