ID A0A8A4R131_PLARL Unreviewed; 361 AA.
AC A0A8A4R131;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 24-JAN-2024, entry version 7.
DE RecName: Full=Cytochrome b {ECO:0000256|ARBA:ARBA00013531, ECO:0000256|RuleBase:RU362117};
DE Flags: Fragment;
GN Name=cytb {ECO:0000313|EMBL:QTD19014.1};
OS Plasmodium relictum.
OG Mitochondrion {ECO:0000313|EMBL:QTD19014.1}.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Haemamoeba).
OX NCBI_TaxID=85471 {ECO:0000313|EMBL:QTD19014.1};
RN [1] {ECO:0000313|EMBL:QTD19014.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PGRW11 {ECO:0000313|EMBL:QTD19014.1};
RA Chavatte J.-M.;
RL Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QTD19014.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PGRW11 {ECO:0000313|EMBL:QTD19014.1};
RX PubMed=33678383;
RA Thorel M., Chavatte J.M., Landau I., Lemberger K., Leclerc A.;
RT "First case of Plasmodium relictum lineage pGRW11 infection in a captive-
RT bred common eider (Somateria Mollissima) in Europe.";
RL Vet Parasitol Reg Stud Reports 23:0-0(0).
CC -!- FUNCTION: Component of the ubiquinol-cytochrome c reductase complex
CC (complex III or cytochrome b-c1 complex) that is part of the
CC mitochondrial respiratory chain. The b-c1 complex mediates electron
CC transfer from ubiquinol to cytochrome c. Contributes to the generation
CC of a proton gradient across the mitochondrial membrane that is then
CC used for ATP synthesis. {ECO:0000256|ARBA:ARBA00002566,
CC ECO:0000256|RuleBase:RU362117}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|RuleBase:RU362117};
CC Note=Binds 2 heme groups non-covalently.
CC {ECO:0000256|RuleBase:RU362117};
CC -!- SUBUNIT: The main subunits of complex b-c1 are: cytochrome b,
CC cytochrome c1 and the Rieske protein. {ECO:0000256|ARBA:ARBA00011649}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004448}.
CC -!- SIMILARITY: Belongs to the cytochrome b family.
CC {ECO:0000256|RuleBase:RU362117}.
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DR EMBL; MT428075; QTD19014.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8A4R131; -.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR CDD; cd00284; Cytochrome_b_N; 1.
DR InterPro; IPR005798; Cyt_b/b6_C.
DR InterPro; IPR036150; Cyt_b/b6_C_sf.
DR InterPro; IPR005797; Cyt_b/b6_N.
DR InterPro; IPR027387; Cytb/b6-like_sf.
DR InterPro; IPR048259; Cytochrome_b_N_euk/bac.
DR InterPro; IPR016174; Di-haem_cyt_TM.
DR PANTHER; PTHR19271; CYTOCHROME B; 1.
DR PANTHER; PTHR19271:SF30; CYTOCHROME B; 1.
DR Pfam; PF00032; Cytochrom_B_C; 1.
DR Pfam; PF00033; Cytochrome_B; 1.
DR SUPFAM; SSF81648; a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase); 1.
DR SUPFAM; SSF81342; Transmembrane di-heme cytochromes; 1.
DR PROSITE; PS51003; CYTB_CTER; 1.
DR PROSITE; PS51002; CYTB_NTER; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|RuleBase:RU362117};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU362117};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU362117};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362117};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362117};
KW Mitochondrion {ECO:0000256|RuleBase:RU362117, ECO:0000313|EMBL:QTD19014.1};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660,
KW ECO:0000256|RuleBase:RU362117};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362117};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362117};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362117};
KW Ubiquinone {ECO:0000256|ARBA:ARBA00023075}.
FT TRANSMEM 25..51
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362117"
FT TRANSMEM 72..94
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362117"
FT TRANSMEM 106..128
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362117"
FT TRANSMEM 140..162
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362117"
FT TRANSMEM 174..193
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362117"
FT TRANSMEM 278..295
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362117"
FT TRANSMEM 315..334
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362117"
FT TRANSMEM 341..360
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362117"
FT DOMAIN 1..200
FT /note="Cytochrome b/b6 N-terminal region profile"
FT /evidence="ECO:0000259|PROSITE:PS51002"
FT DOMAIN 200..361
FT /note="Cytochrome b/b6 C-terminal region profile"
FT /evidence="ECO:0000259|PROSITE:PS51003"
FT NON_TER 361
FT /evidence="ECO:0000313|EMBL:QTD19014.1"
SQ SEQUENCE 361 AA; 41634 MW; 254908A50BCE3A4A CRC64;
MNYYSINLAK AHLIHYPCPL NINFLWNYGF LLGIVFFIQI LTGVLLATCY TPEISYAYYS
VQHILRELWS GWCFRYMHAT GASFVFILTY LHILRGLNYS YSYLPLSWIS GLIIFLISIV
TAFMGYVLPW GQMSFWGATV ITNLLYFIPG LVSWICGGYL VSDPTLKRFF VLHFTFPFIA
LCIVFIHIFF LHLQGSTNPL GYDTALKIPF YPNLLSLDIK GFNNVLVLFL AQSLFGILPL
SHPDNAITVD RYATPLHIVP EWYFLPFYAM LKTIPNKTAG LLVMLASLQI LFLLAEQRNL
TTLIQFKFAF GAREYSVPTI WFICSFYALL WIGCQLPQDI YILYGRLFII LFFFSGLFTL
V
//