MSH3_LODEL
ID MSH3_LODEL Reviewed; 993 AA.
AC A5DYV8;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=DNA mismatch repair protein MSH3;
DE AltName: Full=MutS protein homolog 3;
GN Name=MSH3; ORFNames=LELG_02545;
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC YB-4239;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH981526; EDK44366.1; -; Genomic_DNA.
DR RefSeq; XP_001525987.1; XM_001525937.1.
DR AlphaFoldDB; A5DYV8; -.
DR SMR; A5DYV8; -.
DR STRING; 379508.A5DYV8; -.
DR EnsemblFungi; EDK44366; EDK44366; LELG_02545.
DR GeneID; 5232975; -.
DR KEGG; lel:LELG_02545; -.
DR VEuPathDB; FungiDB:LELG_02545; -.
DR eggNOG; KOG0218; Eukaryota.
DR HOGENOM; CLU_002472_3_1_1; -.
DR InParanoid; A5DYV8; -.
DR OMA; LRNVHMK; -.
DR OrthoDB; 138168at2759; -.
DR Proteomes; UP000001996; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0030983; F:mismatched DNA binding; IEA:InterPro.
DR GO; GO:0006298; P:mismatch repair; IEA:InterPro.
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; 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; 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..993
FT /note="DNA mismatch repair protein MSH3"
FT /id="PRO_0000338523"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..212
FT /note="Mispair-binding domain"
FT /evidence="ECO:0000250"
FT REGION 290..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 787..794
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 993 AA; 112039 MW; 7C914CB1FBEC41EB CRC64;
MASKKQSTIS LFFSSQTRKS PGRDAKKNDI SSSPFNAASS TNNSIGSTPR VSPIAKFQYN
KSTSTLHENT NPRVKRVSTL NVDVEKEHKK IKRARSTKLT PLESQILQLL SEHPDKILLI
QVGYKYKVYG EDARHVARCL NIMFISSSTD PTFSYCSFPE NRLHINLQRI LNTGVKVGVV
KQMESAIIKE VDKIGKSGDL MKRELTGVYT RGTYMNDEFI DSGVNSPEQE ELGYIVCVNE
ISRYQFAIVA IQPLTGEIIY DDFTDDVSHD ELETRLLYLR PSEVLLLGCG GNESNNNNNN
NSNNSSNNND NGTDADAQNQ TSTLQCFQKL VNHNIKIERK PKGLNNLKAV LNAAALNFYR
ELLEPVQVCV SELVKYLEEF NLSNIFTVIE NVSKFDSKKT MILPASTMLS LEIFQNSENS
TTKGTLFSLL NHTKTPFGMR LLESWVSHPL IDKDKIEERY QAVEDLSTGS HFNDCLSRLL
QKIGKNLDLE SIAIKIHYST TTRSLATKIN RKDIFMMLLM YQSALQFVSQ FEKTIKASNL
SPLLKRVLDN LLQLANTDTV DRFMDMINPS YLLGEQQNLH QSSRSTREQK VKFFNLNNGF
EEINRELAEI MNVKMLLEEE LVKVKKLLQR PQLNYVTSNG EPYLIEVRNG KAVESLPIDF
IKINGTTTVS RFRSKEIAHL YKMKQYHEEV LNNRCDEAFN TFLNELDSHY GFFQGITKNL
AVLDCLLSLA AVSNSNSNTH VKPNLSDELI IDVKNARHPI IEHLRDGYVA NDIDIRYDSN
RVLVITGPNM GGKSSYVKMV ALLIIMTQIG CYIPCEAATI GIFDSILIRM GASDNLLKGR
STFMTEMLEC SNIIQKLTPR SLVILDEIGR GTGSIDGYSL AYAILRYLVE SKLKPIVLCI
THYTGLLSET EDEKFDKDAK DENLDTGDDV VKSYYMGYEE ITQPGQVFPE IVFLYNLCPG
VSNSYGLQVA KMAGLPKKVL LEAYLMSSVT DFD
