MSH3_CRYNJ
ID MSH3_CRYNJ Reviewed; 1191 AA.
AC P0CO92; Q55VB4; Q5KKX1;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=DNA mismatch repair protein MSH3;
DE AltName: Full=MutS protein homolog 3;
GN Name=MSH3; OrderedLocusNames=CNC01550;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
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}.
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DR EMBL; AE017343; AAW42187.1; -; Genomic_DNA.
DR RefSeq; XP_569494.1; XM_569494.1.
DR AlphaFoldDB; P0CO92; -.
DR SMR; P0CO92; -.
DR STRING; 5207.AAW42187; -.
DR PaxDb; P0CO92; -.
DR EnsemblFungi; AAW42187; AAW42187; CNC01550.
DR VEuPathDB; FungiDB:CNC01550; -.
DR eggNOG; KOG0218; Eukaryota.
DR HOGENOM; CLU_002472_0_2_1; -.
DR InParanoid; P0CO92; -.
DR OMA; LRNVHMK; -.
DR OrthoDB; 138168at2759; -.
DR Proteomes; UP000002149; Chromosome 3.
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; 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; Reference proteome.
FT CHAIN 1..1191
FT /note="DNA mismatch repair protein MSH3"
FT /id="PRO_0000338519"
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; 132687 MW; 554B1CF88842D3AF 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 LPKQRLSKAT 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
