ID   MSH3_CRYNB              Reviewed;        1191 AA.
AC   P0CO93; Q55VB4; Q5KKX1;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=DNA mismatch repair protein MSH3;
DE   AltName: Full=MutS protein homolog 3;
GN   Name=MSH3; OrderedLocusNames=CNBC5700;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAEY01000016; EAL21706.1; -; Genomic_DNA.
DR   RefSeq; XP_776353.1; XM_771260.1.
DR   AlphaFoldDB; P0CO93; -.
DR   SMR; P0CO93; -.
DR   PRIDE; P0CO93; -.
DR   EnsemblFungi; EAL21706; EAL21706; CNBC5700.
DR   GeneID; 4935236; -.
DR   KEGG; cnb:CNBC5700; -.
DR   VEuPathDB; FungiDB:CNBC5700; -.
DR   HOGENOM; CLU_002472_0_2_1; -.
DR   Proteomes; UP000001435; Chromosome 3.
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; 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   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.
FT   CHAIN           1..1191
FT                   /note="DNA mismatch repair protein MSH3"
FT                   /id="PRO_0000410153"
FT   REGION          1..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          118..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          175..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          233..347
FT                   /note="Mispair-binding domain"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        54..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..137
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        189..203
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         950..957
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1191 AA;  132701 MW;  850505AB6DDCBB4C CRC64;
     MPSEGSQQPS LDSFFKRKNP RVEPYSRTGN NAIIDLTDSP PNKKIKLDDE GSQKNRSMTQ
     TSSSYFKGHP TARPLSVDKR LPRKPSAAIQ AYKLQDVIPP QPSHSGLAFE TCSLVPQASF
     VPDSQPEPSA SPAPQRTTEQ LKRHEEWKTR ILAMSGSFRR KRSLALDEAV AAEAREAAGL
     EDEGTPFDGS DGDDYKSESE KNAEEVGKQL KKYVAKELAG KGKSKGKKKE EIGPSGLAYT
     PLEKQFMEIK EQNRDVLLLM EVGYKYKFHG EDAKTASREL GIVAFPNRNF FTASIPTHRL
     HIHVKKLLSL GYKVGVITQT ETAALKKIGD NRNAPFARKL THLFTAATYV EDPSLSSSSS
     SSSSVRFDDP VVPGTAPPPT NALVAIVEQP VDRASDDRVK VGLVCVVPGT GDITWDEFDD
     SQIRTELETR LAHLSPAELL LPKQRLTKAT EKVLTYFAGE PKHRGRNAVR IERIDNIPEY
     DAAFDFLTNF YHCKEHKATV SKGDVNDERH LMTEGNKQWS LQPKLSQDGA DISLDEEIYL
     ASGVSSSKAI LTLVDFPKQV VISMAVAIRY MKRFGLENAF KHTSSFVRFA NRSHMLLSSN
     TLANLEIYQN QTDGGLYGSL IWLLDHCKTR MGKRLLREWV GRPLLDVAAL KARADAIEEI
     MENNSYHMEK LRSLLINMPD LVRGLTRVQY GKATPNELAT LLITLVRLAS EFKPNMGNVF
     RSCLLNNIPN TLPTILDTSQ RFLNALNLKQ ARENDVANLW ADPDRFPDIQ DVKDCISVCE
     MELNEHLMEL RKILKKPTLR YITVSGIEYL VEVPIRDTKI VPAQWMKISA TRTVNRYHTP
     KILAITKERT QHLEKLSIVA REAFIAFQSE VAEYHELVVV SKQIAVIDCL MSLAQTAAAS
     GYCKPKFVAE PELKILAGRH PMVEMLREES YVPFDIHFSK EEGTTKIITG PNMAGKSSTV
     RAMALIVCMA QIGSFVPAAS VTLSVHDSVQ TRMGASDEIG RGKSTFMVEL SETSDILQTI
     TPRSLVVLDE LGRGTSTYDG IAIAYATLSH IAEIGCNTLF VTHYPTVAQD LAREKPDKIS
     NWHMSFDEIQ MPDGGAEITF LYQLTRGLQE ASFGVWCARL AGLPKPILDT AQMRSSSLKA
     ETQERLRGIV ARRVGWMLHN LFDNKTSSSQ VLRNVEMLHN SLSSSSISFS Q