ID   U3LTB8_9STRA            Unreviewed;       195 AA.
AC   U3LTB8;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   16-JAN-2019, entry version 22.
DE   RecName: Full=Cytochrome c oxidase subunit 2 {ECO:0000256|RuleBase:RU000457};
DE   Flags: Fragment;
GN   Name=COX2 {ECO:0000313|EMBL:AGK25033.1};
OS   Pythium nagaii.
OG   Mitochondrion {ECO:0000313|EMBL:AGK25033.1}.
OC   Eukaryota; Stramenopiles; Oomycetes; Pythiales; Pythiaceae; Pythium.
OX   NCBI_TaxID=289625 {ECO:0000313|EMBL:AGK25033.1};
RN   [1] {ECO:0000313|EMBL:AGK25033.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=P16712 {ECO:0000313|EMBL:AGK25033.1};
RX   PubMed=23709523; DOI=10.3852/12-322;
RA   Bahramisharif A., Lamprecht S.C., Spies C.F., Botha W.J., McLeod A.;
RT   "Pythium cederbergense sp. nov. and related taxa from Pythium clade G
RT   associated with the South African indigenous plant Aspalathus linearis
RT   (rooibos).";
RL   Mycologia 105:1174-1189(2013).
CC   -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory
CC       chain that catalyzes the reduction of oxygen to water. Subunits 1-
CC       3 form the functional core of the enzyme complex. Subunit 2
CC       transfers the electrons from cytochrome c via its binuclear copper
CC       A center to the bimetallic center of the catalytic subunit 1.
CC       {ECO:0000256|RuleBase:RU000457}.
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|RuleBase:RU000457};
CC       Note=Binds a copper A center. {ECO:0000256|RuleBase:RU000457};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|RuleBase:RU000457}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU000457}.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC       {ECO:0000256|RuleBase:RU000457}.
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DR   EMBL; JX397984; AGK25033.1; -; Genomic_DNA.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR   CDD; cd13912; CcO_II_C; 1.
DR   Gene3D; 1.10.287.90; -; 1.
DR   Gene3D; 2.60.40.420; -; 1.
DR   InterPro; IPR002429; CcO_II-like_C.
DR   InterPro; IPR034210; CcO_II_C.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom.
DR   InterPro; IPR036257; Cyt_c_oxidase_su2_TM_sf.
DR   Pfam; PF00116; COX2; 1.
DR   Pfam; PF02790; COX2_TM; 1.
DR   SUPFAM; SSF49503; SSF49503; 1.
DR   SUPFAM; SSF81464; SSF81464; 1.
DR   PROSITE; PS50857; COX2_CUA; 1.
DR   PROSITE; PS50999; COX2_TM; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|RuleBase:RU000457, ECO:0000256|SAAS:SAAS00709548};
KW   Electron transport {ECO:0000256|RuleBase:RU000457,
KW   ECO:0000256|SAAS:SAAS00709556};
KW   Membrane {ECO:0000256|RuleBase:RU000457,
KW   ECO:0000256|SAAS:SAAS00883094, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|RuleBase:RU000457,
KW   ECO:0000256|SAAS:SAAS00709462};
KW   Mitochondrion {ECO:0000256|RuleBase:RU000457,
KW   ECO:0000313|EMBL:AGK25033.1};
KW   Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000457};
KW   Respiratory chain {ECO:0000256|RuleBase:RU000457,
KW   ECO:0000256|SAAS:SAAS00709567};
KW   Transmembrane {ECO:0000256|RuleBase:RU000457,
KW   ECO:0000256|SAAS:SAAS00882981, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00883111,
KW   ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|RuleBase:RU000457,
KW   ECO:0000256|SAAS:SAAS00709552}.
FT   TRANSMEM     16     36       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     57     79       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        1     85       COX2_TM. {ECO:0000259|PROSITE:PS50999}.
FT   DOMAIN       86    195       COX2_CUA. {ECO:0000259|PROSITE:PS50857}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:AGK25033.1}.
FT   NON_TER     195    195       {ECO:0000313|EMBL:AGK25033.1}.
SQ   SEQUENCE   195 AA;  22258 MW;  B9E9F027B274F643 CRC64;
     PATPVMEGII NFHHDLMFFL IVVTIFVCWM LFRVITLFDE KKNKIPSTVV HGATIEIIWT
     SVPALILLTV AVPSFALLYS MDEVIDPIIT LKVIGSQWYW SYEYSDNLEF SDEPLIFDSY
     MVQENDLEIG QFRLLEVDNR VVVPTNSHIR VLITASDVLH SWAIPSLGIK LDACPGRLNQ
     TSMFIKREGV FYGQC
//