EME1_ASHGO
ID EME1_ASHGO Reviewed; 714 AA.
AC Q75B88;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Crossover junction endonuclease EME1;
DE EC=3.1.22.-;
GN Name=EME1; OrderedLocusNames=ADL318C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 359.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016817; AAS51602.2; -; Genomic_DNA.
DR RefSeq; NP_983778.2; NM_209131.2.
DR AlphaFoldDB; Q75B88; -.
DR STRING; 33169.AAS51602; -.
DR EnsemblFungi; AAS51602; AAS51602; AGOS_ADL318C.
DR GeneID; 4619913; -.
DR KEGG; ago:AGOS_ADL318C; -.
DR eggNOG; ENOG502RY0Q; Eukaryota.
DR HOGENOM; CLU_023637_0_0_1; -.
DR InParanoid; Q75B88; -.
DR OMA; ASFANWI; -.
DR Proteomes; UP000000591; Chromosome IV.
DR GO; GO:0048476; C:Holliday junction resolvase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0031297; P:replication fork processing; IBA:GO_Central.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
DR InterPro; IPR006166; ERCC4_domain.
DR InterPro; IPR033310; Mms4/EME1/EME2.
DR PANTHER; PTHR21077; PTHR21077; 1.
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..714
FT /note="Crossover junction endonuclease EME1"
FT /id="PRO_0000223633"
FT REGION 223..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 714 AA; 79362 MW; 0C637D1907D3FF79 CRC64;
MKSIELIDIE SIASDRAGIT REDGVIELLS EADEALGRRP YPSSPTIRST EANIDESIGN
RQLWLQSIEL NGEFQEDDSE EVEETIGKKP DDALVCSDAC SAPDVSIQEL LQTFTPPKPH
AGRVMKAGAG PVRGSSRQTS SKLQTKDVLQ DILVELDDNL SSWDTPSTSG IRSPETVATL
AAKWANKTEK TSGKPLYGRP RSSGNRGNIL LKRTLANRNN ILSSELGGES SPSLQALTTP
LPAKSNDGDK NQTTNVMTTG GFRLGTMEKQ TLNGSACVDR IQQVPVSSPE SVSFLEGLSD
IPISKPVQLT QRCIAATNTG YTKDNCASTP RSAAAVEYLE PIDTDTSILS TAGEALPHSP
VKPSKVSRER SKRDYIVHSK AFTAEESKAK IRQLMSNTAL KKQFNEVNKV TREKQSLLAE
IVLSINEQVH QYLLEQKVPI AEVLGPTTVI HNFESVPIIR FKRKCTSMYD LNNDIYYPCE
TTMCNEPICL LFYNAVDFFT KYKNQKQRLY SEVQDLKRAG NKVIIILNEY SRLEKSLAEL
ENRCMRSRVE QQLTGDKSPR RKTVKEVQLT ALEMNSKDLG RKVNEMIIKC DIDIFPINSA
ASFANWISNL VWVVAKMRYD PMMKNVNWSH INVKIGKTPT EVLSKTLQQI NGVTEIRAGR
VTSTYPSFQQ IFTDFEKGYL VAGKDGNPLM TKVAEKAMNA LLMSEDPEEQ IYIN