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YRF13_YEAST
ID   YRF13_YEAST             Reviewed;        1859 AA.
AC   P0CX14; D6VV70; P53345; Q9UQW1;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Y' element ATP-dependent helicase protein 1 copy 3;
DE            EC=3.6.4.12;
GN   Name=YRF1-3; OrderedLocusNames=YGR296W;
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=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(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; Z73081; CAA97329.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08381.1; -; Genomic_DNA.
DR   PIR; S64633; S64633.
DR   RefSeq; NP_011812.3; NM_001181425.3.
DR   RefSeq; NP_015040.1; NM_001184097.1.
DR   AlphaFoldDB; P0CX14; -.
DR   BioGRID; 33543; 8.
DR   BioGRID; 35932; 8.
DR   STRING; 4932.YGR296W; -.
DR   MaxQB; P0CX14; -.
DR   PaxDb; P0CX14; -.
DR   PRIDE; P0CX14; -.
DR   EnsemblFungi; YGR296W_mRNA; YGR296W; YGR296W.
DR   EnsemblFungi; YPL283C_mRNA; YPL283C; YPL283C.
DR   GeneID; 853213; -.
DR   GeneID; 855846; -.
DR   KEGG; sce:YGR296W; -.
DR   KEGG; sce:YPL283C; -.
DR   SGD; S000003528; YRF1-3.
DR   VEuPathDB; FungiDB:YGR296W; -.
DR   VEuPathDB; FungiDB:YPL283C; -.
DR   eggNOG; ENOG502QWCT; Eukaryota.
DR   HOGENOM; CLU_003044_2_0_1; -.
DR   BioCyc; YEAST:G3O-30952-MON; -.
DR   PRO; PR:P0CX14; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P0CX14; protein.
DR   ExpressionAtlas; P0CX14; baseline and differential.
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; IPR037240; ORC1-binding_dom.
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; SSF144005; SSF144005; 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..1859
FT                   /note="Y' element ATP-dependent helicase protein 1 copy 3"
FT                   /id="PRO_0000102203"
FT   DOMAIN          861..1038
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1095..1244
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1318..1485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1318..1461
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1462..1485
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         874..881
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1859 AA;  211115 MW;  65B3C19E1BFD40D7 CRC64;
     MEIENEQICT CIAQILHLLN SLIITFLDDD KTETGQSFVY IDGFLVKKHN NQHTIVNFET
     YKNKMKVSDR RKFEKANFDE FESALNNKND LVHCPSITLF ESIPTEVRSF YEDEKSGLIK
     VVKFRTGAMD RKRSFEKIVV SVMVGKNVQK FLTFVEDEPD FQGGPIPSKY LIPKKINLMV
     YTLFQVHTLK FNRKDYDTLS LFYLNRGYYN ELSFRVLERC YEIASARPND SSTMRTFTDF
     VSGTPIVRGL QKSTIRKYGY NLAPYMFLLL HVDELSIFSA YQASLPGEKK VDTERLKRDL
     CPRKPTEIKY FSQICNDMMN KKDRLGDILH IILRACALNF GAGPRGGAGD EEDRSITNEE
     PIIPSVDEHG LKVCKLRSPN TPRRLRKTLD AVKALLVSSC ACTARDLDIF DDNNGVAMWK
     WIKILYHEVA QETALKDSYR ITLVPSSDGV SVCGKLFNRE YVRGFYFACK AQFDNLWEEL
     NDCFYMPTVV DIASLILRNR EVLFREPKRG IDEYLENDSF LQMIPVKYRE IVLPKLRRDT
     NKMTAALKNK VTVAIDELTV PLMWMIHFAV GYPYRYPELQ LLAFAGPQRN VYVDDTTRRI
     QLYTDYNKNG SSEPRLKTLD GLTSDYVFYF VTVLRQMQIC ALGNSYDAFN HDPWMDVVGF
     EDPDQVTNRD ISRIVLYSYM FLNTAKGCLV EYATFRQYMR ELPKNAPQKL NFREMRQGLI
     ALGRHCVGSR FETDLYESAT SELMANHSVQ TGRNIYGVDS FSLTSVSGTT ATLLQERASE
     RWIQWLGLES DYHCSFSSTR NAEDVVAGEA ASSDHHQKIS RVTRKRPREP KSTNDILVAG
     QKLFGSSFEF RDLHQLRLCH EIYMADTPSV AVQAPPGYGK TELFHLPLIA LASKGDVKYV
     SFLFVPYTVL LANCMIRLSR CGCLNVAPVR NFIEEGCDGV TDLYVGIYDD LASTNFTDRI
     AAWENIVECT FRTNNVKLGY LIVDEFHNFE TEVYRQSQFG GITNLDFDAF EKAIFLSGTA
     PEAVADAALQ RIGLTGLAKK SMDINELKRS EDLSRGLSSY PTRMFNLIKE KSEVPLGHVH
     KIWKKVESQP EEALKLLLAL FEIEPESKAI VVASTTNEVE ELACSWRKYF RVVWIHGKLG
     AAEKVSRTKE FVTDGSMRVL IGTKLVTEGI DIKQLMMVIM LDNRLNIIEL IQGVGRLRDG
     GLCYLLSRKN SWAARNRKGE LPPIKEGCIT EQVREFYGLE SKKGKKGQHV GCCGSRTDLS
     ADTVELIERM DRLAEKQATA SMSIVALPSS FQESNSSDRC RKYCSSDEDS DTCIHGSANA
     STNATTNSST NATTTASTNV RTSATTTASI NVRTSATTTE STNSSTNATT TASTNVRTSA
     TTTASINVRT SATTTESTNS NTSATTTEST DSNTSATTTE STDSNTSATT TASTNSSTNA
     TTTASTNSST NATTTESTNA SAKEDANKDG NAEDNRFHPV TDINKESYKR KGSQMVLLER
     KKLKAQFPNT SENMNVLQFL GFRSDEIKHL FLYGIDVYFC PEGVFTQYGL CKGCQKMFEL
     CVCWAGQKVS YRRMAWEALA VERMLRNDEE YKEYLEDIEP YHGDPVGYLK YFSVKRGEIY
     SQIQRNYAWY LAITRRRETI SVLDSTRGKQ GSQVFRMSGR QIKELYYKVW SNLRESKTEV
     LQYFLNWDEK KCREEWEAKD DTVFVEALEK VGVFQRLRSM TSAGLQGPQY VKLQFSRHHR
     QLRSRYELSL GMHLRDQLAL GVTPSKVPHW TAFLSMLIGL FCNKTFRQKL EYLLEQISEV
     WLLPHWLDLA NVEVLAADNT RVPLYMLMVA VHKELDSDDV PDGRFDILLC RDSSREVGE
 
 
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