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Database: UniProt
Entry: A0A0G0AT41_TRIHA
LinkDB: A0A0G0AT41_TRIHA
Original site: A0A0G0AT41_TRIHA 
ID   A0A0G0AT41_TRIHA        Unreviewed;       845 AA.
AC   A0A0G0AT41;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=ribonuclease Z {ECO:0000256|ARBA:ARBA00012477};
DE            EC=3.1.26.11 {ECO:0000256|ARBA:ARBA00012477};
GN   ORFNames=THAR02_00370 {ECO:0000313|EMBL:KKP07574.1};
OS   Trichoderma harzianum (Hypocrea lixii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=5544 {ECO:0000313|EMBL:KKP07574.1, ECO:0000313|Proteomes:UP000034112};
RN   [1] {ECO:0000313|Proteomes:UP000034112}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T6776 {ECO:0000313|Proteomes:UP000034112};
RX   PubMed=26067977; DOI=10.1128/genomeA.00647-15;
RA   Baroncelli R., Piaggeschi G., Fiorini L., Bertolini E., Zapparata A.,
RA   Pe M.E., Sarrocco S., Vannacci G.;
RT   "Draft whole-genome sequence of the biocontrol agent Trichoderma harzianum
RT   T6776.";
RL   Genome Announc. 3:E0064715-E0064715(2015).
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:KKP07574.1}.
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DR   EMBL; JOKZ01000005; KKP07574.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0AT41; -.
DR   OMA; MSHCKHT; -.
DR   OrthoDB; 296811at2759; -.
DR   Proteomes; UP000034112; 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; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034112};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          9..68
FT                   /note="tRNase Z endonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF13691"
FT   DOMAIN          580..790
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|Pfam:PF12706"
FT   REGION          173..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   845 AA;  94571 MW;  3F805FCFF5C912E1 CRC64;
     MTTTVELAAV PSVDTPGTCI YMHHDKRSYV FGRVTEGTQR AFGSRKIHMG GTEHVFLSGS
     VNWEQLGGLC GYLLSVGGAI ESAKEFTTQE NAKRQQKGQK LLNKTLHAGI AVHGADNLCH
     TLAACRPVIF RQPICVRTYE HRTDPRATDA TNLEPDWSDD AIKVWKIPVR RARSSSPRKR
     RHSDPTMAVD EDASPEDALF QPRPSVSDPE VASAIVERIM FNGSLKNRSV LIPKKIRDLK
     PTDKAAIVEN GTIRLYKGPY MADGVEISNP DSTVWHFPDI GEIGVDDRSN NVLAINHFPL
     PRTTYGETSM SYIIKTHDRR GKFNAPAAKS LGVEPRDFKL LTAGQSVQGK DGLVTPEMVL
     GETQRGRGII VADISSQDFI ESFMERPEWK NKELMENVAV MYWILGPDMT GDARIQQFIQ
     QHASIKHIFC ADEACPNMIT HPGAATIQTK LRRLDPERFP LLKFENTVRY PAPSEGSPIE
     LGRAGQKFQL MPRLVFDDQA IAPFPDLVEA YDSVDDEVLK MAEEARTEAT NPEFLERVEK
     QEFDIPNRDA EIIPLGTGSS VPSKYRNVSA TLIRVPGIGN YLLDCGEGTL GQIRRLFGAE
     EAADVLRNLR CIVISHVHAD HHMGTPSLIK AWYEQTLRDN SNATLAISCI GRYRILLEEL
     SQIEDIGYHR LRFPSCPWPK EKDRDLTTRE DLGEENFGLA SIKRVPVPHC WRSFGTQLEL
     TSGLKIAYSG DCRPSKLFAQ ECHGAHLLVH ECTFGDDKQD HAKAKKHSTM GEALGVAREM
     GARRTLLTHF SQRYSKSDSL RRERVEGVEH DVLLAFDFMA VKLGDFQKAA CYLPSVERFM
     EKLAD
//
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