ROK1_PICGU
ID ROK1_PICGU Reviewed; 537 AA.
AC A5DIX5;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=ATP-dependent RNA helicase ROK1;
DE EC=3.6.4.13;
GN Name=ROK1; ORFNames=PGUG_03226;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- FUNCTION: ATP-dependent RNA helicase involved in 40S ribosomal subunit
CC biogenesis. Required for the processing and cleavage of 35S pre-rRNA at
CC sites A0, A1, and A2, leading to mature 18S rRNA.
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 the U3 snoRNA and is associated with the 90S
CC and 40S pre-ribosomes. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX52/ROK1
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDK39127.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH408157; EDK39127.2; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001485496.1; XM_001485446.1.
DR AlphaFoldDB; A5DIX5; -.
DR SMR; A5DIX5; -.
DR STRING; 4929.XP_001485496.1; -.
DR PRIDE; A5DIX5; -.
DR EnsemblFungi; EDK39127; EDK39127; PGUG_03226.
DR GeneID; 5127300; -.
DR KEGG; pgu:PGUG_03226; -.
DR eggNOG; KOG0344; Eukaryota.
DR HOGENOM; CLU_003041_1_4_1; -.
DR InParanoid; A5DIX5; -.
DR OrthoDB; 400908at2759; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IEA:InterPro.
DR CDD; cd17957; DEADc_DDX52; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR044764; DDX52/Rok1_DEADc.
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; IPR000629; RNA-helicase_DEAD-box_CS.
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; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 3: Inferred from homology;
KW ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..537
FT /note="ATP-dependent RNA helicase ROK1"
FT /id="PRO_0000294664"
FT DOMAIN 137..313
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 324..488
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 14..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 106..134
FT /note="Q motif"
FT MOTIF 260..263
FT /note="DEAD box"
FT COMPBIAS 14..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 150..157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 537 AA; 60013 MW; 5DC56D6D9E278C16 CRC64;
MDIFRILSRG AALKRSSNSD PGVKSESQNA TKDKQNSLLR QVEKETDFFN TRKHTEVTKD
IEDEAQDEAV PPPKITTEED AAKLRKQNKV NVSGTDIPLP IGSFEDLIAR CNLNRKLLAN
LIASGYSEPT AIQCEAIPAS AEGRDLIACA PTGSGKTLAY LIPMAQALIS SPKTKNYGIR
GVVIAPTNEL AIQIYQTLAP MCRGSNLNVT LLSKQVASKI SSSIISANKF DVLICTPLRL
IDLVKKEQVD LSKVEHLVID EADKLFDHGF VEQTDEILSH CTLPTRRTSM FSATIPSGVE
EMANSIMKDQ IRIIVGHKEG ASTSIDQKLV FTGNEEGKLL AIRQMVQQGE FKPPIIIFLQ
SIPRAKALFH ELIYDKLNVE VIHAERTPKQ REEAIRRFKN GDAWVLITTD VLARGVDFKG
VNLVINYDVP QTSQAYVHRI GRTGRGGKEG KAVTFFTKED KLAIKPVLNV MKQSGCHEGY
SEWMESMEKL TKKEKQQIKQ HEIKRKKIST VPQVVSKKRK QRKEMIEASK RRKEETK
