CCE1_YEAST
ID CCE1_YEAST Reviewed; 353 AA.
AC Q03702; D6VXS5;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Cruciform cutting endonuclease 1, mitochondrial;
DE EC=3.1.21.10 {ECO:0000269|PubMed:8609627};
DE Flags: Precursor;
GN Name=CCE1; OrderedLocusNames=YKL011C; ORFNames=YKL164;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1537343; DOI=10.1002/j.1460-2075.1992.tb05102.x;
RA Kleff S., Kemper B., Sternglanz R.;
RT "Identification and characterization of yeast mutants and the gene for a
RT cruciform cutting endonuclease.";
RL EMBO J. 11:699-704(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP AND SUBUNIT.
RX PubMed=8609627; DOI=10.1006/jmbi.1996.0166;
RA White M.F., Lilley D.M.;
RT "The structure-selectivity and sequence-preference of the junction-
RT resolving enzyme CCE1 of Saccharomyces cerevisiae.";
RL J. Mol. Biol. 257:330-341(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1481574; DOI=10.1002/yea.320081109;
RA Pascolo S., Ghazvini M., Boyer J., Colleaux L., Thierry A., Dujon B.;
RT "The sequence of a 9.3 kb segment located on the left arm of the yeast
RT chromosome XI reveals five open reading frames including the CCE1 gene and
RT putative products related to MYO2 and to the ribosomal protein L10.";
RL Yeast 8:987-995(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
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 MUTAGENESIS, AND MAGNESIUM-BINDING SITES.
RX PubMed=10825168; DOI=10.1074/jbc.m002612200;
RA Wardleworth B.N., Kvaratskhelia M., White M.F.;
RT "Site-directed mutagenesis of the yeast resolving enzyme Cce1 reveals
RT catalytic residues and relationship with the intron-splicing factor Mrs1.";
RL J. Biol. Chem. 275:23725-23728(2000).
CC -!- FUNCTION: Capable of resolving Holliday junctions. Specific for 4-way
CC junctions. Seems to be important for the maintenance of mitochondrial
CC DNA. Cleaves fixed junctions at the point of strand exchange. Cleaves
CC after 5'-CT-3' sequence. {ECO:0000269|PubMed:8609627}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage at a junction such as a reciprocal
CC single-stranded crossover between two homologous DNA duplexes
CC (Holliday junction).; EC=3.1.21.10;
CC Evidence={ECO:0000269|PubMed:8609627};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:8609627};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8609627}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M65275; AAB02883.1; -; Genomic_DNA.
DR EMBL; S53418; AAB24906.1; -; Genomic_DNA.
DR EMBL; Z28011; CAA81846.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09145.1; -; Genomic_DNA.
DR PIR; S19635; S19635.
DR RefSeq; NP_012914.1; NM_001179577.1.
DR AlphaFoldDB; Q03702; -.
DR SMR; Q03702; -.
DR BioGRID; 34121; 113.
DR DIP; DIP-3918N; -.
DR IntAct; Q03702; 5.
DR STRING; 4932.YKL011C; -.
DR MaxQB; Q03702; -.
DR PaxDb; Q03702; -.
DR PRIDE; Q03702; -.
DR EnsemblFungi; YKL011C_mRNA; YKL011C; YKL011C.
DR GeneID; 853858; -.
DR KEGG; sce:YKL011C; -.
DR SGD; S000001494; CCE1.
DR VEuPathDB; FungiDB:YKL011C; -.
DR eggNOG; ENOG502S4DK; Eukaryota.
DR GeneTree; ENSGT00940000176739; -.
DR HOGENOM; CLU_055501_0_0_1; -.
DR InParanoid; Q03702; -.
DR OMA; DTGISNF; -.
DR BioCyc; YEAST:G3O-31820-MON; -.
DR PRO; PR:Q03702; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; Q03702; protein.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0000402; F:crossed form four-way junction DNA binding; IBA:GO_Central.
DR GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0004520; F:endodeoxyribonuclease activity; IDA:SGD.
DR GO; GO:0070336; F:flap-structured DNA binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000403; F:Y-form DNA binding; IBA:GO_Central.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IGI:SGD.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR039197; Mrs1/Cce1.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR015242; Ydc2_cat.
DR PANTHER; PTHR28072; PTHR28072; 1.
DR Pfam; PF09159; Ydc2-catalyt; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
PE 1: Evidence at protein level;
KW Endonuclease; Hydrolase; Magnesium; Metal-binding; Mitochondrion; Nuclease;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..353
FT /note="Cruciform cutting endonuclease 1, mitochondrial"
FT /id="PRO_0000020866"
FT BINDING 293
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 294
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT MUTAGEN 79
FT /note="F->A: >200-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:10825168"
FT MUTAGEN 145
FT /note="E->Q: >200-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:10825168"
FT MUTAGEN 146
FT /note="R->A: 100-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:10825168"
FT MUTAGEN 147
FT /note="Q->A: 70-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:10825168"
FT MUTAGEN 150
FT /note="R->A: 4-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:10825168"
FT MUTAGEN 231
FT /note="R->A: >200-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:10825168"
FT MUTAGEN 231
FT /note="R->K: 47-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:10825168"
FT MUTAGEN 291
FT /note="K->A,R: >200-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:10825168"
FT MUTAGEN 292
FT /note="D->N: 80-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:10825168"
FT MUTAGEN 293
FT /note="D->N: >200-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:10825168"
FT MUTAGEN 294
FT /note="D->N: >200-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:10825168"
SQ SEQUENCE 353 AA; 41000 MW; 5ECC6849A67A626C CRC64;
MSTAQKAKIL QLIDSCCQNA KSTQLKSLSF VIGAVNGTTK EAKRTYIQEQ CEFLEKLRQQ
KIREGRINIL SMDAGVSNFA FSKMQLLNND PLPKVLDWQK INLEEKFFQN LKKLSLNPAE
TSELVFNLTE YLFESMPIPD MFTIERQRTR TMSSRHILDP ILKVNILEQI LFSNLENKMK
YTNKIPNTSK LRYMVCSSDP HRMTSYWCIP REETPTSSKK LKSNKHSKDS RIKLVKKILS
TSILEGNSTS STKLVEFIGV WNNRIRNALT KKKSFKLCDI LEIQDNSGVR KDDDLADSFL
HCLSWMEWLK NYESITELLN SKTLVKTQFG QVFEFCENKV QKLKFLQNTY NND
