MSH2_DICDI
ID MSH2_DICDI Reviewed; 937 AA.
AC Q553L4; Q86HA1;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=DNA mismatch repair protein Msh2;
DE AltName: Full=MutS protein homolog 2;
GN Name=msh2; ORFNames=DDB_G0275809;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Component of the post-replicative DNA mismatch repair system
CC (MMR). Forms two different heterodimers: MutS alpha (msh2-msh6
CC heterodimer) and MutS beta (msh2-msh3 heterodimer) which binds to DNA
CC mismatches thereby initiating DNA repair. When bound, heterodimers bend
CC the DNA helix. MutS alpha recognizes single base mismatches and
CC dinucleotide insertion-deletion loops (IDL) in the DNA. MutS beta
CC recognizes larger insertion-deletion loops. After mismatch binding,
CC MutS alpha or beta 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. The ATPase activity associated with MutS alpha
CC regulates binding similar to a molecular switch: mismatched DNA
CC provokes ADP-->ATP exchange, resulting in a discernible conformational
CC transition that converts MutS alpha into a sliding clamp capable of
CC hydrolysis-independent diffusion along the DNA backbone. This
CC transition is crucial for mismatch repair. MutS alpha may also play a
CC role in DNA homologous recombination repair (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer consisting of msh2-msh6 (MutS alpha) or msh2-msh3
CC (MutS beta). Both heterodimers form a ternary complex with MutL alpha
CC (mlh1-pms1). Interacts with exo1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000013; EAL69655.1; -; Genomic_DNA.
DR RefSeq; XP_643399.1; XM_638307.1.
DR AlphaFoldDB; Q553L4; -.
DR SMR; Q553L4; -.
DR STRING; 44689.DDB0229897; -.
DR PaxDb; Q553L4; -.
DR EnsemblProtists; EAL69655; EAL69655; DDB_G0275809.
DR GeneID; 8619985; -.
DR KEGG; ddi:DDB_G0275809; -.
DR dictyBase; DDB_G0275809; msh2.
DR eggNOG; KOG0219; Eukaryota.
DR HOGENOM; CLU_002472_10_0_1; -.
DR InParanoid; Q553L4; -.
DR OMA; LFRIYQV; -.
DR PhylomeDB; Q553L4; -.
DR Reactome; R-DDI-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
DR Reactome; R-DDI-5358606; Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
DR PRO; PR:Q553L4; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0032301; C:MutSalpha complex; ISS:dictyBase.
DR GO; GO:0032302; C:MutSbeta complex; ISS:dictyBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISS:dictyBase.
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; ISS:dictyBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; ISS:dictyBase.
DR GO; GO:0006298; P:mismatch repair; ISS:dictyBase.
DR GO; GO:0006312; P:mitotic recombination; IBA:GO_Central.
DR GO; GO:0006301; P:postreplication repair; ISS:dictyBase.
DR Gene3D; 3.30.420.110; -; 1.
DR Gene3D; 3.40.1170.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR011184; DNA_mismatch_repair_Msh2.
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; IPR032642; Msh2.
DR InterPro; IPR036678; MutS_con_dom_sf.
DR InterPro; IPR045076; MutS_family.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11361; PTHR11361; 1.
DR PANTHER; PTHR11361:SF35; PTHR11361:SF35; 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; PIRSF005813; MSH2; 1.
DR SMART; SM00534; MUTSac; 1.
DR SMART; SM00533; MUTSd; 1.
DR SUPFAM; SSF48334; SSF48334; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF53150; SSF53150; 1.
DR PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell cycle; DNA damage; DNA repair; DNA-binding;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..937
FT /note="DNA mismatch repair protein Msh2"
FT /id="PRO_0000328238"
FT REGION 635..709
FT /note="Interaction with exo1"
FT /evidence="ECO:0000250"
FT BINDING 707..714
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 937 AA; 104962 MW; 2D24BB8DB9370EA1 CRC64;
MSDNEQEESS QVVLKEDKTF VTFFQSLVSS NEDTDTIRLF DRKGYYSIHG EDAVFVAMMH
FKSKKSLKYW SISDPNPKKK IKIDNDGSLT TTASSSQQQQ QELGLAVLTI RQGYEFENIV
KELLDEKKKI EIWSMKPNSK QQWELIKKGS PGNTQMFEDV LLNGNCEGSV MMALKVTREK
GSIVFGISFG DATFKTIGVS QFMDNDNLSN LSSFIMQMSV KECLLCCDQK NYDYQKVKEK
LSDAGIPFTE LPKSDFSSKN AEQDLTRLLG SVKNNLPDIE QEHAIQSASC LIKHLDLLSN
PNYFGKFKLE KYDLDRYMKL DSSSFKGLHI IDLKDSSVSA AAGGGGAGGA SSSSNKDQSL
YNLLNQCNTP MGSRLLLQWV KQPLLNAEEI EARLNFVEAF YNDLELRQSL RSNDLKKIGD
LDRLSKKLHG QKATLEDCVN LYGIVTRLPV VLQSLNNHSS IHQELIKVNF IESLESIISD
FAKFCAMVEK TIDLDLANDK HEYVIRSSFD ETLRGIQLKK DQISNKIERF RVDIADDLNL
DEAKVKLHYS EKDMFLLRIS RKDEVAIRDK KKYIVHATAK DGVRFATREI DTLNEAYKKW
SAEYLDKQDG LAKRTLQIAA SFVPLIEDLS SLIATLDVFV TLSHVSSIAP IPFIRPEIIP
LGSDENGAGT VIIGGRHPCV EIQDNVNFIA NDIDLTRGQS QFQIITGPNM GGKSTFIRQV
GLIVLMAQIG CFVPAQKATI AVVDCILSRV GAGDSQLRGV STFMAEMLET SYILKVATKN
SLIIIDELGR GTSTYDGFGL AWGIAEYICN QIGGFCLFAT HFHELTILSD LLPMVKNLHV
SASTQNNTFT LLYKVEQGPC DQSFGIHVAI LANFPSQVIE NAKQKAKELE SFESNTLKQN
HNKFLEEFKE INFNSNDVEK SLSLVNSLLN KYSIDIN
