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}.
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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
//