SCE4_YEAST
ID SCE4_YEAST Reviewed; 630 AA.
AC Q9ZZX1; A0A0A7NYD1; Q8W770;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Intron-encoded DNA endonuclease aI5 alpha;
DE AltName: Full=DNA endonuclease I-SceIV;
DE Contains:
DE RecName: Full=Truncated non-functional cytochrome oxidase 1;
DE Contains:
DE RecName: Full=DNA endonuclease aI5 alpha;
DE EC=3.1.-.-;
DE AltName: Full=Intron-encoded endonuclease I-SceIV;
DE Flags: Precursor;
GN Name=AI5_ALPHA; Synonyms=I-SCEIV {ECO:0000303|PubMed:9675098};
GN OrderedLocusNames=Q0070;
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 FUNCTION, CLEAVAGE SITE SPECIFICITY, ENDONUCLEASE ACTIVITY, AND INTRON
RP HOMING.
RX PubMed=1314207; DOI=10.1016/0378-1119(92)90663-a;
RA Seraphin B., Faye G., Hatat D., Jacq C.;
RT "The yeast mitochondrial intron aI5 alpha: associated endonuclease activity
RT and in vivo mobility.";
RL Gene 113:1-8(1992).
RN [4]
RP FUNCTION, COFACTOR, CLEAVAGE SITE SPECIFICITY, ENDONUCLEASE ACTIVITY, PH
RP OPTIMUM, AND SUBUNIT.
RX PubMed=9675098; DOI=10.1006/bbrc.1998.8921;
RA Wernette C.M.;
RT "Structure and activity of the mitochondrial intron-encoded endonuclease,
RT I-SceIV.";
RL Biochem. Biophys. Res. Commun. 248:127-133(1998).
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 limited specificity and cleaves the sequence 5'-
CC ATCTTCTCTTGATTAGCCCTGATCTACGG-3' after the nucleotide sequence ATTA
CC leaving a four-base overhang and a 3'-OH.
CC {ECO:0000250|UniProtKB:P03878, ECO:0000269|PubMed:1314207,
CC ECO:0000269|PubMed:9675098}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:9675098};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 9.5. {ECO:0000269|PubMed:9675098};
CC -!- SUBUNIT: Heterodimer of a 32 kDa catalytic subunit and a larger 60 kDa
CC polypeptide subunit. {ECO:0000269|PubMed:9675098}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}. Membrane
CC {ECO:0000255, ECO:0000305}; Multi-pass membrane protein {ECO:0000255,
CC 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
CC aI5_alpha open reading frame. {ECO:0000269|PubMed:1314207,
CC ECO:0000269|PubMed:9675098}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the heme-copper
CC respiratory oxidase family. {ECO:0000255}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the LAGLIDADG
CC endonuclease family. {ECO:0000255}.
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DR EMBL; KP263414; AIZ98882.1; -; Genomic_DNA.
DR PIR; S78650; S78650.
DR RefSeq; NP_009306.1; NC_001224.1.
DR AlphaFoldDB; Q9ZZX1; -.
DR SMR; Q9ZZX1; -.
DR BioGRID; 34789; 2.
DR STRING; 4932.Q0070; -.
DR PaxDb; Q9ZZX1; -.
DR PRIDE; Q9ZZX1; -.
DR EnsemblFungi; Q0070_mRNA; Q0070; Q0070.
DR GeneID; 854597; -.
DR KEGG; sce:Q0070; -.
DR SGD; S000007265; AI5_ALPHA.
DR VEuPathDB; FungiDB:Q0070; -.
DR eggNOG; KOG4769; Eukaryota.
DR GeneTree; ENSGT00390000001518; -.
DR HOGENOM; CLU_434271_0_0_1; -.
DR InParanoid; Q9ZZX1; -.
DR BioCyc; YEAST:G3O-34376-MON; -.
DR PRO; PR:Q9ZZX1; -.
DR Proteomes; UP000002311; Mitochondrion.
DR RNAct; Q9ZZX1; 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; IMP: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:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR GO; GO:0006316; P:movement of group I intron; IMP:SGD.
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; IPR023615; Cyt_c_Oxase_su1_BS.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR004860; LAGLIDADG_2.
DR PANTHER; PTHR10422; PTHR10422; 1.
DR Pfam; PF00115; COX1; 1.
DR Pfam; PF03161; LAGLIDADG_2; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF55608; SSF55608; 1.
DR SUPFAM; SSF81442; SSF81442; 1.
DR PROSITE; PS50855; COX1; 1.
DR PROSITE; PS00077; COX1_CUB; 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_0000270983"
FT CHAIN ?..630
FT /note="DNA endonuclease aI5 alpha"
FT /id="PRO_0000270984"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 464..483
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..324
FT /note="COX1 exons encoded"
FT /evidence="ECO:0000255"
FT REGION 325..630
FT /note="COX1 intron aI5_alpha encoded"
SQ SEQUENCE 630 AA; 72165 MW; 6EA9AA02CD2A6C16 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
HPEVYILIIP GFGIISHVVS TYSKKPVFGE ISMVYAMASI GLLGFLVWSH HMYIVGLDAD
TRAYFTSATM IIAIPTGIKI FSWLMNPFSK DKNKNKNKKL IRNYQKMNNN NMMKTYLNNN
NMIMMNMYKG NLYDIYPRSN RNYIQPNNIN KELVVYGYNL ESCVGMPTYT NIVKHMVGIP
NNILYIMTGI LLTDGWIDYT SKKDLDKKTI MEINCRFRLK QSMIHSEYLM YVFMLLSHYC
MSYPKMKIAK VKGKSYNQLE FYTRSLPCFT ILRYMFYNGR VKIVPNNLYD LLNYESLAHM
IMCDGSFVKG GGLYLNLQSF TTKELIFIMN ILKIKFNLNC TLHKSRNKYT IYMRVESVKR
LFPMIYKYIL PSMRYKFDIM LWQKKYNMIN
