ID   A0A0S6W662_9BACT        Unreviewed;       923 AA.
AC   A0A0S6W662;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=DNA mismatch repair protein mutL {ECO:0000313|EMBL:GAK53478.1};
GN   ORFNames=U14_04743 {ECO:0000313|EMBL:GAK53478.1};
OS   Candidatus Moduliflexus flocculans.
OC   Bacteria; Candidatus Moduliflexota; Candidatus Moduliflexia;
OC   Candidatus Moduliflexales; Candidatus Moduliflexaceae.
OX   NCBI_TaxID=1499966 {ECO:0000313|EMBL:GAK53478.1};
RN   [1] {ECO:0000313|EMBL:GAK53478.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Sekiguchi Y., Ohashi A., Parks D.H., Yamauchi T., Tyson G.W.,
RA   Hugenholtz P.;
RT   "First genomic representation of candidate bacterial phylum KSB3 points to
RT   enhanced environmental sensing as a trigger of wastewater bulking.";
RL   PeerJ 3:e740-e740(2015).
CC   -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC       {ECO:0000256|ARBA:ARBA00006082}.
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DR   EMBL; DF820459; GAK53478.1; -; Genomic_DNA.
DR   STRING; 1499966.U14_04743; -.
DR   HOGENOM; CLU_316095_0_0_0; -.
DR   Proteomes; UP000030700; 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:InterPro.
DR   CDD; cd00782; MutL_Trans; 2.
DR   Gene3D; 3.30.230.10; -; 2.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 2.
DR   Gene3D; 3.30.1540.20; MutL, C-terminal domain, dimerisation subdomain; 2.
DR   Gene3D; 3.30.1370.100; MutL, C-terminal domain, regulatory subdomain; 1.
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; 2.
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; 2.
DR   Pfam; PF08676; MutL_C; 2.
DR   SMART; SM01340; DNA_mis_repair; 2.
DR   SMART; SM00853; MutL_C; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 2.
DR   SUPFAM; SSF118116; DNA mismatch repair protein MutL; 2.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 2.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030700}.
FT   DOMAIN          79..197
FT                   /note="DNA mismatch repair protein S5"
FT                   /evidence="ECO:0000259|SMART:SM01340"
FT   DOMAIN          306..434
FT                   /note="MutL C-terminal dimerisation"
FT                   /evidence="ECO:0000259|SMART:SM00853"
FT   DOMAIN          511..629
FT                   /note="DNA mismatch repair protein S5"
FT                   /evidence="ECO:0000259|SMART:SM01340"
FT   DOMAIN          738..880
FT                   /note="MutL C-terminal dimerisation"
FT                   /evidence="ECO:0000259|SMART:SM00853"
FT   REGION          237..288
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          670..697
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        273..288
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   923 AA;  102300 MW;  F3BA025277296E60 CRC64;
     MVANVESGAS PGTFIEVSDL FYKTPARLKF LKSPATELSY INNVITDIAL ANPQVGFSVN
     NNGSNQLHLP ADSTLLQRVA GLFGREIVRE LVEIHEVAAT VELRGLIGLP SCNRANRNYQ
     KAFVNNRPVK DKTISHAIQQ AYDTLIPKGR HPVAFLFLSL PVELVDVNVH PTKAEIRFIN
     SQAIHDIVAR GIRKTLSQTL GVSALPSYSA PRAAKTDSDA LQDEVPFDSF GMAQRDIEPP
     ALPFSSSAPT PRFRPSDGFS PEPEMTGQPA SPQLKYRREQ NNALSSDGQL ARSIQGGSAV
     FSRMLPIGQF QETYILAQDG EDLFIIDQHA AHERVFYEKF KTQFQENTLD VQPLLFPVSL
     ELSHREQAIL QEHLDALRQY GFEVEPFGGT TWLIKAVPAL LAKADYKKLL YDMLDQLGET
     KTATIAXIHG GEMVANVESG ASPGTFIEVG DLFYKTPARL KFLKSPATEL GYINNVITDI
     ALANPQVGFS VSNNGSSQLH LPADSTLLQR IAGLFGREIV RELVEIHEMA ATVELRGLIG
     LPSCNRANRN YQKAFVNNRP VKDKTISHAI QQAYDTLIPK GRHPVAFLFL SLPVELVDVN
     VHPTKAEIRF INSQAIHDIV SRGIRKTLSQ TLGVSALPSY AAQRAAKADS DAPQDEVPFE
     SFGMAQRDIE PPALPFSSNA PTPRFKPSDA FSPEPEMTGQ SASFQLRYRR EQNNALSSDG
     QLARSILGGS AVFSRMLPIG QFQDTYILAQ DGEDLFIIDQ HAAHERVFYE KFKAQFQQNT
     LDVQPLLFPV SLELSHREQA ILEEHLDALR QYGFEVEPFG GTTWLLKSVP ALLAKADYKK
     LLYDMLDQLG ETKTATIAQK FDGILKLMAC HGAIRAHHRL QDSQIFALLQ QMDALELPYT
     CPHGRPTVIK ITLQDLEKRF GRI
//