EME1_CANGA
ID EME1_CANGA Reviewed; 580 AA.
AC Q6FM02;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Crossover junction endonuclease EME1;
DE EC=3.1.22.-;
GN Name=EME1; OrderedLocusNames=CAGL0K12122g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Interacts with MUS81 to form a DNA structure-specific
CC endonuclease with substrate preference for branched DNA structures with
CC a 5'-end at the branch nick. Typical substrates include 3'-flap
CC structures, D-loops, replication forks and nicked Holliday junctions.
CC May be required in mitosis for the processing of stalled or collapsed
CC replication fork intermediates. May be required in meiosis for the
CC repair of meiosis-specific double strand breaks subsequent to single-
CC end invasion (SEI) (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Interacts with MUS81. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the EME1/MMS4 family. {ECO:0000305}.
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DR EMBL; CR380957; CAG61705.1; -; Genomic_DNA.
DR RefSeq; XP_448742.1; XM_448742.1.
DR AlphaFoldDB; Q6FM02; -.
DR STRING; 5478.XP_448742.1; -.
DR PRIDE; Q6FM02; -.
DR EnsemblFungi; CAG61705; CAG61705; CAGL0K12122g.
DR GeneID; 2889970; -.
DR KEGG; cgr:CAGL0K12122g; -.
DR CGD; CAL0134259; CAGL0K12122g.
DR VEuPathDB; FungiDB:CAGL0K12122g; -.
DR eggNOG; ENOG502RY0Q; Eukaryota.
DR HOGENOM; CLU_023637_0_0_1; -.
DR InParanoid; Q6FM02; -.
DR Proteomes; UP000002428; Chromosome K.
DR GO; GO:0048476; C:Holliday junction resolvase complex; IEA:EnsemblFungi.
DR GO; GO:0043596; C:nuclear replication fork; IEA:EnsemblFungi.
DR GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IEA:EnsemblFungi.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:EnsemblFungi.
DR GO; GO:0010520; P:regulation of reciprocal meiotic recombination; IEA:EnsemblFungi.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IEA:EnsemblFungi.
DR InterPro; IPR006166; ERCC4_domain.
DR Pfam; PF02732; ERCC4; 1.
DR SMART; SM00891; ERCC4; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA recombination; DNA repair; Endonuclease; Hydrolase;
KW Magnesium; Meiosis; Metal-binding; Nuclease; Nucleus; Reference proteome.
FT CHAIN 1..580
FT /note="Crossover junction endonuclease EME1"
FT /id="PRO_0000223634"
FT REGION 53..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 580 AA; 66736 MW; A845A4BB60C58227 CRC64;
MPTTPVIEIL DDSSLLDDSL IEEIISDNND NVIHPTEIDE SIEISIPYVN DKTAESNSTS
LGNSQKESSL IVTQTASQRK RILDEILSDD LSISTDDFSL DAIPKQTSGR TRDSQKNDSA
LYESSQEKAS IASSPNRLIK KSSSERHKKS QSIDSKDICI KSPTRKINLG VTESMQTDVL
FEDNNFNNIE CTQETDLSFS TATADTPTVG FKEITFKHKE STNEGLNSHN FSDSIFERQR
LKQYITNIRD ITETESQELY NKLIHTEKGL FNAVNQTPRD NFKAREDIIV DFSPSLLSFL
DKQTEILKSI LAPATIQKSI HDELPRIRFF RKCHSFYDLQ HDFFFPSNYK IVEENTTILY
FDSKEFFVKY KEDKRSLFEK LKEIERDNYE IILVLYDLAK FKRELEKIEE TKYRSRVQSQ
IYDSQQSIQQ NKVTTPQSDY GLKKFDVEQR LRYINREWGL KIHIVNSHND FVHSLPNLCS
IIGKQRMDPA IRYMRYAHLN VKSASDRKDT LKKTINEIGK VPDIKASAIS DIYSSFQSLL
HDFEAGSLKA SSDGNYLMSE ALEKRLHKIF TSTDPNEAVD