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MUTS_LIMRD
ID   MUTS_LIMRD              Reviewed;         881 AA.
AC   A5VIW9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=DNA mismatch repair protein MutS {ECO:0000255|HAMAP-Rule:MF_00096};
GN   Name=mutS {ECO:0000255|HAMAP-Rule:MF_00096}; OrderedLocusNames=Lreu_0525;
OS   Limosilactobacillus reuteri (strain DSM 20016) (Lactobacillus reuteri).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=557436;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20016;
RX   PubMed=21379339; DOI=10.1371/journal.pgen.1001314;
RA   Frese S.A., Benson A.K., Tannock G.W., Loach D.M., Kim J., Zhang M.,
RA   Oh P.L., Heng N.C., Patil P.B., Juge N., Mackenzie D.A., Pearson B.M.,
RA   Lapidus A., Dalin E., Tice H., Goltsman E., Land M., Hauser L., Ivanova N.,
RA   Kyrpides N.C., Walter J.;
RT   "The evolution of host specialization in the vertebrate gut symbiont
RT   Lactobacillus reuteri.";
RL   PLoS Genet. 7:E1001314-E1001314(2011).
CC   -!- FUNCTION: This protein is involved in the repair of mismatches in DNA.
CC       It is possible that it carries out the mismatch recognition step. This
CC       protein has a weak ATPase activity. {ECO:0000255|HAMAP-Rule:MF_00096}.
CC   -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family.
CC       {ECO:0000255|HAMAP-Rule:MF_00096}.
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DR   EMBL; CP000705; ABQ82793.1; -; Genomic_DNA.
DR   RefSeq; WP_003667622.1; NZ_AZDD01000007.1.
DR   AlphaFoldDB; A5VIW9; -.
DR   SMR; A5VIW9; -.
DR   STRING; 557436.Lreu_0525; -.
DR   PRIDE; A5VIW9; -.
DR   EnsemblBacteria; ABQ82793; ABQ82793; Lreu_0525.
DR   GeneID; 66470645; -.
DR   KEGG; lre:Lreu_0525; -.
DR   PATRIC; fig|557436.17.peg.1805; -.
DR   eggNOG; COG0249; Bacteria.
DR   HOGENOM; CLU_002472_3_2_9; -.
DR   OMA; TPMMAQY; -.
DR   Proteomes; UP000001991; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR   GO; GO:0006298; P:mismatch repair; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.420.110; -; 1.
DR   Gene3D; 3.40.1170.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00096; MutS; 1.
DR   InterPro; IPR005748; DNA_mismatch_repair_MutS.
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   TIGRFAMs; TIGR01070; mutS1; 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..881
FT                   /note="DNA mismatch repair protein MutS"
FT                   /id="PRO_0000335171"
FT   BINDING         605..612
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00096"
SQ   SEQUENCE   881 AA;  99675 MW;  7C2A077E6EE05772 CRC64;
     MAKKTTPMME QYQKVKDQYP DAFLFYRLGD FYELFNDDAV KGAQLLELTL TTRNHSAKNP
     IPMCGVPHRA VNNYIDILID KGYKVAICEQ MEDPKKAKGM VKRAVTRLIT PGTQMDLNGE
     QARDNNYLAA ISGQNGVFSI AYTDLSTGEL KTTSLNNAND AVNELVNLQS KEVVVDGELP
     VEITTQFKQR NILQSHQPTV LKNAEISYLT QDLDDQAQQH VVALLVSYLL TTQKRSLAHM
     QKAIAYQPSS FMKIDHYSKT NLELMRNMRS GKRQGTLAWL LDETKTAMGS RLLKRWIDRP
     LINQNAISER QDKVQELLDH YFERSNLQQE LIKVYDLERL AGRVAYGSVN GRDLIQLKTS
     LKQVPKIKYV LETLDSPVFE ELQKQLDPLD DVADLIDQSI IEEPPIAVTE GGVIKDGYND
     QLDQYRDAMN NGKQWIVDLQ EHERKLTGIN NLKIGYNHVF GYYIEVTKVN LDKLPKDRYE
     RKQTLVNAER FSTPELKEKE ALIMGAQEKS TALEYDIFVK IREQVKGQIT RLQKLAQQLA
     ELDVLQSFAV VSEDYHFVRP EMNTGHVLKI KDGRHPVVEK FMGHQEYVPN DVLMGEDTDI
     LLITGPNMSG KSTYMRQLAL IAVMAQIGCF VPAKSAELPI FDQVFTRIGA ADDLISGEST
     FMVEMMEANN ALTHATDRSL ILFDEIGRGT ATYDGMALAQ AIIEYVHQHV RAKTLFSTHY
     HELTALENSL ARLKNVHVGA TEKDGELVFL HKVSAGPADK SYGIHVAKLA GMPSSLLKRA
     DTILQKLEQK DVKLPNTPKP ATDNYHTEPI SAKINEAAPV KKEAAPVVED NGQLELFATQ
     PEKKESSVDR RILHQLKELN LMGMTPMDVM NQIYKWQQKL K
 
 
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