ID MUTL_PSYIN Reviewed; 628 AA.
AC A1SZL2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 24-JAN-2024, entry version 89.
DE RecName: Full=DNA mismatch repair protein MutL {ECO:0000255|HAMAP-Rule:MF_00149};
GN Name=mutL {ECO:0000255|HAMAP-Rule:MF_00149}; OrderedLocusNames=Ping_3240;
OS Psychromonas ingrahamii (strain DSM 17664 / CCUG 51855 / 37).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Psychromonadaceae; Psychromonas.
OX NCBI_TaxID=357804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17664 / CCUG 51855 / 37;
RX PubMed=18460197; DOI=10.1186/1471-2164-9-210;
RA Riley M., Staley J.T., Danchin A., Wang T.Z., Brettin T.S., Hauser L.J.,
RA Land M.L., Thompson L.S.;
RT "Genomics of an extreme psychrophile, Psychromonas ingrahamii.";
RL BMC Genomics 9:210-210(2008).
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:0000255|HAMAP-Rule:MF_00149}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC {ECO:0000255|HAMAP-Rule:MF_00149}.
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DR EMBL; CP000510; ABM04927.1; -; Genomic_DNA.
DR RefSeq; WP_011771479.1; NC_008709.1.
DR AlphaFoldDB; A1SZL2; -.
DR SMR; A1SZL2; -.
DR STRING; 357804.Ping_3240; -.
DR KEGG; pin:Ping_3240; -.
DR eggNOG; COG0323; Bacteria.
DR HOGENOM; CLU_004131_5_1_6; -.
DR OrthoDB; 9763467at2; -.
DR Proteomes; UP000000639; 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; cd03482; MutL_Trans_MutL; 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; DNA repair; Reference proteome.
FT CHAIN 1..628
FT /note="DNA mismatch repair protein MutL"
FT /id="PRO_1000071509"
FT REGION 333..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 628 AA; 70468 MW; B2763327C46AD23D CRC64;
MPIQILAARL ANQIAAGEVV ERPASVVKEL IENSLDAGAT KIEIDIEKGG AKCIRVKDNG
AGVCQEQLTL ALSRHATSKI SHLDDLEAIV SLGFRGEALA SVSSVSRLTF TSKPADQEQA
WQAIAEGRDM QVTIQPAAHP QGTTVEVLDL FFNTPARRRF LKTEKTEFQH IDELIRRIAL
SRFEITFVLK HNHKIVHQYR ATQTQSQQEK RLASICSESF VSSALYFQNS DNALKISGWV
SDKLSARSSN DVQYCYINGR VIRDKLINHA IKQVYAYSLP QGKFPAYVIY IECDPDQVDV
NVHPSKHEVR FHQARWVHDF IVSTLTVTLN ESPLSASEPQ SQPKPSEHAY LPANRGEEKT
DSQYEPKEKN KSAGRVNEQT AAPSSGYAKR ETNPQLDQAK MAAYCDFVAE AHLPFSADEQ
QSSTLSDLTF ATVVCLIDRQ YLLIKLNAKQ QLLNIDSPFL VLSLENVDLM IKQMELFAAW
SDGEVIAQPL LLPVRVELDA LLLKTSEDFN ELFMRLGFVF KIQGSKLIIS KVPALLRQAP
VAKIIPELLT FLSQTDNNMD AQQVNLFCVF LVNTLKQQQA ENINWTEQSA KALFDLLLSL
FSEKLSDWQK QLFRVPDLSL LVQGFSHE
//
