ID A0A068F6G0_9NEOP Unreviewed; 262 AA. AC A0A068F6G0; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 07-JUN-2017, entry version 12. DE RecName: Full=Cytochrome c oxidase subunit 3 {ECO:0000256|RuleBase:RU003375}; GN Name=COX3 {ECO:0000313|EMBL:AID61642.1}; OS Grapholita dimorpha. OG Mitochondrion {ECO:0000313|EMBL:AID61642.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Lepidoptera; Glossata; Ditrysia; OC Tortricoidea; Tortricidae; Olethreutinae; Grapholitini; Grapholita. OX NCBI_TaxID=934274 {ECO:0000313|EMBL:AID61642.1}; RN [1] {ECO:0000313|EMBL:AID61642.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=24841435; RA Niu F.F., Fan X.L., Wei S.J.; RT "Complete mitochondrial genome of the Grapholita dimorpha Komai RT (Lepidoptera: Tortricidae)."; RL Mitochondrial DNA 0:0-0(2014). CC -!- FUNCTION: Subunits I, II and III form the functional core of the CC enzyme complex. {ECO:0000256|RuleBase:RU003375}. CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 3 family. CC {ECO:0000256|RuleBase:RU003375, ECO:0000256|SAAS:SAAS00709834}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KJ671625; AID61642.1; -; Genomic_DNA. DR RefSeq; YP_009048931.1; NC_024582.1. DR GeneID; 19909119; -. DR CTD; 4514; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro. DR GO; GO:0019646; P:aerobic electron transport chain; IEA:InterPro. DR CDD; cd01665; Cyt_c_Oxidase_III; 1. DR Gene3D; 1.20.120.80; -; 1. DR InterPro; IPR024791; Cyt_c/ubiquinol_Oxase_su3. DR InterPro; IPR033945; Cyt_c_oxase_su3_dom. DR InterPro; IPR000298; Cyt_c_oxidase-like_su3. DR InterPro; IPR013833; Cyt_c_oxidase_su3_a-hlx. DR PANTHER; PTHR11403; PTHR11403; 1. DR Pfam; PF00510; COX3; 1. DR SUPFAM; SSF81452; SSF81452; 1. DR PROSITE; PS50253; COX3; 1. PE 3: Inferred from homology; KW Membrane {ECO:0000256|SAAS:SAAS00709742, ECO:0000256|SAM:Phobius}; KW Mitochondrion {ECO:0000256|RuleBase:RU003375, KW ECO:0000313|EMBL:AID61642.1}; KW Transmembrane {ECO:0000256|RuleBase:RU003375, KW ECO:0000256|SAAS:SAAS00709762, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00709799, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 39 59 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 80 103 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 128 152 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 164 183 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 203 221 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 241 261 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 5 262 COX3. {ECO:0000259|PROSITE:PS50253}. SQ SEQUENCE 262 AA; 30641 MW; 43B58048BF197D48 CRC64; MTTHHNHPYH LVDYSPWPLT GAIGVLTLVT GMVKWFHNFN MNLLILGYII TLLTMYQWWR DICREGTMQG KHTILVSKGL RWGMILFIIS EVFFFLSFFW AFFHSSLSPN IEIGMMWPPV SIIPFNPFQI PLLNTIILIT SGITVTWAHH ALMENNFTQT TQGLFITVML GIYFTILQAY EYIEAPFTIA DSIYGSTFFM ATGFHGLHVM IGTIFLFICL LRHMNNHFSS NHHFGFEAAA WYWHFVDVVW LFLYISIYWW GN //