RNZ_DROME
ID RNZ_DROME Reviewed; 766 AA.
AC Q8MKW7; Q8MRT4; Q9GZ73;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Ribonuclease Z, mitochondrial {ECO:0000303|PubMed:14715923};
DE Short=RNase Z {ECO:0000303|PubMed:14715923};
DE EC=3.1.26.11;
DE AltName: Full=Juvenile hormone-inducible protein 1 {ECO:0000303|PubMed:10926782};
DE AltName: Full=dRNAse Z;
DE AltName: Full=tRNA 3 endonuclease;
DE Short=DmeZ;
DE AltName: Full=tRNase Z;
DE Flags: Precursor;
GN Name=RNaseZ {ECO:0000303|PubMed:14715923, ECO:0000312|FlyBase:FBgn0028426};
GN Synonyms=JhI-1 {ECO:0000303|PubMed:10926782};
GN ORFNames=CG3298 {ECO:0000312|FlyBase:FBgn0028426};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE, AND INDUCTION.
RX PubMed=10926782; DOI=10.1006/dbio.2000.9800;
RA Dubrovsky E.B., Dubrovskaya V.A., Bilderback A.L., Berger E.M.;
RT "The isolation of two juvenile hormone-inducible genes in Drosophila
RT melanogaster.";
RL Dev. Biol. 224:486-495(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP FUNCTION, PROBABLE SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=14715923; DOI=10.1093/nar/gkh182;
RA Dubrovsky E.B., Dubrovskaya V.A., Levinger L., Schiffer S., Marchfelder A.;
RT "Drosophila RNase Z processes mitochondrial and nuclear pre-tRNA 3' ends in
RT vivo.";
RL Nucleic Acids Res. 32:255-262(2004).
CC -!- FUNCTION: Zinc phosphodiesterase, which displays some tRNA 3'-
CC processing endonuclease activity of nuclear and mitochondrial pre-tRNA.
CC Probably involved in tRNA maturation, by removing a 3'-trailer from
CC precursor tRNA. May participate in tRNA processing in the developing
CC embryo. {ECO:0000269|PubMed:14715923}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of RNA, removing extra 3' nucleotides
CC from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy
CC group is left at the tRNA terminus and a 5'-phosphoryl group is left
CC at the trailer molecule.; EC=3.1.26.11;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Mitochondrion
CC {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Maternally expressed. Highly expressed in ovarian
CC nurse cells and transferred into the nascent oocyte.
CC {ECO:0000269|PubMed:14715923}.
CC -!- INDUCTION: By juvenile hormone (JH). {ECO:0000269|PubMed:10926782}.
CC -!- MISCELLANEOUS: The dual subcellular location may be due to some
CC alternative splicing and/or initiation that changes the initiator
CC methionine.
CC -!- SIMILARITY: Belongs to the RNase Z family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF99588.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF215894; AAF99588.1; ALT_INIT; mRNA.
DR EMBL; AE013599; AAM68783.1; -; Genomic_DNA.
DR EMBL; AY119279; AAM51139.1; -; mRNA.
DR RefSeq; NP_724916.1; NM_165763.3.
DR AlphaFoldDB; Q8MKW7; -.
DR SMR; Q8MKW7; -.
DR BioGRID; 61905; 3.
DR IntAct; Q8MKW7; 3.
DR STRING; 7227.FBpp0087449; -.
DR PaxDb; Q8MKW7; -.
DR PRIDE; Q8MKW7; -.
DR EnsemblMetazoa; FBtr0088360; FBpp0087449; FBgn0028426.
DR GeneID; 36086; -.
DR KEGG; dme:Dmel_CG3298; -.
DR CTD; 36086; -.
DR FlyBase; FBgn0028426; RNaseZ.
DR VEuPathDB; VectorBase:FBgn0028426; -.
DR eggNOG; KOG2121; Eukaryota.
DR GeneTree; ENSGT00730000111191; -.
DR HOGENOM; CLU_006220_2_0_1; -.
DR InParanoid; Q8MKW7; -.
DR PhylomeDB; Q8MKW7; -.
DR BRENDA; 3.1.26.11; 1994.
DR BioGRID-ORCS; 36086; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 36086; -.
DR PRO; PR:Q8MKW7; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0028426; Expressed in egg chamber and 25 other tissues.
DR Genevisible; Q8MKW7; DM.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0042781; F:3'-tRNA processing endoribonuclease activity; IDA:FlyBase.
DR GO; GO:0016891; F:endoribonuclease activity, producing 5'-phosphomonoesters; IMP:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0036093; P:germ cell proliferation; IMP:FlyBase.
DR GO; GO:0140040; P:mitochondrial polycistronic RNA processing; IMP:FlyBase.
DR GO; GO:0072684; P:mitochondrial tRNA 3'-trailer cleavage, endonucleolytic; IMP:FlyBase.
DR GO; GO:1902375; P:nuclear tRNA 3'-trailer cleavage, endonucleolytic; IMP:FlyBase.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:FlyBase.
DR GO; GO:0045727; P:positive regulation of translation; IMP:FlyBase.
DR GO; GO:0001558; P:regulation of cell growth; IMP:FlyBase.
DR GO; GO:0042780; P:tRNA 3'-end processing; IMP:FlyBase.
DR GO; GO:0034414; P:tRNA 3'-trailer cleavage, endonucleolytic; IDA:FlyBase.
DR GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IMP:UniProtKB.
DR GO; GO:0007419; P:ventral cord development; HMP:FlyBase.
DR Gene3D; 3.60.15.10; -; 3.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR027794; tRNase_Z_dom.
DR Pfam; PF12706; Lactamase_B_2; 1.
DR Pfam; PF13691; Lactamase_B_4; 1.
DR SUPFAM; SSF56281; SSF56281; 2.
PE 2: Evidence at transcript level;
KW Developmental protein; Endonuclease; Hydrolase; Metal-binding;
KW Mitochondrion; Nuclease; Nucleus; Reference proteome; Transit peptide;
KW tRNA processing; Zinc.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 26..766
FT /note="Ribonuclease Z, mitochondrial"
FT /id="PRO_0000030990"
FT CONFLICT 4
FT /note="V -> I (in Ref. 4; AAM51139)"
FT /evidence="ECO:0000305"
FT CONFLICT 8
FT /note="G -> R (in Ref. 2; AAM68783)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="I -> T (in Ref. 1; AAF99588)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="V -> A (in Ref. 1; AAF99588)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="P -> S (in Ref. 1; AAF99588)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="V -> E (in Ref. 1; AAF99588)"
FT /evidence="ECO:0000305"
FT CONFLICT 312..317
FT /note="VESFSS -> LENFSP (in Ref. 1; AAF99588)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="Y -> N (in Ref. 1; AAF99588)"
FT /evidence="ECO:0000305"
FT CONFLICT 556
FT /note="E -> K (in Ref. 1; AAF99588)"
FT /evidence="ECO:0000305"
FT CONFLICT 690
FT /note="T -> S (in Ref. 2; AAM68783)"
FT /evidence="ECO:0000305"
FT CONFLICT 722
FT /note="I -> V (in Ref. 2; AAM68783)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 766 AA; 85492 MW; 293ED2F8B521EDAB CRC64;
MYLVKSAGSP IYRTLRTLTT SNLMAATIAS AKDPLTGPRY EREPNVLRKK LASVVPGTVN
LQVLGSGANG APAAVYLFTD QARYLFNCGE GTQRLAHEHK TRLSRLEQIF LTQNTWASCG
GLPGLTLTIQ DAGVRDIGLH GPPHLGSMLQ SMRRFVVLKN LQVRPNDCSE GACFEDSILK
VDSLPLINSE DPTKSVINYI CQLKPRAGAL NLVKCVEQGV PPGPLLGQLK NGNDITLPDG
KVVRSVDVTE ASETALSFVF LDVPSENYLP ALLTHGKRLK KLGEEKLTEV ALVVHFTPYH
ISSRQVYKDF VVESFSSEAQ HIYLSSPLNQ FSGYAAAHRI QHQLHQLAPQ VFPLLGEQLS
CQSQTLSLNL KKTKLDEADS EDKANAKANE TEEQGVVAMT NYHLRPRKGL DRTLESKLTP
EEYVKETHAV PGFLELLAKF KEEYSFPDNS ADSYPKIIFL GTGSCIPNKT RNVSSILIRT
AIDAYVLLDC GEGTYGQIVR LYGHEKGQLI LRQLQAIYVS HLHADHHIGL IGLLRERRQL
KPRADPLILL APRQIEPWLE FYNRQIETVE DAYTLVGNGE LLASPLSGEQ VERLGITSIS
TCLVRHCPNS FGISLTLAAK HNSEPVKITY SGDTMPCQDL IDLGRDSTVL IHEATMEDDL
EEEARLKTHS TVSQAIQQGR NMNARHTILT HFSQRYAKCP RLPSDEDMQR VAIAFDNMEV
TIEDLQHYHK LYPALFAMYA EYTEELEQRA VKRELKQERK RKLAET
