SCE3_YEAST
ID SCE3_YEAST Reviewed; 415 AA.
AC P03877; A0A0A7P044; Q35790; Q9ZZX3;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Intron-encoded DNA endonuclease aI3;
DE AltName: Full=DNA endonuclease I-SceIII;
DE Contains:
DE RecName: Full=Truncated non-functional cytochrome oxidase 1;
DE Contains:
DE RecName: Full=DNA endonuclease aI3;
DE EC=3.1.-.-;
DE AltName: Full=Intron-encoded endonuclease I-SceIII;
DE Flags: Precursor;
GN Name=AI3; Synonyms=ENS3, I-SCEIII; OrderedLocusNames=Q0060;
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].
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 [GENOMIC DNA].
RC STRAIN=Capensis / YB4237;
RX PubMed=8112577; DOI=10.1016/0378-1119(94)90516-9;
RA Szczepanek T., Macadre C., Meunier B., Lazowska J.;
RT "Two homologous introns from related Saccharomyces species differ in their
RT mobility.";
RL Gene 139:1-7(1994).
RN [3]
RP ERRATUM OF PUBMED:8112577.
RX DOI=10.1016/0378-1119(94)90224-0;
RA Szczepanek T., Macadre C., Meunier B., Lazowska J.;
RL Gene 144:149-149(1994).
RN [4]
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 [5]
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 [6]
RP FUNCTION, ENDONUCLEASE ACTIVITY, COFACTOR, PH OPTIMUM, AND CLEAVAGE SITE
RP SPECIFICITY.
RX PubMed=8367285; DOI=10.1093/nar/21.16.3683;
RA Schapira M., Desdouets C., Jacq C., Perea J.;
RT "I-Sce III an intron-encoded DNA endonuclease from yeast mitochondria.
RT Asymmetrical DNA binding properties and cleavage reaction.";
RL Nucleic Acids Res. 21:3683-3689(1993).
RN [7]
RP FUNCTION, ENDONUCLEASE ACTIVITY, PROTEOLYTIC CLEAVAGE, AND INTRON HOMING.
RX PubMed=7797552; DOI=10.1074/jbc.270.26.15563;
RA Guo W.-W., Moran J.V., Hoffman P.W., Henke R.M., Butow R.A., Perlman P.S.;
RT "The mobile group I intron 3 alpha of the yeast mitochondrial COXI gene
RT encodes a 35-kDa processed protein that is an endonuclease but not a
RT maturase.";
RL J. Biol. Chem. 270:15563-15570(1995).
CC -!- FUNCTION: Mitochondrial DNA endonuclease involved in intron homing. It
CC introduces a specific double-strand break in the DNA of the COX1 gene
CC and thus mediates the insertion of an intron, containing its own coding
CC sequence (group I intron), into an intronless gene. Recognizes with
CC high specificity and cleaves the sequence 5'-GGTTTTGGTAACTATTTATTAC-3'.
CC {ECO:0000269|PubMed:7797552, ECO:0000269|PubMed:8367285}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:8367285};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:8367285};
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- PTM: The mature protein may arise from proteolytic cleavage of an in-
CC frame translation of some COX1 exons plus the intron containing the aI3
CC open reading frame. {ECO:0000269|PubMed:7797552,
CC ECO:0000269|PubMed:8367285}.
CC -!- MISCELLANEOUS: Strain Capensis / YB4237 has two stop codons in position
CC 276 and 407, which disrupt the gene coding for this protein.
CC Consequently, the corresponding intron containing its coding sequence
CC is not mobile.
CC -!- SIMILARITY: In the C-terminal section; belongs to the LAGLIDADG
CC endonuclease family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA17560.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAA17560.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA24061.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA24062.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; V00694; CAA24062.1; ALT_SEQ; Genomic_DNA.
DR EMBL; V00694; CAA24061.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U00801; AAA17560.1; ALT_SEQ; Unassigned_DNA.
DR EMBL; KP263414; AIZ98884.1; -; Genomic_DNA.
DR PIR; A04510; QXBY33.
DR PIR; S78646; S78646.
DR RefSeq; NP_009308.2; NC_001224.1.
DR AlphaFoldDB; P03877; -.
DR SMR; P03877; -.
DR BioGRID; 34787; 2.
DR STRING; 4932.Q0060; -.
DR PaxDb; P03877; -.
DR PRIDE; P03877; -.
DR EnsemblFungi; Q0060_mRNA; Q0060; Q0060.
DR GeneID; 854595; -.
DR KEGG; sce:Q0060; -.
DR SGD; S000007263; AI3.
DR VEuPathDB; FungiDB:Q0060; -.
DR eggNOG; KOG4769; Eukaryota.
DR HOGENOM; CLU_559205_0_0_1; -.
DR InParanoid; P03877; -.
DR OMA; YIMSAIA; -.
DR BioCyc; YEAST:G3O-34374-MON; -.
DR PRO; PR:P03877; -.
DR Proteomes; UP000002311; Mitochondrion.
DR RNAct; P03877; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IEA:UniProtKB-KW.
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; IEA:UniProtKB-KW.
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; Membrane; Mitochondrion;
KW mRNA processing; mRNA splicing; Nuclease; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..?
FT /note="Truncated non-functional cytochrome oxidase 1"
FT /id="PRO_0000045049"
FT CHAIN ?..415
FT /note="DNA endonuclease aI3"
FT /id="PRO_0000045050"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..81
FT /note="COX1 exons 1 to 3 encoded"
FT REGION 82..415
FT /note="COX1 intron 3 encoded"
FT VARIANT 55
FT /note="F -> Y (in strain: Capensis / YB4237)"
FT VARIANT 60
FT /note="V -> A (in strain: Capensis / YB4237)"
FT VARIANT 71
FT /note="V -> W (in strain: Capensis / YB4237)"
FT VARIANT 76
FT /note="I -> M (in strain: Capensis / YB4237)"
FT VARIANT 399
FT /note="R -> M (in strain: Capensis / YB4237)"
FT CONFLICT 122
FT /note="T -> S (in Ref. 1; CAA24062)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="T -> P (in Ref. 1; CAA24062)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="E -> G (in Ref. 1; CAA24062)"
FT /evidence="ECO:0000305"
FT CONFLICT 217..218
FT /note="TI -> NQ (in Ref. 1; CAA24062)"
FT /evidence="ECO:0000305"
FT CONFLICT 247..248
FT /note="GM -> IL (in Ref. 1; CAA24062)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="A -> T (in Ref. 1; CAA24062)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="N -> I (in Ref. 1; CAA24062)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="K -> N (in Ref. 1; CAA24062)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 415 AA; 47917 MW; D86BD856933C8548 CRC64;
MVQRWLYSTN AKDIAVLYFM LAIFSGMAGT AMSLIIRLEL AAPGSQYLHG NSQLFNVLVV
GHAVLMIFFL VMPALIGGFG NQKRYESNNN NNQVMENKEY NLKLNYDKLG PYLAGLIEGD
GTITVQNSSS MKKSKYRPLI VVVFKLEDLE LANYLCNLTK CGKVYKKINR NYVLWTIHDL
KGVYTLLNII NGYMRTPKYE AFVRGAEFMN NYINSTTITH NKLKNMDNIK IKPLDTSDIG
SNAWLAGMTD ADGNFSINLM NGKNRSSRAM PYYCLELRQN YQKNSNNNNI NFSYFYIMSA
IATYFNVNLY SRERNLNLLV STNNTYKTYY SYKVMVANTY KNIKVMEYFN KYSLLSSKHL
DFLDWSKLVI LINNEGQSMK TNGSWELGMN LRKDYNKTRT TFTWSHLKNT YLENK
