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Database: UniProt
Entry: A0A1E3PLR9_9ASCO
LinkDB: A0A1E3PLR9_9ASCO
Original site: A0A1E3PLR9_9ASCO 
ID   A0A1E3PLR9_9ASCO        Unreviewed;       416 AA.
AC   A0A1E3PLR9;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Cytochrome b-c1 complex subunit 2, mitochondrial {ECO:0000256|ARBA:ARBA00040751};
DE   AltName: Full=Complex III subunit 2 {ECO:0000256|ARBA:ARBA00041778};
DE   AltName: Full=Core protein II {ECO:0000256|ARBA:ARBA00041372};
DE   AltName: Full=Ubiquinol-cytochrome-c reductase complex core protein 2 {ECO:0000256|ARBA:ARBA00042707};
GN   ORFNames=NADFUDRAFT_82214 {ECO:0000313|EMBL:ODQ66379.1};
OS   Nadsonia fulvescens var. elongata DSM 6958.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetales incertae sedis; Nadsonia.
OX   NCBI_TaxID=857566 {ECO:0000313|EMBL:ODQ66379.1, ECO:0000313|Proteomes:UP000095009};
RN   [1] {ECO:0000313|EMBL:ODQ66379.1, ECO:0000313|Proteomes:UP000095009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6958 {ECO:0000313|EMBL:ODQ66379.1,
RC   ECO:0000313|Proteomes:UP000095009};
RX   PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA   Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA   Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA   Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA   Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA   Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA   Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA   Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|ARBA:ARBA00004443}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004443}; Matrix side
CC       {ECO:0000256|ARBA:ARBA00004443}.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family. UQCRC2/QCR2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00038146}.
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DR   EMBL; KV454408; ODQ66379.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E3PLR9; -.
DR   STRING; 857566.A0A1E3PLR9; -.
DR   OrthoDB; 1330839at2759; -.
DR   Proteomes; UP000095009; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004420; F:hydroxymethylglutaryl-CoA reductase (NADPH) activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0015936; P:coenzyme A metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR   InterPro; IPR002202; HMG_CoA_Rdtase.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR11851:SF209; CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR   PROSITE; PS50065; HMG_COA_REDUCTASE_4; 1.
PE   3: Inferred from homology;
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Hydrolase {ECO:0000313|EMBL:ODQ66379.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00022792};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095009};
KW   Respiratory chain {ECO:0000256|ARBA:ARBA00022660};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          36..170
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          177..345
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   416 AA;  42669 MW;  632ECFBB9261354F CRC64;
     MFAISRSKVI ASSTRCFSTL ESAGVKIAAQ QEGASAYGSK LSVVVRGGSR YNTKPGVAHV
     LEKFAFKNNN HKSALRLTRE AELVGAQLTS GVSRENIVLS ANFLKEDLEY FVQNLGAVVN
     GTVFNKYELV ERVAPLVAAE VNHANSDPVY LATEAAYETA FRSGLGNSVL AEAHSPVTIE
     DVVDYASKVY NKSNIALVAS GVIPADLQKF VANSYFAELS AGSALKAESV KTFSGESRIK
     AAGVNAVTVA FPIQGASSAA LAVLAKVVGG KSHIKWANSS SLLGSVAGGV EVSTSVASFS
     DASLFYITIS GASASAVSSA AKEAVAAIKT AAAGVSDAAL AAANAQAKLE AAAVFESFSN
     EIVGQQALSG SKVGLASLAK VSAEQVKDAA ASLLKGKTVV SVVGNTHELP HADELF
//
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