ID A0A022R2M6_ERYGU Unreviewed; 395 AA.
AC A0A022R2M6;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Cytochrome b561 and DOMON domain-containing protein {ECO:0000256|PIRNR:PIRNR037471};
GN ORFNames=MIMGU_mgv1a024240mg {ECO:0000313|EMBL:EYU33858.1};
OS Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU33858.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU33858.1, ECO:0000313|Proteomes:UP000030748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA Schmutz J., Willis J.H., Rokhsar D.S.;
RT "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT population shotgun sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
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 EMBL; KI630752; EYU33858.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A022R2M6; -.
DR STRING; 4155.A0A022R2M6; -.
DR eggNOG; KOG4293; Eukaryota.
DR PhylomeDB; A0A022R2M6; -.
DR Proteomes; UP000030748; Unassembled WGS sequence.
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:SF167; 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:UP000030748};
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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..395
FT /note="Cytochrome b561 and DOMON domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001504453"
FT TRANSMEM 211..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 244..265
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 285..304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 316..337
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 349..373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 45..159
FT /note="DOMON"
FT /evidence="ECO:0000259|PROSITE:PS50836"
FT DOMAIN 172..373
FT /note="Cytochrome b561"
FT /evidence="ECO:0000259|PROSITE:PS50939"
FT BINDING 213
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 249
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 282
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 318
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 395 AA; 43851 MW; 8161094485A968E7 CRC64;
MAISKIIIFF MFVSSLFVSS SSQNCSNYTF RDNKTYAACK TLPVLNSFLH WNYYESNHSV
DIAYRHTSLT ASNWAAWSLN PSGGAMIGAQ CLVAFRNTSG LMSAYTSPIT SYRTRLEEGP
LSFEVPRVAA EFDGDQITIY ATIKLPNVTT AFTHVWQHGV LFGDTPGMHP SGDNLNSIGI
VDFASGVTLD NNARPTTTVA TRLSRKNRMK FVHGVLNVVS WGILVPIGAM LARYLRVFEI
ANPMWFYLHV ACQLSGYVVG VAGWATGIKL GSDSPGIVHT THRNIGITIF ALATLQVLSL
KFRPKPNHKY RSYWNYYHKS IGYSVIVLSA VNIFQGFDIL DSEKKWKKAY IGVIIFLGAV
CVVLEAITQF IIFKRKEQSA DNPKVANGID ELDNV
//