MSH3_YARLI
ID MSH3_YARLI Reviewed; 990 AA.
AC Q6CHE5;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=DNA mismatch repair protein MSH3;
DE AltName: Full=MutS protein homolog 3;
GN Name=MSH3; OrderedLocusNames=YALI0A09724g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Component of the post-replicative DNA mismatch repair system
CC (MMR). Heterodimerizes with MSH2 to form MutS beta, which binds to DNA
CC mismatches thereby initiating DNA repair. MSH3 provides substrate-
CC binding and substrate specificity to the complex. When bound, the MutS
CC beta heterodimer bends the DNA helix and shields approximately 20 base
CC pairs. Acts mainly to repair insertion-deletion loops (IDLs) from 2 to
CC 13 nucleotides in size, but can also repair base-base and single
CC insertion-deletion mismatches that occur during replication. After
CC mismatch binding, forms a ternary complex with the MutL alpha
CC heterodimer, which is thought to be responsible for directing the
CC downstream MMR events, including strand discrimination, excision, and
CC resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch
CC repair functions (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer consisting of MSH2-MSH3 (MutS beta). Forms a
CC ternary complex with MutL alpha (MLH1-PMS1) (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family. MSH3
CC subfamily. {ECO:0000305}.
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DR EMBL; CR382127; CAG83843.1; -; Genomic_DNA.
DR RefSeq; XP_499916.1; XM_499916.1.
DR AlphaFoldDB; Q6CHE5; -.
DR SMR; Q6CHE5; -.
DR STRING; 4952.CAG83843; -.
DR PRIDE; Q6CHE5; -.
DR EnsemblFungi; CAG83843; CAG83843; YALI0_A09724g.
DR GeneID; 2906382; -.
DR KEGG; yli:YALI0A09724g; -.
DR VEuPathDB; FungiDB:YALI0_A09724g; -.
DR HOGENOM; CLU_002472_1_3_1; -.
DR InParanoid; Q6CHE5; -.
DR OMA; LRNVHMK; -.
DR Proteomes; UP000001300; Chromosome A.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
DR GO; GO:0006312; P:mitotic recombination; IBA:GO_Central.
DR Gene3D; 3.30.420.110; -; 1.
DR Gene3D; 3.40.1170.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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 PANTHER; PTHR11361; PTHR11361; 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 SUPFAM; SSF48334; SSF48334; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF53150; SSF53150; 1.
DR SUPFAM; SSF55271; SSF55271; 1.
DR PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Nucleotide-binding;
KW Nucleus; Reference proteome.
FT CHAIN 1..990
FT /note="DNA mismatch repair protein MSH3"
FT /id="PRO_0000338533"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..261
FT /note="Mispair-binding domain"
FT /evidence="ECO:0000250"
FT COMPBIAS 73..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 789..796
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 990 AA; 110540 MW; B38DA85D69047332 CRC64;
MKRSKQATLS RFFKKPKTGA DAVHTEAVIG KKPTDSGSPA EQKDAKSPQQ VTDEPPLEPV
TVTTDVVAMD TQPDLSIGSE INSKSRPKSL ASFKSGKSIN TDHNPELKQK FRAKLELVRN
KNDEDLPVIT KKTKLNATEF QWYEIKKQHR DTLLFVQVGY KYHIYGDDAE IAHAQTRLFL
SPGITNLKDI GNDGVVQQGS KYIKLAYSSF PVHRIDFYTK QLVEKGFKVG HVQQMEVAAL
KNVENKKGPM IRELTNTFTK GTYIESGNGG SVNDVQYSSY LVALHESKGD KPTVTLLATE
VSTGDVIWDS FNDDYVKSEL EIRLLTLAPC EILNCGVSSS TLKMCQKYMH RNKGRLAEMN
VLEEEVEDPD AQVALFFEGK ANAGTCSTVL ELPAMVKTLI LATSRYLTHC KLDSLFLLTN
NFTRYTGSYM RLSANTVASL ELFANTTDHT AKGSLFWVLN RCLTVFGSRE LKKWVSRPLT
DRTAILQRLS AVEAIIKSIY GAESDELTTL INKLVKLLKP IPDLSKMLMR LHYGQLNRKE
VYLLLRELLF VAQEFKPGSG DKYIDTNPVL GEIFNSLGIH VSDIEKLLEE INPDAARQDE
ALTFFVTDPP SLVDRKKDLK KVEAELQIEL LALRAELNRP KLQYSSVAGI DYLIEVANKD
TKKLPLEWTK ISGTKSVSRF RTPTLNSLVK RHEYCVEKLK AACDIEFNMF RSRCATHYEF
FRSMVVAMSQ FDCLFALAKV SGQSGWVKAD YVDEGGIDLK DSRHVITEKL MTNYISNDIK
IRCPTVVTGP NMGGKSSLVR QIALSVLLAH IGCYVPASKA QIPITDSILC RMGAQDNIMS
GQSTFMVELC ECAEILRNAT SKSLVLLDEI GRGTTTTDGI AIAHSVLKHF IELEALTLFI
THYPLGQLLD SEDSNKCDLV HMDITNTNPP IFTYKMKPGS ATDSYGLNVA GLAGIPQAII
NRAEEMGKDM KHDVMYQEGV RMLTDIKKVM
