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YP204_YEAST
ID   YP204_YEAST             Reviewed;        1032 AA.
AC   Q08995; D6W4K2;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Y' element ATP-dependent helicase YPR204W;
DE            EC=3.6.4.12;
GN   OrderedLocusNames=YPR204W;
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=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(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.
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   -!- SIMILARITY: Belongs to the helicase family. Yeast subtelomeric Y'
CC       repeat subfamily. {ECO:0000305}.
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DR   EMBL; Z73541; CAA97896.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11618.1; -; Genomic_DNA.
DR   PIR; S65341; S65341.
DR   RefSeq; NP_015530.1; NM_001184301.1.
DR   AlphaFoldDB; Q08995; -.
DR   BioGRID; 36374; 4.
DR   IntAct; Q08995; 3.
DR   STRING; 4932.YPR204W; -.
DR   MaxQB; Q08995; -.
DR   PaxDb; Q08995; -.
DR   EnsemblFungi; YPR204W_mRNA; YPR204W; YPR204W.
DR   GeneID; 856334; -.
DR   KEGG; sce:YPR204W; -.
DR   SGD; S000006408; YPR204W.
DR   VEuPathDB; FungiDB:YPR204W; -.
DR   eggNOG; ENOG502QWCT; Eukaryota.
DR   GeneTree; ENSGT00940000153173; -.
DR   HOGENOM; CLU_011178_2_0_1; -.
DR   BioCyc; YEAST:G3O-34324-MON; -.
DR   PRO; PR:Q08995; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; Q08995; protein.
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; IDA:SGD.
DR   GO; GO:0032508; P:DNA duplex unwinding; IDA:SGD.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00271; Helicase_C; 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.
FT   CHAIN           1..1032
FT                   /note="Y' element ATP-dependent helicase YPR204W"
FT                   /id="PRO_0000268169"
FT   DOMAIN          1..175
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          232..381
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          455..658
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           121..124
FT                   /note="DEAH box"
FT   COMPBIAS        455..634
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        635..658
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         11..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1032 AA;  115156 MW;  9D276DE8865CEB2A CRC64;
     MADTPSVAVQ APPGYGKTEL FHLPLIALAS KGDVKYVSFL FVPYTVLLAN CMIRLGRCGC
     LNVAPVRNFI EEGCDGVTDL YVGIYDDLAS TNFTDRIAAW ENIVECTFRT NNVKLGYLIV
     DEFHNFETEV YRQSQFGGIT NLDFDAFEKA IFLSGTAPEA VADAALQRIG LTGLAKKSMD
     INELKRSEDL SRGLSSYPTR MFNLIKEKSE VPLGHVHKIW KKVESQPEEA LKLLLALFEI
     EPESKAIVVA STTNEVEELA CSWRKYFRVV WIHGKLGAAE KVSRTKEFVT DGSMRVLIGT
     KLVTEGIDIK QLMMVIMLDN RLNIIELIQG VGRLRDGGLC YLLSRKNSWA ARNRKGELPP
     IKEGCITEQV REFYGLESKK GKKGQHVGCC GSRTDLSADT VELIERMDRL AEKQATASMS
     IVALPSSFQE SNSSDRCRKY CSSDEDSNTC IHGSANASTN ATTNSSTNAT TTASTNVRTS
     ATTTASINVR TSATTTESTN SSTNATTTAS TNVRTSATTT ASINVRTSAT TTESTNSNTS
     ATTTESTDSN TSATTTESTN SSTNATTTAS INVRTSATTT ESTNSNTNAT TTESTNSSTN
     ATTTEGTNSN TSATTTASTN SSTNATTTES TNASAKEDAN KDGNAEDNRF HPVTDINKES
     YKRKGSQMVL LERKKLKAQF PNTSENMNVL QFLGFRSDEI KHLFLYGIDV YFCPEGVFTQ
     YGLCKGCQKM FELCVCWAGQ KVSYRRMAWE ALAVERMLRN DEEYKEYLED IEPYHGDPVG
     YLKYFSVKRG EIYSQIQRNY AWYLAITRRR ETISVLDSTR GKQGSQVFRM SGRQIKELYY
     KVWSNLRESK TEVLQYFLNW DEKKCREEWE AKDDTVFVEA LEKVGVFQRL RSMTSAGLQG
     PQYVKLQFSR HHRQLRSRYE LSLGMHLRDQ LALGVTPSKV PHWTAFLSML IGLFCNKTFR
     QKLEYLLEQI SEVWLLPHWL DLANVEVLAA DNTRVPLYML MVAVHKELDS DDVPDGRFDI
     LLCRDSSREV GE
 
 
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