ID   A0A0N9GCA2_9ARAC        Unreviewed;       195 AA.
AC   A0A0N9GCA2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   17-FEB-2016, entry version 2.
DE   RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369};
DE            EC=1.9.3.1 {ECO:0000256|RuleBase:RU000369};
DE   Flags: Fragment;
GN   Name=COI {ECO:0000313|EMBL:ALF74431.1};
OS   Rilaena triangularis.
OG   Mitochondrion {ECO:0000313|EMBL:ALF74431.1}.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Opiliones; Palpatores; Phalangioidea; Phalangiidae; Rilaena.
OX   NCBI_TaxID=475616 {ECO:0000313|EMBL:ALF74431.1};
RN   [1] {ECO:0000313|EMBL:ALF74431.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=26379469;
RA   Telfer A.C., Young M.R., Quinn J., Perez K., Sobel C.N., Sones J.E.,
RA   Levesque-Beaudin V., Derbyshire R., Fernandez-Triana J., Rougerie R.,
RA   Thevanayagam A., Boskovic A., Borisenko A.V., Cadel A., Brown A.,
RA   Pages A., Castillo A.H., Nicolai A., Glenn Mockford B.M., Bukowski B.,
RA   Wilson B., Trojahn B., Lacroix C.A., Brimblecombe C., Hay C., Ho C.,
RA   Steinke C., Warne C.P., Garrido Cortes C., Engelking D., Wright D.,
RA   Lijtmaer D.A., Gascoigne D., Hernandez Martich D., Morningstar D.,
RA   Neumann D., Steinke D., Marco DeBruin D.D., Dobias D., Sears E.,
RA   Richard E., Damstra E., Zakharov E.V., Laberge F., Collins G.E.,
RA   Blagoev G.A., Grainge G., Ansell G., Meredith G., Hogg I., McKeown J.,
RA   Topan J., Bracey J., Guenther J., Sills-Gilligan J., Addesi J.,
RA   Persi J., Layton K.K., D'Souza K., Dorji K., Grundy K., Nghidinwa K.,
RA   Ronnenberg K., Lee K.M., Xie L., Lu L., Penev L., Gonzalez M.,
RA   Rosati M.E., Kekkonen M., Kuzmina M., Iskandar M., Mutanen M.,
RA   Fatahi M., Pentinsaari M., Bauman M., Nikolova N., Ivanova N.V.,
RA   Jones N., Weerasuriya N., Monkhouse N., Lavinia P.D., Jannetta P.,
RA   Hanisch P.E., McMullin R.T., Ojeda Flores R., Mouttet R., Vender R.,
RA   Labbee R.N., Forsyth R., Lauder R., Dickson R., Kroft R., Miller S.E.,
RA   MacDonald S., Panthi S., Pedersen S., Sobek-Swant S., Naik S.,
RA   Lipinskaya T., Eagalle T., Decaens T., Kosuth T., Braukmann T.,
RA   Woodcock T., Roslin T., Zammit T., Campbell V., Dinca V., Peneva V.,
RA   Hebert P.D., deWaard J.R.;
RT   "Biodiversity inventories in high gear: DNA barcoding facilitates a
RT   rapid biotic survey of a temperate nature reserve.";
RL   Biodivers Data J 3:E6313-E6313(2015).
RN   [2] {ECO:0000313|EMBL:ALF74431.1}
RP   NUCLEOTIDE SEQUENCE.
RG   Swine Surveillance;
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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. CO I is the
CC       catalytic subunit of the enzyme. Electrons originating in
CC       cytochrome c are transferred via the copper A center of subunit 2
CC       and heme A of subunit 1 to the bimetallic center formed by heme A3
CC       and copper B. {ECO:0000256|RuleBase:RU000369}.
CC   -!- CATALYTIC ACTIVITY: 4 ferrocytochrome c + O(2) + 4 H(+) = 4
CC       ferricytochrome c + 2 H(2)O. {ECO:0000256|RuleBase:RU000369}.
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000256|RuleBase:RU000369}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|RuleBase:RU000369}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU000369}.
CC   -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC       {ECO:0000256|RuleBase:RU000369}.
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DR   EMBL; KT703079; ALF74431.1; -; Genomic_DNA.
DR   UniPathway; UPA00705; -.
DR   Gene3D; 1.20.210.10; -; 1.
DR   InterPro; IPR000883; COX1.
DR   InterPro; IPR023616; Cyt_c_Oxase_su1_dom.
DR   PANTHER; PTHR10422; PTHR10422; 1.
DR   Pfam; PF00115; COX1; 1.
DR   PRINTS; PR01165; CYCOXIDASEI.
DR   SUPFAM; SSF81442; SSF81442; 1.
DR   PROSITE; PS50855; COX1; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|RuleBase:RU000369};
KW   Electron transport {ECO:0000256|RuleBase:RU000369};
KW   Heme {ECO:0000256|RuleBase:RU000369};
KW   Iron {ECO:0000256|RuleBase:RU000369};
KW   Membrane {ECO:0000256|RuleBase:RU000369};
KW   Metal-binding {ECO:0000256|RuleBase:RU000369};
KW   Mitochondrion {ECO:0000256|RuleBase:RU000369,
KW   ECO:0000313|EMBL:ALF74431.1};
KW   Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000369};
KW   Respiratory chain {ECO:0000256|RuleBase:RU000369};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|RuleBase:RU000369};
KW   Transport {ECO:0000256|RuleBase:RU000369}.
FT   SIGNAL        1     18       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        19    195       Cytochrome c oxidase subunit 1.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5006035096.
FT   NON_TER       1      1       {ECO:0000313|EMBL:ALF74431.1}.
FT   NON_TER     195    195       {ECO:0000313|EMBL:ALF74431.1}.
SQ   SEQUENCE   195 AA;  21166 MW;  AA59BD2ADCBB8195 CRC64;
     SMYMIFGMWA AMVGTALSMX IRTELGQPGS LMNDDQIYNV IVTAHAFVMI FFMVMPIMIG
     GFGNWLVPLM LGAPDMAFPR LNNMSFWLLP PSFLLLLSSA LVENGAGTGW TVYPPLSSNI
     AHTGASVDLT IFSLHLAGVS SILGAINFIT TIIXMRTQGM ILERMPLFVW SVKITAILLL
     LSLPVLAGAI TMLLT
//