MSH3_NEUCR
ID MSH3_NEUCR Reviewed; 1145 AA.
AC Q7SD11;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=DNA mismatch repair protein msh-3;
DE AltName: Full=MutS protein homolog 3;
GN Name=msh-3; ORFNames=NCU08115;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- FUNCTION: Component of the post-replicative DNA mismatch repair system
CC (MMR). Heterodimerizes with msh-2 to form MutS beta, which binds to DNA
CC mismatches thereby initiating DNA repair. Msh-3 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 msh-2-msh-3 (MutS beta). Forms a
CC ternary complex with MutL alpha (mlh-1-pms-1) (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; CM002236; EAA34638.1; -; Genomic_DNA.
DR RefSeq; XP_963874.1; XM_958781.2.
DR AlphaFoldDB; Q7SD11; -.
DR SMR; Q7SD11; -.
DR STRING; 5141.EFNCRP00000009619; -.
DR PRIDE; Q7SD11; -.
DR EnsemblFungi; EAA34638; EAA34638; NCU08115.
DR GeneID; 3880023; -.
DR KEGG; ncr:NCU08115; -.
DR VEuPathDB; FungiDB:NCU08115; -.
DR HOGENOM; CLU_002472_0_0_1; -.
DR InParanoid; Q7SD11; -.
DR OMA; LRNVHMK; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
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; 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; 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 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..1145
FT /note="DNA mismatch repair protein msh-3"
FT /id="PRO_0000338526"
FT REGION 1..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..307
FT /note="Mispair-binding domain"
FT /evidence="ECO:0000250"
FT REGION 857..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..875
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 882..889
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1145 AA; 125692 MW; EECDACC223403275 CRC64;
MAGPSRLPDK KQASISSFFT PRNTSPLVNL SQNASKKPPP AESKSSKSTS SRKRPEPQTD
DSEDDVPRDA KRRRSNGPSA ATDTEDAVAS LKLSSSSRTE RYALNSSRPS QDEQEKEEDV
AERKKKEELH RKFVKKLGHP DSMFSYRQRD TESAAVEGEG EEGEDDEEEP APKTTAKKKG
AKTGKLTPME LQFLEIKRKH MDTLLIVEVG YKFRFFGEDA RIAARELSIV CIPGKFRYDE
HPSEAHLDRF ASASIPVHRL PVHAKRLVAA GYKVGVVRQI ETAALKKAGD NRNAPFVRKL
TNVYTKGTYI DETGELDQPG ETTGASSGGY LLCLTETPAK GMGTDEKVNV GIIAVQPATG
DIIYDEFEDG FMRREIETRL LHISPCEFLI VGDLSKATDK LIQHLSGSST NVFGDKSRVE
RVPKSKTMAA ESYSNVTDFY AGKAKDSDER SAALLNKVLK LPEAVMICLS AMITHLTEYG
LQHIFDLTKY FQSFSTRQHM LINGTTLESL EVYRNATDHS EKGSLLWALD KTHTRFGQRL
LRKWIGRPLL DQQRLEERVS AVEELLNNQS TAKVDKLVNM LKSIKADLER SLIRIYYGKC
TRPELLSTLQ TLQKISFEYA RVKSPADTGF SSTLLTSAIM TLPSISPMVT AHLSKINAEA
ARKDDKYAFF LEQHETEDIS EHKLGIAAVE QDLDEHRSEA AKDLGKKVPV NYVTVAGIEY
LIEVPNTDLK RVPASWAKIS GTKKVSRFHT PTVLRLIAER DQHKESLASA CDQAFSDLLS
QIAGEYQPLR DAVSSLSTLD CLLSLSTVAA LPGYTKPTFL PSSHPSFLSI TEGRHPIAEH
LLPNGYIPFT MSLGTLSSSA SSPDPNPTSP SGKPALAQLI TGPNMGGKSS YTRAVALLVL
LAQIGSFVPA TSMSLTLSDA IFTRMGARDN LFKGESTFMV EVSETAAILR QATPRSLVVL
DELGRGTSTH DGRAIAGAVL EYVVRDVGCL MLFVTHYQDL AGVAEGLTVG EGEEKRRGVE
CVHMRFASNK SRTSMDDDAM EVDGDGDGQE GAGADKDEEE EITFLYDLAP GVAHRSYGLN
VARLARIPRK VLEVAARKSS ELEKEVRAKR IKGAMGLVGG VLYGGGAPGD QEEKLEQLVG
LVEQL
