MOC1_ARATH
ID MOC1_ARATH Reviewed; 273 AA.
AC Q8GWA2; O81023;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Holliday junction resolvase MOC1, chloroplastic {ECO:0000305};
DE EC=3.1.21.10 {ECO:0000305};
DE AltName: Full=Protein MONOKARYOTIC CHLOROPLAST 1 {ECO:0000303|PubMed:28495749};
DE Short=AtMOC1 {ECO:0000303|PubMed:28495749};
DE Flags: Precursor;
GN Name=MOC1; OrderedLocusNames=At2g26840 {ECO:0000312|Araport:AT2G26840};
GN ORFNames=F12C20.12 {ECO:0000312|EMBL:AAC32241.1};
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY,
RP COFACTOR, DNA-BINDING, AND MUTAGENESIS OF ASP-88; GLU-152; ASP-230 AND
RP GLU-235.
RX PubMed=28495749; DOI=10.1126/science.aan0038;
RA Kobayashi Y., Misumi O., Odahara M., Ishibashi K., Hirono M., Hidaka K.,
RA Endo M., Sugiyama H., Iwasaki H., Kuroiwa T., Shikanai T., Nishimura Y.;
RT "Holliday junction resolvases mediate chloroplast nucleoid segregation.";
RL Science 356:631-634(2017).
CC -!- FUNCTION: A structure-specific endonuclease that resolves Holliday
CC junction (HJ) intermediates during genetic recombination. Cleaves 4-way
CC DNA junctions introducing paired nicks in opposing strands, leaving a
CC 5'-terminal phosphate and a 3'-terminal hydroxyl group that are ligated
CC to produce recombinant products. Mediates chloroplast nucleoid
CC segregation during chloroplast division. {ECO:0000269|PubMed:28495749}.
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; Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:28495749};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:28495749};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma, chloroplast nucleoid
CC {ECO:0000269|PubMed:28495749}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. {ECO:0000305};
CC Name=1;
CC IsoId=Q8GWA2-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: Albino phenotype and decrease in cpDNA copy
CC number. {ECO:0000269|PubMed:28495749}.
CC -!- MISCELLANEOUS: RNAi mutant displays chloroplasts with no chlorophyll
CC and aberrant nucleoid morphology. {ECO:0000269|PubMed:28495749}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC32241.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC005168; AAC32241.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC07896.1; -; Genomic_DNA.
DR EMBL; AK118981; BAC43557.1; -; mRNA.
DR EMBL; BT005620; AAO64040.1; -; mRNA.
DR PIR; T02651; T02651.
DR RefSeq; NP_180252.2; NM_128241.3. [Q8GWA2-1]
DR AlphaFoldDB; Q8GWA2; -.
DR SMR; Q8GWA2; -.
DR PRIDE; Q8GWA2; -.
DR ProteomicsDB; 238298; -. [Q8GWA2-1]
DR EnsemblPlants; AT2G26840.1; AT2G26840.1; AT2G26840. [Q8GWA2-1]
DR GeneID; 817225; -.
DR Gramene; AT2G26840.1; AT2G26840.1; AT2G26840. [Q8GWA2-1]
DR KEGG; ath:AT2G26840; -.
DR Araport; AT2G26840; -.
DR PhylomeDB; Q8GWA2; -.
DR BRENDA; 3.1.21.10; 399.
DR PRO; PR:Q8GWA2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8GWA2; baseline and differential.
DR GO; GO:0042644; C:chloroplast nucleoid; IDA:UniProtKB.
DR GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IDA:UniProtKB.
DR GO; GO:0000400; F:four-way junction DNA binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0090143; P:nucleoid organization; IMP:UniProtKB.
DR InterPro; IPR045290; MOC1-like.
DR PANTHER; PTHR36015; PTHR36015; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; DNA recombination; DNA-binding;
KW Endonuclease; Hydrolase; Magnesium; Manganese; Metal-binding; Nuclease;
KW Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..53
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 54..273
FT /note="Holliday junction resolvase MOC1, chloroplastic"
FT /id="PRO_0000441067"
FT BINDING 88
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:28495749"
FT BINDING 152
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:28495749"
FT BINDING 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:28495749"
FT BINDING 235
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:28495749"
FT MUTAGEN 88
FT /note="D->A: Abolishes endonucleolytic activity; when
FT associated with A-152; A-230 and A-235."
FT /evidence="ECO:0000269|PubMed:28495749"
FT MUTAGEN 152
FT /note="E->A: Abolishes endonucleolytic activity; when
FT associated with A-88; A-230 and A-235."
FT /evidence="ECO:0000269|PubMed:28495749"
FT MUTAGEN 230
FT /note="D->A: Abolishes endonucleolytic activity; when
FT associated with A-88; A-152 and A-235."
FT /evidence="ECO:0000269|PubMed:28495749"
FT MUTAGEN 235
FT /note="E->A: Abolishes endonucleolytic activity; when
FT associated with A-88; A-152 and A-230."
FT /evidence="ECO:0000269|PubMed:28495749"
SQ SEQUENCE 273 AA; 30046 MW; CE09EEB2E3DB79AB CRC64;
MATTVYGQAS LPQMHSLFSK VRPFLSHSPS FTAPFTRRRS FPFSALPTTK AIDAALMKEK
WLDSLSLTSQ DEDTTPENAE SSCIIGIDPD LSGALALLKF DHLGSSSFAQ VYDTPHIPVL
VGKRVRKRLD AKSIVQLIQS LDVPSGSRVY IEQSNPFPKD GKQGWYSGGF GYGLWIGTLV
ASGFCVIPVS ASLWKRHFQL ASGSCTKDDS RRVAAELFPS LSSQLKRKKD HGRAEALLIA
AYGEALKTEK LLIQPKELLS QVNYLENQLV EVK
