ID   A0A0F6UV47_ERYTA        Unreviewed;       236 AA.
AC   A0A0F6UV47; A0A0F6S1Z1;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 2.
DT   29-MAY-2024, entry version 21.
DE   RecName: Full=Cytochrome b {ECO:0000256|ARBA:ARBA00013531};
DE   AltName: Full=Complex III subunit 3 {ECO:0000256|ARBA:ARBA00031681};
DE   AltName: Full=Complex III subunit III {ECO:0000256|ARBA:ARBA00032600};
DE   AltName: Full=Cytochrome b-c1 complex subunit 3 {ECO:0000256|ARBA:ARBA00029812};
DE   AltName: Full=Ubiquinol-cytochrome-c reductase complex cytochrome b subunit {ECO:0000256|ARBA:ARBA00032818};
DE   Flags: Fragment;
OS   Eryx tataricus (Tartar sand boa).
OG   Mitochondrion {ECO:0000313|EMBL:AKE78823.2}.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Henophidia; Boidae; Erycinae; Eryx.
OX   NCBI_TaxID=51873 {ECO:0000313|EMBL:AKE78823.2};
RN   [1] {ECO:0000313|EMBL:AKE78823.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=1_Fariman {ECO:0000313|EMBL:AKE78825.2}, 22_Birjand
RC   {ECO:0000313|EMBL:AKE78823.2}, 30_Shaskoh
RC   {ECO:0000313|EMBL:AKE78822.2}, 4_Fariman
RC   {ECO:0000313|EMBL:AKE78819.2}, 6_Fariman
RC   {ECO:0000313|EMBL:AKE78821.2}, and ERP_1051_Torbat_Jam
RC   {ECO:0000313|EMBL:AKE78809.2};
RA   Rastegar-Pouyani E., Eskandarzadeh N., Darvish J.;
RT   "Re-evaluation of the taxonomic status of sand boas of the genus Eryx
RT   (Daudin, 1803) (Serpentes: Boidae) in northeastern Iran using sequences of
RT   the mitochondrial genome.";
RL   Zool Middle East 60:320-326(2014).
RN   [2] {ECO:0000313|EMBL:AKE78823.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=1_Fariman {ECO:0000313|EMBL:AKE78825.2}, 22_Birjand
RC   {ECO:0000313|EMBL:AKE78823.2}, 30_Shaskoh
RC   {ECO:0000313|EMBL:AKE78822.2}, 4_Fariman
RC   {ECO:0000313|EMBL:AKE78819.2}, 6_Fariman
RC   {ECO:0000313|EMBL:AKE78821.2}, and ERP_1051_Torbat_Jam
RC   {ECO:0000313|EMBL:AKE78809.2};
RA   Ploux O.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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   -!- 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:0000256|ARBA:ARBA00011660}.
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}.
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DR   EMBL; KJ841054; AKE78809.2; -; Genomic_DNA.
DR   EMBL; KJ841064; AKE78819.2; -; Genomic_DNA.
DR   EMBL; KJ841066; AKE78821.2; -; Genomic_DNA.
DR   EMBL; KJ841067; AKE78822.2; -; Genomic_DNA.
DR   EMBL; KJ841068; AKE78823.2; -; Genomic_DNA.
DR   EMBL; KJ841070; AKE78825.2; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F6UV47; -.
DR   GO; GO:0005750; C:mitochondrial respiratory chain complex III; IEA:TreeGrafter.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:TreeGrafter.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IEA:TreeGrafter.
DR   CDD; cd00284; Cytochrome_b_N; 1.
DR   InterPro; IPR005798; Cyt_b/b6_C.
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:SF16; CYTOCHROME B; 1.
DR   Pfam; PF00033; Cytochrome_B; 1.
DR   SUPFAM; SSF81342; Transmembrane di-heme cytochromes; 1.
DR   PROSITE; PS51003; CYTB_CTER; 1.
DR   PROSITE; PS51002; CYTB_NTER; 1.
PE   4: Predicted;
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128, ECO:0000313|EMBL:AKE78823.2};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Respiratory chain {ECO:0000256|ARBA:ARBA00022660};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW   Ubiquinone {ECO:0000256|ARBA:ARBA00023075}.
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        81..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        108..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        147..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        198..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..178
FT                   /note="Cytochrome b/b6 N-terminal region profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51002"
FT   DOMAIN          179..236
FT                   /note="Cytochrome b/b6 C-terminal region profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51003"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AKE78823.2"
FT   NON_TER         236
FT                   /evidence="ECO:0000313|EMBL:AKE78823.2"
SQ   SEQUENCE   236 AA;  26567 MW;  4FB435A8E1044D2B CRC64;
     NFGSMLLACS SMQVLTGFFL AVHYTANINL AFSSIVHITR DVPYGWMMQN LHAIGASMFF
     ICIYIHIARG LYYGSYLNKK TWLSGTTLLI MLMATAFFGY VLPWGQMSFW AATVITNLLT
     AIPYLGTTMT TWLWGGFAIN DPTLTRFFAL HFILPFGIIS LSSLHIMLLH EDGSSNPLGT
     NSDIDKIPFH PYHTYKDLLM LSLMVLMLLM TVSFLPDIFN DPENFSKANP LVTPQH
//