ID A0A0D9VQP1_9ORYZ Unreviewed; 388 AA.
AC A0A0D9VQP1;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Cytochrome b561 and DOMON domain-containing protein {ECO:0000256|PIRNR:PIRNR037471};
OS Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR03G06210.1, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR03G06210.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:LPERR03G06210.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR03G06210.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|PIRNR:PIRNR037471};
CC Note=Binds 2 heme b groups non-covalently.
CC {ECO:0000256|PIRNR:PIRNR037471};
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DR AlphaFoldDB; A0A0D9VQP1; -.
DR STRING; 77586.A0A0D9VQP1; -.
DR EnsemblPlants; LPERR03G06210.1; LPERR03G06210.1; LPERR03G06210.
DR Gramene; LPERR03G06210.1; LPERR03G06210.1; LPERR03G06210.
DR eggNOG; KOG4293; Eukaryota.
DR HOGENOM; CLU_036675_1_1_1; -.
DR Proteomes; UP000032180; Chromosome 3.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd08760; Cyt_b561_FRRS1_like; 1.
DR CDD; cd09629; DOMON_CIL1_like; 1.
DR Gene3D; 1.20.120.1770; -; 1.
DR InterPro; IPR045265; AIR12_DOMON.
DR InterPro; IPR006593; Cyt_b561/ferric_Rdtase_TM.
DR InterPro; IPR005018; DOMON_domain.
DR InterPro; IPR017214; UCP037471.
DR PANTHER; PTHR23130; CYTOCHROME B561 AND DOMON DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR23130:SF220; CYTOCHROME B561 AND DOMON DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF03188; Cytochrom_B561; 1.
DR Pfam; PF04526; DUF568; 1.
DR PIRSF; PIRSF037471; UCP037471; 1.
DR SMART; SM00665; B561; 1.
DR PROSITE; PS50939; CYTOCHROME_B561; 1.
DR PROSITE; PS50836; DOMON; 1.
PE 4: Predicted;
KW Electron transport {ECO:0000256|PIRNR:PIRNR037471};
KW Iron {ECO:0000256|PIRSR:PIRSR037471-1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR037471};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR037471-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000032180};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037471}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..388
FT /note="Cytochrome b561 and DOMON domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002348230"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 240..261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 281..298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 345..368
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 51..165
FT /note="DOMON"
FT /evidence="ECO:0000259|PROSITE:PS50836"
FT DOMAIN 171..369
FT /note="Cytochrome b561"
FT /evidence="ECO:0000259|PROSITE:PS50939"
FT BINDING 209
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR037471-1"
FT BINDING 245
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR037471-1"
FT BINDING 278
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR037471-1"
FT BINDING 314
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR037471-1"
SQ SEQUENCE 388 AA; 41408 MW; 4ACEDA66971883A5 CRC64;
MARQGHTAWL FIAGLLLASS IASAQTSGDC GSASFQNGAR TFQRCNTMAV LGASLHWTYH
AENGTADIAF RAPQTSSGWV AWGINTQGSG MPGSSVFIAS QDGAGAVSVT QTVLESTSPS
LNPSTLRFRV PVAPSAEYAN GVYTMFATIE LPSNSTTQNT VWQAGSGNTA SLGAHPTSGA
NLQSVQRLDF LSGQSTGASN SRLRRRNLHG ILNAVSWGIL IPLGAMIARY LRMFEAADPA
WFYLHITCQL SGYILGVAGW GLGLKLGSES KGTTYDDHRN IGIAIFCLAT LQVFALLLRP
DKKNKYRVYW NAYHHSVGYS AIILSAVNIF KGLNILKPAS GWKRSYIAIL ATLGGVALLL
EAITWVIVIR RKKSNKSQYG GANGNGRA
//
