YRF18_YEAST
ID YRF18_YEAST Reviewed; 1796 AA.
AC P0CX22; D6VTG2; O94087; P24088; P24089; Q53WX0; Q99313;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Y' element ATP-dependent helicase protein 1 copy 8;
DE EC=3.6.4.12;
GN Name=YRF1-8; OrderedLocusNames=YOR396W; ORFNames=O7535;
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].
RC STRAIN=ATCC 90839 / S288c / YP1;
RX PubMed=1628806; DOI=10.1093/genetics/131.3.559;
RA Louis E.J., Haber J.E.;
RT "The structure and evolution of subtelomeric Y' repeats in Saccharomyces
RT cerevisiae.";
RL Genetics 131:559-574(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 90839 / S288c / YP1;
RX PubMed=7785338; DOI=10.1002/yea.320110410;
RA Pryde F.E., Huckle T.C., Louis E.J.;
RT "Sequence analysis of the right end of chromosome XV in Saccharomyces
RT cerevisiae: an insight into the structural and functional significance of
RT sub-telomeric repeat sequences.";
RL Yeast 11:371-382(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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, 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=AAC48994.1; Type=Frameshift; Note=Produces 2 separate ORFs.; Evidence={ECO:0000305};
CC Sequence=AAC48995.1; Type=Frameshift; Note=Produces 2 separate ORFs.; Evidence={ECO:0000305};
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DR EMBL; U23472; AAC48994.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U23472; AAC48995.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z75302; CAA99727.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11154.1; -; Genomic_DNA.
DR PIR; S65004; S65004.
DR RefSeq; NP_010834.1; NM_001180853.1.
DR RefSeq; NP_013572.3; NM_001182355.3.
DR RefSeq; NP_061495.4; NM_001184447.3.
DR AlphaFoldDB; P0CX22; -.
DR BioGRID; 31723; 19.
DR BioGRID; 32590; 30.
DR BioGRID; 34775; 4.
DR iPTMnet; P0CX22; -.
DR PRIDE; P0CX22; -.
DR EnsemblFungi; YDR545W_mRNA; YDR545W; YDR545W.
DR EnsemblFungi; YLR467W_mRNA; YLR467W; YLR467W.
DR EnsemblFungi; YOR396W_mRNA; YOR396W; YOR396W.
DR GeneID; 851189; -.
DR GeneID; 852158; -.
DR GeneID; 854577; -.
DR KEGG; sce:YDR545W; -.
DR KEGG; sce:YLR467W; -.
DR KEGG; sce:YOR396W; -.
DR SGD; S000007526; YRF1-8.
DR VEuPathDB; FungiDB:YDR545W; -.
DR VEuPathDB; FungiDB:YLR467W; -.
DR VEuPathDB; FungiDB:YOR396W; -.
DR GeneTree; ENSGT00940000153173; -.
DR HOGENOM; CLU_003044_2_0_1; -.
DR BioCyc; YEAST:G3O-33895-MON; -.
DR PRO; PR:P0CX22; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P0CX22; protein.
DR ExpressionAtlas; P0CX22; baseline.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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..1796
FT /note="Y' element ATP-dependent helicase protein 1 copy 8"
FT /id="PRO_0000409757"
FT DOMAIN 797..974
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1031..1180
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 743..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1254..1278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1294..1421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..767
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1294..1397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1398..1421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 810..817
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CONFLICT 1293
FT /note="I -> T (in Ref. 1; AAC48995)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1796 AA; 203781 MW; BC241E78ABBB6FF1 CRC64;
MKVSDRRKFE KANFDEFESA LNNKNDLVHC PSITLFESIP TEVRSFYEDE KSGLIKVVKF
RTGAMDRKRS FEKIVISVMV GKNVQKFLTF VEDEPDFQGG PIPSKYLIPK KINLMVYTLF
QVHTLKFNRK DYDTLSLFYL NRGYYNELSF RVLERCHEIA SARPNDSSTM RTFTDFVSGA
PIVRSLQKST IRKYGYNLAP YMFLLLHVDE LSIFSAYQAS LPGEKKVDTE RLKRDLCPRK
PIEIKYFSQI CNDMMNKKDR LGDILHIILR ACALNFGAGP RGGAGDEEDR SITNEEPIIP
SVDEHGLKVC KLRSPNTPRR LRKTLDAVKA LLVSSCACTA RDLDIFDDTN GVAMWKWIKI
LYHEVAQETT LKDSYRITLV PSSDGISVCG KLFNREYVRG FYFACKAQFD NLWGELNNCF
YMPTVVDIAS LILRNREVLF REPKRGIDEY LENDSFLQMI PVKYREIVLP KLRRDTNKMT
AALKNKVTVA IDELTVPLMW MVHFAVGYPY RYPELQLLAF AGPQRNVYVD DTTRRIQLYT
DYNKNGSSEP RLKTLDGLTS DYVFYFVTVL RQMQICALGN SYDAFNHDPW MDVVGFEDPD
QVTNRDISRI VLYSYMFLNT AKGCLVEYAT FRQYMRELPK NAPQKLNFRE MRQGLIALGR
HCVGSRFETD LYESATSELM ANHSVQTGRN IYGVDSFSLT SVSGTTATLL QERASERWIQ
WLGLESDYHC SFSSTRNAED VVAGEAASSD HDQKISRVTR KRPREPKSTN DILVAGQKLF
GSSFEFRDLH QLRLCHEIYM ADTPSVAVQA PPGYGKTELF HLPLIALASK GDVKYVSFLF
VPYTVLLANC MIRLSRCGCL NVAPVRNFIE EGCDGVTDLY VGIYDDLAST NFTDRIAAWE
NIVECTFRTN NVKLGYLIVD EFHNFETEVY RQSQFGGITN LDFDAFEKAI FLSGTAPEAV
ADAALQRIGL TGLAKKSMDI NELKRSEDLS RGLSSYPTRM FNLIKEKSEV PLGHVHKIWK
KVESQPEEAL KLLLALFEIE PESKAIVVAS TTNEVEELAC SWRKYFRVVW IHGKLGAAEK
VSRTKEFVTD GSMRVLIGTK LVTEGIDIKQ LMMVIMLDNR LNIIELIQGV GRLRDGGLCY
LLSRKNSWAA RNRKGELPPI KEGCITEQVR EFYGLESKKG KKGQHVGCCG SRTDLSADTV
ELIERMDRLA EKQATASMSI IALPSSFQES NSSDRCRKYC SSDEDSDTCI HGSANASTNA
TTNSSTNATT TASTNVRTSA TTTASINVRT SAITTESTNS STNATTTAST NVRTSATTTA
SINVRTSATT TESTNSNTSA TTTESTDSNT SATTTESTDS NTSATTTAST NSSTNATTTA
STNSSTNATT TESTNASAKE DANKDGNAED NRFHPVTDIN KESYKRKGSQ MVLLERKKLK
AQFPNTSENM NVLQFLGFRS DEIKHLFLYG IDVYFCPEGV FTQYGLCKGC QKMFELCVCW
AGQKVSYRRM AWEALAVERM LRNDEEYKEY LEDIEPYHGD PVGYLKYFSV KRGEIYSQIQ
RNYAWYLAIT RRRETISVLD STRGKQGSQV FRMSGRQIKE LYYKVWSNLR ESKTEVLQYF
LNWDEKKCRE EWEAKDDTVF VEALEKVGVF QRLRSMTSAG LQGPQYVKLQ FSRHHRQLRS
RYELSLGMHL RDQLALGVTP SKVPHWTAFL SMLIGLFYNK TFRQKLEYLL EQISEVWLLP
HWLDLANVEV LAADNTRVPL YMLMVAVHKE LDSDDVPDGR FDIILLCRDS SREVGE