ID A0A0N7EV94_9DIPT Unreviewed; 183 AA.
AC A0A0N7EV94;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 08-JUN-2016, entry version 5.
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:ALF74250.1};
OS Orthocladiinae sp. BOLD:ABA1222.
OG Mitochondrion {ECO:0000313|EMBL:ALF74250.1}.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC Pterygota; Neoptera; Endopterygota; Diptera; Nematocera;
OC Chironomoidea; Chironomidae; unclassified Orthocladiinae.
OX NCBI_TaxID=1724779 {ECO:0000313|EMBL:ALF74250.1};
RN [1] {ECO:0000313|EMBL:ALF74250.1}
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:ALF74250.1}
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; KT702898; ALF74250.1; -; 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:respiratory chain; IEA:UniProtKB-KW.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0009060; P:aerobic respiration; IEA:InterPro.
DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
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, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|RuleBase:RU000369};
KW Mitochondrion {ECO:0000256|RuleBase:RU000369,
KW ECO:0000313|EMBL:ALF74250.1};
KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000369};
KW Respiratory chain {ECO:0000256|RuleBase:RU000369};
KW Transmembrane {ECO:0000256|RuleBase:RU000369,
KW ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|RuleBase:RU000369}.
FT TRANSMEM 18 48 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 111 136 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 148 175 Helical. {ECO:0000256|SAM:Phobius}.
FT DOMAIN 1 183 COX1. {ECO:0000259|PROSITE:PS50855}.
FT NON_TER 1 1 {ECO:0000313|EMBL:ALF74250.1}.
FT NON_TER 183 183 {ECO:0000313|EMBL:ALF74250.1}.
SQ SEQUENCE 183 AA; 19587 MW; F9FE4C1EFF251837 CRC64;
LIRAELGHSG SLIGDDQIYN VIVTAHAFVM IFFMVMPILI GGFGNWLVPL MLGAPDMAFP
RMNNMSFWLL PPSLTLLLSS SIVENGAGTG WTVYPPLSSG IAHAGASVDL AIFSLHLAGI
SSILGAVNFI TTVINMRSEG ISYDRMPLFV WSVIITAILL LLSLPVLAGA ITMLLTDRNL
NTS
//