MSH6_DICDI
ID MSH6_DICDI Reviewed; 1260 AA.
AC Q55GU9;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=DNA mismatch repair protein Msh6;
GN Name=msh6; ORFNames=DDB_G0268614;
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=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). Heterodimerizes with msh2 to form MutS alpha, which binds to DNA
CC mismatches thereby initiating DNA repair. When bound, MutS alpha bends
CC the DNA helix and recognizes single base mismatches and dinucleotide
CC insertion-deletion loops (IDL) in the DNA. After mismatch binding,
CC forms a ternary complex with the MutL alpha heterodimer, which is
CC thought to be responsible for directing the downstream MMR events,
CC including strand discrimination, excision, and resynthesis. ATP binding
CC and hydrolysis play a pivotal role in mismatch repair functions. The
CC ATPase activity associated with MutS alpha regulates binding similar to
CC a molecular switch: mismatched DNA provokes ADP-->ATP exchange,
CC resulting in a discernible conformational transition that converts MutS
CC alpha into a sliding clamp capable of hydrolysis-independent diffusion
CC along the DNA backbone. This transition is crucial for mismatch repair.
CC MutS alpha may also play a role in DNA homologous recombination repair
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer consisting of msh2-msh6 (MutS alpha). Forms a
CC ternary complex with MutL alpha (mlh1-pms1). Interacts with exo1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000003; EAL73760.1; -; Genomic_DNA.
DR RefSeq; XP_647085.1; XM_641993.1.
DR AlphaFoldDB; Q55GU9; -.
DR SMR; Q55GU9; -.
DR STRING; 44689.DDB0229918; -.
DR PaxDb; Q55GU9; -.
DR PRIDE; Q55GU9; -.
DR EnsemblProtists; EAL73760; EAL73760; DDB_G0268614.
DR GeneID; 8615889; -.
DR KEGG; ddi:DDB_G0268614; -.
DR dictyBase; DDB_G0268614; msh6.
DR eggNOG; KOG0217; Eukaryota.
DR HOGENOM; CLU_002472_1_0_1; -.
DR InParanoid; Q55GU9; -.
DR OMA; TPMMAQY; -.
DR PhylomeDB; Q55GU9; -.
DR Reactome; R-DDI-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
DR PRO; PR:Q55GU9; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0032301; C:MutSalpha complex; ISS:dictyBase.
DR GO; GO:0005634; C:nucleus; ISS:dictyBase.
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:0006298; P:mismatch 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; 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; SSF53150; SSF53150; 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..1260
FT /note="DNA mismatch repair protein Msh6"
FT /id="PRO_0000328561"
FT REGION 1..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..295
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1260 AA; 142747 MW; 4A3DEA3D20B03584 CRC64;
MKPNNMKQTN ISQFFAPTKQ PEPIIEEGFD SFFDDIPTEE LEPDLNSIPI SSSQQTSTSN
TSSQQTSSAN TSSSATTTTT TNTNSQIPKA PTTPSKLKLP TSFTSKSNTP TKSLPPSNFS
LVVNEQEEEN EMNDNSKPQQ QQQQQQQQNL FKSNITSNSG GSSNDLFSRF KDEKPKTTTT
LSTPSKPLSQ PQRNNTNEIS KKRKEMDFNE DESNTNYDNN NNDVEDLDEF CFVNKNKPSS
SSSSLNTNTT TTPKAPTITP KTPTKTPTRR PVVTYDEDDD DDEQDDDEDD DDDDDDKKSK
STTTTAVKKK GNAFGKKDKK EIEERYSFLV NIKDANGNPK DHPDYDKRTL HIPASCLSKF
SPFERQFWDI KSKNYDTVVF FKKGKFYELY ESDADIGHQQ LHLKLTDRVN MRMVGVPEMS
FNHWASKLIH LGHKVAKVDQ METSIGMAKR QNEKGGRNKK DSIIQRELTS ILTAGTLLDE
QMITDQTSTY LMAIKENEYD KQYGVCFVDV SIGEFYLCTI QDDDNRMQFE TLLLQMMPKE
IVYEKGATSP KTISIMKRVL STVKPVMNAR LSLEYWDPTD TMERITQLCG GKTPETLCQM
KNEEYLMGAL GGCISYLMDI KIGNSVVEQA RFKRFNPLDI GNSMILDGQC LVNLEIFNNS
TDGSTEGTLF KLMDRCTTAF GKRMFRQWIC RPLANKNAIV DRQKAIEFLR DSPETLQKVT
AILNKLPDLE RMIARIRAQT SKISDLISVL NHFDNIHSKL LELLDEAEQI ESIHLRSCLF
MDNQQDNDDI DEQENSNNNN NIRYSGYPNL KPYIERVRKS FTIEQDRVVP SKGLFLEFDQ
CLGNIQSLEQ SFAKHLEEQK AHFKCNKIEY KHMGKEIYQI EIPVAFTKKL PAGFSLKSSS
SKVNRYHSPF VTKNLTSLLE ERDTYEVLSK EVLKKILSNF AIYFNHFQIA ITKLSQLDCL
LSLYKVSFQS SIQMCRPLFV SSDQRGFIDV KDMRHPCIYS KSGDDFIPND ISLNTENNPP
SLMVLTGPNM GGKSTLLRQS CILVIMAQMG CYVSASSCEM SIVDRIFTRL GANDNILAGQ
STFMVELAET SAVLKYATKR SLVILDELGR GTSTFDGYSI AYSVLNYLAT KVQSMCIFAT
HYQSLAYEPT VRDLISTAYM TCHVDEEAKK VIFLYKLASG VCPNSYGLHV ASMAGLPREI
ITKAEEKSTQ MEKDSVLVSF IHGTISRSKL VEKIVQSYKQ KDLNQLIQLS NTLKDLNLNK
