ID A0A0K1E651_CHOCO Unreviewed; 767 AA.
AC A0A0K1E651;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=DNA mismatch repair protein MutL {ECO:0000256|HAMAP-Rule:MF_00149};
GN Name=mutL {ECO:0000256|HAMAP-Rule:MF_00149,
GN ECO:0000313|EMBL:AKT36329.1};
GN ORFNames=CMC5_004430 {ECO:0000313|EMBL:AKT36329.1};
OS Chondromyces crocatus.
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae;
OC Chondromyces.
OX NCBI_TaxID=52 {ECO:0000313|EMBL:AKT36329.1, ECO:0000313|Proteomes:UP000067626};
RN [1] {ECO:0000313|EMBL:AKT36329.1, ECO:0000313|Proteomes:UP000067626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cm c5 {ECO:0000313|EMBL:AKT36329.1,
RC ECO:0000313|Proteomes:UP000067626};
RA Zaburannyi N., Bunk B., Maier J., Overmann J., Mueller R.;
RT "Genome analysis of myxobacterium Chondromyces crocatus Cm c5 reveals a
RT high potential for natural compound synthesis and the genetic basis for the
RT loss of fruiting body formation.";
RL Submitted (JUL-2015) 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; CP012159; AKT36329.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K1E651; -.
DR STRING; 52.CMC5_004430; -.
DR KEGG; ccro:CMC5_004430; -.
DR PATRIC; fig|52.7.peg.472; -.
DR OrthoDB; 9763467at2; -.
DR Proteomes; UP000067626; Chromosome.
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:UP000067626}.
FT DOMAIN 218..336
FT /note="DNA mismatch repair protein S5"
FT /evidence="ECO:0000259|SMART:SM01340"
FT DOMAIN 582..724
FT /note="MutL C-terminal dimerisation"
FT /evidence="ECO:0000259|SMART:SM00853"
FT REGION 343..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 767 AA; 80695 MW; 3A413E2877955D87 CRC64;
MSSGARGDTP RDERRVAVLP DDLANQIAAG EVVERPASVV KELVENALDA GARRVRVDIE
GGGVILTRVA DDGSGMARED ASLAVLRHAT SKITHIDDLH AIQSFGFRGE ALPSVASVSR
FSLRTRREQD QEGTEVRLEG GGPPKVTPCG CAAGTVVEVR DLFFNVPARR KFLRAVATES
AHVTEVVQAA ALSEPGVTVI LSREGRVVRE WLRAGSRAER VRAALDGEEL ATCAGERGPL
RVEAFVSRPE RARAGAGWLW LFVNGRHVRD RTLARAVGLA YGSVLEPGRY PVGAVFLDLP
ATLVDVNVHP QKAEVRFAEG RAVAESLQRI IAGQVAAAFG LPSPGPGGGG WGHRKQKPAA
ESQGAAWLWS NAPSASAPTP SASMPLPSAF EGAPVPLDGA LPVEARDERR PGSHGLAEVQ
RGEAHEVEET PAGGAWRGEE GVTLARASAQ AAPGAEAPFG QRGLAHDATP SPSSTTGLAP
RHAQPSVSLA SSEASVGADA DPEHRATATP ADPWDLGGEV TSPGASPRVE PRAATPAPTQ
LPIAGLGVAS SSTSAPLTAY PTAGQLLATA ADRPMVFRNL RFAAQVRGMF LVCEGADGIY
FLDQHAAAER VTFHRLREAY LARQVASQKL LFPVLVQATP AEVALVEEAQ DDIDRTGLEM
RPAGPAQLAI HAVPKILSRA APERLARDLL DELSHAGERA FSGAVDLSLA TMACHGSVRA
GDPMAPDEAQ ALLNALDEVD FAGHCPHGRP VVMRVGWPEL EHRVGRR
//
