ID D7L858_ARALL Unreviewed; 403 AA.
AC D7L858;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 03-MAY-2023, entry version 52.
DE RecName: Full=Cytochrome b561 and DOMON domain-containing protein {ECO:0000256|PIRNR:PIRNR037471};
GN ORFNames=ARALYDRAFT_480117 {ECO:0000313|EMBL:EFH59925.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
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; GL348715; EFH59925.1; -; Genomic_DNA.
DR RefSeq; XP_002883666.1; XM_002883620.1.
DR AlphaFoldDB; D7L858; -.
DR STRING; 81972.D7L858; -.
DR EnsemblPlants; fgenesh2_kg.3__2818__AT2G04850.1; fgenesh2_kg.3__2818__AT2G04850.1; fgenesh2_kg.3__2818__AT2G04850.1.
DR Gramene; fgenesh2_kg.3__2818__AT2G04850.1; fgenesh2_kg.3__2818__AT2G04850.1; fgenesh2_kg.3__2818__AT2G04850.1.
DR eggNOG; KOG4293; Eukaryota.
DR HOGENOM; CLU_036675_1_1_1; -.
DR OrthoDB; 469478at2759; -.
DR Proteomes; UP000008694; 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:SF60; 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:UP000008694};
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..403
FT /note="Cytochrome b561 and DOMON domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003101599"
FT TRANSMEM 219..240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 252..277
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 321..342
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 354..379
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 42..172
FT /note="DOMON"
FT /evidence="ECO:0000259|PROSITE:PS50836"
FT DOMAIN 179..379
FT /note="Cytochrome b561"
FT /evidence="ECO:0000259|PROSITE:PS50939"
FT BINDING 218
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 254
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 287
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 323
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 403 AA; 43813 MW; 47CBC49AB67EA034 CRC64;
MATLILTFLF LLATKLPSSL AGHCTTTTAT KSFEKCISLP TQQASIAWTY HPHNATLDLC
FFGTFISPSG WVGWGINPDS PAQMTGSRVF IAFPDPNSGQ LILLPYVLDS SVKLQKGPLL
SRPLDLVRLS SSSASLYGGK MATIRNGASV QIYASVKLSS NNTKIHHVWN RGLYVQGYSP
TIHPTTSIDL SSFSTFDVAS GFATVNRNSG SRALKVTHGV INAVAWGFLL PAGAVTARYL
RQMQSIGPTW FYIHAAIQLT GFLLGTIGFS IGIVLGHNSP GVTYGLHRSL GIATFTAAAL
QTLALLFRPK TTNKFRRYWK SYHHFVGYAC VVMGVVNVFQ GFEVLREGRS YAKLGYCLCL
STLVGVCVAM EVNSWVVFCR KAKEEKMKRD GLTGDDRCSG SHS
//
