CYT19_NEUCR
ID CYT19_NEUCR Reviewed; 626 AA.
AC Q1K8F7;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=ATP-dependent RNA helicase cyt-19, mitochondrial {ECO:0000305};
DE EC=3.6.4.13 {ECO:0000269|PubMed:25002474};
GN Name=cyt-19 {ECO:0000303|PubMed:12086675};
GN ORFNames=NCU07670 {ECO:0000303|PubMed:12712197};
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [2]
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=12086675; DOI=10.1016/s0092-8674(02)00771-7;
RA Mohr S., Stryker J.M., Lambowitz A.M.;
RT "A DEAD-box protein functions as an ATP-dependent RNA chaperone in group I
RT intron splicing.";
RL Cell 109:769-779(2002).
RN [3]
RP FUNCTION.
RX PubMed=15618406; DOI=10.1073/pnas.0407896101;
RA Huang H.-R., Rowe C.E., Mohr S., Jiang Y., Lambowitz A.M., Perlman P.S.;
RT "The splicing of yeast mitochondrial group I and group II introns requires
RT a DEAD-box protein with RNA chaperone function.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:163-168(2005).
RN [4]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=16505350; DOI=10.1073/pnas.0600332103;
RA Mohr S., Matsuura M., Perlman P.S., Lambowitz A.M.;
RT "A DEAD-box protein alone promotes group II intron splicing and reverse
RT splicing by acting as an RNA chaperone.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3569-3574(2006).
RN [5]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=17075070; DOI=10.1073/pnas.0603127103;
RA Tijerina P., Bhaskaran H., Russell R.;
RT "Nonspecific binding to structured RNA and preferential unwinding of an
RT exposed helix by the CYT-19 protein, a DEAD-box RNA chaperone.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:16698-16703(2006).
RN [6]
RP FUNCTION, RNA-BINDING, AND DOMAIN.
RX PubMed=17311413; DOI=10.1021/bi0619472;
RA Grohman J.K., Del Campo M., Bhaskaran H., Tijerina P., Lambowitz A.M.,
RA Russell R.;
RT "Probing the mechanisms of DEAD-box proteins as general RNA chaperones: the
RT C-terminal domain of CYT-19 mediates general recognition of RNA.";
RL Biochemistry 46:3013-3022(2007).
RN [7]
RP FUNCTION.
RX PubMed=17081564; DOI=10.1016/j.jmb.2006.09.083;
RA Halls C., Mohr S., Del Campo M., Yang Q., Jankowsky E., Lambowitz A.M.;
RT "Involvement of DEAD-box proteins in group I and group II intron splicing.
RT Biochemical characterization of Mss116p, ATP hydrolysis-dependent and
RT -independent mechanisms, and general RNA chaperone activity.";
RL J. Mol. Biol. 365:835-855(2007).
RN [8]
RP FUNCTION.
RX PubMed=17960235; DOI=10.1038/nature06235;
RA Bhaskaran H., Russell R.;
RT "Kinetic redistribution of native and misfolded RNAs by a DEAD-box
RT chaperone.";
RL Nature 449:1014-1018(2007).
RN [9]
RP FUNCTION.
RX PubMed=19088196; DOI=10.1073/pnas.0811075106;
RA Chen Y., Potratz J.P., Tijerina P., Del Campo M., Lambowitz A.M.,
RA Russell R.;
RT "DEAD-box proteins can completely separate an RNA duplex using a single
RT ATP.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:20203-20208(2008).
RN [10]
RP FUNCTION.
RX PubMed=19393667; DOI=10.1016/j.jmb.2009.04.043;
RA Del Campo M., Mohr S., Jiang Y., Jia H., Jankowsky E., Lambowitz A.M.;
RT "Unwinding by local strand separation is critical for the function of DEAD-
RT box proteins as RNA chaperones.";
RL J. Mol. Biol. 389:674-693(2009).
RN [11]
RP FUNCTION.
RX PubMed=21878649; DOI=10.1074/jbc.m111.287706;
RA Sinan S., Yuan X., Russell R.;
RT "The Azoarcus group I intron ribozyme misfolds and is accelerated for
RT refolding by ATP-dependent RNA chaperone proteins.";
RL J. Biol. Chem. 286:37304-37312(2011).
RN [12]
RP FUNCTION, RNA-BINDING, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=25002474; DOI=10.1073/pnas.1404307111;
RA Jarmoskaite I., Bhaskaran H., Seifert S., Russell R.;
RT "DEAD-box protein CYT-19 is activated by exposed helices in a group I
RT intron RNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:E2928-E2936(2014).
RN [13]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=25350280; DOI=10.1371/journal.pbio.1001981;
RA Pan C., Potratz J.P., Cannon B., Simpson Z.B., Ziehr J.L., Tijerina P.,
RA Russell R.;
RT "DEAD-box helicase proteins disrupt RNA tertiary structure through helix
RT capture.";
RL PLoS Biol. 12:E1001981-E1001981(2014).
CC -!- FUNCTION: Acts as an RNA chaperone to resolve non-native structures
CC formed during RNA folding to promote mitochondrial group I, but also
CC group II, intron splicing. Functions predominantly by disrupting
CC accessible RNA secondary structure and depends on spontaneous openings
CC in tightly packed RNAs to gain access to RNA helices.
CC {ECO:0000269|PubMed:12086675, ECO:0000269|PubMed:15618406,
CC ECO:0000269|PubMed:16505350, ECO:0000269|PubMed:17075070,
CC ECO:0000269|PubMed:17081564, ECO:0000269|PubMed:17311413,
CC ECO:0000269|PubMed:17960235, ECO:0000269|PubMed:19088196,
CC ECO:0000269|PubMed:19393667, ECO:0000269|PubMed:21878649,
CC ECO:0000269|PubMed:25002474, ECO:0000269|PubMed:25350280}.
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 Evidence={ECO:0000269|PubMed:25002474};
CC -!- ACTIVITY REGULATION: Activated by exposed helices in a group I intron
CC RNA. {ECO:0000269|PubMed:25002474}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P15424}.
CC -!- DOMAIN: The C-ter region (residues 578-626) is not directly involved in
CC DNA unwinding activity but functions by tethering cyt-19 to structured
CC RNAs, so that it can efficiently disrupt exposed, non-native structural
CC elements, allowing them to refold. {ECO:0000269|PubMed:17311413}.
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 {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family.
CC {ECO:0000255|RuleBase:RU000492}.
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DR EMBL; CM002239; EAA33076.1; -; Genomic_DNA.
DR RefSeq; XP_962312.1; XM_957219.2.
DR AlphaFoldDB; Q1K8F7; -.
DR SMR; Q1K8F7; -.
DR STRING; 5141.EFNCRP00000008046; -.
DR EnsemblFungi; EAA33076; EAA33076; NCU07670.
DR GeneID; 3878451; -.
DR KEGG; ncr:NCU07670; -.
DR VEuPathDB; FungiDB:NCU07670; -.
DR HOGENOM; CLU_003041_26_6_1; -.
DR InParanoid; Q1K8F7; -.
DR OMA; KTQREGC; -.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR GO; GO:0005759; C:mitochondrial matrix; 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:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; 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 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; 2.
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 1: Evidence at protein level;
KW ATP-binding; Chaperone; Helicase; Hydrolase; Mitochondrion;
KW mRNA processing; mRNA splicing; Nucleotide-binding; Reference proteome;
KW RNA-binding.
FT CHAIN 1..626
FT /note="ATP-dependent RNA helicase cyt-19, mitochondrial"
FT /id="PRO_0000431670"
FT DOMAIN 106..297
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 329..493
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 569..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..626
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:17311413"
FT MOTIF 74..103
FT /note="Q motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00552"
FT MOTIF 241..244
FT /note="DEAD box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 569..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..620
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 119..126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 626 AA; 69397 MW; 99BFC63467711E17 CRC64;
MRTSVLRQAG LCRAALAARH LQISSKPSAA LLSQVTRAIA VQSLPSASLP RFYSAEATAQ
SNTAASNGLV TRFADLAALG VHENVVRAIT HGMGYENMTE VQSMTISPAL KGKDIVAQAK
TGTGKTLGFL VPVIQKIITQ DPDLAHRFGG KRARSDDIRA IIISPTRELA EQIGEEARKL
VKGTGIIVQT AVGGTQKNAM LYKTRQQGCH ILVGTPGRLN DLLSDSHSGI DAPRLSTLVL
DEADRMLEVG FNEELRQIIN YLPDRKVLPR QTLLYSATIP KDVVGLARSY IDKNNFEFVQ
TVKADEVLTH DRIPQYIVPC KGFENIYPAM LELIEKALNE SRTNPEALPF KAIVFLPTTA
EVIMANAIFK RLQWKFKHIP KTWDIHSKLT QNARTRAADE FKNARTGILF SSDVTARGMD
FPNVSHVIQT HIPPNREQYI HRLGRTGRAN KPGQGWLIVP DIELHAARSR LPGLPIKRND
ELECASVNAA DSGADKHANF QHILDAASRL PEDLFKDCYS SYLGGALQGI DRQALVYALN
DLAKFGWGLE EPPAVRQSIM KHMGRVQGLR VETREHSMRP MGSGPGHRRD FNSRGPRRQS
DDPFENALHR AQDLDRRPTR RQQASF
