ID G2LI24_CHLTF Unreviewed; 656 AA.
AC G2LI24;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=DNA mismatch repair protein MutL {ECO:0000256|HAMAP-Rule:MF_00149};
GN Name=mutL {ECO:0000256|HAMAP-Rule:MF_00149};
GN OrderedLocusNames=Cabther_A0479 {ECO:0000313|EMBL:AEP11240.1};
OS Chloracidobacterium thermophilum (strain B).
OC Bacteria; Acidobacteriota; Blastocatellia; Chloracidobacterium.
OX NCBI_TaxID=981222 {ECO:0000313|EMBL:AEP11240.1, ECO:0000313|Proteomes:UP000006791};
RN [1] {ECO:0000313|EMBL:AEP11240.1, ECO:0000313|Proteomes:UP000006791}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:AEP11240.1,
RC ECO:0000313|Proteomes:UP000006791};
RX PubMed=21951563; DOI=10.1111/j.1462-2920.2011.02592.x;
RA Garcia Costas A.M., Liu Z., Tomsho L.P., Schuster S.C., Ward D.M.,
RA Bryant D.A.;
RT "Complete genome of Candidatus Chloracidobacterium thermophilum, a
RT chlorophyll-based photoheterotroph belonging to the phylum Acidobacteria.";
RL Environ. Microbiol. 14:177-190(2012).
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; CP002514; AEP11240.1; -; Genomic_DNA.
DR RefSeq; WP_014098978.1; NC_016024.1.
DR AlphaFoldDB; G2LI24; -.
DR STRING; 981222.Cabther_A0479; -.
DR KEGG; ctm:Cabther_A0479; -.
DR HOGENOM; CLU_004131_4_2_0; -.
DR OrthoDB; 9763467at2; -.
DR Proteomes; UP000006791; Chromosome 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000006791}.
FT DOMAIN 209..327
FT /note="DNA mismatch repair protein S5"
FT /evidence="ECO:0000259|SMART:SM01340"
FT DOMAIN 470..613
FT /note="MutL C-terminal dimerisation"
FT /evidence="ECO:0000259|SMART:SM00853"
FT REGION 331..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..350
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..400
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 656 AA; 71215 MW; B0918760619916E2 CRC64;
MSKIRILPDV VANRIAAGEV VERPASIVKE CLENALDAQA HQIDLAVERG GKESIRIRDD
GEGMTQDDAI LAFERHATSK IRTAEELMAI QTFGFRGEAL AAIGSVARVT LTTKLHGATS
GTEVCLEGGK LRHVREVAAP GGTEILVRDL FFNLPARRKF LKTEATEAFH ITNLVTHYAL
AHPQCGFTLQ HNGRQVLAVT ATTDLRARAY QLFGANMLDS LAPVEFAQGG IAVGGFVSRP
HVQRTSRDGQ YLFVNRRFVR DKLIGRALSD AYRNILPPGV FPAAMLFVEV PPDMVDVNVH
PQKTEVRFRT PQHVLESIVT AVQQALGRSP QFAPFPTTAA TPPAHPPISP AATSPSTETR
RPSAPAVQAA LQALAPPPPV TVPASPGRNE RQPPPFFTAT PHPDAGSGSA TPSAATLPTP
EPLDEATARL HSILGGRPRT RCAGTVRQAH PTRPTAELHP PDGRRTDVRI LGQIHDSYIV
AADADGLLLI DQHVAHERIL FEQRVRALLA RDVLVQMLLT PLVVDLSPAQ ATVFDALESE
LEAAGFRTTR LAGRTVAVQG VPADLSAEDA KTLLTELLDA LVSEQQTVSR EHFLRELAAS
LACRAAIKVN MNLTPEKMTW LVDELFQCEQ PTNCPHGRPI ILRFDMSLIE RGFKRS
//
