DHR1_YEAST
ID DHR1_YEAST Reviewed; 1267 AA.
AC Q04217; D6VZV1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Probable ATP-dependent RNA helicase DHR1;
DE EC=3.6.4.13;
DE AltName: Full=DEAH box RNA helicase DHR1;
DE AltName: Full=Extracellular mutant protein 16;
GN Name=ECM16; Synonyms=DHR1; OrderedLocusNames=YMR128W; ORFNames=YM9553.04;
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, INTERACTION WITH SNORNA U3, AND SUBCELLULAR LOCATION.
RX PubMed=10982841; DOI=10.1128/mcb.20.19.7238-7246.2000;
RA Colley A., Beggs J.D., Tollervey D., Lafontaine D.L.J.;
RT "Dhr1p, a putative DEAH-Box RNA helicase, is associated with the box C+D
RT snoRNP U3.";
RL Mol. Cell. Biol. 20:7238-7246(2000).
RN [4]
RP IDENTIFICATION IN SSU PROCESSOME BY MASS SPECTROMETRY.
RX PubMed=12068309; DOI=10.1038/nature00769;
RA Dragon F., Gallagher J.E.G., Compagnone-Post P.A., Mitchell B.M.,
RA Porwancher K.A., Wehner K.A., Wormsley S., Settlage R.E., Shabanowitz J.,
RA Osheim Y., Beyer A.L., Hunt D.F., Baserga S.J.;
RT "A large nucleolar U3 ribonucleoprotein required for 18S ribosomal RNA
RT biogenesis.";
RL Nature 417:967-970(2002).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Probable ATP-binding RNA helicase. Required for 18S rRNA
CC synthesis. May play a role in restructuring of the pre-rRNA.
CC {ECO:0000269|PubMed:10982841}.
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=3.6.4.13;
CC -!- SUBUNIT: Interacts with snoRNA U3. Component of the ribosomal small
CC subunit (SSU) processome composed of at least 40 protein subunits and
CC snoRNA U3. {ECO:0000269|PubMed:10982841, ECO:0000269|PubMed:12068309}.
CC -!- INTERACTION:
CC Q04217; P47083: MPP10; NbExp=2; IntAct=EBI-1820, EBI-11168;
CC Q04217; P53254: UTP22; NbExp=3; IntAct=EBI-1820, EBI-1878;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10982841}.
CC -!- MISCELLANEOUS: Present with 2000 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000305}.
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DR EMBL; Z48622; CAA88553.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10025.1; -; Genomic_DNA.
DR PIR; S53058; S53058.
DR RefSeq; NP_013847.1; NM_001182629.1.
DR PDB; 6H57; X-ray; 2.30 A; A=1-1267.
DR PDB; 6ZQD; EM; 3.80 A; JD=1-1267.
DR PDB; 6ZQE; EM; 7.10 A; JD=1-1267.
DR PDB; 6ZQF; EM; 4.90 A; JD=1-1267.
DR PDB; 6ZQG; EM; 3.50 A; JD=1-1267.
DR PDB; 7AJU; EM; 3.80 A; JD=1-1267.
DR PDB; 7D4I; EM; 4.00 A; RZ=1-1267.
DR PDB; 7D5T; EM; 6.00 A; RZ=1-1267.
DR PDB; 7D63; EM; 12.30 A; RZ=1-1267.
DR PDB; 7MQJ; X-ray; 2.23 A; A=379-1174.
DR PDBsum; 6H57; -.
DR PDBsum; 6ZQD; -.
DR PDBsum; 6ZQE; -.
DR PDBsum; 6ZQF; -.
DR PDBsum; 6ZQG; -.
DR PDBsum; 7AJU; -.
DR PDBsum; 7D4I; -.
DR PDBsum; 7D5T; -.
DR PDBsum; 7D63; -.
DR PDBsum; 7MQJ; -.
DR AlphaFoldDB; Q04217; -.
DR SMR; Q04217; -.
DR BioGRID; 35305; 513.
DR ComplexPortal; CPX-1604; Small ribosomal subunit processome, variant 1.
DR ComplexPortal; CPX-1607; Small ribosomal subunit processome, variant 2.
DR ComplexPortal; CPX-1608; Small ribosomal subunit processome, variant 3.
DR DIP; DIP-6722N; -.
DR IntAct; Q04217; 34.
DR MINT; Q04217; -.
DR STRING; 4932.YMR128W; -.
DR iPTMnet; Q04217; -.
DR MaxQB; Q04217; -.
DR PaxDb; Q04217; -.
DR PRIDE; Q04217; -.
DR EnsemblFungi; YMR128W_mRNA; YMR128W; YMR128W.
DR GeneID; 855158; -.
DR KEGG; sce:YMR128W; -.
DR SGD; S000004735; ECM16.
DR VEuPathDB; FungiDB:YMR128W; -.
DR eggNOG; KOG0926; Eukaryota.
DR GeneTree; ENSGT00550000074985; -.
DR HOGENOM; CLU_001832_0_1_1; -.
DR InParanoid; Q04217; -.
DR OMA; GHQHGCM; -.
DR BioCyc; YEAST:G3O-32821-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:Q04217; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04217; protein.
DR GO; GO:0030686; C:90S preribosome; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0032040; C:small-subunit processome; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IDA:SGD.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IC:ComplexPortal.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0042254; P:ribosome biogenesis; IDA:SGD.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR007502; Helicase-assoc_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; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Helicase; Hydrolase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..1267
FT /note="Probable ATP-dependent RNA helicase DHR1"
FT /id="PRO_0000055162"
FT DOMAIN 401..580
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 675..858
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 516..519
FT /note="DEAH box"
FT COMPBIAS 1..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..285
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..718
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 414..421
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT HELIX 382..390
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 392..395
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 397..406
FT /evidence="ECO:0007829|PDB:7MQJ"
FT STRAND 408..413
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 420..430
FT /evidence="ECO:0007829|PDB:7MQJ"
FT TURN 431..434
FT /evidence="ECO:0007829|PDB:7MQJ"
FT STRAND 443..450
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 452..465
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 467..472
FT /evidence="ECO:0007829|PDB:7MQJ"
FT STRAND 473..476
FT /evidence="ECO:0007829|PDB:7MQJ"
FT STRAND 489..493
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 494..503
FT /evidence="ECO:0007829|PDB:7MQJ"
FT STRAND 510..515
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 518..520
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 523..545
FT /evidence="ECO:0007829|PDB:7MQJ"
FT TURN 547..549
FT /evidence="ECO:0007829|PDB:7MQJ"
FT STRAND 554..562
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 565..568
FT /evidence="ECO:0007829|PDB:7MQJ"
FT TURN 571..573
FT /evidence="ECO:0007829|PDB:7MQJ"
FT STRAND 580..582
FT /evidence="ECO:0007829|PDB:7MQJ"
FT STRAND 590..594
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 602..616
FT /evidence="ECO:0007829|PDB:7MQJ"
FT STRAND 621..625
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 629..642
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 651..654
FT /evidence="ECO:0007829|PDB:7MQJ"
FT TURN 666..668
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 673..675
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 685..691
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 693..696
FT /evidence="ECO:0007829|PDB:7MQJ"
FT STRAND 729..734
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 740..743
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 744..747
FT /evidence="ECO:0007829|PDB:7MQJ"
FT STRAND 755..760
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 763..766
FT /evidence="ECO:0007829|PDB:7MQJ"
FT STRAND 773..778
FT /evidence="ECO:0007829|PDB:7MQJ"
FT STRAND 781..788
FT /evidence="ECO:0007829|PDB:7MQJ"
FT TURN 789..792
FT /evidence="ECO:0007829|PDB:7MQJ"
FT STRAND 793..800
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 803..811
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 812..814
FT /evidence="ECO:0007829|PDB:7MQJ"
FT STRAND 815..825
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 827..833
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 841..844
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 847..856
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 873..885
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 897..903
FT /evidence="ECO:0007829|PDB:7MQJ"
FT STRAND 905..907
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 909..916
FT /evidence="ECO:0007829|PDB:7MQJ"
FT TURN 919..922
FT /evidence="ECO:0007829|PDB:6H57"
FT HELIX 924..936
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 943..946
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 976..993
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 1002..1013
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 1018..1020
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 1021..1028
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 1032..1053
FT /evidence="ECO:0007829|PDB:7MQJ"
FT STRAND 1054..1056
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 1064..1067
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 1074..1087
FT /evidence="ECO:0007829|PDB:7MQJ"
FT TURN 1088..1090
FT /evidence="ECO:0007829|PDB:7MQJ"
FT STRAND 1092..1095
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 1096..1099
FT /evidence="ECO:0007829|PDB:7MQJ"
FT STRAND 1100..1104
FT /evidence="ECO:0007829|PDB:7MQJ"
FT STRAND 1108..1110
FT /evidence="ECO:0007829|PDB:6H57"
FT HELIX 1112..1114
FT /evidence="ECO:0007829|PDB:7MQJ"
FT STRAND 1117..1119
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 1128..1131
FT /evidence="ECO:0007829|PDB:7MQJ"
FT STRAND 1133..1135
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 1140..1143
FT /evidence="ECO:0007829|PDB:7MQJ"
FT STRAND 1150..1158
FT /evidence="ECO:0007829|PDB:7MQJ"
FT STRAND 1160..1164
FT /evidence="ECO:0007829|PDB:7MQJ"
FT STRAND 1166..1172
FT /evidence="ECO:0007829|PDB:7MQJ"
FT HELIX 1175..1184
FT /evidence="ECO:0007829|PDB:6H57"
FT STRAND 1188..1190
FT /evidence="ECO:0007829|PDB:6H57"
FT TURN 1197..1199
FT /evidence="ECO:0007829|PDB:6H57"
FT STRAND 1202..1205
FT /evidence="ECO:0007829|PDB:6H57"
FT STRAND 1208..1213
FT /evidence="ECO:0007829|PDB:6H57"
FT STRAND 1215..1219
FT /evidence="ECO:0007829|PDB:6H57"
FT STRAND 1234..1241
FT /evidence="ECO:0007829|PDB:6H57"
FT STRAND 1244..1251
FT /evidence="ECO:0007829|PDB:6H57"
FT HELIX 1253..1262
FT /evidence="ECO:0007829|PDB:6H57"
SQ SEQUENCE 1267 AA; 144955 MW; 576DAAE6D934CC77 CRC64;
MGTYRKRFNE KARSGHMAKL KELKRIRNKQ FTRQDENDER VENPDSAPAE SSTTEPNANA
EILEPLTEEE KKMKKRKLQE LFTPKESKVS RLKKKRLDKF IEHQLKREER KTIIGKLQDY
KIDTSLLTSS KRLGEGRQTK KEEFKEALSL ERQGRGNEQT NEILYEEYEP KVWDEYGEGG
SSEDDDGEDD FEASFGSMPK PTDNEEKKSS GFIDHRPAKF GGSGLSFGFS NIKVINKESK
TPKKKYNWRQ RVEMEELKKH GKEDEMDFDT TSEDDDEEED QEEEDKMHPS ENPLEEVESA
DSETGSEKFD QNDVANEFKD WANQEIKKLE GRDQELVTPT LNIDYKPIIR KEDLDDGLQE
AYVPINENST RKAFYVEVSR SDEIQKARIQ LPVFGEEHKI MEAIHHNDVV IICGETGSGK
TTQVPQFLYE AGFGAEDSPD YPGMVGITQP RRVAAVSMAE RVANELGDHG HKVGYQIRFD
STAKEDTKVK FMTDGVLLRE MMHDFKLTKY SSIIIDEAHE RNINTDILIG MLSRCVRLRA
KLHKENPIEH KKLKLIIMSA TLRVSDFSEN KTLFPIAPPV LQVDARQFPV SIHFNRRTAF
NYTDEAFRKT CKIHQKLPPG AILVFLTGQQ EITHMVKRLR KEFPFKKNSK YNKDLETPVS
KMGINSKTTD LEAEDIDFSV QVIDQDKFKS AIRYEEDEGN SGNGEDEEDE EEEGFEEVLT
EGQTANDPLY VLPLYSLLPT KEQMRVFQKP PQGSRLCIVA TNVAETSLTI PGVRYVVDSG
RSKERKYNES NGVQSFEVGW VSKASANQRS GRAGRTGPGH CYRLYSSAVF EHDFEQFSKP
EILRMPVESI VLQMKSMAIH NIINFPFPTP PDRVALSKAI QLLQYLGALD NKEMITEDGK
KMSLFPLSPR FSKMLLVSDE KACLPYIVAI VSALSVGDPF INEFELGINE ISRKPNPDEN
LDDKIREHDE STPGMDPELK KELRSKFYKS RSQFSKLDKF SDVFRLLSVV SAMDYVPKEQ
KEIFMKKNFL RGKLMEEIVK LRKQLMYIIK SNTSKENIAV VIRNEDLKSD IPSVIQIKLL
KQMICAGFVD HVAVRADVLF PDDAKITNRT SIINIPYIPV LATRTPNIED CFVYIHPTSI
LNNLGEMPPK YMLYYSLHLG GNNKTRMNTL CDIASTPLAN IARKGLLLTY SKPLTGQGLK
TVNLSPTERY CYVVPRFGST VDNDLKIGWD LNPIAVHQKK QKGQWTVIKF ITRKGFQTIT
GEEKEKK
