ID A0A367E8J1_9ACTN Unreviewed; 335 AA.
AC A0A367E8J1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Cytochrome d ubiquinol oxidase subunit II {ECO:0000313|EMBL:RCG13975.1};
GN Name=cydB {ECO:0000313|EMBL:RCG13975.1};
GN ORFNames=DTL70_32880 {ECO:0000313|EMBL:RCG13975.1};
OS Streptomyces diacarni.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2800381 {ECO:0000313|EMBL:RCG13975.1, ECO:0000313|Proteomes:UP000252914};
RN [1] {ECO:0000313|EMBL:RCG13975.1, ECO:0000313|Proteomes:UP000252914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LHW51701 {ECO:0000313|EMBL:RCG13975.1,
RC ECO:0000313|Proteomes:UP000252914};
RA Li L.;
RT "Streptomyces reniochalinae sp. nov. and Streptomyces diacarnus sp. nov.
RT from marine sponges.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cytochrome ubiquinol oxidase subunit 2
CC family. {ECO:0000256|ARBA:ARBA00007543}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RCG13975.1}.
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DR EMBL; QOIN01000073; RCG13975.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367E8J1; -.
DR OrthoDB; 9776710at2; -.
DR Proteomes; UP000252914; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR003317; Cyt-d_oxidase_su2.
DR NCBIfam; TIGR00203; cydB; 1.
DR PANTHER; PTHR43141:SF5; CYTOCHROME BD-I UBIQUINOL OXIDASE SUBUNIT 2; 1.
DR PANTHER; PTHR43141; CYTOCHROME BD2 SUBUNIT II; 1.
DR Pfam; PF02322; Cyt_bd_oxida_II; 1.
DR PIRSF; PIRSF000267; Cyt_oxidse_sub2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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 Reference proteome {ECO:0000313|Proteomes:UP000252914};
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}.
FT TRANSMEM 6..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 82..99
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 119..138
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 158..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 194..216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 222..243
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 250..269
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 297..320
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 335 AA; 36909 MW; 546459C43029A71A CRC64;
MQLTDVWFVV IAILWIGYFF LEGFDFGVGI LTRLLARDRA ERRVLINTIG PVWDGNEVWL
LSAGGATFAA FPEWYATLFS GFYLPFLLIL VCLIVRGVAF EYRAKRQEER WQRNWEHAIF
LTSLLTAFLW GLVFANIVRG VKIDSHLEYV GNLTDLFSPY ALLGGLVTLA LFTFHGAVFT
ALKTLGDIRA RARRLATGLG IATAVLAAGF LLWTQADSGG TASLVALVVA VVALVAALAA
NLAGREGWSF TFSGLTVVAA VAMLFFSLFP DVMPSTLHAD WSLTVDNASS TPYTLKIMTW
CAAFATPIVL LYQGWTYWVF RKRIGTHHLA PSGGH
//
