ID A0A160DRQ2_9GAMM Unreviewed; 384 AA.
AC A0A160DRQ2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Cytochrome d oxidase cyd, subunit II {ECO:0000313|EMBL:ANB16875.1};
GN ORFNames=I596_839 {ECO:0000313|EMBL:ANB16875.1};
OS Dokdonella koreensis DS-123.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dokdonella.
OX NCBI_TaxID=1300342 {ECO:0000313|EMBL:ANB16875.1, ECO:0000313|Proteomes:UP000076830};
RN [1] {ECO:0000313|EMBL:ANB16875.1, ECO:0000313|Proteomes:UP000076830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-123 {ECO:0000313|EMBL:ANB16875.1,
RC ECO:0000313|Proteomes:UP000076830};
RA Kim J.F., Lee H., Kwak M.-J.;
RT "Complete genome sequence of Dokdonella koreensis DS-123T.";
RL Submitted (APR-2016) 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}.
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DR EMBL; CP015249; ANB16875.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A160DRQ2; -.
DR STRING; 1300342.I596_839; -.
DR KEGG; dko:I596_839; -.
DR PATRIC; fig|1300342.3.peg.824; -.
DR OrthoDB; 9776710at2; -.
DR Proteomes; UP000076830; Chromosome.
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:UP000076830};
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 16..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 85..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 126..148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 209..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 271..290
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 297..321
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 384 AA; 42256 MW; B330D73A7021F624 CRC64;
MSELIGFLMS YETLRAVWWL FLGVLLIGFA ITGGYDLGVG ALLRVVARDD DERRVLLNAV
GPTWEGNQVW FILGGGAIFA AYPLIYAAAF SGFFVALILV LFALILRPVG FDYRSKLPSR
RWRDTWDWCL FIGGFVPALV FGVAFGNLLQ GVPFRYDEVL RVHYEGSFFG LLNPFGLLAG
VISLSMLVMQ GAAFLLIKTT GDVRQRAQRW FGIAVLVFCA SFALAGVWVA FGIDGYRIVA
FAGTEAYSNP VAKTVERAAG AWFANYRAMP VLWAIPALAF AGALAAWRLA PARPGLGFVL
SSVAVACTIL TAGVAMFPFM MPSSLVPSHS LTAWDATSSL LTLRWMFWLT VFFLPLIVAY
TSWVFRVMRG PVHIEHVRGS DAHY
//
