MSH3_CANAL
ID MSH3_CANAL Reviewed; 1037 AA.
AC Q59Y41; A0A1D8PI80;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=DNA mismatch repair protein MSH3;
DE AltName: Full=MutS protein homolog 3;
GN Name=MSH3; OrderedLocusNames=CAALFM_C208680WA;
GN ORFNames=CaO19.11091, CaO19.3608;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017624; AOW27856.1; -; Genomic_DNA.
DR RefSeq; XP_714452.1; XM_709359.1.
DR AlphaFoldDB; Q59Y41; -.
DR SMR; Q59Y41; -.
DR BioGRID; 1226940; 1.
DR STRING; 237561.Q59Y41; -.
DR PRIDE; Q59Y41; -.
DR GeneID; 3643889; -.
DR KEGG; cal:CAALFM_C208680WA; -.
DR CGD; CAL0000179035; MSH3.
DR VEuPathDB; FungiDB:C2_08680W_A; -.
DR eggNOG; KOG0218; Eukaryota.
DR HOGENOM; CLU_002472_0_2_1; -.
DR InParanoid; Q59Y41; -.
DR OrthoDB; 138168at2759; -.
DR PRO; PR:Q59Y41; -.
DR Proteomes; UP000000559; Chromosome 2.
DR GO; GO:0032302; C:MutSbeta complex; IEA:EnsemblFungi.
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:0000406; F:double-strand/single-strand DNA junction binding; IEA:EnsemblFungi.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0000404; F:heteroduplex DNA loop binding; IEA:EnsemblFungi.
DR GO; GO:0000403; F:Y-form DNA binding; IEA:EnsemblFungi.
DR GO; GO:0000710; P:meiotic mismatch repair; IEA:EnsemblFungi.
DR GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
DR GO; GO:0006312; P:mitotic recombination; IBA:GO_Central.
DR GO; GO:0000735; P:removal of nonhomologous ends; IEA:EnsemblFungi.
DR GO; GO:0043111; P:replication fork arrest; IEA:EnsemblFungi.
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; 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..1037
FT /note="DNA mismatch repair protein MSH3"
FT /id="PRO_0000338515"
FT REGION 1..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..221
FT /note="Mispair-binding domain"
FT /evidence="ECO:0000250"
FT REGION 229..249
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..50
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 800..807
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1037 AA; 118896 MW; 7E11A06924ED3D78 CRC64;
MSSQKRQSTL SRFFTTIKPS QSTESTLTEK VSSKSPPLPP PPPPPTASPS LPSEKLLEFG
FDGTKDSTST RTTTTKSKDV EKRKSTTSSG SSFSSESKPK RPKEKRLTPL EKQILELTEQ
HQDKILLIQI GYKYKVFGIN ALKVSKILNI MYISNDIEDT RFHYCSIPDT RLHIHLQRIL
SHGYKVGVVK QIESTIVKQI EKTSKSSDVM RREVTGVYTK ATYLGDESNE NTKGSWDGLS
SSSSSSSSDV PEYIVCINEV SEKQFAIVAV QPLIGEVIFD SFKDDISRQE LETRLLYLRP
VEVIVITNGS SEQISGPTLM TLKLINHNCN IIHKSGSPSE NGNENENENE NEAIEAIMSK
YLNEKLVEYY SINFSIPIQQ CFEYLLLYLN EFKLTNIFTI PENITNFQDS KKYMILPANT
LNSLEIFTNT TDHTTKGSLF KLLNNTKTIF GSRLLQKWVS RPLVHIQDIK DRHQAIEDLQ
SEYNHVVDSI SNFLTKIKYL DLEGLLSKIH YSSTNNNNNN LRINRKQVYL LLSNLQEILI
LVQKFEKSIK SFKFKSSLLI QIFDELLTIS QTDIIIIENF LSMIDLSFID CKESSEQCRK
FFKRNSFDSI ELQYQNIAQY QQQIEQEQLE IIRKELGNSK LKYVQKDGER YLIEIRNNQR
DKLSKILDDK DYILIKSTQT ITRYRKKSVT EYLKLLQYHE EMLIKTCDEE FQNFLKDLDS
NYTLFYKIIK NLAIFDCLLS LTTTSSLPNY TRPTLIDDDL TILVKQARHP TIEQLRPNYV
ANDININIEY DKNRVLIITG PNMGGKSSYV KTVALLTVMT QIGCYLPCQN ATMGIFDSIF
IRMGANDNIL KGYSTFMMEM LQCKNIISMM SNRSLIILDE IGRGTGTIDG ISLAYSILKY
LIESEFKPLV LFITHYPSIH VLEQEYPNQL VVNYHMGYQE IKNNTPGEIP EIIFLYNLCR
GVVNNSYGLN VAKLAGISHD IIKQAYRVSE KVKSDIELKE YWKFAHSLNK ALKEGGSSSP
NQLDDIDYYI LSKHSSL
