ID A5DIT1_PICGU Unreviewed; 693 AA.
AC A5DIT1;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 2.
DT 24-JAN-2024, entry version 85.
DE RecName: Full=MutL C-terminal dimerisation domain-containing protein {ECO:0000259|SMART:SM00853};
GN ORFNames=PGUG_03182 {ECO:0000313|EMBL:EDK39083.2};
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK39083.2, ECO:0000313|Proteomes:UP000001997};
RN [1] {ECO:0000313|EMBL:EDK39083.2, ECO:0000313|Proteomes:UP000001997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC Y-324 {ECO:0000313|Proteomes:UP000001997};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC {ECO:0000256|ARBA:ARBA00006082}.
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DR EMBL; CH408157; EDK39083.2; -; Genomic_DNA.
DR RefSeq; XP_001485452.1; XM_001485402.1.
DR AlphaFoldDB; A5DIT1; -.
DR STRING; 294746.A5DIT1; -.
DR GeneID; 5127200; -.
DR KEGG; pgu:PGUG_03182; -.
DR VEuPathDB; FungiDB:PGUG_03182; -.
DR eggNOG; KOG1977; Eukaryota.
DR HOGENOM; CLU_005415_1_0_1; -.
DR InParanoid; A5DIT1; -.
DR OMA; HACDERV; -.
DR OrthoDB; 9570at2759; -.
DR Proteomes; UP000001997; 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:0006298; P:mismatch repair; IEA:InterPro.
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 InterPro; IPR014762; DNA_mismatch_repair_CS.
DR InterPro; IPR036890; HATPase_C_sf.
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 PANTHER; PTHR10073; DNA MISMATCH REPAIR PROTEIN MLH, PMS, MUTL; 1.
DR PANTHER; PTHR10073:SF47; DNA MISMATCH REPAIR PROTEIN MLH3; 1.
DR Pfam; PF13589; HATPase_c_3; 1.
DR Pfam; PF08676; MutL_C; 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 PROSITE; PS00058; DNA_MISMATCH_REPAIR_1; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001997}.
FT DOMAIN 486..653
FT /note="MutL C-terminal dimerisation"
FT /evidence="ECO:0000259|SMART:SM00853"
FT REGION 420..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 693 AA; 78163 MW; 41E6E1449C5B426C CRC64;
MDLRASEEKL VHQKKHQHRA ELYSDHFQQP TWSIQHRSMP GTGPAASIWA AIVFLAKLSL
SFVKSLINSQ NDFPRILIAR SLHGAMGKLH QLDKDVIQQL VAPLSVSGYA SAVRELLHNS
IDAQATFISV KIHLDSMSVM VTDNGFGINE ADLGLVGTQN YTSKAEKDLS SVKTMGFRGE
ALFAISQVSS TTIVSKVDGF GANTRHLGDP NVDLFEPDAQ VCNDIFAIDP TCLGTSWTVV
IVRGLFANFK VRRAQLLSQN IQSILSELKN EVAECSLLFP RVKIEVNVVP AEQSIVVSPS
MENPLVSTIR SVYGFRALPA YELVNVRYQQ YRISGIIGKW SWVSPLKFIF INERKYIASS
QDLKEFNKLV HNSAYVLMVT CPTDEITQDP AKVLYRVHHW KVVKRMILEL LEKFGVLDSP
MKERSPRKSH LSPRKSLSSP RKSPSKPRSP VKSPTKGLFS SRQLHPNHSI SSFKTISAIN
VDSFRVLKQL DRKYILFVAI VESHSRLFIV DQHACDERIR VESYLKDYIQ RTKVNQHQNK
AQLSQQLQLE LSPTQILHLQ SHHAQLQSFG FDIEFRENHA FLLQVPEVLY DKSVSAVSLG
IAQYLEHLAA NQKSSRIGEP HHWTHAVKDV PQIILDSINM RACRSAIMFG IPLTLAEMNY
MLQCLFRCQH PFHCAHGRPS VVEVRASLHP LSP
//
