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MSH3_PICST
ID   MSH3_PICST              Reviewed;        1025 AA.
AC   A3LU10;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 3.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=DNA mismatch repair protein MSH3;
DE   AltName: Full=MutS protein homolog 3;
GN   Name=MSH3; ORFNames=PICST_59113;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
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=ABN66162.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000498; ABN66162.2; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_001384191.2; XM_001384154.1.
DR   AlphaFoldDB; A3LU10; -.
DR   SMR; A3LU10; -.
DR   STRING; 4924.XP_001384191.2; -.
DR   PRIDE; A3LU10; -.
DR   EnsemblFungi; ABN66162; ABN66162; PICST_59113.
DR   GeneID; 4838728; -.
DR   KEGG; pic:PICST_59113; -.
DR   eggNOG; KOG0218; Eukaryota.
DR   HOGENOM; CLU_002472_0_0_1; -.
DR   InParanoid; A3LU10; -.
DR   OrthoDB; 138168at2759; -.
DR   Proteomes; UP000002258; Chromosome 4.
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; 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..1025
FT                   /note="DNA mismatch repair protein MSH3"
FT                   /id="PRO_0000338529"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          114..235
FT                   /note="Mispair-binding domain"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        1..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         792..799
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1025 AA;  117247 MW;  40D6FDAC3D958A94 CRC64;
     MSYRSKQASI SRFFKSTKSN NSAKNEPAVQ HIPKKTGVML KFSYNNKENV VEGGKDTEGP
     HIVGSHVELP GQSVNSVVNS DSIVVNSNLE IDPKISSVLK RKPDIDIQLK TTKKRSKTLT
     PLEKQIRELR ESHKDKVLVI QIGYKYKMFG DDAKLGSKIL DIMYIRGGDD GTRDEFSYCS
     FPDFKLHINL KRLLTHGLKI GVVKQLESAI VKTVEKSSKS SDLMKREITG VYTRGTYMGD
     EYVQSSGNSA DTESPYYIIC INEINQKELS MVAVQPKTGD IVQDTFKDGL NRDELETRLM
     YLNPSEVIVL SSEQPSVETL KTIRLVASDV QLLPRKRKGE DEVFNGLIEF FDSIDNGKYK
     HLGDYFSVNF SKHIQSCFYE LINYLSEFKL SNVFTIPDNI SNFTNSRKYM VLPNNTLYAL
     EIFQNYTNPA SQKGTLIWLL NHTRTRFGNR LLNKWVSKPL IEKEKIEERL LAIEDLTGDF
     NNVVDALKIQ LDKMGKSLDL EELLMKTHYA ATYNLDKINR RDIYNMLDCF QSVLESMNRF
     EKGITEFSKT KKSPLLTNIL LELSEMSKTT VVSNLLNKIN RSYVMNESKD PEEQVTQFFN
     LDNHNWEDIR SEFSELDKIE KLFEEELLNI RRVLKRPQLQ YITNNKEPYL IEVRNGKQVD
     ELPTDFHRIN GTTTVSRFRS ERTAQLYIKK QYHKEKLLVN CNVAFNDFLK EIDEQYEFFS
     KIVKNLSVFD CLLSLTAASL ASKNTRPILV DQQLIEVQKG RNPIIESLHN RNDYVPNDID
     ICYDNKVLII TGPNMGGKSS YVKQVALLVI MSQIGCYIPC DRATLGVFDS IFIRMGASDN
     ILKGNSTFMN EMLECSNIIH GISNKSLVIL DEIGRGTGTS DGIALAYSIL RYLIESPLRP
     LVLFITHYPS LHVLEDSFPT VVTNYHMGFQ QIHKDDNDFP EIIFLYNLVK GVINNSYGLN
     VAKLAGLPVS VISGAHRVSE SLKYKVEIQQ KEQFTMKFGS ILQMLKKDEI NSNNILELEN
     LFSYI
 
 
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