RNZ_CAEEL
ID RNZ_CAEEL Reviewed; 833 AA.
AC O44476; Q688B7;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Ribonuclease Z;
DE Short=RNase Z;
DE EC=3.1.26.11;
DE AltName: Full=CeELAC2;
DE AltName: Full=Homolog of ELAC2 protein 1;
DE AltName: Full=tRNA 3 endonuclease;
DE AltName: Full=tRNase Z;
GN Name=hoe-1; ORFNames=E04A4.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=14729485; DOI=10.1016/j.ydbio.2003.10.016;
RA Smith M.M., Levitan D.J.;
RT "The Caenorhabditis elegans homolog of the putative prostate cancer
RT susceptibility gene ELAC2, hoe-1, plays a role in germline proliferation.";
RL Dev. Biol. 266:151-160(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Zinc phosphodiesterase, which displays some tRNA 3'-
CC processing endonuclease activity. Probably involved in tRNA maturation,
CC by removing a 3'-trailer from precursor tRNA (By similarity). Involved
CC in germline proliferation. May be required for both mitosis and meiosis
CC in germ cells. {ECO:0000250, ECO:0000269|PubMed:14729485}.
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}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=O44476-1; Sequence=Displayed;
CC Name=b;
CC IsoId=O44476-2; Sequence=VSP_009390;
CC -!- TISSUE SPECIFICITY: Highly expressed in the germline.
CC {ECO:0000269|PubMed:14729485}.
CC -!- SIMILARITY: Belongs to the RNase Z family. {ECO:0000305}.
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DR EMBL; FO081039; CCD68705.1; -; Genomic_DNA.
DR EMBL; FO081039; CCD68706.1; -; Genomic_DNA.
DR PIR; T32608; T32608.
DR RefSeq; NP_001023109.1; NM_001027938.4. [O44476-1]
DR RefSeq; NP_001023110.1; NM_001027939.2. [O44476-2]
DR AlphaFoldDB; O44476; -.
DR SMR; O44476; -.
DR BioGRID; 42370; 7.
DR STRING; 6239.E04A4.4a; -.
DR iPTMnet; O44476; -.
DR EPD; O44476; -.
DR PaxDb; O44476; -.
DR PeptideAtlas; O44476; -.
DR PRIDE; O44476; -.
DR EnsemblMetazoa; E04A4.4a.1; E04A4.4a.1; WBGene00001983. [O44476-1]
DR EnsemblMetazoa; E04A4.4b.1; E04A4.4b.1; WBGene00001983. [O44476-2]
DR GeneID; 177241; -.
DR KEGG; cel:CELE_E04A4.4; -.
DR UCSC; E04A4.4a; c. elegans. [O44476-1]
DR CTD; 177241; -.
DR WormBase; E04A4.4a; CE29748; WBGene00001983; hoe-1. [O44476-1]
DR WormBase; E04A4.4b; CE36588; WBGene00001983; hoe-1. [O44476-2]
DR eggNOG; KOG2121; Eukaryota.
DR InParanoid; O44476; -.
DR OMA; YICQLKP; -.
DR OrthoDB; 454909at2759; -.
DR PhylomeDB; O44476; -.
DR BRENDA; 3.1.26.11; 1045.
DR PRO; PR:O44476; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001983; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; O44476; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042781; F:3'-tRNA processing endoribonuclease activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007281; P:germ cell development; IMP:WormBase.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:WormBase.
DR GO; GO:0072684; P:mitochondrial tRNA 3'-trailer cleavage, endonucleolytic; IBA:GO_Central.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0040026; P:positive regulation of vulval development; IGI:WormBase.
DR Gene3D; 3.60.15.10; -; 2.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF12706; Lactamase_B_2; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Endonuclease; Hydrolase; Metal-binding; Nuclease;
KW Nucleus; Reference proteome; tRNA processing; Zinc.
FT CHAIN 1..833
FT /note="Ribonuclease Z"
FT /id="PRO_0000155833"
FT REGION 624..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..645
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..73
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:14729485"
FT /id="VSP_009390"
SQ SEQUENCE 833 AA; 93864 MW; 3803C0A48C99F143 CRC64;
MLGAIARKTV ENRILVSRHL ISSTSCLFKD NNEELLESIK ERIARNRRIL QKHSSSHLKA
REVNASISNL RQSMAAVQKK QKAAHEPPAN SIVNIPSQVS IEVLGNGTGL LRACFILRTP
LKTYMFNCPE NACRFLWQLR IRSSSVVDLF ITSANWDNIA GISSILLSKE SNALSTRLHG
AMNIKHFLEC IRPFQDSDYG SCKYPSQVEE RPYTMENYED AGLKVTYIPL SPPLNIGSNN
EKSKNVKVNN VDIAFLIEMK EAARRIDTMK LMELKVPKGP LIGKLKSGEA VTLPDGRTIQ
PDQVFSSDKV EGDKPLLLVT ECTTEDHVKA LIDSSSLQPF LNGEKQLDYM VHISDDAVIN
TPTYRHLMEK LNNPSITHLL INGGNPVIPA VESVYKHTRL LRSIAPSLFP ALHPIDWSGI
ITQNEELSQR QDQFIRVAPM QRYWMRRGAS FNEEPIVNNL LAAEPELSDK AKELIKEYQK
LEKENKMDCE FPKLTFFGTS SAVPSKYRNV TGYLVEASEN SAILIDVGEG TYGQMRAVFG
EDGCKQLLVN LNCVLITHAH QDHMNGLYTI IARRKEAFES LGAPYRPLVL VCNRNVLKPM
KTYSICFENI EHLLEIVDIS RYPLTPPGSP GGPPGKRPRL PSPHLPPSRD VLQDMSSSFD
KKAWKLDELK AVQVHHTRMA NGFVMRVAGK RIVFSGDTKP CDLLVEEGKD ADVLVHESTF
EDGHEADAMR KRHSTMGQAV DVGKRMNAKH IILTHFSARY PKVPVLPEYL DKENIGVAMD
MLRVRFDHLP LVSKLLPIFR EVFVAELFEL TIKKEQRVLK DKELSEKRGQ LKA
