YM04_YEAST
ID YM04_YEAST Reviewed; 368 AA.
AC Q04471; D6VZT7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Abasic site processing protein YMR114C;
DE EC=3.4.-.- {ECO:0000250|UniProtKB:Q8R1M0};
GN OrderedLocusNames=YMR114C; ORFNames=YM9718.13C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
CC -!- FUNCTION: Sensor of abasic sites in single-stranded DNA (ssDNA)
CC required to preserve genome integrity by promoting error-free repair of
CC abasic sites. Recognizes and binds abasic sites in ssDNA at replication
CC forks and chemically modifies the lesion by forming a covalent cross-
CC link with DNA: forms a stable thiazolidine linkage between a ring-
CC opened abasic site and the alpha-amino and sulfhydryl substituents of
CC its N-terminal catalytic cysteine residue (By similarity). Acts as a
CC protease: mediates autocatalytic processing of its N-terminal
CC methionine in order to expose the catalytic cysteine (By similarity).
CC {ECO:0000250|UniProtKB:Q8R1M0, ECO:0000250|UniProtKB:Q96FZ2}.
CC -!- SUBCELLULAR LOCATION: Note=Localizes to replication forks.
CC {ECO:0000250|UniProtKB:Q96FZ2}.
CC -!- SIMILARITY: Belongs to the SOS response-associated peptidase family.
CC {ECO:0000305}.
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DR EMBL; Z49702; CAA89751.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10011.1; -; Genomic_DNA.
DR PIR; S54575; S54575.
DR RefSeq; NP_013832.1; NM_001182614.1.
DR AlphaFoldDB; Q04471; -.
DR SMR; Q04471; -.
DR BioGRID; 35290; 31.
DR DIP; DIP-5315N; -.
DR STRING; 4932.YMR114C; -.
DR iPTMnet; Q04471; -.
DR MaxQB; Q04471; -.
DR PaxDb; Q04471; -.
DR PRIDE; Q04471; -.
DR EnsemblFungi; YMR114C_mRNA; YMR114C; YMR114C.
DR GeneID; 855141; -.
DR KEGG; sce:YMR114C; -.
DR SGD; S000004720; YMR114C.
DR VEuPathDB; FungiDB:YMR114C; -.
DR eggNOG; KOG2618; Eukaryota.
DR GeneTree; ENSGT00390000018439; -.
DR HOGENOM; CLU_035990_0_1_1; -.
DR InParanoid; Q04471; -.
DR OMA; AGMYDYV; -.
DR BioCyc; YEAST:G3O-32809-MON; -.
DR PRO; PR:Q04471; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04471; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR GO; GO:0018142; P:protein-DNA covalent cross-linking; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1680.10; -; 1.
DR InterPro; IPR003738; SRAP.
DR InterPro; IPR036590; SRAP-like.
DR PANTHER; PTHR13604; PTHR13604; 1.
DR Pfam; PF02586; SRAP; 1.
DR SUPFAM; SSF143081; SSF143081; 1.
PE 1: Evidence at protein level;
KW Covalent protein-DNA linkage; DNA damage; DNA-binding; Hydrolase;
KW Phosphoprotein; Protease; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8R1M0"
FT CHAIN 2..368
FT /note="Abasic site processing protein YMR114C"
FT /id="PRO_0000203292"
FT REGION 25..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q96FZ2"
FT MOD_RES 2
FT /note="Thiazolidine linkage to a ring-opened DNA abasic
FT site"
FT /evidence="ECO:0000250|UniProtKB:Q96FZ2"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
SQ SEQUENCE 368 AA; 42901 MW; 0FC101AA7C918F7D CRC64;
MCGRFALAYD SGDLPQLLRD WNLPVNTPKD ASSNSQHPHD EEDTKDQPTV SKDIFKASYN
ISPTNYSAVY RPDTKAIQFM RWGLVPFWTK DVSQFKTYRT FNARLENLQE SKMWMRPCEK
KRCAVLMSGY FEWKTVGKKK TPYFISRRDG RLMFVAGMYD YVEKDDLYTF TIITAQGPRE
LEWLHERMPC VLEPGTESWD AWMDVDKTTW STEELVKLLK PDYDESKLQF YQVTDDVGKT
TNTGERLIKP LLKEDSDMFS VKREKEEALL ENDNEQGIDN RGVKGDKSLK GEDVFNQKKS
LKRNSYDGLK KNEEQEETTL PEEGSIGDRV KREEANLSPK REGNREKRNI VNMLGNQKDS
RGKKKIKK
