ID A0A3D8SEM8_9HELO Unreviewed; 934 AA.
AC A0A3D8SEM8;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=ribonuclease Z {ECO:0000256|ARBA:ARBA00012477};
DE EC=3.1.26.11 {ECO:0000256|ARBA:ARBA00012477};
GN ORFNames=BP6252_02154 {ECO:0000313|EMBL:RDW84564.1};
OS Coleophoma cylindrospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Dermateaceae; Coleophoma.
OX NCBI_TaxID=1849047 {ECO:0000313|EMBL:RDW84564.1, ECO:0000313|Proteomes:UP000256645};
RN [1] {ECO:0000313|EMBL:RDW84564.1, ECO:0000313|Proteomes:UP000256645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BP6252 {ECO:0000313|EMBL:RDW84564.1,
RC ECO:0000313|Proteomes:UP000256645};
RX PubMed=30018880; DOI=10.5598/imafungus.2018.09.01.13;
RA Wingfield B.D., Bills G.F., Dong Y., Huang W., Nel W.J.,
RA Swalarsk-Parry B.S., Vaghefi N., Wilken P.M., An Z., de Beer Z.W.,
RA De Vos L., Chen L., Duong T.A., Gao Y., Hammerbacher A., Kikkert J.R.,
RA Li Y., Li H., Li K., Li Q., Liu X., Ma X., Naidoo K., Pethybridge S.J.,
RA Sun J., Steenkamp E.T., van der Nest M.A., van Wyk S., Wingfield M.J.,
RA Xiong C., Yue Q., Zhang X.;
RT "IMA Genome-F 9: Draft genome sequence of Annulohypoxylon stygium,
RT Aspergillus mulundensis, Berkeleyomyces basicola (syn. Thielaviopsis
RT basicola), Ceratocystis smalleyi, two Cercospora beticola strains,
RT Coleophoma cylindrospora, Fusarium fracticaudum, Phialophora cf. hyalina,
RT and Morchella septimelata.";
RL IMA Fungus 9:199-223(2018).
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:RDW84564.1}.
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DR EMBL; PDLM01000002; RDW84564.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8SEM8; -.
DR STRING; 1849047.A0A3D8SEM8; -.
DR Proteomes; UP000256645; 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:UP000256645};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 111..173
FT /note="tRNase Z endonuclease"
FT /evidence="ECO:0000259|Pfam:PF13691"
FT DOMAIN 675..881
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|Pfam:PF12706"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 934 AA; 104198 MW; 8D197357ADB2F30A CRC64;
MHQLVPKIIK SPGSRNPAST LPRILRYSPP VKNADNRQSI LYQQNLRKQI RRLKNSANLP
FDRVHPGPKL EFDREDYWIV FDKRRKDNVS SVPPTILPNP GFYVKMRSWA SIITTPTADT
PGTAILLHFD NKRYLFGNIG EGTQRACIQR KIGLRNVEDL FITGTTSWDS TGGLLGMILT
LADQTSTARE SIEKTRQERL AKKGIVEVAP EAKKAFLNIH GAKNLTHLLC TARRFIFRKG
MPVNTNEIKP GRDGKQQDWE PTWSDLNIKV WAMAIEPEAT ASRSRKRSHE EMSDPDSENA
LSKAREEQED EEDRNDQMRK SILSSMFNST WRLDNLSSTK LSAVKLPAAI FVRNSAGKIE
KYNGPPWDPI LKNVPDVDVL VRSPWPGASI ESLPPTTPSK SSISYIIKNH TQRGKFNAKE
AKRLGVPPGP AFGKLSNGES VTAKDGSIVT PEMVMGTSRE GAGFAVIEIP DVSYIAPTLA
REEWSAPELM DGFTSIIWIL APGVLEDSRL QKFMQDHPMW KHVVSSSDCC SNYLALESAA
TAAIRLHLLD SERFPLPKHI NDVTLSDAQK VAKFDRARPG KILLLEPNFE VNDSGIVPYL
DTTKVVNEAS ADVAALAEIA RKQVTSPEYQ KKLDEQQADI PCRDAEIITL GTGSALPSKY
RNVSATLLRV PGYGNYLFDC GENTLGQLKR VFGNELPSIL SDLKVLWISH LHADHHLGTA
AVVKAWNQAT KDEPSKKLMV SSDGHMLSWL REYSEVEDFG FERLELAHLG RLNNKFEYEL
SETQTTSFGL TSIAATSVNH CAGALACVLR FPNGFSVAYS GDCRPSKSFE ELGYGATLLI
HEATFDDELK GDAMAKKHST TSEALQVGKN MNARRIMLTH FSQRYQKIPV MNTDGDKDQI
AIVAFDYMRV KLADFAKIEA YRTALLKLYE NEGE
//
