ID A0A1Y6FH12_9BACI Unreviewed; 638 AA.
AC A0A1Y6FH12;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=DNA mismatch repair protein MutL {ECO:0000256|HAMAP-Rule:MF_00149};
GN Name=mutL {ECO:0000256|HAMAP-Rule:MF_00149};
GN ORFNames=SAMN05444673_2140 {ECO:0000313|EMBL:SMQ72172.1};
OS Bacillus sp. OV166.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1882763 {ECO:0000313|EMBL:SMQ72172.1, ECO:0000313|Proteomes:UP000194454};
RN [1] {ECO:0000313|EMBL:SMQ72172.1, ECO:0000313|Proteomes:UP000194454}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV166 {ECO:0000313|EMBL:SMQ72172.1};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|HAMAP-Rule:MF_00149}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC {ECO:0000256|ARBA:ARBA00006082, ECO:0000256|HAMAP-Rule:MF_00149}.
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DR EMBL; FXWM01000001; SMQ72172.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y6FH12; -.
DR OrthoDB; 9763467at2; -.
DR Proteomes; UP000194454; Unassembled WGS sequence.
DR GO; GO:0032300; C:mismatch repair complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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:UniProtKB-UniRule.
DR CDD; cd16926; HATPase_MutL-MLH-PMS-like; 1.
DR CDD; cd00782; MutL_Trans; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.1540.20; MutL, C-terminal domain, dimerisation subdomain; 1.
DR Gene3D; 3.30.1370.100; MutL, C-terminal domain, regulatory subdomain; 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; IPR013507; DNA_mismatch_S5_2-like.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR002099; MutL/Mlh/PMS.
DR InterPro; IPR038973; MutL/Mlh/Pms-like.
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_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR00585; mutl; 1.
DR PANTHER; PTHR10073; DNA MISMATCH REPAIR PROTEIN MLH, PMS, MUTL; 1.
DR PANTHER; PTHR10073:SF12; DNA MISMATCH REPAIR PROTEIN MLH1; 1.
DR Pfam; PF01119; DNA_mis_repair; 1.
DR Pfam; PF13589; HATPase_c_3; 1.
DR Pfam; PF08676; MutL_C; 1.
DR SMART; SM01340; DNA_mis_repair; 1.
DR SMART; SM00853; MutL_C; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF118116; DNA mismatch repair protein MutL; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS00058; DNA_MISMATCH_REPAIR_1; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_00149};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_00149}.
FT DOMAIN 208..326
FT /note="DNA mismatch repair protein S5"
FT /evidence="ECO:0000259|SMART:SM01340"
FT DOMAIN 452..594
FT /note="MutL C-terminal dimerisation"
FT /evidence="ECO:0000259|SMART:SM00853"
FT REGION 397..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 638 AA; 71994 MW; C1DE19D909788F65 CRC64;
MGKIIQLDDA LSNKIAAGEV VERPASVVKE LVENSIDAGS TVIEIEVEEA GLAKIRITDN
GNGIEEEDVL LAFQRHATSK IKNENDLFRI RTLGFRGEAL PSVASVSRLE MKTSTGEGAG
NRLVIEGGKV ETFEKASSRR GTDISITDLF FNTPARLKYM KTIHTELGNI TDVVNRLALS
HPEVAFRLIH NDRKLLQTNG NGDVRQVLAS IYGMGIAKQL VPITGQSLDY KISGFASMPE
VTRASRNYIS TMINGRFIKN YPLAKAIQEG YHTLLPIGRF PIVLLNIEMD PLLVDVNVHP
SKMEVRISKE AELNELVTSI IKEAFKSKIL IPTAYTAVKK DVPKEEQTSL VLDEGTRPAP
DEKEFEWNQP VAAATILENR PWLEVPVETP VKKLPSFQRD EATGGRDSWQ SINPFSESDD
EPDVSNQTIE LNVDTVETGN VSVESRVPRL YPIGQMHGTY IFAQNENGLY IIDQHAAQER
LKYEYFREKV GQVQSELQEM LVPLTFEYST DEFLKINEYQ SELEKVGVFL EEFGLNSFIV
RSHPQWFPKG EEKQIIEDMI EQLLLMKKVD IKKLREEAAI MMSCKASIKA NRHLRNDEIQ
ALLDDLRKAS DPFTCPHGRP IIVHYSVYEM EKMFKRVM
//
