ID   YRF14_YEAST             Reviewed;        1382 AA.
AC   O13559; D6VZ97;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=Y' element ATP-dependent helicase protein 1 copy 4;
DE            EC=3.6.4.12;
GN   Name=YRF1-4; OrderedLocusNames=YLR466W;
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=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(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}.
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DR   EMBL; U22383; AAB64729.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09763.1; -; Genomic_DNA.
DR   PIR; S70310; S70310.
DR   RefSeq; NP_013571.3; NM_001182354.3.
DR   AlphaFoldDB; O13559; -.
DR   SMR; O13559; -.
DR   BioGRID; 31722; 5.
DR   DIP; DIP-8268N; -.
DR   IntAct; O13559; 2.
DR   MINT; O13559; -.
DR   STRING; 4932.YLR466W; -.
DR   PaxDb; O13559; -.
DR   PRIDE; O13559; -.
DR   EnsemblFungi; YLR466W_mRNA; YLR466W; YLR466W.
DR   GeneID; 851187; -.
DR   KEGG; sce:YLR466W; -.
DR   SGD; S000004458; YRF1-4.
DR   VEuPathDB; FungiDB:YLR466W; -.
DR   eggNOG; ENOG502QWCT; Eukaryota.
DR   GeneTree; ENSGT00940000153173; -.
DR   HOGENOM; CLU_003044_2_0_1; -.
DR   BioCyc; YEAST:G3O-32516-MON; -.
DR   PRO; PR:O13559; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; O13559; protein.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IC: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; IDA:SGD.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0000722; P:telomere maintenance via recombination; IGI:SGD.
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   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 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..1382
FT                   /note="Y' element ATP-dependent helicase protein 1 copy 4"
FT                   /id="PRO_0000102204"
FT   DOMAIN          383..560
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          617..766
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          840..864
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          880..1007
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        880..983
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        984..1007
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         396..403
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1382 AA;  156367 MW;  47C392C1444B7AB8 CRC64;
     MWKTLGRVEQ LLPYASLILR NREVLFREPK RGIDEYLEND SFFQMIPVKY REIVLPKLRR
     DTNKMTAALK NKVAVAIDEL TVPLMWMIHF AVGYPYRYPE LQLLAFAGPQ RNVYVDDTTR
     RIQLYTDYNK NGSSEPRLKT LDGLTSDYVF YFVTVLRQMQ ICALGNSYDA FNHDPWMDVV
     GFEDPDQVTN RDISRIVLYS YMFLNTAKGC LVEYATFRQY MRELPKNAPQ KLNFREMRQG
     LIALGRHCVG SRFETDLYES ATSELMANHS VQTGRNIYGV DSFSLTSVSG TTATLLQERA
     SERWIQWLGL ESDYHCSFSS TRNAEDVVAG EAASSDHHQK ISRVTRKRPR EPKSTNDILV
     AGRKLFGSSF EFRDLHQLRL CHEIYMADTP SVAVQAPPGY GKTELFHLPL IALASKGDVK
     YVSFLFVPYT VLLANCMIRL SRCGCLNVAP VRNFIEEGCD GVTDLYVGIY DDLASTNFTD
     RIAAWENIVE CTFRTNNVKL GYLIVDEFHN FETEVYRQSQ FGGITNLDFD AFEKAIFLSG
     TAPEAVADAA LQRIGLTGLA KKSMDINELK RSEDLSRGLS SYPTRMFNLI KEKSEVPLGH
     VHKIWKKVES QPEEALKLLL ALFEIEPESK AIVVASTTNE VEELACSWRK YFRVVWIHGK
     LGAAEKVSRT KEFVTDGSMR VLIGTKLVTE GIDIKQLMMV IMLDNRLNII ELIQGVGRLR
     DGGLCYLLSR KNSWAARNRK GELPPIKEGC ITEQVREFYG LESKKGKKGQ HVGCCGSRTD
     LSADTVELIE RMDRLAEKQA TASMSIIALP SSFQESNSSD RCRKYCSSDE DSDTCIHGSA
     NASTNATTNS STNATTTAST NVRTSATTTA SINVRTSAIT TESTNSSTNA TTTASTNVRT
     SATTTASINV RTSATTTEST NSNTSATTTE STDSNTSATT TESTDSNTSA TTTASTNSST
     NATTTASTNS STNATTTEST NASAKEDANK DGNAEDNRFH PVTDINKESY KRKGSQMVLL
     ERKKLKAQFP NTSENMNVLQ FLGFRSDEIK HLFLYGIDVY FCPEGVFTQY GLCKGCQKMF
     ELCVCWAGQK VSYRRMAWEA LAVERMLRND EEYKEYLEDI EPYHGDPVGY LKYFSVKRGE
     IYSQIQRNYA WYLAITRRRE TISVLDSTRG KQGSQVFRMS GRQIKELYYK VWSNLRESKT
     EVLQYFLNWD EKKCREEWEA KDDTVFVEAL EKVGVFQRLR SMTSAGLQGP QYVKLQFSRH
     HRQLRSRYEL SLGMHLRDQL ALGVTPSKVP HWTAFLSMLI GLFYNKTFRQ KLEYLLEQIS
     EVWLLPHWLD LANVEVLAAD NTRVPLYMLM VAVHKELDSD DVPDGRFDII LLCRDSSREV
     GE