ID I7IH71_BABMR Unreviewed; 425 AA. AC I7IH71; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 15-MAR-2017, sequence version 2. DT 24-JUL-2024, entry version 31. DE SubName: Full=Cytochrome c oxidase subunit XV assembly protein {ECO:0000313|EMBL:CCF75302.2}; GN ORFNames=BmR1_04g05520 {ECO:0000313|EMBL:CCF75302.2}; OS Babesia microti (strain RI). OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida; OC Babesiidae; Babesia. OX NCBI_TaxID=1133968 {ECO:0000313|EMBL:CCF75302.2, ECO:0000313|Proteomes:UP000002899}; RN [1] {ECO:0000313|EMBL:CCF75302.2, ECO:0000313|Proteomes:UP000002899} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RI {ECO:0000313|EMBL:CCF75302.2, RC ECO:0000313|Proteomes:UP000002899}; RX PubMed=22833609; DOI=10.1093/nar/gks700; RA Cornillot E., Hadj-Kaddour K., Dassouli A., Noel B., Ranwez V., RA Vacherie B., Augagneur Y., Bres V., Duclos A., Randazzo S., Carcy B., RA Debierre-Grockiego F., Delbecq S., Moubri-Menage K., Shams-Eldin H., RA Usmani-Brown S., Bringaud F., Wincker P., Vivares C.P., Schwarz R.T., RA Schetters T.P., Krause P.J., Gorenflot A., Berry V., Barbe V., RA Ben Mamoun C.; RT "Sequencing of the smallest Apicomplexan genome from the human pathogen RT Babesia microti."; RL Nucleic Acids Res. 40:9102-9114(2012). RN [2] {ECO:0000313|EMBL:CCF75302.2, ECO:0000313|Proteomes:UP000002899} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RI {ECO:0000313|EMBL:CCF75302.2, RC ECO:0000313|Proteomes:UP000002899}; RX PubMed=24023759; DOI=10.1371/journal.pone.0072657; RA Cornillot E., Dassouli A., Garg A., Pachikara N., Randazzo S., Depoix D., RA Carcy B., Delbecq S., Frutos R., Silva J.C., Sutton R., Krause P.J., RA Mamoun C.B.; RT "Whole genome mapping and re-organization of the nuclear and mitochondrial RT genomes of Babesia microti isolates."; RL PLoS ONE 8:e72657-e72657(2013). RN [3] {ECO:0000313|EMBL:CCF75302.2, ECO:0000313|Proteomes:UP000002899} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RI {ECO:0000313|EMBL:CCF75302.2, RC ECO:0000313|Proteomes:UP000002899}; RX PubMed=27752055; DOI=10.1038/srep35284; RA Silva J.C., Cornillot E., McCracken C., Usmani-Brown S., Dwivedi A., RA Ifeonu O.O., Crabtree J., Gotia H.T., Virji A.Z., Reynes C., Colinge J., RA Kumar V., Lawres L., Pazzi J.E., Pablo J.V., Hung C., Brancato J., RA Kumari P., Orvis J., Tretina K., Chibucos M., Ott S., Sadzewicz L., RA Sengamalay N., Shetty A.C., Su Q., Tallon L., Fraser C.M., Frutos R., RA Molina D.M., Krause P.J., Ben Mamoun C.; RT "Genome-wide diversity and gene expression profiling of Babesia microti RT isolates identify polymorphic genes that mediate host-pathogen RT interactions."; RL Sci. Rep. 6:35284-35284(2016). CC -!- CATALYTIC ACTIVITY: CC Reaction=2 A + Fe(II)-heme o + H2O = 2 AH2 + Fe(II)-heme a; CC Xref=Rhea:RHEA:63388, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:17499, ChEBI:CHEBI:60530, ChEBI:CHEBI:61715; CC EC=1.17.99.9; Evidence={ECO:0000256|ARBA:ARBA00044475}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63389; CC Evidence={ECO:0000256|ARBA:ARBA00044475}; CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; CC Evidence={ECO:0000256|ARBA:ARBA00001970}; CC -!- PATHWAY: Porphyrin-containing compound metabolism; heme A biosynthesis; CC heme A from heme O: step 1/1. {ECO:0000256|ARBA:ARBA00044501}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. 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; LN871599; CCF75302.2; -; Genomic_DNA. DR AlphaFoldDB; I7IH71; -. DR VEuPathDB; PiroplasmaDB:BmR1_04g05520; -. DR OrthoDB; 7506at2759; -. DR Proteomes; UP000002899; Chromosome iv. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:TreeGrafter. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016653; F:oxidoreductase activity, acting on NAD(P)H, heme protein as acceptor; IEA:InterPro. DR GO; GO:0006784; P:heme A biosynthetic process; IEA:InterPro. DR InterPro; IPR003780; COX15/CtaA_fam. DR InterPro; IPR023754; HemeA_Synthase_type2. DR PANTHER; PTHR23289; CYTOCHROME C OXIDASE ASSEMBLY PROTEIN COX15; 1. DR PANTHER; PTHR23289:SF2; CYTOCHROME C OXIDASE ASSEMBLY PROTEIN COX15 HOMOLOG; 1. DR Pfam; PF02628; COX15-CtaA; 1. PE 4: Predicted; KW Heme biosynthesis {ECO:0000256|ARBA:ARBA00023133}; KW Iron {ECO:0000256|ARBA:ARBA00023004}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Reference proteome {ECO:0000313|Proteomes:UP000002899}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 84..104 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 168..186 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 198..216 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 236..258 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 278..301 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 347..364 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 376..396 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 402..422 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" SQ SEQUENCE 425 AA; 47353 MW; F8AD471F20DBDDC4 CRC64; MTTIRASSLF FKNARNLNCI FINCIGQKCV FTPYHFRNLR NQLLSSSLTN ISVPATVNAC RLYTNTSVNP LRNVFVSSQF DKPIAFWLMG CSSLTLAIML LGSYTRLTES GLSMTEWSPL GSGLPKTDEE WLNEFDKYKS TPEYRTVHTN ISIDDFKGIY FIEWMHRLVA RLTGLIYLGG FAYFTYVKAI KPPLKKSLLA IALLGASQAL IGMVMVNSGL KEPKDEQIVR VSPLILSFHF LNALGIYSLC FLNALSLLKP NSAVDTANKL KDLDNLKLIK KLTYLLSGVT LVTLFSGSIV AGNDAGFICN TWPKINEKFV PDEFTPLKTG LNGFMSDPVI IQFNHRSMAY LTSFSSLALA FATFKSKNLP PKIKKSVIYV LLSVLVQVII GIDTLLRGVP VYMGVAHHLG ALSVWTCLLH LLKRF //