ROK1_CRYNB
ID ROK1_CRYNB Reviewed; 620 AA.
AC P0CR05; Q55PV3; Q5KDK3;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=ATP-dependent RNA helicase ROK1;
DE EC=3.6.4.13;
GN Name=ROK1; OrderedLocusNames=CNBG1110;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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}.
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DR EMBL; AAEY01000036; EAL19818.1; -; Genomic_DNA.
DR RefSeq; XP_774465.1; XM_769372.1.
DR AlphaFoldDB; P0CR05; -.
DR SMR; P0CR05; -.
DR EnsemblFungi; EAL19818; EAL19818; CNBG1110.
DR GeneID; 4937145; -.
DR KEGG; cnb:CNBG1110; -.
DR VEuPathDB; FungiDB:CNBG1110; -.
DR HOGENOM; CLU_003041_1_4_1; -.
DR Proteomes; UP000001435; Chromosome 7.
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:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 2.
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 Pfam; PF00270; DEAD; 2.
DR Pfam; PF00271; Helicase_C; 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 3: Inferred from homology;
KW ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..620
FT /note="ATP-dependent RNA helicase ROK1"
FT /id="PRO_0000410263"
FT DOMAIN 154..382
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 394..556
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 53..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 142..150
FT /note="Q motif"
FT MOTIF 329..332
FT /note="DEAD box"
FT COMPBIAS 81..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..281
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 167..174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 620 AA; 67192 MW; 646C295FD5845A41 CRC64;
MASAFSLLTA GGAKFDKNRF KDDFQLFEAK KRKDRKGKSK QIDALAAGSA LPSSLDFFGD
HPHPQHKPEP EPESESESDF ESDSGSSSTS IPAPPPQKIT LTGSEPLPKS LHTNLPSLVN
HESHSLTSAE GGPLLSALSR ANIHSLWGVQ CAVGGCLLED RDTLCVAPTG SGKTLSYVLP
TIVKLREPAR KLKGTEEGKG VRALVVVPTH DLAVQIQGVI KAVTMGRHWR SMVLTKATEK
AVWESAPGEA VKTGEDGDSE MKDGEDSGDE EEDEDDNEST GSVDEFAPKV SGNPEGLGID
VLVATPERLH HLIDSRRISL ARTKYVILDE SDRLLSSDFL PQVEPILSAC SNPAVQKCFL
SATMPAGAES LAKKWLKDGG VRVVVGVKDS AVTTVDQSLL YTGSESGKLL ALRNLISSGQ
LPYPSLIFVQ SIDRAEELYK TLVLDGIKVD AVHGGKAKTK RDEAIKDFRV GAVWMLVVTE
VLARGMDFRG VKVVINYDFP QTVPSYIHRI GRTGRAGRPG KAITFFNIED GPYLRTIANV
LRSSGCPVPE YMLDMKKPTK NEKKKLAKAP PKRKAVGGGG RDLNREAGKK KKQMVEASKK
RKMLERKGKG GNEEKNDDEE