CCE1_SCHPO
ID CCE1_SCHPO Reviewed; 258 AA.
AC Q10423;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Cruciform cutting endonuclease 1, mitochondrial;
DE EC=3.1.21.10 {ECO:0000269|PubMed:9343409};
DE AltName: Full=Protein ydc2;
DE Flags: Precursor;
GN Name=cce1; Synonyms=ydc2; ORFNames=SPAC25G10.02;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBUNIT.
RX PubMed=9343409; DOI=10.1128/mcb.17.11.6465;
RA White M.F., Lilley D.M.J.;
RT "Characterization of a Holliday junction-resolving enzyme from
RT Schizosaccharomyces pombe.";
RL Mol. Cell. Biol. 17:6465-6471(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP GENE NAME, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10954073; DOI=10.1007/s004380000256;
RA Doe C.L., Osman F., Dixon J., Whitby M.C.;
RT "The Holliday junction resolvase SpCCE1 prevents mitochondrial DNA
RT aggregation in Schizosaccharomyces pombe.";
RL Mol. Gen. Genet. 263:889-897(2000).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=11726496; DOI=10.1093/emboj/20.23.6601;
RA Ceschini S., Keeley A., McAlister M.S.B., Oram M., Phelan J., Pearl L.H.,
RA Tsaneva I.R., Barrett T.E.;
RT "Crystal structure of the fission yeast mitochondrial Holliday junction
RT resolvase Ydc2.";
RL EMBO J. 20:6601-6611(2001).
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' and 5'-TT-3' sequences. {ECO:0000269|PubMed:10954073,
CC ECO:0000269|PubMed:9343409}.
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:9343409};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9343409}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10954073}.
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DR EMBL; CU329670; CAA94631.1; -; Genomic_DNA.
DR PIR; T38373; T38373.
DR RefSeq; NP_594522.1; NM_001019951.2.
DR PDB; 1KCF; X-ray; 2.30 A; A/B=1-258.
DR PDBsum; 1KCF; -.
DR AlphaFoldDB; Q10423; -.
DR SMR; Q10423; -.
DR BioGRID; 279186; 16.
DR STRING; 4896.SPAC25G10.02.1; -.
DR PaxDb; Q10423; -.
DR EnsemblFungi; SPAC25G10.02.1; SPAC25G10.02.1:pep; SPAC25G10.02.
DR GeneID; 2542736; -.
DR KEGG; spo:SPAC25G10.02; -.
DR PomBase; SPAC25G10.02; cce1.
DR VEuPathDB; FungiDB:SPAC25G10.02; -.
DR eggNOG; ENOG502S4DK; Eukaryota.
DR HOGENOM; CLU_1042654_0_0_1; -.
DR InParanoid; Q10423; -.
DR OMA; MAITWIE; -.
DR PhylomeDB; Q10423; -.
DR EvolutionaryTrace; Q10423; -.
DR PRO; PR:Q10423; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0000262; C:mitochondrial chromosome; IC:PomBase.
DR GO; GO:0005739; C:mitochondrion; IDA:PomBase.
DR GO; GO:0000402; F:crossed form four-way junction DNA binding; IDA:PomBase.
DR GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IDA:PomBase.
DR GO; GO:0004520; F:endodeoxyribonuclease activity; IBA:GO_Central.
DR GO; GO:0070336; F:flap-structured DNA binding; IDA:PomBase.
DR GO; GO:0000400; F:four-way junction DNA binding; IDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000403; F:Y-form DNA binding; IDA:PomBase.
DR GO; GO:0032042; P:mitochondrial DNA metabolic process; IMP:PomBase.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IMP:PomBase.
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; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR015242; Ydc2_cat.
DR PANTHER; PTHR28072; PTHR28072; 2.
DR Pfam; PF09159; Ydc2-catalyt; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR PROSITE; PS50800; SAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endonuclease; Hydrolase; Magnesium; Metal-binding;
KW Mitochondrion; Nuclease; Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..258
FT /note="Cruciform cutting endonuclease 1, mitochondrial"
FT /id="PRO_0000020865"
FT DOMAIN 1..35
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT BINDING 46
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT HELIX 6..15
FT /evidence="ECO:0007829|PDB:1KCF"
FT HELIX 26..33
FT /evidence="ECO:0007829|PDB:1KCF"
FT STRAND 40..47
FT /evidence="ECO:0007829|PDB:1KCF"
FT STRAND 52..59
FT /evidence="ECO:0007829|PDB:1KCF"
FT STRAND 65..73
FT /evidence="ECO:0007829|PDB:1KCF"
FT HELIX 91..109
FT /evidence="ECO:0007829|PDB:1KCF"
FT STRAND 112..118
FT /evidence="ECO:0007829|PDB:1KCF"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:1KCF"
FT HELIX 128..151
FT /evidence="ECO:0007829|PDB:1KCF"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:1KCF"
FT HELIX 168..179
FT /evidence="ECO:0007829|PDB:1KCF"
FT HELIX 191..200
FT /evidence="ECO:0007829|PDB:1KCF"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:1KCF"
FT HELIX 209..217
FT /evidence="ECO:0007829|PDB:1KCF"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:1KCF"
FT HELIX 224..253
FT /evidence="ECO:0007829|PDB:1KCF"
SQ SEQUENCE 258 AA; 30206 MW; 5661166AEB7C6C7A CRC64;
MATVKLSFLQ HICKLTGLSR SGRKDELLRR IVDSPIYPTS RVLGIDLGIK NFSYCFASQN
EDSKVIIHNW SVENLTEKNG LDIQWTEDFQ PSSMADLSIQ LFNTLHEKFN PHVILMERQR
YRSGIATIPE WTLRVNMLES MLYALHYAEK RNSIEQKIQY PFLLSLSPKS TYSYWASVLN
TKASFSKKKS RVQMVKELID GQKILFENEE ALYKWNNGSR VEFKKDDMAD SALIASGWMR
WQAQLKHYRN FCKQFLKQ
