SCE2_YEAST
ID SCE2_YEAST Reviewed; 556 AA.
AC P03878; A0A0A7P354; Q02339; Q35798; Q9ZZX2;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Intron-encoded DNA endonuclease aI4;
DE AltName: Full=DNA endonuclease I-SceII;
DE Contains:
DE RecName: Full=Truncated non-functional cytochrome oxidase 1;
DE Contains:
DE RecName: Full=DNA endonuclease aI4;
DE EC=3.1.-.-;
DE AltName: Full=Intron-encoded endonuclease I-SceII;
DE Flags: Precursor;
GN Name=AI4; Synonyms=ENS2, I-SCEII; OrderedLocusNames=Q0065;
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 [GENOMIC DNA], AND VARIANT 457-LYS-THR-458.
RC STRAIN=ATCC 24657 / D273-10B;
RX PubMed=6254986; DOI=10.1016/s0021-9258(19)70224-5;
RA Bonitz S.G., Coruzzi G., Thalenfeld B.E., Tzagoloff A., Macino G.;
RT "Assembly of the mitochondrial membrane system. Structure and nucleotide
RT sequence of the gene coding for subunit 1 of yeast cytochrome oxidase.";
RL J. Biol. Chem. 255:11927-11941(1980).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 245-531, MUTAGENESIS OF GLU-362, AND
RP MRNA MATURASE ACTIVITY.
RX PubMed=6285204; DOI=10.1038/298628a0;
RA Dujardin G., Jacq C., Slonimski P.P.;
RT "Single base substitution in an intron of oxidase gene compensates splicing
RT defects of the cytochrome b gene.";
RL Nature 298:628-632(1982).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 299-556.
RC STRAIN=ATCC 201238 / W303-1B;
RX PubMed=1310149; DOI=10.1128/mcb.12.2.696-705.1992;
RA Goguel V., Delahodde A., Jacq C.;
RT "Connections between RNA splicing and DNA intron mobility in yeast
RT mitochondria: RNA maturase and DNA endonuclease switching experiments.";
RL Mol. Cell. Biol. 12:696-705(1992).
RN [6]
RP FUNCTION, AND ENDONUCLEASE AND MRNA MATURASE ACTIVITY.
RX PubMed=2536593; DOI=10.1016/0092-8674(89)90246-8;
RA Delahodde A., Goguel V., Becam A.-M., Creusot F., Perea J., Banroques J.,
RA Jacq C.;
RT "Site-specific DNA endonuclease and RNA maturase activities of two
RT homologous intron-encoded proteins from yeast mitochondria.";
RL Cell 56:431-441(1989).
RN [7]
RP FUNCTION, AND INTRON HOMING.
RX PubMed=2536592; DOI=10.1016/0092-8674(89)90245-6;
RA Wenzlau J.M., Saldanha R.J., Butow R.A., Perlman P.S.;
RT "A latent intron-encoded maturase is also an endonuclease needed for intron
RT mobility.";
RL Cell 56:421-430(1989).
RN [8]
RP FUNCTION, COFACTOR, DIMERIZATION, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=2172241; DOI=10.1016/s0021-9258(17)30611-7;
RA Wernette C.M., Saldanha R.J., Perlman P.S., Butow R.A.;
RT "Purification of a site-specific endonuclease, I-Sce II, encoded by intron
RT 4 alpha of the mitochondrial coxI gene of Saccharomyces cerevisiae.";
RL J. Biol. Chem. 265:18976-18982(1990).
RN [9]
RP FUNCTION, AND CLEAVAGE SITE SPECIFICITY.
RX PubMed=2216759; DOI=10.1093/nar/18.19.5659;
RA Sargueil B., Hatat D., Delahodde A., Jacq C.;
RT "In vivo and in vitro analyses of an intron-encoded DNA endonuclease from
RT yeast mitochondria. Recognition site by site-directed mutagenesis.";
RL Nucleic Acids Res. 18:5659-5665(1990).
RN [10]
RP FUNCTION, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=8352597; DOI=10.1146/annurev.bi.62.070193.003103;
RA Lambowitz A.M., Belfort M.;
RT "Introns as mobile genetic elements.";
RL Annu. Rev. Biochem. 62:587-622(1993).
CC -!- FUNCTION: Mitochondrial DNA endonuclease involved in intron homing. It
CC introduces a specific double-strand break at the junction of the two
CC exons a4-a5 of the COX1 gene and thus mediates the insertion of an
CC intron, containing its own coding sequence (group I intron), into an
CC intronless gene. Recognizes with limited specificity and cleaves the
CC sequence 5'-TTTGGTCACCCTGAAGTA-3'. The protein may acquire mRNA
CC maturase activity, like the closely related bI4, through a single amino
CC acid substitution Glu-362 to Lys or when present together with a mutant
CC form of the imported mitochondrial leucyl-tRNA synthetase NAM2.
CC {ECO:0000269|PubMed:2172241, ECO:0000269|PubMed:2216759,
CC ECO:0000269|PubMed:2536592, ECO:0000269|PubMed:2536593,
CC ECO:0000269|PubMed:8352597}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:2172241};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:2172241};
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- PTM: The mature protein may arise from proteolytic cleavage of an in-
CC frame translation of COX1 exons 1 to 4 plus intron 4, containing the
CC aI4 open reading frame. Cleavage would take place close to the Met-299
CC resulting in an active endonuclease of about 30 kDa.
CC {ECO:0000269|PubMed:2172241, ECO:0000269|PubMed:2216759,
CC ECO:0000269|PubMed:8352597}.
CC -!- MISCELLANEOUS: Residues 299 to 556 are sufficient for endonuclease and
CC intron homing activity.
CC -!- SIMILARITY: In the C-terminal section; belongs to the LAGLIDADG
CC endonuclease family. {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the heme-copper
CC respiratory oxidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA24064.1; Type=Erroneous gene model prediction; Note=COX1 was not predicted to be expressed alternatively as a fusion with intron 4.; Evidence={ECO:0000305};
CC Sequence=CAA24070.1; Type=Erroneous gene model prediction; Note=COX1 was not predicted to be expressed alternatively as a fusion with intron 4.; Evidence={ECO:0000305};
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DR EMBL; V00694; CAA24070.1; ALT_SEQ; Genomic_DNA.
DR EMBL; V00694; CAA24064.1; ALT_SEQ; Genomic_DNA.
DR EMBL; KP263414; AIZ98883.1; -; Genomic_DNA.
DR EMBL; V00703; CAA24076.1; -; Genomic_DNA.
DR EMBL; S76641; AAB21126.1; -; Genomic_DNA.
DR PIR; S26762; S26762.
DR PIR; S78649; QXBY34.
DR RefSeq; NP_009307.2; NC_001224.1.
DR AlphaFoldDB; P03878; -.
DR SMR; P03878; -.
DR BioGRID; 34788; 2.
DR STRING; 4932.Q0065; -.
DR REBASE; 2616; I-SceII.
DR MaxQB; P03878; -.
DR PaxDb; P03878; -.
DR PRIDE; P03878; -.
DR EnsemblFungi; Q0065_mRNA; Q0065; Q0065.
DR GeneID; 854596; -.
DR KEGG; sce:Q0065; -.
DR SGD; S000007264; AI4.
DR VEuPathDB; FungiDB:Q0065; -.
DR eggNOG; KOG4769; Eukaryota.
DR GeneTree; ENSGT00390000001518; -.
DR HOGENOM; CLU_490203_0_0_1; -.
DR InParanoid; P03878; -.
DR BioCyc; YEAST:G3O-34375-MON; -.
DR PRO; PR:P03878; -.
DR Proteomes; UP000002311; Mitochondrion.
DR RNAct; P03878; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; TAS:SGD.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IDA:SGD.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central.
DR GO; GO:0006314; P:intron homing; IMP:SGD.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0022904; P:respiratory electron transport chain; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; IDA:SGD.
DR Gene3D; 1.20.210.10; -; 1.
DR Gene3D; 3.10.28.10; -; 2.
DR InterPro; IPR023616; Cyt_c_oxase-like_su1_dom.
DR InterPro; IPR036927; Cyt_c_oxase-like_su1_sf.
DR InterPro; IPR000883; Cyt_C_Oxase_1.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR004860; LAGLIDADG_2.
DR PANTHER; PTHR10422; PTHR10422; 1.
DR Pfam; PF00115; COX1; 1.
DR Pfam; PF00961; LAGLIDADG_1; 2.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF55608; SSF55608; 2.
DR SUPFAM; SSF81442; SSF81442; 1.
DR PROSITE; PS50855; COX1; 1.
PE 1: Evidence at protein level;
KW Endonuclease; Hydrolase; Intron homing; Mitochondrion; mRNA processing;
KW mRNA splicing; Nuclease; Reference proteome.
FT CHAIN 1..?
FT /note="Truncated non-functional cytochrome oxidase 1"
FT /id="PRO_0000013489"
FT CHAIN ?..556
FT /note="DNA endonuclease aI4"
FT /id="PRO_0000013490"
FT REGION 1..240
FT /note="COX1 exons 1 to 4 encoded"
FT REGION 241..556
FT /note="COX1 intron 4 encoded"
FT VARIANT 457..458
FT /note="IS -> KT (in strain: D273-10B)"
FT MUTAGEN 362
FT /note="E->K: Confers mRNA maturase activity."
FT /evidence="ECO:0000269|PubMed:6285204"
FT CONFLICT 57
FT /note="Missing (in Ref. 1; CAA24070)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="F -> CT (in Ref. 1; CAA24070)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="S -> A (in Ref. 1; CAA24070)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="M -> I (in Ref. 5; AAB21126)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="M -> I (in Ref. 5; AAB21126)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 556 AA; 63311 MW; 4F1D968F23DABA7A CRC64;
MVQRWLYSTN AKDIAVLYFM LAIFSGMAGT AMSLIIRLEL AAPGSQYLHG NSQLFNVLVV
GHAVLMIFFL VMPALIGGFG NYLLPLMIGA TDTAFPRINN IAFWVLPMGL VCLVTSTLVE
SGAGTGWTVY PPLSSIQAHS GPSVDLAIFA LHLTSISSLL GAINFIVTTL NMRTNGMTMH
KLPLFVWSIF ITAFLLLLSL PVLSAGITML LLDRNFNTSF FEVSGGGDPI LYEHLFWFFG
QTVATIIMLM MYNDMHFSKC WKLLKKWITN IMSTLFKALF VKMFMSYNNQ QDKMMNNTML
KKDNIKRSSE TTRKMLNNSM NKKFNQWLAG LIDGDGYFGI VSKKYVSLEI TVALEDEMAL
KEIQNKFGGS IKLRSGVKAI RYRLTNKTGM IKLINAVNGN IRNTKRLVQF NKVCILLGID
FIYPIKLTKD NSWFVGFFDA DGTINYSFKN NHPQLTISVT NKYLQDVQEY KNILGGNIYF
DKSQNGYYKW SIQSKDMVLN FINDYIKMNP SRTTKMNKLY LSKEFYNLKE LKAYNKSSDS
MQYKAWLNFE NKWKNK
