ID Q0CMC4_ASPTN Unreviewed; 1076 AA.
AC Q0CMC4;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=ribonuclease Z {ECO:0000256|ARBA:ARBA00012477};
DE EC=3.1.26.11 {ECO:0000256|ARBA:ARBA00012477};
GN ORFNames=ATEG_05160 {ECO:0000313|EMBL:EAU34229.1};
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU34229.1, ECO:0000313|Proteomes:UP000007963};
RN [1] {ECO:0000313|Proteomes:UP000007963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) 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}.
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DR EMBL; CH476600; EAU34229.1; -; Genomic_DNA.
DR RefSeq; XP_001214338.1; XM_001214338.1.
DR AlphaFoldDB; Q0CMC4; -.
DR STRING; 341663.Q0CMC4; -.
DR EnsemblFungi; EAU34229; EAU34229; ATEG_05160.
DR GeneID; 4320770; -.
DR VEuPathDB; FungiDB:ATEG_05160; -.
DR eggNOG; KOG2121; Eukaryota.
DR HOGENOM; CLU_006220_0_0_1; -.
DR OMA; MSHCKHT; -.
DR OrthoDB; 296811at2759; -.
DR Proteomes; UP000007963; 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 GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
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:UP000007963};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 6..68
FT /note="tRNase Z endonuclease"
FT /evidence="ECO:0000259|Pfam:PF13691"
FT DOMAIN 609..663
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|Pfam:PF12706"
FT REGION 93..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 995..1076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1009
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1067
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1076 AA; 118699 MW; F45DA590C5FD5C7F CRC64;
MKFYFQVVTT PTADTPGTSV LLYFPDKRYF FGQISEGTQR ACTERGVRLS YLTDVFLTGR
MEWANTGGLI GVILTQADTL ASSTAAIETA AREKQARRQN NAKDGSTQPQ KLEHGVPYAV
EDGQAVAQRG RLTIHGPRNL AHTLATARRF VFRKGMPVYT KEYDSETMAR TMPGTEDPFE
NPTWSDSNIK VWAMPIRPAT SLPPKTASRQ PSPQSPRKRS LDEYEERNVP LDPMDEHTKN
QIMRQTVITD MFNSTWRMDA LVETPLAEVK MPAVMFVRNP ETKDLDRYTG PLPGSGEPLP
DIKVLVRQPW PGATVEKLPP TTWCDEAVSY IVRNHDIRGK FRPDVAKNLN VTPGPDYAKL
ARGESVLSKD NQTITPDMVL GPTRLGKGLA IIDLPTPEYV DGLVNRSEWN SPSVTTNLEA
FLWILGPGVG DHPRLHEFVA KMSHCKHTVS SSDYSPNYLS LASVAGSSVR MAQLRKENFP
VPVHDNVTIP QPGTPTAGTE IAKIPSFEPV EPGLVIDMEP KFVLNRSEVM PLFNTSKIAN
KMPRAVDQRM RTIQKRIKKP EFQQKLEDYR KGLPGADVEI IALGTGSSSP SKYRNVSSTL
LHVPGYGYYL LDCGENTLGQ LKRVFEPEQL REVLQNLRMI WISHLHADHH LGTASLIRAW
FHENYPDGVP HTTAVETDMA KILNEKRLFV VSEEMMVGWL EEYAGVENYG FGRLIPLSAN
PDLTNGVYRT ELLYRHCRAD GSYPGSESDE KPQITSLRLD DDTSPLTPLL RKATGLSNLL
ATKVSHCRGA MAVSLVFPDG FKISFSGDCR PSPIFAAVGH GSTVLIHEAT FQDNMQMSAI
AKKHSTVAEA LEIGRRMEAR SILLTHFSQR YQKVAHLDKQ DASVAAKLDR QVVTDQPPVS
NDVPDIPDNE PGDAAPELQG PVDSAPDAEP QLPLKAPVVA AFDYMRVRVG DMPLAQAYAP
AVGKLIDIFE RASAQETEKA KLELEKQMAV KAEAKKSKKK LKQEKLAAES AKAAKPAQPA
DSTKPAGSES AVPAEAPADA NKEPSKSVWS ASESESGWDT SGSDSEDAAL SNEKKQ
//
