ID   EME1B_ARATH             Reviewed;         551 AA.
AC   C5H8J1; Q9SIF0;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Crossover junction endonuclease EME1B;
DE            EC=3.1.22.-;
DE   AltName: Full=Essential meiotic endonuclease 1B;
DE            Short=AtEME1B;
GN   Name=EME1B; OrderedLocusNames=At2g22140; ORFNames=T26C19.20;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH MUS81.
RC   STRAIN=cv. Columbia;
RX   PubMed=19339504; DOI=10.1104/pp.109.136846;
RA   Geuting V., Kobbe D., Hartung F., Duerr J., Focke M., Puchta H.;
RT   "Two distinct MUS81-EME1 complexes from Arabidopsis process Holliday
RT   junctions.";
RL   Plant Physiol. 150:1062-1071(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
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, nicked Holliday junctions and
CC       also intact Holliday junctions with a reduced efficiency. May be
CC       required in mitosis for the processing of stalled or collapsed
CC       replication fork intermediates. Plays a role in DNA repair and in
CC       genotoxic stress-induced homologous recombination (HR) in somatic
CC       cells. Mediates a subset of meiotic recombination events that are
CC       insensitive to crossover interference. {ECO:0000269|PubMed:19339504}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305};
CC   -!- SUBUNIT: Forms a heterodimer with MUS81.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the EME1/MMS4 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD23625.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; FJ161970; ACN24999.1; -; mRNA.
DR   EMBL; AC007168; AAD23625.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC07270.1; -; Genomic_DNA.
DR   PIR; D84609; D84609.
DR   RefSeq; NP_179804.5; NM_127782.6.
DR   AlphaFoldDB; C5H8J1; -.
DR   SMR; C5H8J1; -.
DR   STRING; 3702.AT2G22140.1; -.
DR   iPTMnet; C5H8J1; -.
DR   PaxDb; C5H8J1; -.
DR   PRIDE; C5H8J1; -.
DR   ProteomicsDB; 224420; -.
DR   EnsemblPlants; AT2G22140.1; AT2G22140.1; AT2G22140.
DR   GeneID; 816748; -.
DR   Gramene; AT2G22140.1; AT2G22140.1; AT2G22140.
DR   KEGG; ath:AT2G22140; -.
DR   Araport; AT2G22140; -.
DR   TAIR; locus:2055961; AT2G22140.
DR   eggNOG; ENOG502QV6A; Eukaryota.
DR   HOGENOM; CLU_022160_1_0_1; -.
DR   InParanoid; C5H8J1; -.
DR   OrthoDB; 525637at2759; -.
DR   PhylomeDB; C5H8J1; -.
DR   PRO; PR:C5H8J1; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; C5H8J1; baseline and differential.
DR   GO; GO:0048476; C:Holliday junction resolvase complex; IEA:InterPro.
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; IDA:TAIR.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IDA:TAIR.
DR   GO; GO:0006281; P:DNA repair; IDA:TAIR.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.150.670; -; 1.
DR   InterPro; IPR042530; EME1/EME2_C.
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   1: Evidence at protein level;
KW   Calcium; Cell cycle; Cell division; Coiled coil; DNA damage;
KW   DNA recombination; DNA repair; Endonuclease; Hydrolase; Magnesium; Meiosis;
KW   Metal-binding; Mitosis; Nuclease; Nucleus; Reference proteome.
FT   CHAIN           1..551
FT                   /note="Crossover junction endonuclease EME1B"
FT                   /id="PRO_0000418428"
FT   DOMAIN          287..484
FT                   /note="ERCC4"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          187..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          203..253
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        35..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..239
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   551 AA;  62193 MW;  278DE488CC21144D CRC64;
     MNDHILISDG EDQTTPLPSL SKRARKYPIS AILISDSDPT PQKQPPESSF TPIFVPETPL
     SDDFSVVKCS FGSRALASNR EDKFSGKRII SLDSEFEDSP RPETSKKNES VLAGLREPRF
     GLEAETSEAY YKNTRIPETN LDDDTSWMHE VSFRSSPTND TIEVVSDQEK EDISVEKIGR
     KKKIRTTTLP VPGEALPKKR QSKEDKTSAM EEKKLRKEQE RLEKAASKAE EAERKRLEKE
     KKKWEKGKLA LKSIVAEIDT KVLEGSIGGL LLSRFSEKGI TIHVGPNPIE RSIVWTMTIP
     EDIAPLFPQG PKIPYLLLVY DAEEFCNLVA NGKFLEIISR VQDRYPSYTV CCLTNKLMSY
     VKKREKEEYK NPGNWRRPPI DEVLAKLTTH YVKVHSRHCV DEAEVAEHIV GLTSSLASCQ
     FRKKLTMLSV SANGALVSKD SVDKHLIKKS PWLKALVAIP KVQPRYALAV WKKYPSMKSL
     LKVYMDRNKS VHEKEFLLKD LKVEGLVGGD IRLGEICSKR IYRVLMSHDG AIKTDDVENG
     AAFFTDSPGV N