MBI3_YEAST
ID MBI3_YEAST Reviewed; 517 AA.
AC Q9ZZW7; A0A0A7NYF0; Q36758;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Cytochrome b mRNA maturase bI3;
GN Name=BI3; OrderedLocusNames=Q0115;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OG Mitochondrion.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9872396; DOI=10.1016/s0014-5793(98)01467-7;
RA Foury F., Roganti T., Lecrenier N., Purnelle B.;
RT "The complete sequence of the mitochondrial genome of Saccharomyces
RT cerevisiae.";
RL FEBS Lett. 440:325-331(1998).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 144-517, MUTAGENESIS OF PHE-151 AND
RP GLY-407, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 44821 / 777-3A;
RX PubMed=2538624; DOI=10.1016/0022-2836(89)90341-0;
RA Lazowska J., Claisse M., Gargouri A., Kotylak Z., Spyridakis A.,
RA Slonimski P.P.;
RT "Protein encoded by the third intron of cytochrome b gene in Saccharomyces
RT cerevisiae is an mRNA maturase. Analysis of mitochondrial mutants, RNA
RT transcripts, proteins and evolutionary relationships.";
RL J. Mol. Biol. 205:275-289(1989).
RN [4]
RP FUNCTION, AND SUBUNIT.
RX PubMed=11773622; DOI=10.1073/pnas.012579299;
RA Bassi G.S., de Oliveira D.M., White M.F., Weeks K.M.;
RT "Recruitment of intron-encoded and co-opted proteins in splicing of the bI3
RT group I intron RNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:128-133(2002).
RN [5]
RP FUNCTION.
RX PubMed=12924947; DOI=10.1021/bi0346906;
RA Bassi G.S., Weeks K.M.;
RT "Kinetic and thermodynamic framework for assembly of the six-component bI3
RT group I intron ribonucleoprotein catalyst.";
RL Biochemistry 42:9980-9988(2003).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 257-517, AND RNA-BINDING.
RX PubMed=16116439; DOI=10.1038/nsmb976;
RA Longo A., Leonard C.W., Bassi G.S., Berndt D., Krahn J.M.,
RA Tanaka Hall T.M., Weeks K.M.;
RT "Evolution from DNA to RNA recognition by the bI3 LAGLIDADG maturase.";
RL Nat. Struct. Mol. Biol. 12:779-787(2005).
CC -!- FUNCTION: Mitochondrial mRNA maturase required for splicing of intron 3
CC of the cytochrome b (COB) gene, containing its own coding sequence. In
CC vivo splicing requires the formation of a ribonucleoprotein complex
CC together with the imported mitochondrial RNA-splicing protein MRS1. The
CC complex seems to stimulate the intrinsic ribozyme activity of intron
CC bI3 through binding to and stabilizing specific secondary and tertiary
CC structure elements in the RNA. {ECO:0000269|PubMed:11773622,
CC ECO:0000269|PubMed:12924947}.
CC -!- SUBUNIT: Forms a ribonucleoprotein complex composed of maturase bI3 and
CC 2 dimers of MRS1 that assemble around the bI3 RNA.
CC {ECO:0000269|PubMed:11773622}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- MISCELLANEOUS: Encoded from partially processed COB mRNA that
CC terminates with the in-frame coding sequence of the third intron.
CC -!- SIMILARITY: In the N-terminal section; belongs to the cytochrome b
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the LAGLIDADG
CC endonuclease family. {ECO:0000305}.
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DR EMBL; KP263414; AIZ98892.1; -; Genomic_DNA.
DR EMBL; X14637; CAA32785.1; -; Genomic_DNA.
DR PIR; S07845; S07845.
DR PIR; S78664; S78664.
DR RefSeq; NP_009317.1; NC_001224.1.
DR PDB; 2AB5; X-ray; 2.20 A; A/B=256-517.
DR PDBsum; 2AB5; -.
DR AlphaFoldDB; Q9ZZW7; -.
DR SMR; Q9ZZW7; -.
DR BioGRID; 34796; 5.
DR ComplexPortal; CPX-1331; bI3 intron splicing factor complex.
DR STRING; 4932.Q0115; -.
DR PaxDb; Q9ZZW7; -.
DR PRIDE; Q9ZZW7; -.
DR EnsemblFungi; Q0115_mRNA; Q0115; Q0115.
DR GeneID; 854605; -.
DR KEGG; sce:Q0115; -.
DR SGD; S000007272; BI3.
DR VEuPathDB; FungiDB:Q0115; -.
DR eggNOG; KOG4663; Eukaryota.
DR GeneTree; ENSGT00390000017948; -.
DR HOGENOM; CLU_526993_0_0_1; -.
DR InParanoid; Q9ZZW7; -.
DR BioCyc; YEAST:G3O-34381-MON; -.
DR EvolutionaryTrace; Q9ZZW7; -.
DR PRO; PR:Q9ZZW7; -.
DR Proteomes; UP000002311; Mitochondrion.
DR RNAct; Q9ZZW7; protein.
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:0005739; C:mitochondrion; IC:SGD.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0000372; P:Group I intron splicing; IDA:SGD.
DR GO; GO:0090615; P:mitochondrial mRNA processing; IDA:SGD.
DR GO; GO:0006397; P:mRNA processing; IDA:ComplexPortal.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR CDD; cd00284; Cytochrome_b_N; 1.
DR Gene3D; 1.20.810.10; -; 1.
DR Gene3D; 3.10.28.10; -; 2.
DR InterPro; IPR005797; Cyt_b/b6_N.
DR InterPro; IPR027387; Cytb/b6-like_sf.
DR InterPro; IPR016174; Di-haem_cyt_TM.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR004860; LAGLIDADG_2.
DR Pfam; PF00033; Cytochrome_B; 1.
DR Pfam; PF00961; LAGLIDADG_1; 2.
DR SUPFAM; SSF55608; SSF55608; 2.
DR SUPFAM; SSF81342; SSF81342; 1.
DR PROSITE; PS51002; CYTB_NTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW mRNA processing; mRNA splicing; Reference proteome; RNA-binding;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..517
FT /note="Cytochrome b mRNA maturase bI3"
FT /id="PRO_0000061915"
FT TOPO_DOM 1..31
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT TOPO_DOM 53..84
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT TOPO_DOM 106..115
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT TOPO_DOM 137..145
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT TOPO_DOM 167..184
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT TOPO_DOM 206..224
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..242
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT TOPO_DOM 243..517
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT REGION 1..169
FT /note="Cytochrome b"
FT REGION 170..517
FT /note="Maturase"
FT VARIANT 269
FT /note="G -> V (in strain: 777-3A)"
FT VARIANT 350
FT /note="D -> N (in strain: 777-3A)"
FT VARIANT 412
FT /note="E -> K (in strain: 777-3A)"
FT VARIANT 434
FT /note="Q -> M (in strain: 777-3A)"
FT VARIANT 437
FT /note="S -> N (in strain: 777-3A)"
FT VARIANT 451..452
FT /note="TQ -> NN (in strain: 777-3A)"
FT VARIANT 456..458
FT /note="TDK -> MNE (in strain: 777-3A)"
FT VARIANT 463
FT /note="R -> K (in strain: 777-3A)"
FT VARIANT 471
FT /note="G -> D (in strain: 777-3A)"
FT VARIANT 515
FT /note="P -> S (in strain: 777-3A)"
FT MUTAGEN 151
FT /note="F->C: In M2011; leads to absence of functional
FT cytochrome b, but does not affect splicing."
FT /evidence="ECO:0000269|PubMed:2538624"
FT MUTAGEN 407
FT /note="G->D: In G5037; blocks formation of mature
FT cytochrome b mRNA."
FT /evidence="ECO:0000269|PubMed:2538624"
FT HELIX 264..275
FT /evidence="ECO:0007829|PDB:2AB5"
FT STRAND 276..283
FT /evidence="ECO:0007829|PDB:2AB5"
FT STRAND 286..295
FT /evidence="ECO:0007829|PDB:2AB5"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:2AB5"
FT HELIX 300..310
FT /evidence="ECO:0007829|PDB:2AB5"
FT STRAND 314..321
FT /evidence="ECO:0007829|PDB:2AB5"
FT STRAND 327..335
FT /evidence="ECO:0007829|PDB:2AB5"
FT HELIX 338..343
FT /evidence="ECO:0007829|PDB:2AB5"
FT HELIX 345..351
FT /evidence="ECO:0007829|PDB:2AB5"
FT HELIX 359..370
FT /evidence="ECO:0007829|PDB:2AB5"
FT HELIX 376..378
FT /evidence="ECO:0007829|PDB:2AB5"
FT HELIX 392..396
FT /evidence="ECO:0007829|PDB:2AB5"
FT HELIX 401..412
FT /evidence="ECO:0007829|PDB:2AB5"
FT STRAND 413..418
FT /evidence="ECO:0007829|PDB:2AB5"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:2AB5"
FT STRAND 427..433
FT /evidence="ECO:0007829|PDB:2AB5"
FT HELIX 438..447
FT /evidence="ECO:0007829|PDB:2AB5"
FT STRAND 454..457
FT /evidence="ECO:0007829|PDB:2AB5"
FT STRAND 462..466
FT /evidence="ECO:0007829|PDB:2AB5"
FT HELIX 469..481
FT /evidence="ECO:0007829|PDB:2AB5"
FT HELIX 489..501
FT /evidence="ECO:0007829|PDB:2AB5"
FT HELIX 505..508
FT /evidence="ECO:0007829|PDB:2AB5"
SQ SEQUENCE 517 AA; 61172 MW; FBCE3D178D92D850 CRC64;
MAFRKSNVYL SLVNSYIIDS PQPSSINYWW NMGSLLGLCL VIQIVTGIFM AMHYSSNIEL
AFSSVEHIMR DVHNGYILRY LHANGASFFF MVMFMHMAKG LYYGSYRSPR VTLWNVGVII
FILTIATAFL GYCCVYGQMS HWGATVITNL FSAIPFVGND IVSWLWGGFN MEDPYYSNMM
LNKSVLCWNI FIWMMNYYII QLIIYNNMIW NKNNMVKMFI MRRKLAVINM YMYMKLIIQR
TYSYYMNNTI IYDKNHKLNT DNPIYAYIGG LFEGDGWITI SKKGKYLLYE LGIEMHIRDI
QLLYKIKNIL GIGKVTIKKL KMKDGTIKEM CKFNVRNKNH LKNIIIPIFD KYPMLTNKHY
DYLYFKDNLL KDIKYYNDLS YYLRPIKPFN TTEDILNKNY FSSWLIGFFE AESCFSIYKP
MNKKMKTASF EVSQNNSMEV MLAIKSYLKI TQNIYTDKFN NSRMTTKSIN GIKNVVMFIN
NNPIKLLGYK KLQYLLFLKD LRTITKYNNY FKIPPKY
