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EME1A_ARATH
ID   EME1A_ARATH             Reviewed;         546 AA.
AC   Q84M98; C5IHG3; Q9SJ19;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Crossover junction endonuclease EME1A;
DE            EC=3.1.22.-;
DE   AltName: Full=Essential meiotic endonuclease 1A;
DE            Short=AtEME1A;
GN   Name=EME1A; OrderedLocusNames=At2g21800; ORFNames=F7D8.12;
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] (ISOFORM 2), FUNCTION, AND INTERACTION WITH
RP   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).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q84M98-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q84M98-2; Sequence=VSP_044051;
CC   -!- SIMILARITY: Belongs to the EME1/MMS4 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD20399.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; FJ936556; ACR43775.1; -; mRNA.
DR   EMBL; AC007019; AAD20399.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC07223.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07224.1; -; Genomic_DNA.
DR   EMBL; BT006456; AAP21264.1; -; mRNA.
DR   EMBL; AK228007; BAE99972.1; -; mRNA.
DR   PIR; C84605; C84605.
DR   RefSeq; NP_001189572.1; NM_001202643.1. [Q84M98-2]
DR   RefSeq; NP_179771.2; NM_127749.5. [Q84M98-1]
DR   AlphaFoldDB; Q84M98; -.
DR   SMR; Q84M98; -.
DR   STRING; 3702.AT2G21800.2; -.
DR   iPTMnet; Q84M98; -.
DR   PaxDb; Q84M98; -.
DR   PRIDE; Q84M98; -.
DR   ProteomicsDB; 220496; -. [Q84M98-1]
DR   EnsemblPlants; AT2G21800.1; AT2G21800.1; AT2G21800. [Q84M98-1]
DR   EnsemblPlants; AT2G21800.2; AT2G21800.2; AT2G21800. [Q84M98-2]
DR   GeneID; 816716; -.
DR   Gramene; AT2G21800.1; AT2G21800.1; AT2G21800. [Q84M98-1]
DR   Gramene; AT2G21800.2; AT2G21800.2; AT2G21800. [Q84M98-2]
DR   KEGG; ath:AT2G21800; -.
DR   Araport; AT2G21800; -.
DR   TAIR; locus:2052484; AT2G21800.
DR   eggNOG; ENOG502SDU4; Eukaryota.
DR   InParanoid; Q84M98; -.
DR   OrthoDB; 525637at2759; -.
DR   PhylomeDB; Q84M98; -.
DR   PRO; PR:Q84M98; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q84M98; baseline and differential.
DR   Genevisible; Q84M98; AT.
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   Alternative splicing; Calcium; Cell cycle; Cell division; Coiled coil;
KW   DNA damage; DNA recombination; DNA repair; Endonuclease; Hydrolase;
KW   Magnesium; Meiosis; Metal-binding; Mitosis; Nuclease; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..546
FT                   /note="Crossover junction endonuclease EME1A"
FT                   /id="PRO_0000418427"
FT   DOMAIN          278..478
FT                   /note="ERCC4"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          88..232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          188..245
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        14..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..115
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..149
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..172
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..232
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         259
FT                   /note="G -> GVIT (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:19339504"
FT                   /id="VSP_044051"
SQ   SEQUENCE   546 AA;  61239 MW;  4A586F27AE951311 CRC64;
     MSDFILISDG EDEATPPPSK RARKNRTPTD LNLDTEPSLQ KQPPGSASTP FFLDETPLSD
     DVTVLKSSFG SGTGASSGRE NNFFGKRVIS LESDSEDSPG PESSKKYEPV YTDSWKKPCR
     LEFGSSDANS DDDPSWMRRA SFQSSLSKDA IEVDSDHEKE DTGVEKMGRK KQTITSKSTS
     LSADSLPKKK MSKDEKTRAA EEKKLQKEQE KLQKAASKAE DAEHKKLERE KQKWAKEKDK
     ALKCIVAWID NKVLEGSFGG LLISGLKEKC ITYHVTTNPI QRSIVWTMTL PEDIAQSLPL
     GSKIPYVLLL YEAEDFCNLV AKKELLENVY RVRDEYPSYT MCYLTNKLLS YVNKKERVEY
     KDPVNGCGWR KPPIDEAIAK LSTHYIGVHS RHCVDEAEVA DHVVRLTSSL AHCQVRKKLT
     RLSVYADGTL MSKNAADKHL IRESIWLKVL VAIPKVQPRY AIAVSKKYPS LKSLLKVYMD
     PNISVHEKEF LLKDLKVENL VGRDTSVGEA CSKRIYRVLM SLDGTIKTDD VENGAASFTL
     PPSDLI
 
 
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