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MSH3_SCHPO
ID   MSH3_SCHPO              Reviewed;         993 AA.
AC   P26359;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=DNA mismatch repair protein msh3;
DE   AltName: Full=Mating-type switching protein swi4;
DE   AltName: Full=MutS protein homolog 3;
GN   Name=msh3; Synonyms=swi4; ORFNames=SPAC8F11.03;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=1317550; DOI=10.1093/nar/20.9.2271;
RA   Fleck O., Michael H., Heim L.;
RT   "The swi4+ gene of Schizosaccharomyces pombe encodes a homologue of
RT   mismatch repair enzymes.";
RL   Nucleic Acids Res. 20:2271-2278(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   FUNCTION.
RX   PubMed=11333218; DOI=10.1093/genetics/158.1.65;
RA   Tornier C., Bessone S., Varlet I., Rudolph C., Darmon M., Fleck O.;
RT   "Requirement for Msh6, but not for Swi4 (Msh3), in Msh2-dependent repair of
RT   base-base mismatches and mononucleotide loops in Schizosaccharomyces
RT   pombe.";
RL   Genetics 158:65-75(2001).
RN   [4]
RP   FUNCTION.
RX   PubMed=11333219; DOI=10.1093/genetics/158.1.77;
RA   Mansour A.A., Tornier C., Lehmann E., Darmon M., Fleck O.;
RT   "Control of GT repeat stability in Schizosaccharomyces pombe by mismatch
RT   repair factors.";
RL   Genetics 158:77-85(2001).
RN   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
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). Involved in termination of copy-
CC       synthesis during mating-type switching. {ECO:0000250,
CC       ECO:0000269|PubMed:11333218, ECO:0000269|PubMed:11333219}.
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:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family. MSH3
CC       subfamily. {ECO:0000305}.
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DR   EMBL; X61306; CAA43603.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB52164.2; -; Genomic_DNA.
DR   PIR; S22569; S21964.
DR   RefSeq; NP_593952.1; NM_001019379.2.
DR   AlphaFoldDB; P26359; -.
DR   SMR; P26359; -.
DR   STRING; 4896.SPAC8F11.03.1; -.
DR   iPTMnet; P26359; -.
DR   PaxDb; P26359; -.
DR   PRIDE; P26359; -.
DR   GeneID; 2543392; -.
DR   KEGG; spo:SPAC8F11.03; -.
DR   PomBase; SPAC8F11.03; msh3.
DR   eggNOG; KOG0218; Eukaryota.
DR   HOGENOM; CLU_002472_0_1_1; -.
DR   InParanoid; P26359; -.
DR   PhylomeDB; P26359; -.
DR   Reactome; R-SPO-5358606; Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
DR   PRO; PR:P26359; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0000228; C:nuclear chromosome; ISO:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0035861; C:site of double-strand break; IDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0000406; F:double-strand/single-strand DNA junction binding; ISO:PomBase.
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:0006281; P:DNA repair; NAS:PomBase.
DR   GO; GO:0007534; P:gene conversion at mating-type locus; IMP:PomBase.
DR   GO; GO:0043570; P:maintenance of DNA repeat elements; IMP:PomBase.
DR   GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
DR   GO; GO:0006312; P:mitotic recombination; IBA:GO_Central.
DR   GO; GO:0007131; P:reciprocal meiotic recombination; IMP:PomBase.
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; 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..993
FT                   /note="DNA mismatch repair protein msh3"
FT                   /id="PRO_0000115196"
FT   REGION          97..211
FT                   /note="Mispair-binding domain"
FT                   /evidence="ECO:0000250"
FT   BINDING         759..766
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        499
FT                   /note="R -> RCTPSEMFHVLK (in Ref. 2; CAB52164)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   993 AA;  113362 MW;  44B80E553A59B708 CRC64;
     MRGMSYNITH ECDAINILSD NLHEGAISED MVALSGPAIE LLENNVGSSK NSYQEDEGSS
     SIDENAPLIS IKRKRRIRTV KSTSNKELVQ RKASKPTKQK SVFTPLEQQY LELKKNYQET
     ILAIEVGYKF RFFGKDAKIA SEVLGISCYF EHNFLNASVP SYRIDYHLER LINFGLKVAV
     VRQTETAALK STSSSRNTLF DRRVARVLTK GTTLDDSFFR FEQTQHGTLQ ASQFILCVAD
     NVDKSKAKSG RVQVGLIAIQ LSSGTTVYDH FQDDFLRSEL QTRLSHFQPC ELIYSNKLSS
     ESVALLNHYV STEKTCGRVV RVQHAVQQDV KLALENLQDF FSSKCIMSGS KIIELHMEKV
     KSLHSLSIIC LDMAISYLME FSLEDLFVAS NFYQPFDSIS SMVLSKQALE GLELFVNQTD
     HTPVGSLFWV LDRTYTRFGQ RMLQRWLQKP LVDKENIIER LDAVEELAFN SNSQVQAIRK
     MLYRLPDLEK GLSRIYYQRG FYKAASAFSK NSYSCFKSAL LRRLIQQLPS ISSIIDHFLG
     MFDQKEAENN NKVDMFKDID NFDLSEEPND VDYELAQEIR ELKMSILMVR TEMDFHLQEL
     RDYLEYPNLE FSIWGNVKFC IEVSKGCKKI PPDWIKLSST RSLFRFHTPK IQSLLIELSS
     HEENLTISSE KIYRSFLSRI SEHYNELRNV TTVLGTLDCL ISFARISSQS GYTRPEFSDK
     ELLIHESRHP MIELLSDKSF VPNHIHLSSD GVRCLLITGP NMGGKSSFVK QLALSAIMAQ
     SGCFVPAKSA LLPIFDSILI RMGSSDNLSV NMSTFMVEML ETKEVLSKAT EKSMVIIDEL
     GRGTSTIDGE AISYAVLHYL NQYIKSYLLF VTHFPSLGIL ERRFEGQLRC FHMGYLKSKE
     DFETSVSQSI SFLYKLVPGV ASKSYGLNVA RMAGIPFSIL SRATEISENY EKKHRNARKN
     VFIRKVAKLL MILNAEEIDF KRLFYDLTAF EEI
 
 
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