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MSH3_DICDI
ID   MSH3_DICDI              Reviewed;        1428 AA.
AC   Q1ZXH0;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=DNA mismatch repair protein Msh3;
DE   AltName: Full=MutS protein homolog 3;
GN   Name=msh3; ORFNames=DDB_G0281683;
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 beta, which binds to DNA
CC       mismatches thereby initiating DNA repair. When bound, the MutS beta
CC       heterodimer bends the DNA helix and shields approximately 20 base
CC       pairs. MutS beta recognizes large insertion-deletion loops (IDL) up to
CC       13 nucleotides long. After mismatch binding, forms a ternary complex
CC       with the MutL alpha heterodimer, which is thought to be responsible for
CC       directing the downstream MMR events, including strand discrimination,
CC       excision, and resynthesis (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer consisting of msh2-msh3 (MutS beta). Forms a
CC       ternary complex with MutL alpha (mlh1-pms1). Interacts with exo1 (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family. MSH3
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AAFI02000042; EAS66875.1; -; Genomic_DNA.
DR   RefSeq; XP_001134558.1; XM_001134558.1.
DR   AlphaFoldDB; Q1ZXH0; -.
DR   SMR; Q1ZXH0; -.
DR   STRING; 44689.DDB0232960; -.
DR   PaxDb; Q1ZXH0; -.
DR   EnsemblProtists; EAS66875; EAS66875; DDB_G0281683.
DR   GeneID; 8623184; -.
DR   KEGG; ddi:DDB_G0281683; -.
DR   dictyBase; DDB_G0281683; msh3.
DR   eggNOG; KOG0218; Eukaryota.
DR   HOGENOM; CLU_002472_0_2_1; -.
DR   InParanoid; Q1ZXH0; -.
DR   OMA; LRNVHMK; -.
DR   PhylomeDB; Q1ZXH0; -.
DR   Reactome; R-DDI-5358606; Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
DR   PRO; PR:Q1ZXH0; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0032302; C:MutSbeta complex; ISS:dictyBase.
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:0032135; F:DNA insertion or deletion binding; ISS:dictyBase.
DR   GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR   GO; GO:0006310; P:DNA recombination; ISS:dictyBase.
DR   GO; GO:0006298; P:mismatch repair; ISS:dictyBase.
DR   GO; GO:0006312; P:mitotic recombination; ISS:dictyBase.
DR   GO; GO:0000735; P:removal of nonhomologous ends; 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; 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; 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   Reference proteome.
FT   CHAIN           1..1428
FT                   /note="DNA mismatch repair protein Msh3"
FT                   /id="PRO_0000328253"
FT   REGION          1..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          405..451
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          592..612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..98
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..127
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..167
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..205
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..258
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        259..287
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..307
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        424..440
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        592..607
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1428 AA;  161570 MW;  9634B4FBA4E20C8C CRC64;
     MPRLKLPKSF KDELESEKTT TTSSRKKAPV VDPKQTLMSS FFTPVSKSTD TKEINNKEDK
     DEDKDKDKDN KKTKKSKDTS DNEDMVDDNN KQQKEKKATP NKSNSPQSPQ TSKSPLTRRS
     SANGNSDSKI DNKEKEKEKE KEKEKDKSTP TKTTSSRVKK DTEVSKSIPP KLSKQTKKKQ
     ISSDNDIYDD EKDSEEEDLE DDHDDEEEKV VVKKPSKPTS KSITAKPAST KATTTTTTTT
     TTTSTGRTRV NRVNLDISFS SESEEDEKPK KKIIGKKRKK KDDSDFDSES ESDTISEASE
     VEPESEEDLD SFKFNSKKKN NNKNNNNKKK NDEYEDEEED EDDELFKDIE MKDKPEEEEK
     EEEGDPIVIG SGRVVLPKGT PDFQPDPKAG KKLLKAHLEI QSKEEAKRLQ QANGGGGDGG
     GGQIKGSDDE DEEVKKPTKG GSKASAKKKG PAYTPLEQQY IAIKKENPDT VLMVECGYKY
     KFFGEDAEVA NKVLNIYSYV AKNFLNCSIP TQRLFFHLRR LVMAGYKVGI VEQTETAALK
     AISSSKSQPF ERKLTRVYTS STFIDDDIDD QLTSSSPQFL VSFYESTPKN KNDDVIKKQR
     DNEEEGIDSS NESSTSTISF VAVSVKTGEI IYDTFKDNVM RSQLETILTH IKPSEILIPP
     TTTTVNKQKV NNGIGTNHYY FSNLTSKCLK TYTKSTNVRT QAMDSQLYDY EYSLGKLIDF
     YEDESNNNNN NNNCEDVLKF VKSTLNKEQI ICLGILLSYL NEFIHFGSIL KVESNFKAFR
     VSNHLVLPHS TIVNLELLVN ESDNKEKGSL IWLMNRTSTF SGSRMFINWI CKPLNQLELI
     KERQDAVEEL VNGIKTNSPP IVSIISLFKS HIPDLQRNLS RIYYKVQCTP KEFLNTMTSL
     QRIVELFKEI NNNNSSYKFN STLLNSIFKL QNDNKDGDSD SFDYIGGEDK LSKRIKYFLS
     NINKETAKEY GTVGCDKSNL WVDLEKYEKI RETKEKIEQV EKEFKNVLKN IRKELSKPSL
     EYHHMPGLGL EYLLELPPSF KAVPKSWIKV NSTQKMARYH APEVLEQLKI LSQSRETLKI
     QSQESWISFL GEFSVDYSLF SNFVNKISNL DCLFSLAKVS SLEGYIRPQF VKEKKDGGIQ
     IENGRHPVVE AILSGSDGSY VPNTIELRES ACKSMIITGP NMGGKSSLLR QTALIVIMAQ
     VGCFVPATSC SLSVFDAIYT RMGARDSIGT GKSTFFIELE ETSDILKNST QNTLVILDEL
     GRGTSTNDGV AIAYSTLKYI VEVMKCYCLF VTHYPLLAQL ELQYPTQVGN FHMGYLEEKQ
     DQQLQKSVIP KVIFLYKLVK GAAQNSYGLN IARLAGLPME VIADALKKSN EMKESITRRA
     NLSDGKDQQQ IENEIKSIIK NWNSNRTTLN SNDLLQFIEK FKSIQLKL
 
 
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