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MSH3_PICGU
ID   MSH3_PICGU              Reviewed;         960 AA.
AC   A5DEV6;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=DNA mismatch repair protein MSH3;
DE   AltName: Full=MutS protein homolog 3;
GN   Name=MSH3; ORFNames=PGUG_01807;
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS   / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(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}.
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DR   EMBL; CH408156; EDK37709.2; -; Genomic_DNA.
DR   RefSeq; XP_001486136.1; XM_001486086.1.
DR   AlphaFoldDB; A5DEV6; -.
DR   SMR; A5DEV6; -.
DR   STRING; 4929.XP_001486136.1; -.
DR   EnsemblFungi; EDK37709; EDK37709; PGUG_01807.
DR   GeneID; 5127810; -.
DR   KEGG; pgu:PGUG_01807; -.
DR   eggNOG; KOG0218; Eukaryota.
DR   HOGENOM; CLU_002472_0_2_1; -.
DR   InParanoid; A5DEV6; -.
DR   OMA; LRNVHMK; -.
DR   OrthoDB; 138168at2759; -.
DR   Proteomes; UP000001997; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; 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; 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; 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; 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..960
FT                   /note="DNA mismatch repair protein MSH3"
FT                   /id="PRO_0000338528"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          53..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          87..209
FT                   /note="Mispair-binding domain"
FT                   /evidence="ECO:0000250"
FT   BINDING         734..741
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   960 AA;  107853 MW;  BEBEC1746CB4720D CRC64;
     MKRGIDIVQA LKNSKRSKSS DDSVESKLSK ASPDLSQYAA VQISKEDVTV NPEVKSTIDN
     HKKEPPSIAS SIKKSPKTVI GKHANSTKKP KKRTPLDQQF IDLKNEYPDC VLAIQVGYKY
     KFFGVDAVPV SRILNIMFIP GNLTERDATH DKFAYCSVPD NRLHIHLQRL LTNGLKVAVV
     SQTESAVLRE AESSKGLFLR EVTAIYTKAT YIEEGSGDFI SCITWNGTSA GAVTVQPCTG
     EIIVEDFSEK EPEALSELQT YLHHLRPSEI IVTDNEATKE NDKLSRLLKS FGGARISYKP
     FDEVSPIEEL LPASIANYYV TNHSTTTTQC ISQLITYLKD FSLDQIFTVP SNVSKFSTKM
     YMNLPGNTLK ALEIFQNSSG TEKGTLFWHL DHTHTKMGRR MLQKWVSKPL IDNASIQERL
     DAIESLMNYN YAVEVFEGII KKIGRDESDW EKSMIKIHYT ANGSQNRVTR KEVVQLLLQF
     RSVIDTVYKF KSSFKDSSIS KLLQSMFSEL AELASTPIVN DLLSRVKIEA VYREEVEDQK
     KEFFDLDSHP HEGIKSELNA ISELEQALQD ELVEIKKIIK KPVDYMTVSR EPYLIALRGD
     SGPQDWLKIS ATKTVTRYRP PKVSKLYKEL LYHQEKLIQQ CDEAFATFLK DIDSHYTYFS
     RLIKIVAEID CLLSLKATSS SNSGYSKPIL SDKQMIKAKR SRNPVIENLT STSQYVANDI
     EISYDENRVL IITGPNMGGK SSYVKQVALI ALMTQIGCYL PCESAIVGIF DTILVRMGAE
     DNILKGESTF MVEMSECSTI IKSLTNKSLV ILDEIGRGTG TEDGIAIAYS IISYLIEEPR
     LPLTLFITHY PSLKVLEDTH PKNVANYHMG FMEVAKADQE WPDVTFLYTL KRGVVSNSYG
     LNVARLAGIP SEIITKAFKV AEALKQDIED SELSSMGQIL KSEQSSASKL VEIDRIVSYI
 
 
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