MSH3_EMENI
ID MSH3_EMENI Reviewed; 1105 AA.
AC Q5B6T1; C8V799;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=DNA mismatch repair protein msh3;
DE AltName: Full=MutS protein homolog 3;
GN Name=msh3; ORFNames=AN3749;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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 -!- SEQUENCE CAUTION:
CC Sequence=CBF75474.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAA59957.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AACD01000061; EAA59957.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001302; CBF75474.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_661353.1; XM_656261.1.
DR AlphaFoldDB; Q5B6T1; -.
DR SMR; Q5B6T1; -.
DR STRING; 162425.CADANIAP00004973; -.
DR EnsemblFungi; EAA59957; EAA59957; AN3749.2.
DR GeneID; 2873172; -.
DR KEGG; ani:AN3749.2; -.
DR eggNOG; KOG0218; Eukaryota.
DR HOGENOM; CLU_002472_0_0_1; -.
DR InParanoid; Q5B6T1; -.
DR OrthoDB; 138168at2759; -.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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; 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; 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..1105
FT /note="DNA mismatch repair protein msh3"
FT /id="PRO_0000338521"
FT REGION 1..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..316
FT /note="Mispair-binding domain"
FT /evidence="ECO:0000250"
FT COMPBIAS 8..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 877..884
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1105 AA; 122140 MW; FDFBFAC11D59626F CRC64;
MPLPSSQPSA SSSPNLKRKQ PTISSFFTKK PQAPKQSTSN EGPAPIDNDS EITDKLAEDD
EEDIVAPVPK RTKSNGSLTV NRPQSPKAKS VSRVEQESSQ RTELSKFASS PAIETEGNEA
TELDGSAKVR QQEREKLHQR FVRKLGGPDC LVGIGRNCVG ETTSIEEAAE GDEDDETPQP
VQPKGKAGKK GGGKLTPMEK QVIEIKKKHM DTILLIEVGY KFRFFGEDAR IAAKELSIVC
IPGKFRYDEH PSEAHLDRFA SASIPVQRLH VHVKRLVAAG HKVGVVRQLE TAALKAAGDN
RNAPFVRKLT NVYTKSTYID DIESLEGSTA GASGASATGY ILCITETNAR GWGNDEKVHV
GIVAVQPTTG DIVYDEFDDG FMRSEIETRL LHIAPCEMLI VGELSKATEK LVQHLSGSKM
NVFGDKVRVE RAPKAKTAAA ESHSHVSSFY AEKMKSADAA DDEVASNLLQ KVLGLPDQVT
ICLSAMIKHM TEYGLEHVLQ LTKYFQHFSS RSHMLLNGNT LTSLEIYQNQ TDYSSKGSLF
WTLDRTQTRF GQRMLRKWVG RPLLDRRQLE DRVNAVEELK DFRNVVMVER IKGLLGKIKH
DLEKGLIRIY YGKCSRPELL TILQTMQMIA QEFADIESPA DTGFSSPAIS QAIMSLPTIL
KDVVFFLNKI NMHAARNDDK YEFFREEEET EEISEHKLGI GAVEHELEEH RPVAGEALGK
KMVTYVSVAG IDYLVEVENN SPAIKRVPAS WMKISGTKKV SRFHTPEVVK MIRQRDQHRE
ALAAACDKAF LALQAEIATN YQALRDCVQS LATLDCLVSL ATLASQPGYV KPEYTEETCI
HVEQGRHPMV EQLLLDSYVP NDINLDSSKT RALLVTGPNM GGKSSYVRQV ALIAIMGQIG
SYVPAQAAKL GMLDAVFTRM GAFDNMLAGE STFMVELSET ADILKQATPR SLVILDELGR
GTSTHDGVAI AQAVLDYMVR SIRSLTLFIT HYQHLSAMVH SFPDGELRNV HMRFSESGTG
ADEDITFLYE IGEGVAHRSY GLNVARLANL PAPLLEMAKQ KSAELEEKIR RRRLAGFVAA
VGAVVQSNQA DESVIERLVS SMEEL
