ID   MBI3_DEBHA              Reviewed;         522 AA.
AC   A9RAG7;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   23-FEB-2022, entry version 67.
DE   RecName: Full=Cytochrome b mRNA maturase bI3;
GN   Name=bI3;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OG   Mitochondrion.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=18673395; DOI=10.1111/j.1567-1364.2008.00409.x;
RA   Sacerdot C., Casaregola S., Lafontaine I., Tekaia F., Dujon B.,
RA   Ozier-Kalogeropoulos O.;
RT   "Promiscuous DNA in the nuclear genomes of hemiascomycetous yeasts.";
RL   FEMS Yeast Res. 8:846-857(2008).
CC   -!- FUNCTION: Mitochondrial mRNA maturase required for splicing of intron 3
CC       of the cytochrome b (COB) gene, containing its own coding sequence.
CC       {ECO:0000250}.
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; DQ508940; ABF58068.1; -; Genomic_DNA.
DR   RefSeq; YP_001621419.1; NC_010166.1.
DR   STRING; 284592.A9RAG7; -.
DR   GeneID; 5845845; -.
DR   InParanoid; A9RAG7; -.
DR   Proteomes; UP000000599; Mitochondrion.
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:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; mRNA processing;
KW   mRNA splicing; Reference proteome; RNA-binding; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..522
FT                   /note="Cytochrome b mRNA maturase bI3"
FT                   /id="PRO_0000355042"
FT   TOPO_DOM        1..31
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250"
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:0000250"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT   TOPO_DOM        106..110
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        111..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT   TOPO_DOM        132..154
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        155..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT   TOPO_DOM        176..522
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250"
FT   REGION          1..163
FT                   /note="Cytochrome b"
FT   REGION          164..522
FT                   /note="Maturase"
SQ   SEQUENCE   522 AA;  61859 MW;  436D31CF9BD9FF09 CRC64;
     MTIRKSNPYL SLVNSYLMDS PQPSSMNYWW NVGSLLGLCL VMQMASGMFL AMHYSSSMEL
     AFNSVEHMMR DVNAGWLMRY IHANGASFFF MCLYLHMGKA LYYGSYKSPR VLVWSMGVMM
     FMLTMATAFM GYCLVYGQMS HWGATVITNL LSAMPFMGGD LVPLSIILSL YLLYISLKTF
     MKMIFNQSYM CPAKGWVKKV LDNTFCIKKY MHMYLSSRTS PXLYINTMSN MQHMKIMSTK
     SHTKDRDTSF LEKDIKNMDR NLLALMVGFM DGDGYIRMNK KSKDNMNYIY MSLIMNLNKN
     DLKLLQYFHQ QLNMGKVYNM TPKKGNKLAR WEMNKLDLFN KMEPLLEYHN MKFLTETRQK
     QYLLLKYIKH NKLVYYEDII NNNNYINEFI ENNTLMDNFI KLDYFNNWLV GFTMAEGSFL
     IKKNKDICFQ LKQKYNLELF NNMTLFFNTT RKLNINKNKY MQFNVSSKND IQNMINFFSF
     SNNQPLLGNK LISYNKWLFT IKNSMRYKEL KTPYMSWHQK EQ