ID A0A0S0IGF3_ACAPO Unreviewed; 329 AA. AC A0A0S0IGF3; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 13-APR-2016, entry version 3. DE RecName: Full=Cytochrome c oxidase subunit 3 {ECO:0000256|RuleBase:RU003375}; GN Name=cox3 {ECO:0000313|EMBL:ALG41015.1}; OS Acanthamoeba polyphaga (Amoeba). OG Mitochondrion {ECO:0000313|EMBL:ALG41015.1}. OC Eukaryota; Amoebozoa; Discosea; Longamoebia; Centramoebida; OC Acanthamoebidae; Acanthamoeba. OX NCBI_TaxID=5757 {ECO:0000313|EMBL:ALG41015.1}; RN [1] {ECO:0000313|EMBL:ALG41015.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Linc Ap-1 {ECO:0000313|EMBL:ALG41015.1}; RA Karlyshev A.V.; RT "Complete sequence of mtDNA of Acanthamoeba polyphaga strain Linc Ap- RT 1."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. 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}. 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; KP054475; ALG41015.1; -; Genomic_DNA. DR GO; GO:0016020; C:membrane; IEA:InterPro. 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 Gene3D; 1.20.120.80; -; 1. DR InterPro; IPR024791; Cyt_c/ubiquinol_Oxase_su3. DR InterPro; IPR013833; Cyt_c_oxidase_su3_a-hlx. DR InterPro; IPR000298; Cyt_c_oxidase_su3_dom. DR PANTHER; PTHR11403; PTHR11403; 2. DR Pfam; PF00510; COX3; 2. DR SUPFAM; SSF81452; SSF81452; 1. DR PROSITE; PS50253; COX3; 1. PE 3: Inferred from homology; KW Membrane {ECO:0000256|SAM:Phobius}; KW Mitochondrion {ECO:0000256|RuleBase:RU003375, KW ECO:0000313|EMBL:ALG41015.1}; KW Transmembrane {ECO:0000256|RuleBase:RU003375, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 54 72 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 78 98 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 119 142 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 171 191 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 217 237 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 257 281 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 301 323 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 42 322 COX3. {ECO:0000259|PROSITE:PS50253}. SQ SEQUENCE 329 AA; 38843 MW; 2384486A69C20628 CRC64; MKLNYDFFLN KFSNVYNNDI RLVDLSNKWW YHNCRVHFAG NQKHSFHIVT RSPWPLYSSI AALMFTFGMV MHMHNYSYGN LLSLAGFLLI LLMMFVWWRD VIRESTFSGY HTKKVQQGLR LGVILFIISE VMFFFSFFWA FFHASLSPSV VLGSVWPPLG INVLNPLKIP LLNTLILLLS GLTVTWSHHV IRDKSWQKFF FSSTDNEEFK TPLLDNYVIC AFALFLTIFL GLEFTVWQGY EYYKASFYIY DGVYGSTFYM TTGLHGLHVI IGTLFLIVCF FRLIDLHFIY NHHFGYEAAI WYWHFVDVVW IFLFLSIYCW GSGVDSFFK //