ID Q69MX6_ORYSJ Unreviewed; 1253 AA.
AC Q69MX6;
DT 13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2004, sequence version 1.
DT 24-JAN-2024, entry version 108.
DE RecName: Full=DNA mismatch repair protein {ECO:0000256|PIRNR:PIRNR037677};
GN ORFNames=OJ1261_A08.53 {ECO:0000313|EMBL:BAD36299.1}, P0465E03.5
GN {ECO:0000313|EMBL:BAD36244.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947 {ECO:0000313|EMBL:BAD36299.1, ECO:0000313|Proteomes:UP000000763};
RN [1] {ECO:0000313|EMBL:BAD36299.1}
RP NUCLEOTIDE SEQUENCE.
RA Sasaki T., Matsumoto T., Hattori M., Sakaki Y., Katayose Y.;
RT "Oryza sativa nipponbare(GA3) genomic DNA, chromosome 9, BAC
RT clone:OJ1261_A08.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAD36244.1}
RP NUCLEOTIDE SEQUENCE.
RA Sasaki T., Matsumoto T., Katayose Y.;
RT "Oryza sativa nipponbare(GA3) genomic DNA, chromosome 9, PAC
RT clone:P0465E03.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000000763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000000763};
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RA Matsumoto T., Wu J., Kanamori H., Katayose Y., Fujisawa M., Namiki N.,
RA Mizuno H., Yamamoto K., Antonio B.A., Baba T., Sakata K., Nagamura Y.,
RA Aoki H., Arikawa K., Arita K., Bito T., Chiden Y., Fujitsuka N.,
RA Fukunaka R., Hamada M., Harada C., Hayashi A., Hijishita S., Honda M.,
RA Hosokawa S., Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M.,
RA Ito K., Ito S., Ito T., Ito Y., Ito Y., Iwabuchi A., Kamiya K.,
RA Karasawa W., Kurita K., Katagiri S., Kikuta A., Kobayashi H., Kobayashi N.,
RA Machita K., Maehara T., Masukawa M., Mizubayashi T., Mukai Y., Nagasaki H.,
RA Nagata Y., Naito S., Nakashima M., Nakama Y., Nakamichi Y., Nakamura M.,
RA Meguro A., Negishi M., Ohta I., Ohta T., Okamoto M., Ono N., Saji S.,
RA Sakaguchi M., Sakai K., Shibata M., Shimokawa T., Song J., Takazaki Y.,
RA Terasawa K., Tsugane M., Tsuji K., Ueda S., Waki K., Yamagata H.,
RA Yamamoto M., Yamamoto S., Yamane H., Yoshiki S., Yoshihara R., Yukawa K.,
RA Zhong H., Yano M., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA Moffat K., Hill J., Bera J., Fadrosh D., Jin S., Johri S., Kim M.,
RA Overton L., Reardon M., Tsitrin T., Vuong H., Weaver B., Ciecko A.,
RA Tallon L., Jackson J., Pai G., Aken S.V., Utterback T., Reidmuller S.,
RA Feldblyum T., Hsiao J., Zismann V., Iobst S., de Vazeille A.R., Buell C.R.,
RA Ying K., Li Y., Lu T., Huang Y., Zhao Q., Feng Q., Zhang L., Zhu J.,
RA Weng Q., Mu J., Lu Y., Fan D., Liu Y., Guan J., Zhang Y., Yu S., Liu X.,
RA Zhang Y., Hong G., Han B., Choisne N., Demange N., Orjeda G., Samain S.,
RA Cattolico L., Pelletier E., Couloux A., Segurens B., Wincker P., D'Hont A.,
RA Scarpelli C., Weissenbach J., Salanoubat M., Quetier F., Yu Y., Kim H.R.,
RA Rambo T., Currie J., Collura K., Luo M., Yang T., Ammiraju J.S.S.,
RA Engler F., Soderlund C., Wing R.A., Palmer L.E., de la Bastide M.,
RA Spiegel L., Nascimento L., Zutavern T., O'Shaughnessy A., Dike S.,
RA Dedhia N., Preston R., Balija V., McCombie W.R., Chow T., Chen H.,
RA Chung M., Chen C., Shaw J., Wu H., Hsiao K., Chao Y., Chu M., Cheng C.,
RA Hour A., Lee P., Lin S., Lin Y., Liou J., Liu S., Hsing Y., Raghuvanshi S.,
RA Mohanty A., Bharti A.K., Gaur A., Gupta V., Kumar D., Ravi V., Vij S.,
RA Kapur A., Khurana P., Khurana P., Khurana J.P., Tyagi A.K., Gaikwad K.,
RA Singh A., Dalal V., Srivastava S., Dixit A., Pal A.K., Ghazi I.A.,
RA Yadav M., Pandit A., Bhargava A., Sureshbabu K., Batra K., Sharma T.R.,
RA Mohapatra T., Singh N.K., Messing J., Nelson A.B., Fuks G., Kavchok S.,
RA Keizer G., Linton E., Llaca V., Song R., Tanyolac B., Young S., Ho-Il K.,
RA Hahn J.H., Sangsakoo G., Vanavichit A., de Mattos Luiz.A.T., Zimmer P.D.,
RA Malone G., Dellagostin O., de Oliveira A.C., Bevan M., Bancroft I.,
RA Minx P., Cordum H., Wilson R., Cheng Z., Jin W., Jiang J., Leong S.A.,
RA Iwama H., Gojobori T., Itoh T., Niimura Y., Fujii Y., Habara T., Sakai H.,
RA Sato Y., Wilson G., Kumar K., McCouch S., Juretic N., Hoen D., Wright S.,
RA Bruskiewich R., Bureau T., Miyao A., Hirochika H., Nishikawa T.,
RA Kadowaki K., Sugiura M., Burr B., Sasaki T.;
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4] {ECO:0000313|Proteomes:UP000000763}
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000000763};
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
CC -!- FUNCTION: Component of the post-replicative DNA mismatch repair system
CC (MMR). {ECO:0000256|PIRNR:PIRNR037677, ECO:0000256|RuleBase:RU003756}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family.
CC {ECO:0000256|PIRNR:PIRNR037677, ECO:0000256|RuleBase:RU003756}.
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DR EMBL; AP005707; BAD36244.1; -; Genomic_DNA.
DR EMBL; AP005722; BAD36299.1; -; Genomic_DNA.
DR AlphaFoldDB; Q69MX6; -.
DR Proteomes; UP000000763; Chromosome 9.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0030983; F:mismatched DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006298; P:mismatch repair; IEA:InterPro.
DR CDD; cd20404; Tudor_Agenet_AtEML-like; 1.
DR Gene3D; 1.10.1420.10; -; 2.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 3.40.1170.10; DNA repair protein MutS, domain I; 1.
DR Gene3D; 3.30.420.110; MutS, connector domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR007695; DNA_mismatch_repair_MutS-lik_N.
DR InterPro; IPR017261; DNA_mismatch_repair_MutS/MSH.
DR InterPro; IPR000432; DNA_mismatch_repair_MutS_C.
DR InterPro; IPR007861; DNA_mismatch_repair_MutS_clamp.
DR InterPro; IPR007696; DNA_mismatch_repair_MutS_core.
DR InterPro; IPR016151; DNA_mismatch_repair_MutS_N.
DR InterPro; IPR036187; DNA_mismatch_repair_MutS_sf.
DR InterPro; IPR007860; DNA_mmatch_repair_MutS_con_dom.
DR InterPro; IPR036678; MutS_con_dom_sf.
DR InterPro; IPR045076; MutS_family.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002999; Tudor.
DR PANTHER; PTHR11361:SF150; DNA MISMATCH REPAIR PROTEIN MSH6; 1.
DR PANTHER; PTHR11361; DNA MISMATCH REPAIR PROTEIN MUTS FAMILY MEMBER; 1.
DR Pfam; PF01624; MutS_I; 1.
DR Pfam; PF05188; MutS_II; 1.
DR Pfam; PF05192; MutS_III; 1.
DR Pfam; PF05190; MutS_IV; 1.
DR Pfam; PF00488; MutS_V; 1.
DR PIRSF; PIRSF037677; DNA_mis_repair_Msh6; 1.
DR SMART; SM00534; MUTSac; 1.
DR SMART; SM00533; MUTSd; 1.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF55271; DNA repair protein MutS, domain I; 1.
DR SUPFAM; SSF53150; DNA repair protein MutS, domain II; 1.
DR SUPFAM; SSF48334; DNA repair protein MutS, domain III; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR037677};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|PIRNR:PIRNR037677};
KW DNA repair {ECO:0000256|PIRNR:PIRNR037677, ECO:0000256|RuleBase:RU003756};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR037677};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR037677}.
FT DOMAIN 65..123
FT /note="Tudor"
FT /evidence="ECO:0000259|SMART:SM00333"
FT DOMAIN 636..977
FT /note="DNA mismatch repair protein MutS core"
FT /evidence="ECO:0000259|SMART:SM00533"
FT DOMAIN 997..1188
FT /note="DNA mismatch repair proteins mutS family"
FT /evidence="ECO:0000259|SMART:SM00534"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..63
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..198
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1253 AA; 138526 MW; 6CE7D78D4ADF7248 CRC64;
MASPSSRRLS NGRSPLLRKQ SQITAFFSSP TAKPSPSPLN PRATKPPLAV PSPPPPNPPS
PPQEEETAVG RRLRVYWPLD DAWYEGRVEG YDVGSRRHRV RYDDGEEEVV DLASERYEWA
AAADEEEVTP QPSRKLRRLR RMSDAATAKS PGAVDGGGGG DETADSAEEE DEDWKNDAAA
ENDSEEVELD DEEDDEEEVV AVKTRKGKKN NPLSTSASTP KLASGLGSAS ISGSTLSKKR
RKVDAGEQPL ENALTALTGE VAERFAQRQA EKFKFLGEGR KDAKGRRPGN PNYDPRTLSL
PSQFLNSLTG GQRQWWEFKS QHMDKVLFFK MGKFYELFEM DAHVGAKELD LQYMKGDKPH
CGFPEKNFEL NLEKLAKKGY RVLVIEQTET PEQLDLRRKE TGVKDKVVRR EICAMVTKGT
LTEGESLLAN PDPSYLFSVA ESYQCGSEKD QDGHTIGVCI VDVSTSKFIV GQFQDDAERH
GLCSILSEIR PAEIIKPAKM LSPETEKALK SNTRDPLINN LLPSMEFWDA EKTIHEIKQY
YCSLDTPGAG AQISSAYLPE LLSELIEAGD KTYALSALGG SLFYLRQSLL DEKLLPCAEF
ERLTCSGLTN PIRKHMILDA AALENLEILE NARNGGLSGT LYAQLNHCVT GFGKRLLKRW
IARPLYERQA ILQRQSAIAT FKGSGHECAI QFRKDLSRLP DMERLLARLF SSCDKNGRSS
KSVVLYEDAS KRLLHQFTAA LRGCQQMFQA CSSISMLTST DGSSLLNDLL SLGKGLPHVS
SILDHFRDAF DWSEADRNGR IIPHEGCDPQ YDAACIAIEE IESSLQKYLK EQRKLLSDSS
VKYVDVGKDT YLLEVSENLR GSVPHNYELQ STKKGFYRYW TPEVKELISE LSKAEAEKEA
KLKCILQNLI QLFVEHHSKW RQLVSVVAEL DVLISLAIAS DFFEGPTCCP IIKESYGPDD
TPTLHARNLG HPTLRSDSLG SGSFVPNDIK MGGPGNASFI VLTGPNMGGK STLLRQVCLT
IILAQIGANV PAESFELSLV DRMFVRMGAR DHIMAGQSTF LVELMETASV LSSATKNSLV
ALDELGRGTS TSDGQAIAAS VLEYLVHHVQ CLGLFSTHYH RLAAENKDSK VSLCHMACEI
SKGEGGLEEV TFLYKLTPGS CPKSYGVNVA RLAGIPASVL QRANEKSSDF EASYGKRPGI
TKNKPSCAQE DKFAAIKDLF RVVKAMHHRE DHASSLGMLH EVQKRAKVQV IGE
//