ID B9T190_RICCO Unreviewed; 399 AA.
AC B9T190;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=Cytochrome b561 and DOMON domain-containing protein {ECO:0000256|PIRNR:PIRNR037471};
GN ORFNames=RCOM_0495460 {ECO:0000313|EMBL:EEF30382.1};
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN [1] {ECO:0000313|Proteomes:UP000008311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
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; EQ974328; EEF30382.1; -; Genomic_DNA.
DR RefSeq; XP_002532009.1; XM_002531963.2.
DR AlphaFoldDB; B9T190; -.
DR STRING; 3988.B9T190; -.
DR GeneID; 8275955; -.
DR KEGG; rcu:8275955; -.
DR eggNOG; KOG4293; Eukaryota.
DR InParanoid; B9T190; -.
DR OrthoDB; 469478at2759; -.
DR Proteomes; UP000008311; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; 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 Monooxygenase {ECO:0000313|EMBL:EEF30382.1};
KW Oxidoreductase {ECO:0000313|EMBL:EEF30382.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008311};
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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..399
FT /note="Cytochrome b561 and DOMON domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002891858"
FT TRANSMEM 211..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 244..266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 286..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..374
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 40..168
FT /note="DOMON"
FT /evidence="ECO:0000259|PROSITE:PS50836"
FT DOMAIN 175..374
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 399 AA; 43952 MW; FC15C4A7DC857563 CRC64;
MLLLFFIFLF FCHFHNAISA HCTTVTSSKT FEKCMTFPTQ QTSMAWTFHK HNSTLDLVFF
GAFISPSGWV GWGINPTSPE MAGTRALIAF PDPNSGQLVV LPYILDPTVK LQKSPLLSRP
LDVHLLSSSA TLYGGKMASI HNGAAVQIYA TIRLSPNKTK LHFVWNRGLY VQGYSPTIHP
TTSNDLSSIA TIDVLSGFNA AHKDNTRMLK IIHGIANAIS WGVLLPTGAV TARYLRHIQA
LGPAWFYAHA GIQLSAFLLG TVGFAIGIRL GESSPGVVYS LHRKLGFAVF CLGALQTLAL
LFRPKTTNKY RKYWKSYHHF VGYACVVLGV VNVFQGFEVL GEGRSYAKLG YCLCLSTLVG
ASIALEVNSW VIFCRKSKEE KMRREGLISV SDKVSVIHN
//
