ID   A0A420YBL5_9PEZI        Unreviewed;      1042 AA.
AC   A0A420YBL5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=ribonuclease Z {ECO:0000256|ARBA:ARBA00012477};
DE            EC=3.1.26.11 {ECO:0000256|ARBA:ARBA00012477};
GN   ORFNames=DL546_008136 {ECO:0000313|EMBL:RKU45207.1};
OS   Coniochaeta pulveracea.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX   NCBI_TaxID=177199 {ECO:0000313|EMBL:RKU45207.1, ECO:0000313|Proteomes:UP000275385};
RN   [1] {ECO:0000313|EMBL:RKU45207.1, ECO:0000313|Proteomes:UP000275385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CAB683 {ECO:0000313|EMBL:RKU45207.1,
RC   ECO:0000313|Proteomes:UP000275385};
RA   Borstlap C.J., De Witt R.N., Botha A., Volschenk H.;
RT   "Draft genome of the lignicolous fungus Coniochaeta pulveracea.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|ARBA:ARBA00000402};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC   -!- SIMILARITY: Belongs to the RNase Z family.
CC       {ECO:0000256|ARBA:ARBA00007823}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RKU45207.1}.
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; QVQW01000023; RKU45207.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A420YBL5; -.
DR   STRING; 177199.A0A420YBL5; -.
DR   Proteomes; UP000275385; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0042781; F:3'-tRNA processing endoribonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd07718; RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold; 1.
DR   Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 2.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   InterPro; IPR047151; RNZ2-like.
DR   InterPro; IPR027794; tRNase_Z_dom.
DR   PANTHER; PTHR12553; ZINC PHOSPHODIESTERASE ELAC PROTEIN 2; 1.
DR   PANTHER; PTHR12553:SF49; ZINC PHOSPHODIESTERASE ELAC PROTEIN 2; 1.
DR   Pfam; PF12706; Lactamase_B_2; 1.
DR   Pfam; PF13691; Lactamase_B_4; 1.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000275385};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          161..223
FT                   /note="tRNase Z endonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF13691"
FT   DOMAIN          729..958
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|Pfam:PF12706"
FT   REGION          1..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          241..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          332..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        333..348
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1042 AA;  115867 MW;  ED3E872A88643162 CRC64;
     MGRPPTPILR QHLIKDPSRA TSRSKTPWTI SLQKATSDAS SAKHNQYRSN PSVVPRTQVP
     FRQGKELPRA TTHSTDLDDR LKPSWLKADK KLFPSRSYIP YYKHRRNTRL SFYNQALRTP
     AWKPDQIPKY FIFANQEPNL DKIGHTPPPL WAQAQMVGTV EILTTPTADT PGGAVFLRFD
     HRSYVFGNAS EGTQRVFTSR GLSMAKIEDI FLTGLVDWHG NGGLLGMVLT LADIRTNKMM
     SRKEKDAERR KKGLATGDRD PREMDRLNIH GGKNLMQMLA TARGFIYRNG FPMRPQEVRD
     DPRPGETCSA EHDWEDENIR VWRVPVIAPE VEREPAQSRK RTFDSMSTDD GDANEAVTGQ
     AHGPGRPGTD IQSTEDVAAS YRRTSLDEQR NVELVHGVVL SMFNTDGYVD GLYEVDAQEA
     GGAQQLYIEK KQPGAIEPYT GNGATRTKVL VRKPSLVTTL PPTAPARMSM CYVVKTKTTR
     GKFFPNKAIS LGVQKTDFKR LTAGESVTGH GGLLVTPEMV MDAPPEPNGF AVVELPDGSY
     IEPFLARPEW KNEDIMRGLR AFYWNIRDPK ILENERITSF MDSHSKPKHI VMSRTAGANP
     IVLEGSAMET TKLHMIDSEI FPLLPFSDPA PASPSKHEKL AYNDNSIIPP FDMRRAIEQF
     ASENKEIIAL AKAAQNKVSD PAFQSAVDAL DADIPSRDAE IIPLGTGSAL PSKTRNVSCT
     LIRIPGIGNY LLDCGENSLG QLRRMYGYSG ADEILRDLKA IWISHSHADH HLGTISMLRR
     YSEVMPASSP TNPYSQPHTT DKPLALIAHP LYHQFISEYA EVENFGLDTH VHQMINAPAS
     GKRGRHYSRI DNDSHATSLL NKFGIQALAV CKVDHCADAQ AVAITFTSGL KIAYSGDCRP
     SHDFASDGVG RDAHLLIHEA TLEDGKQADA IMKKHCTVGE ALSVAKEMRA RNVLLTHFSQ
     RYPTMPVFDQ GAMVVDSGEG EKDVPVLVAF DFMRVKLGGF RRAREFLPAL QKLYEKSEEE
     DDGGGELDGV EKEVVKKKRI DS
//