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Database: UniProt
Entry: Q6C6B8_YARLI
LinkDB: Q6C6B8_YARLI
Original site: Q6C6B8_YARLI 
ID   Q6C6B8_YARLI            Unreviewed;       893 AA.
AC   Q6C6B8;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   24-JAN-2024, entry version 127.
DE   SubName: Full=YALI0E10769p {ECO:0000313|EMBL:CAG79385.1};
GN   ORFNames=YALI0_E10769g {ECO:0000313|EMBL:CAG79385.1};
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591 {ECO:0000313|EMBL:CAG79385.1, ECO:0000313|Proteomes:UP000001300};
RN   [1] {ECO:0000313|EMBL:CAG79385.1, ECO:0000313|Proteomes:UP000001300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150 {ECO:0000313|Proteomes:UP000001300};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC       {ECO:0000256|ARBA:ARBA00006082}.
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DR   EMBL; CR382131; CAG79385.1; -; Genomic_DNA.
DR   RefSeq; XP_503794.1; XM_503794.1.
DR   AlphaFoldDB; Q6C6B8; -.
DR   STRING; 284591.Q6C6B8; -.
DR   EnsemblFungi; CAG79385; CAG79385; YALI0_E10769g.
DR   GeneID; 2912642; -.
DR   KEGG; yli:YALI0E10769g; -.
DR   VEuPathDB; FungiDB:YALI0_E10769g; -.
DR   HOGENOM; CLU_004131_0_2_1; -.
DR   InParanoid; Q6C6B8; -.
DR   OMA; RCSKIRS; -.
DR   OrthoDB; 4698638at2759; -.
DR   Proteomes; UP000001300; Chromosome E.
DR   GO; GO:0032389; C:MutLalpha complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
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:0061982; P:meiosis I cell cycle process; IEA:UniProt.
DR   GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
DR   CDD; cd16926; HATPase_MutL-MLH-PMS-like; 1.
DR   CDD; cd03484; MutL_Trans_hPMS_2_like; 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   InterPro; IPR014762; DNA_mismatch_repair_CS.
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:SF52; MISMATCH REPAIR ENDONUCLEASE PMS2; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001300}.
FT   DOMAIN          215..351
FT                   /note="DNA mismatch repair protein S5"
FT                   /evidence="ECO:0000259|SMART:SM01340"
FT   DOMAIN          702..847
FT                   /note="MutL C-terminal dimerisation"
FT                   /evidence="ECO:0000259|SMART:SM00853"
FT   REGION          459..635
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          649..682
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        464..478
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        479..506
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        527..547
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        548..628
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        659..682
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   893 AA;  99968 MW;  DE96DC0002B8672D CRC64;
     MAIKAIDTAS IRQITSAQVV TDLNSAVKEV VENSLDANAK NVEIKIFDYG KDRVEIIDDG
     DGIPKSEFDH VARKHMTSKI IEFDDLASVL SYGFRGEALA SICEMAELEI VTCGNTSEPA
     TRLEFNRDGS IKSTKPVAGK RGTTVTIRRL FHSAIVRRKE FEKNAKNSHP GLIRMLETYA
     IIRSDVRFSI VHVTNNKNRN VQLTTDGSGD MIKTVGRVFG NELKAHLMDV NFSFDVNYTK
     RGFLSSEELP NYVVRVTGLV SKPVFGMGRN ANDKQLLFIN KRPFTMKKLQ KVFQDVYTSF
     VHLQKPVLII NLDIPPSAYD VNVSPDKRTI MLHNEVDVIN CIRENLVDVF ESSGQSVPRH
     TVDVKVQPMS SQSYWGVKDD VGEQEIEEVE DVEESGEVGP VELDHNVQLD EAATSDDVPN
     QLEVRQAAAG QIERAGLFVT DQEQEEDVSM TYVEETESLV INDMTTDEAD HPREQEDEGM
     VDDEAEEVEE EEEEEEEEEG QAEEEDPEKI PPEYAYIDTA ATLEDEGEDR GNDDETNDDD
     DDDNDNDPTS SLSYSQSDTS MNSVSDTSIS LTTPITSRRR VTKSNVNKLN LSQFSASSRP
     SSSSSTRPST ASSLPSLPAS QRASSRKRTY ANLPEFDTFG HRESLTITAE DLERGERASE
     TLSTFNTSSS TSQPQTSALD DSSAESKLNL TISRNDFLNF NIIGQFNEAF IIVSDPENLF
     IIDQHASDEK YNFERLQRDT KITPQPFVNP LTVELTPLEE SVVSSNLELL KKNGFLVTID
     NSLPPGEKCQ IRGFPQTGNI VFGMPDFREL VVLFEDNPGN DSVRPKKVRD VFASRACRGS
     VMVGTALKEK EMDRIVRNLA GLDKPWNCPH GRPTMRHLME IDKWPVFTQD YEF
//
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