ID   YMN3_YEAST              Reviewed;        1374 AA.
AC   Q03099; D6W0F2; Q12054;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Y' element ATP-dependent helicase YML133C;
DE            EC=3.6.4.12;
GN   OrderedLocusNames=YML133C; ORFNames=YM4987.01C, YM4987.02C;
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   FUNCTION, AND INDUCTION.
RX   PubMed=9837911; DOI=10.1074/jbc.273.50.33360;
RA   Yamada M., Hayatsu N., Matsuura A., Ishikawa F.;
RT   "Y'-Help1, a DNA helicase encoded by the yeast subtelomeric Y' element, is
RT   induced in survivors defective for telomerase.";
RL   J. Biol. Chem. 273:33360-33366(1998).
CC   -!- FUNCTION: Catalyzes DNA unwinding and is involved in telomerase-
CC       independent telomere maintenance. {ECO:0000269|PubMed:9837911}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC   -!- INDUCTION: Induced in absence of telomerase TLC1.
CC       {ECO:0000269|PubMed:9837911}.
CC   -!- SIMILARITY: Belongs to the helicase family. Yeast subtelomeric Y'
CC       repeat subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA90549.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAA90550.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; Z50178; CAA90549.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; Z50178; CAA90550.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BK006946; DAA09766.1; -; Genomic_DNA.
DR   PIR; S69875; S69875.
DR   RefSeq; NP_013573.1; NM_001182496.1.
DR   AlphaFoldDB; Q03099; -.
DR   SMR; Q03099; -.
DR   BioGRID; 35072; 24.
DR   DIP; DIP-7582N; -.
DR   STRING; 4932.YML133C; -.
DR   PaxDb; Q03099; -.
DR   PRIDE; Q03099; -.
DR   EnsemblFungi; YML133C_mRNA; YML133C; YML133C.
DR   GeneID; 854906; -.
DR   KEGG; sce:YML133C; -.
DR   SGD; S000004602; YML133C.
DR   VEuPathDB; FungiDB:YML133C; -.
DR   eggNOG; ENOG502QWCT; Eukaryota.
DR   GeneTree; ENSGT00940000153173; -.
DR   HOGENOM; CLU_003044_2_0_1; -.
DR   OMA; SATTTXS; -.
DR   BioCyc; YEAST:G3O-32711-MON; -.
DR   Reactome; R-SCE-5689880; Ub-specific processing proteases.
DR   Reactome; R-SCE-936440; Negative regulators of DDX58/IFIH1 signaling.
DR   PRO; PR:Q03099; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; Q03099; protein.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004386; F:helicase activity; ISS:SGD.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0000722; P:telomere maintenance via recombination; IEA:UniProt.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR021646; Sir1_ORC-binding.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF11603; Sir1; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Reference proteome;
KW   Repeat.
FT   CHAIN           1..1374
FT                   /note="Y' element ATP-dependent helicase YML133C"
FT                   /id="PRO_0000102209"
FT   DOMAIN          375..552
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          609..758
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          832..999
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        832..975
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        976..999
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         388..395
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1374 AA;  155553 MW;  9867CAC68D2C497E CRC64;
     MKVSDRRKFE KANFDEFESA LNNKNDLVHC PSITLFESIP TEVRSFYEDE KSGLIKVVKF
     RTGAMDRKRS FEKIVVSVMV GKNVQKFLTF VEDEPDFQGG PIPSKYLIPK KINLMVYTLF
     QVHTLKFNRK DYDTLSLFYL NRGYYNELSF RVLERCHEIA SARPNDSSTM RTFTDFVSGA
     PIVRSLQKST IRRYGYNLAP HMFLLLHVDE LSIFSAYQAS LPGEKKVDTE RLKRDLCPRK
     PIEIKYFSQI CNDMMNKKDR LGDVLATAQR IRRRYNKNSS SEPRLKTLDG LTSERWIQWL
     GLESDYHCSF SSTRNAEDVV AGEAASSDHH QKISRVTRKR PREPKSTNDI LVAGQKLFGS
     SFEFRDLHQL RLCHEIYMAD TPSVAVQAPP GYGKTELFHL PLIALASKGD VKYVSFLFVP
     YTVLLANCMI RLSRCGCLNV APVRNFIEEG CDGVTDLYVG IYDDLASTNF TDRIAAWENI
     VECTFRTNNV KLGYLIVDEF HNFETEVYRQ SQFGGITNLD FDAFEKAIFL SGTAPEAVAD
     AALQRIGLTG LAKKSMDINE LKRSEDLSRG LSSYPTRMFN LIKEKSEVPL GHVHKIWKKV
     ESQPEEALKL LLALFEIEPE SKAIVVASTT NEVEELACSW RKYFRVVWIH GKLGAAEKVS
     RTKEFVTDGS MRVLIGTKLV TEGIDIKQLM MVIMLDNRLN IIELIQGVGR LRDGGLCYLL
     SRKNSWAARN RKGELPPIKE GCITEQVREF YGLESKKGKK GQHVGCCGSR TDLSADTVEL
     IERMDRLAEK QATASMSIVA LPSSFQESNS SDRCRKYCSS DEDSDTCIHG SANASTNATT
     NSSTNATTTA STNVRTSATT TASINVRTSA TTTESTNSST NATTTASTNV RTSATTTASI
     NVRTSATTTE STNSNTSATT TESTDSNTSA TTTESTDSNT SATTTASTNS STNATTTAST
     NSSTNATTTE STNASAKEDA NKDGNAEDNR FHPVTDINKE SYKRKGSQMV LLERKKLKAQ
     FPNTSENMNV LQFLGFRSDE IKHLFLYGID IYFCPEGVFT QYGLCKGCQK MFELCVCWAG
     QKVSYRRMAW EALAVERMLR NDEEYKEYLE DIEPYHGDPV GYLKFFSVKR GEIYSQIQRN
     YAWYLAITRR RETISVLDST RGKQGSQVFR MSGRQIKELY YKVWSNLRES KTEVLQYFLN
     WDEKKCREEW EAKDDTVFVE ALEKVGVFQR LRSMTSAGLQ GPQYVKLQFS RHHRQLRSRY
     ELSLGMHLRD QLALGVTPSK VPHWTAFLSM LIGLFYNKTF RQKLEYLLEQ ISEVWLLPHW
     VDLANVEVLA ADNTRVPLYM LMVAVHKELD SDDVPDGRFD IILLCRDSSR EVGE