ID G8YPU3_PICSO Unreviewed; 1008 AA.
AC G8YPU3;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=DNA mismatch repair protein MSH3 {ECO:0000256|ARBA:ARBA00019000};
DE AltName: Full=DNA mismatch repair protein msh3 {ECO:0000256|ARBA:ARBA00022151};
DE AltName: Full=MutS protein homolog 3 {ECO:0000256|ARBA:ARBA00029792};
GN Name=Piso0_000705 {ECO:0000313|EMBL:CCE78678.1};
GN ORFNames=GNLVRS01_PISO0D02335g {ECO:0000313|EMBL:CCE78678.1};
OS Pichia sorbitophila (strain ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC
OS 10061 / NRRL Y-12695) (Hybrid yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Millerozyma.
OX NCBI_TaxID=559304 {ECO:0000313|EMBL:CCE78678.1, ECO:0000313|Proteomes:UP000005222};
RN [1] {ECO:0000313|Proteomes:UP000005222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC 10061 / NRRL
RC Y-12695 {ECO:0000313|Proteomes:UP000005222};
RX DOI=10.1534/g3.111.000745;
RA Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., Mallet S.,
RA Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., Seret M.L.,
RA Talla E., Samson G., Jubin C., Poulain J., Vacherie B., Barbe V.,
RA Pelletier E., Sherman D.J., Westhof E., Weissenbach J., Baret P.V.,
RA Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps of
RT genome resolution following polyploidization.";
RL G3 (Bethesda) 2:299-311(2012).
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. {ECO:0000256|ARBA:ARBA00025373}.
CC -!- SUBUNIT: Heterodimer consisting of MSH2-MSH3 (MutS beta). Forms a
CC ternary complex with MutL alpha (MLH1-PMS1).
CC {ECO:0000256|ARBA:ARBA00025902}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family. MSH3
CC subfamily. {ECO:0000256|ARBA:ARBA00007094}.
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DR EMBL; FO082056; CCE78678.1; -; Genomic_DNA.
DR AlphaFoldDB; G8YPU3; -.
DR STRING; 559304.G8YPU3; -.
DR eggNOG; KOG0218; Eukaryota.
DR HOGENOM; CLU_002472_0_2_1; -.
DR InParanoid; G8YPU3; -.
DR OMA; HIAPCEL; -.
DR Proteomes; UP000005222; Chromosome D.
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; 1.10.1420.10; -; 2.
DR Gene3D; 3.40.1170.10; DNA repair protein MutS, domain I; 1.
DR Gene3D; 3.30.420.110; MutS, connector domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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:SF122; DNA MISMATCH REPAIR PROTEIN MSH3; 1.
DR PANTHER; PTHR11361; DNA MISMATCH REPAIR PROTEIN MUTS FAMILY MEMBER; 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; 2.
DR SMART; SM00534; MUTSac; 1.
DR SMART; SM00533; MUTSd; 1.
DR SUPFAM; SSF55271; DNA repair protein MutS, domain I; 1.
DR SUPFAM; SSF53150; DNA repair protein MutS, domain II; 1.
DR SUPFAM; SSF48334; DNA repair protein MutS, domain III; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU003756};
KW DNA repair {ECO:0000256|RuleBase:RU003756};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU003756};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003756}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000005222}.
FT DOMAIN 853..869
FT /note="DNA mismatch repair proteins mutS family"
FT /evidence="ECO:0000259|PROSITE:PS00486"
FT REGION 1..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 593..620
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 11..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1008 AA; 114335 MW; BFB7F866B7047CA6 CRC64;
MGTKSKGQPC ISEFFKKKET KKDGDQKCQK ASTQNTEPKN HNLKAFEHGS SIQSVKKTST
IPLQEKHKIN DEEEQAQAYP SKRPKQQNGN SVSGNSKSKP DTRKLTPLEK QFLELKANNK
DKVLAIQVGY KYKFFCEDAV IASKVLNIVL VPGANNSCDT SSDRFAYCSI PDNRLHIHLR
RLLSYGLKVG VVKQMETASI KSVESDNKSG LFVREMTGVY TKATYLGDED PPRNQNDISM
NEDDEGVGDY IVCIDASDKK VGIVAVQPAT GDIIYDTFDD DSARNELETR LIFLNPSEII
IIGDEEANIG LKKMVNIITK SGNVISKKRK SESDYRSSIN TFFSKSEDIG QYYLLKFPSN
ILSCISELLE YLQEFKLSNM FLIKDNMSSF SNAKKYMHLP GSTLQALEVF QNSTDYSTKG
TLFWLLDYTK TKMGKRLLKK WVAMPLVSRN LIQDRLDAID DLSRGYNNFI DSLKNKIVKL
SRTGLDLEKS LIKVHYSSSH NVSKIDKKEI YLLLLNLDEI SSLFRSFSSQ IALFKDSVTS
RLLEDILQDI LDISESTTVE KLLKYITPSA LDNNQFEQKV YFFNLQNYPD EGILSELEKI
KDIEKKLDEE LEKIRVQLNR PHLNYVTNLK DAYLIEVRNG KMINDIPSDW IKINGTKTVS
RFRSPEVTKL YKELQYHNDT LLRNCDIAYG RFLKEVDENY ASLKTLSDVI ARFDCLFSLC
DLSSSYGYSK PSLTDSFSSI MIEKGRHPII EKLGSSTQGY IANDIHMSKD NNRVLIITGP
NMGGKSSYVK QVALLILMAQ IGCYIPCDKA TIGIFDSIFV RMGAKDDILR NKSTFMTELQ
ECSNIIRSMT SRSLIILDEL GRGTGTNDGI AIAFSVLNYL IENPAKPLTL FITHFPSLHV
FEQNYIGIVS NYHMGYVENY KKDQEFPEIL FLYNLVKGVV SKSYGLNVAN LAGIPNSIVR
YAFQKAEDMR KEKEELNLLK VISKLKVVPQ QAHDESKAQL EEIFNSIQ
//
