MET18_YEAST
ID MET18_YEAST Reviewed; 1032 AA.
AC P40469; D6VVF9; P89106; Q45U11;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=DNA repair/transcription protein MET18/MMS19;
DE AltName: Full=Methyl methanesulfonate-sensitivity protein 19;
GN Name=MET18; Synonyms=MMS19; OrderedLocusNames=YIL128W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=8943333; DOI=10.1128/mcb.16.12.6783;
RA Lauder S., Bankmann M., Guzder S.N., Sung P., Prakash L., Prakash S.;
RT "Dual requirement for the yeast MMS19 gene in DNA repair and RNA polymerase
RT II transcription.";
RL Mol. Cell. Biol. 16:6783-6793(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS 111-SER-PHE-112; GLY-329;
RP MET-335; ILE-444; SER-697; SER-814; THR-930GLN-963 AND CYS-969.
RC STRAIN=SK1;
RX PubMed=16273108; DOI=10.1038/ng1674;
RA Deutschbauer A.M., Davis R.W.;
RT "Quantitative trait loci mapped to single-nucleotide resolution in yeast.";
RL Nat. Genet. 37:1333-1340(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP FUNCTION.
RX PubMed=392238; DOI=10.1007/bf00333097;
RA Prakash L., Prakash S.;
RT "Three additional genes involved in pyrimidine dimer removal in
RT Saccharomyces cerevisiae: RAD7, RAD14 and MMS19.";
RL Mol. Gen. Genet. 176:351-359(1979).
RN [6]
RP FUNCTION.
RX PubMed=9321645; DOI=10.1093/nar/25.20.3974;
RA Lombaerts M., Tijsterman M., Verhage R.A., Brouwer J.;
RT "Saccharomyces cerevisiae mms19 mutants are deficient in transcription-
RT coupled and global nucleotide excision repair.";
RL Nucleic Acids Res. 25:3974-3979(1997).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP FUNCTION.
RX PubMed=18836076; DOI=10.1073/pnas.0710736105;
RA Kou H., Zhou Y., Gorospe R.M., Wang Z.;
RT "Mms19 protein functions in nucleotide excision repair by sustaining an
RT adequate cellular concentration of the TFIIH component Rad3.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:15714-15719(2008).
RN [9]
RP FUNCTION, AND IDENTIFICATION IN THE CIA COMPLEX.
RX PubMed=22678362; DOI=10.1126/science.1219723;
RA Stehling O., Vashisht A.A., Mascarenhas J., Jonsson Z.O., Sharma T.,
RA Netz D.J., Pierik A.J., Wohlschlegel J.A., Lill R.;
RT "MMS19 assembles iron-sulfur proteins required for DNA metabolism and
RT genomic integrity.";
RL Science 337:195-199(2012).
CC -!- FUNCTION: Key component of the cytosolic iron-sulfur protein assembly
CC (CIA) machinery that mediates the incorporation of iron-sulfur cluster
CC into apoproteins specifically involved in DNA metabolism and genomic
CC integrity. Acts as an adapter between early-acting CIA components and a
CC subset of cellular target iron-sulfur proteins such as RAD3/XPD and
CC DNA2, thereby playing a key role in nucleotide excision repair (NER)
CC and RNA polymerase II (POL II) transcription.
CC {ECO:0000269|PubMed:18836076, ECO:0000269|PubMed:22678362,
CC ECO:0000269|PubMed:392238, ECO:0000269|PubMed:8943333,
CC ECO:0000269|PubMed:9321645}.
CC -!- INTERACTION:
CC P40469; Q05583: CIA1; NbExp=3; IntAct=EBI-11492, EBI-32145;
CC P40469; P38829: YHR122W; NbExp=4; IntAct=EBI-11492, EBI-24704;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 3150 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the MET18/MMS19 family. {ECO:0000305}.
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DR EMBL; U70559; AAB38865.1; -; Genomic_DNA.
DR EMBL; DQ115392; AAZ22499.1; -; Genomic_DNA.
DR EMBL; Z38059; CAA86150.1; -; Genomic_DNA.
DR EMBL; Z46833; CAA86864.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08425.1; -; Genomic_DNA.
DR PIR; S53571; S53571.
DR RefSeq; NP_012138.1; NM_001179476.1.
DR AlphaFoldDB; P40469; -.
DR SMR; P40469; -.
DR BioGRID; 34863; 296.
DR DIP; DIP-1438N; -.
DR IntAct; P40469; 42.
DR MINT; P40469; -.
DR STRING; 4932.YIL128W; -.
DR CarbonylDB; P40469; -.
DR iPTMnet; P40469; -.
DR MaxQB; P40469; -.
DR PaxDb; P40469; -.
DR PRIDE; P40469; -.
DR EnsemblFungi; YIL128W_mRNA; YIL128W; YIL128W.
DR GeneID; 854678; -.
DR KEGG; sce:YIL128W; -.
DR SGD; S000001390; MET18.
DR VEuPathDB; FungiDB:YIL128W; -.
DR eggNOG; KOG1967; Eukaryota.
DR GeneTree; ENSGT00390000015583; -.
DR HOGENOM; CLU_005943_1_0_1; -.
DR InParanoid; P40469; -.
DR OMA; FSFMPEF; -.
DR BioCyc; YEAST:G3O-31379-MON; -.
DR PRO; PR:P40469; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40469; protein.
DR GO; GO:0097361; C:CIA complex; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0006259; P:DNA metabolic process; IMP:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IMP:UniProtKB.
DR GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IMP:SGD.
DR GO; GO:0010033; P:response to organic substance; NAS:UniProtKB.
DR GO; GO:0009411; P:response to UV; NAS:UniProtKB.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR039920; MET18/MMS19.
DR InterPro; IPR024687; MMS19_C.
DR InterPro; IPR029240; MMS19_N.
DR PANTHER; PTHR12891; PTHR12891; 1.
DR Pfam; PF12460; MMS19_C; 1.
DR Pfam; PF14500; MMS19_N; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; Nucleus; Reference proteome; Repeat; Transcription.
FT CHAIN 1..1032
FT /note="DNA repair/transcription protein MET18/MMS19"
FT /id="PRO_0000096445"
FT REPEAT 862..901
FT /note="HEAT 1"
FT REPEAT 905..943
FT /note="HEAT 2"
FT REPEAT 946..988
FT /note="HEAT 3"
FT REPEAT 991..1029
FT /note="HEAT 4"
FT VARIANT 111..112
FT /note="AL -> SF (in strain: SK1)"
FT VARIANT 329
FT /note="D -> G (in strain: SK1)"
FT /evidence="ECO:0000269|PubMed:16273108"
FT VARIANT 335
FT /note="V -> M (in strain: SK1)"
FT /evidence="ECO:0000269|PubMed:16273108"
FT VARIANT 444
FT /note="T -> I (in strain: SK1)"
FT /evidence="ECO:0000269|PubMed:16273108"
FT VARIANT 697
FT /note="N -> S (in strain: SK1)"
FT /evidence="ECO:0000269|PubMed:16273108"
FT VARIANT 814
FT /note="A -> S (in strain: SK1)"
FT /evidence="ECO:0000269|PubMed:16273108"
FT VARIANT 816
FT /note="K -> M (in strain: SK1)"
FT VARIANT 930
FT /note="A -> T (in strain: SK1)"
FT VARIANT 963
FT /note="H -> Q (in strain: SK1)"
FT VARIANT 969
FT /note="S -> C (in strain: SK1)"
FT /evidence="ECO:0000269|PubMed:16273108"
FT CONFLICT 230
FT /note="P -> Q (in Ref. 1; AAB38865)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="D -> G (in Ref. 1; AAB38865)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="V -> M (in Ref. 1; AAB38865)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="V -> I (in Ref. 1; AAB38865)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1032 AA; 117883 MW; D05DCC488E098814 CRC64;
MTPDELNSAV VTFMANLNID DSKANETAST VTDSIVHRSI KLLEVVVALK DYFLSENEVE
RKKALTCLTT ILAKTPKDHL SKNECSVIFQ FYQSKLDDQA LAKEVLEGFA ALAPMKYVSI
NEIAQLLRLL LDNYQQGQHL ASTRLWPFKI LRKIFDRFFV NGSSTEQVKR INDLFIETFL
HVANGEKDPR NLLLSFALNK SITSSLQNVE NFKEDLFDVL FCYFPITFKP PKHDPYKISN
QDLKTALRSA ITATPLFAED AYSNLLDKLT ASSPVVKNDT LLTLLECVRK FGGSSILENW
TLLWNALKFE IMQNSEGNEN TLLNPYNKDQ QSDDVGQYTN YDACLKIINL MALQLYNFDK
VSFEKFFTHV LDELKPNFKY EKDLKQTCQI LSAIGSGNVE IFNKVISSTF PLFLINTSEV
AKLKLLIMNF SFFVDSYIDL FGRTSKESLG TPVPNNKMAE YKDEIIMILS MALTRSSKAE
VTIRTLSVIQ FTKMIKMKGF LTPEEVSLII QYFTEEILTD NNKNIYYACL EGLKTISEIY
EDLVFEISLK KLLDLLPDCF EEKIRVNDEE NIHIETILKI ILDFTTSRHI LVKESITFLA
TKLNRVAKIS KSREYCFLLI STIYSLFNNN NQNENVLNEE DALALKNAIE PKLFEIITQE
SAIVSDNYNL TLLSNVLFFT NLKIPQAAHQ EELDRYNELF ISEGKIRILD TPNVLAISYA
KILSALNKNC QFPQKFTVLF GTVQLLKKHA PRMTETEKLG YLELLLVLSN KFVSEKDVIG
LFDWKDLSVI NLEVMVWLTK GLIMQNSLES SEIAKKFIDL LSNEEIGSLV SKLFEVFVMD
ISSLKKFKGI SWNNNVKILY KQKFFGDIFQ TLVSNYKNTV DMTIKCNYLT ALSLVLKHTP
SQSVGPFIND LFPLLLQALD MPDPEVRVSA LETLKDTTDK HHTLITEHVS TIVPLLLSLS
LPHKYNSVSV RLIALQLLEM ITTVVPLNYC LSYQDDVLSA LIPVLSDKKR IIRKQCVDTR
QVYYELGQIP FE
