MOC1_CHLRE
ID MOC1_CHLRE Reviewed; 882 AA.
AC A8ITB0;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2017, sequence version 2.
DT 03-AUG-2022, entry version 61.
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=CreMOC1 {ECO:0000303|PubMed:28495749};
DE Flags: Precursor;
GN Name=MOC1 {ECO:0000303|PubMed:28495749};
GN Synonyms=MOCH72 {ECO:0000303|PubMed:28495749};
GN ORFNames=CHLREDRAFT_171080 {ECO:0000312|EMBL:EDP04285.1},
GN Cre04.g21800 {ECO:0000303|PubMed:28495749};
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP IDENTIFICATION, FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=137c / CC-125;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503;
RX PubMed=17932292; DOI=10.1126/science.1143609;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J.,
RA Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT "The Chlamydomonas genome reveals the evolution of key animal and plant
RT functions.";
RL Science 318:245-250(2007).
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 (By similarity). Mediates chloroplast
CC nucleoid segregation during chloroplast division (PubMed:28495749).
CC {ECO:0000250|UniProtKB:Q8GWA2, 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:0000250|UniProtKB:Q8GWA2};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q8GWA2};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:28495749}.
CC -!- DISRUPTION PHENOTYPE: Defective in chloroplast nucleoid segregation
CC during chloroplast divisions. {ECO:0000269|PubMed:28495749}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDP04285.1; Type=Erroneous translation; Evidence={ECO:0000305};
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DR EMBL; DS496122; EDP04285.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; A8ITB0; -.
DR PaxDb; A8ITB0; -.
DR EnsemblPlants; PNW84022; PNW84022; CHLRE_04g218000v5.
DR Gramene; PNW84022; PNW84022; CHLRE_04g218000v5.
DR HOGENOM; CLU_224466_0_0_1; -.
DR InParanoid; A8ITB0; -.
DR OrthoDB; 1728705at2759; -.
DR BRENDA; 3.1.21.10; 1318.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Chloroplast; DNA recombination; DNA-binding; Endonuclease; Hydrolase;
KW Magnesium; Manganese; Metal-binding; Nuclease; Plastid; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000303|PubMed:28495749"
FT CHAIN ?..882
FT /note="Holliday junction resolvase MOC1, chloroplastic"
FT /id="PRO_0000441068"
FT REGION 87..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..817
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..847
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 397
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8GWA2"
FT BINDING 552
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8GWA2"
FT BINDING 629
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8GWA2"
FT BINDING 634
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8GWA2"
SQ SEQUENCE 882 AA; 85331 MW; 66368E463BDA7442 CRC64;
MRVLGFLSSH AGTGTAAAHT RWRWLAPLGI QAIRPASASA GGNAVSSATP QAPPCPIHAN
VGVGRASALG PGPSGFMAPS AGIVTAIRDG PNSNSRCSTV RTHATRSKST GPSRATSSGP
ATAAPPRRRR RTSNDTQDGG LTSEQTPTNT AVAAVAATAA AAAGASASAA APALPVALNP
TWRTPPTAEA ARRITQAASA SAAYSGSSAA AAAAAVAAGP SSAASVARGG SAAAARSAAA
SALAANANTS SGAASAAAIA ATASTAPGKL LLGGDLSRAL AAAGSTTAPP LPLPSRAGLS
APKHTASAAA AAAAAASVLP ASTPAAASQT PPTTVTSCGT GSGAPATPRA ARSPTAAVSV
SSADAAAAAA AAAAPASAAA TAAAAVLPTR HIVAAVDPDL NGALALIYWD EDPNDPTTAT
ASGPAAATTD AAAAAAAAAA AATGPAARLA TLAAAAPPGS GAAAAADEAA AAALLWLPTP
PRPPADASRW RVCVWDMPVS AAERQKRTAS GQVARRRLLH VAGARAVLSA ALAAALPPPG
EARPVALYGY VEVPPILPGD GNIAAYTSLW STGSWLGLLT GMGFTVGSTP VRRWKTDLGL
YGAKGKDASL ALARALFPGQ QPILRHKKNH GRADALLIAA WALGACLPRG LGASLRRNGI
TLDQLLQQQP GTTVGLVWGP PRPPAPTDAY GNLLTPEQDM WDEIEAAETK VERKAQARSS
TARRRKTAGT QEEPEAQAEE EQAEAGTGVV AAAAGAAAPK RRRAKKAAVE SGSEAAVAEV
AAGPQEEGSE GEVAGQGGRA CRSKSRSKSS GKSSSKAEAG GAGSGRRRAA SVGSSSVGSS
SVGSSSGGGG GGGGGVKAPG ASRRRGGAKA GSDGGVSGSE SE
