ID   CYB_CHEMY               Reviewed;         381 AA.
AC   Q9TEC1;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=Cytochrome b;
DE   AltName: Full=Complex III subunit 3;
DE   AltName: Full=Complex III subunit III;
DE   AltName: Full=Cytochrome b-c1 complex subunit 3;
DE   AltName: Full=Ubiquinol-cytochrome-c reductase complex cytochrome b subunit;
GN   Name=MT-CYB; Synonyms=COB, CYTB, MTCYB;
OS   Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX   NCBI_TaxID=8469;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10368956; DOI=10.1093/oxfordjournals.molbev.a026163;
RA   Kumazawa Y., Nishida M.;
RT   "Complete mitochondrial DNA sequences of the green turtle and blue-tailed
RT   mole skink: statistical evidence for archosaurian affinity of turtles.";
RL   Mol. Biol. Evol. 16:784-792(1999).
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:0000250|UniProtKB:P00157}.
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000250|UniProtKB:P00157};
CC       Note=Binds 2 heme b groups non-covalently.
CC       {ECO:0000250|UniProtKB:P00157};
CC   -!- SUBUNIT: The cytochrome bc1 complex contains 3 respiratory subunits
CC       (MT-CYB, CYC1 and UQCRFS1), 2 core proteins (UQCRC1 and UQCRC2) and
CC       probably 6 low-molecular weight proteins.
CC       {ECO:0000250|UniProtKB:P00157}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P00157}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P00157}.
CC   -!- MISCELLANEOUS: Heme 1 (or BL or b562) is low-potential and absorbs at
CC       about 562 nm, and heme 2 (or BH or b566) is high-potential and absorbs
CC       at about 566 nm. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome b family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00967, ECO:0000255|PROSITE-ProRule:PRU00968}.
CC   -!- CAUTION: The full-length protein contains only eight transmembrane
CC       helices, not nine as predicted by bioinformatics tools.
CC       {ECO:0000250|UniProtKB:P00157}.
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DR   EMBL; AB012104; BAA79209.1; -; Genomic_DNA.
DR   RefSeq; NP_008776.1; NC_000886.1.
DR   AlphaFoldDB; Q9TEC1; -.
DR   SMR; Q9TEC1; -.
DR   GeneID; 808644; -.
DR   KEGG; cmy:808644; -.
DR   CTD; 4519; -.
DR   OrthoDB; 232320at2759; -.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045275; C:respiratory chain complex III; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:InterPro.
DR   GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR   CDD; cd00290; cytochrome_b_C; 1.
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; IPR030689; Cytochrome_b.
DR   InterPro; IPR048260; Cytochrome_b_C_euk/bac.
DR   InterPro; IPR048259; Cytochrome_b_N_euk/bac.
DR   InterPro; IPR016174; Di-haem_cyt_TM.
DR   PANTHER; PTHR19271; CYTOCHROME B; 1.
DR   PANTHER; PTHR19271:SF16; CYTOCHROME B; 1.
DR   Pfam; PF00032; Cytochrom_B_C; 1.
DR   Pfam; PF00033; Cytochrome_B; 1.
DR   PIRSF; PIRSF038885; COB; 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; Heme; Iron; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Respiratory chain; Transmembrane;
KW   Transmembrane helix; Transport; Ubiquinone.
FT   CHAIN           1..381
FT                   /note="Cytochrome b"
FT                   /id="PRO_0000060775"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   TRANSMEM        78..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   TRANSMEM        227..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   TRANSMEM        289..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   TRANSMEM        321..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   TRANSMEM        348..368
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   BINDING         84
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="b562"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   BINDING         98
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="b566"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   BINDING         183
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="b562"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   BINDING         197
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="b566"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
FT   BINDING         202
FT                   /ligand="a ubiquinone"
FT                   /ligand_id="ChEBI:CHEBI:16389"
FT                   /evidence="ECO:0000250|UniProtKB:P00157"
SQ   SEQUENCE   381 AA;  42859 MW;  DE980F3AFE9E17D7 CRC64;
     MATNLRKTHP MMKIINNLVI DLPSPSNISA WWNFGSLLAT CLALQIITGI FLAMHYSPDI
     SMAFSSIAHI TRDVQYGWLI RNMHANGASL FFMCIYLHIG RGIYYGSYLY KETWNTGIIL
     LLLVMATAFV GYVLPWGQMS FWGATVITNL LSAIPYIGNT LVQWIWGGFS VDNATLTRFF
     TFHFLLPFAI TGLTAVHLLF LHETGSNNPT GLNSNTDKIP FHPYFSYKDL LGLILMLTFL
     LTLTLFSPYL LGDPDNFTPA NPLSTPPHIK PEWYFLFAYA ILRSIPNKLG GVLALLFSIL
     ILFLMPTLHT SKQRTASFRP LTQILFWSLV ADLLVLTWIG GQPVEDPFII IGQVASTFYF
     LILLLLMPAA GMIENKMLNL K
//

ID   I1TF54_CHEMY            Unreviewed;       381 AA.
AC   I1TF54;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=Cytochrome b {ECO:0000256|ARBA:ARBA00013531, ECO:0000256|RuleBase:RU362117};
GN   Name=CYTB {ECO:0000313|EMBL:AEX26966.1};
OS   Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OG   Mitochondrion {ECO:0000313|EMBL:AEX26966.1}.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX   NCBI_TaxID=8469 {ECO:0000313|EMBL:AEX26966.1};
RN   [1] {ECO:0000313|EMBL:AEX26966.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=22432442; DOI=10.1111/j.1365-294X.2012.05530.x;
RA   Shamblin B.M., Bjorndal K.A., Bolten A.B., Hillis-Starr Z.M., Lundgren I.,
RA   Naro-Maciel E., Nairn C.J.;
RT   "Mitogenomic sequences better resolve stock structure of southern Greater
RT   Caribbean green turtle rookeries.";
RL   Mol. Ecol. 21:2330-2340(2012).
RN   [2] {ECO:0000313|EMBL:AFP52671.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=28666 {ECO:0000313|EMBL:AFP52723.1}, 71270
RC   {ECO:0000313|EMBL:AFP52839.1}, CGG-01Cmyd
RC   {ECO:0000313|EMBL:AFP52904.1}, and Sample ID 9277
RC   {ECO:0000313|EMBL:AFP52671.1};
RX   PubMed=22750111; DOI=10.1016/j.ympev.2012.06.010;
RA   Duchene S., Frey A., Alfaro-Nunez A., Dutton P.H., Thomas P Gilbert M.,
RA   Morin P.A.;
RT   "Marine turtle mitogenome phylogenetics and evolution.";
RL   Mol. Phylogenet. Evol. 65:241-250(2012).
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   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRSR:PIRSR038885-2};
CC       Note=Binds 2 heme groups non-covalently.
CC       {ECO:0000256|PIRSR:PIRSR038885-2};
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; JQ026233; AEW68207.1; -; Genomic_DNA.
DR   EMBL; JQ034420; AEX26966.1; -; Genomic_DNA.
DR   EMBL; JX454972; AFP52671.1; -; Genomic_DNA.
DR   EMBL; JX454976; AFP52723.1; -; Genomic_DNA.
DR   EMBL; JX454985; AFP52839.1; -; Genomic_DNA.
DR   EMBL; JX454990; AFP52904.1; -; Genomic_DNA.
DR   RefSeq; NP_008776.1; NC_000886.1.
DR   AlphaFoldDB; I1TF54; -.
DR   SMR; I1TF54; -.
DR   GeneID; 808644; -.
DR   KEGG; cmy:808644; -.
DR   CTD; 4519; -.
DR   OrthoDB; 232320at2759; -.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045275; C:respiratory chain complex III; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:InterPro.
DR   GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR   CDD; cd00290; cytochrome_b_C; 1.
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; IPR030689; Cytochrome_b.
DR   InterPro; IPR048260; Cytochrome_b_C_euk/bac.
DR   InterPro; IPR048259; Cytochrome_b_N_euk/bac.
DR   InterPro; IPR016174; Di-haem_cyt_TM.
DR   PANTHER; PTHR19271; CYTOCHROME B; 1.
DR   PANTHER; PTHR19271:SF16; CYTOCHROME B; 1.
DR   Pfam; PF00032; Cytochrom_B_C; 1.
DR   Pfam; PF00033; Cytochrome_B; 1.
DR   PIRSF; PIRSF038885; COB; 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|PIRSR:PIRSR038885-2};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR038885-2};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362117};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR038885-2};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW   ECO:0000256|RuleBase:RU362117};
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        31..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   TRANSMEM        146..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   TRANSMEM        179..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   TRANSMEM        230..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   TRANSMEM        289..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   TRANSMEM        320..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   TRANSMEM        347..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   DOMAIN          1..210
FT                   /note="Cytochrome b/b6 N-terminal region profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51002"
FT   DOMAIN          211..381
FT                   /note="Cytochrome b/b6 C-terminal region profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51003"
FT   BINDING         84
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="b562"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038885-2"
FT   BINDING         98
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="b566"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038885-2"
FT   BINDING         183
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="b562"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038885-2"
FT   BINDING         197
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="b566"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038885-2"
FT   BINDING         202
FT                   /ligand="a ubiquinone"
FT                   /ligand_id="ChEBI:CHEBI:16389"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038885-1"
SQ   SEQUENCE   381 AA;  42859 MW;  DE980F3AFE9E17D7 CRC64;
     MATNLRKTHP MMKIINNLVI DLPSPSNISA WWNFGSLLAT CLALQIITGI FLAMHYSPDI
     SMAFSSIAHI TRDVQYGWLI RNMHANGASL FFMCIYLHIG RGIYYGSYLY KETWNTGIIL
     LLLVMATAFV GYVLPWGQMS FWGATVITNL LSAIPYIGNT LVQWIWGGFS VDNATLTRFF
     TFHFLLPFAI TGLTAVHLLF LHETGSNNPT GLNSNTDKIP FHPYFSYKDL LGLILMLTFL
     LTLTLFSPYL LGDPDNFTPA NPLSTPPHIK PEWYFLFAYA ILRSIPNKLG GVLALLFSIL
     ILFLMPTLHT SKQRTASFRP LTQILFWSLV ADLLVLTWIG GQPVEDPFII IGQVASTFYF
     LILLLLMPAA GMIENKMLNL K
//