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MUTL_VIBCH
ID   MUTL_VIBCH              Reviewed;         653 AA.
AC   Q9KV13;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=DNA mismatch repair protein MutL;
GN   Name=mutL; OrderedLocusNames=VC_0345;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
CC   -!- FUNCTION: This protein is involved in the repair of mismatches in DNA.
CC       It is required for dam-dependent methyl-directed DNA mismatch repair.
CC       May act as a 'molecular matchmaker', a protein that promotes the
CC       formation of a stable complex between two or more DNA-binding proteins
CC       in an ATP-dependent manner without itself being part of a final
CC       effector complex (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC       {ECO:0000305}.
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DR   EMBL; AE003852; AAF93518.1; -; Genomic_DNA.
DR   PIR; A82334; A82334.
DR   RefSeq; NP_229999.1; NC_002505.1.
DR   RefSeq; WP_000155485.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KV13; -.
DR   SMR; Q9KV13; -.
DR   STRING; 243277.VC_0345; -.
DR   DNASU; 2615058; -.
DR   EnsemblBacteria; AAF93518; AAF93518; VC_0345.
DR   KEGG; vch:VC_0345; -.
DR   PATRIC; fig|243277.26.peg.322; -.
DR   eggNOG; COG0323; Bacteria.
DR   HOGENOM; CLU_004131_5_1_6; -.
DR   OMA; ATQEQAW; -.
DR   BioCyc; VCHO:VC0345-MON; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0032300; C:mismatch repair complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
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; IBA:GO_Central.
DR   Gene3D; 3.30.1370.100; -; 1.
DR   Gene3D; 3.30.1540.20; -; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   HAMAP; MF_00149; DNA_mis_repair; 1.
DR   InterPro; IPR014762; DNA_mismatch_repair_CS.
DR   InterPro; IPR020667; DNA_mismatch_repair_MutL.
DR   InterPro; IPR002099; DNA_mismatch_repair_N.
DR   InterPro; IPR013507; DNA_mismatch_S5_2-like.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR038973; MutL/Mlh/Pms.
DR   InterPro; IPR014790; MutL_C.
DR   InterPro; IPR042120; MutL_C_dimsub.
DR   InterPro; IPR042121; MutL_C_regsub.
DR   InterPro; IPR037198; MutL_C_sf.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   PANTHER; PTHR10073; PTHR10073; 2.
DR   Pfam; PF01119; DNA_mis_repair; 1.
DR   Pfam; PF08676; MutL_C; 1.
DR   SMART; SM01340; DNA_mis_repair; 1.
DR   SMART; SM00853; MutL_C; 1.
DR   SUPFAM; SSF118116; SSF118116; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   TIGRFAMs; TIGR00585; mutl; 1.
DR   PROSITE; PS00058; DNA_MISMATCH_REPAIR_1; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA repair; Reference proteome.
FT   CHAIN           1..653
FT                   /note="DNA mismatch repair protein MutL"
FT                   /id="PRO_0000177989"
FT   REGION          375..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..398
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        408..422
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   653 AA;  72631 MW;  5D970C21A17C66FF CRC64;
     MTIRILPARL ANQIAAGEVV ERPASVVKEL VENSLDAGAT RIDIDLEKGG AKLIRIRDNG
     SGIDKDELGL ALSRHATSKI HTLDDLEAIM SLGFRGEALA SISSVSRLTL TSRTVAQEEA
     WSAYSEGRDM AVKLQPAAHP VGTTVEVLDL FFNTPARRKF LRTEKTEFTH IDELLKRIAL
     SRFDVSFTLR HNGKIVRQYR AATTLPQQEK RLAAVCGNPF VQHMLRIELE HQGLKLHGWI
     TTPEGARQQS DLQYCYVNGR MMRDKLINHA IRQSYETSLR VDQFATYVLF IELDPHQVDV
     NVHPAKHEVR FHQARLVHDF IYQALSSALV QGAQVMAPTI NEGAFHLPHC AEEVNPPVVP
     MIDTTQQERV WQAVQNTPDY PRKAPRDNDR DESDNPQVRE RAVSNPWVAS PKTASTGKER
     YGSASVSKKE AAVYQTLMQT PDLSDEEPST ASTIVSSIEA VKANIAIEKL GKAIQVVAGQ
     YLLMSSPQGC VLISLYQAQQ LKLRGLLNAQ HGALKAQPLL VPLALKLNES EWQVAQRHSS
     ALLQLGIELK SRTNHSIMVM AVPQPLRQQN LQQLLPDLLS YAASCSESQA LSHQALADWL
     TQRIVVEKRD YTLAEAIGLI AELEQLWQGN LPLQDPHFIT LVDFSASITA LHS
 
 
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