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Database: UniProt
Entry: A0A182UAI9_9DIPT
LinkDB: A0A182UAI9_9DIPT
Original site: A0A182UAI9_9DIPT 
ID   A0A182UAI9_9DIPT        Unreviewed;       794 AA.
AC   A0A182UAI9;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=ribonuclease Z {ECO:0000256|ARBA:ARBA00012477};
DE            EC=3.1.26.11 {ECO:0000256|ARBA:ARBA00012477};
OS   Anopheles melas.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=34690 {ECO:0000313|EnsemblMetazoa:AMEC016901-PA, ECO:0000313|Proteomes:UP000075902};
RN   [1] {ECO:0000313|Proteomes:UP000075902}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM1001059 {ECO:0000313|Proteomes:UP000075902};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles melas CM1001059_A (V2).";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AMEC016901-PA}
RP   IDENTIFICATION.
RC   STRAIN=CM1001059 {ECO:0000313|EnsemblMetazoa:AMEC016901-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
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   AlphaFoldDB; A0A182UAI9; -.
DR   STRING; 34690.A0A182UAI9; -.
DR   EnsemblMetazoa; AMEC016901-RA; AMEC016901-PA; AMEC016901.
DR   VEuPathDB; VectorBase:AMEC016901; -.
DR   Proteomes; UP000075902; 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   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          41..92
FT                   /note="tRNase Z endonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF13691"
FT   DOMAIN          496..709
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|Pfam:PF12706"
FT   REGION          163..183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   794 AA;  89793 MW;  6FEE7C4516EC44E5 CRC64;
     MPLDPKHIAE AQKQRLKLKQ KVSKVSPGIV NLQVLGCGAP GTPASVYLFT DQTRYLFNCG
     EGTQRLAYEH KTKLSCLENI FMTRTNWERI GGLPGICLTM QDVGVPAVSL HGPPGLDELF
     KAMRRFVILK DMKVEASEYA TGDVYEDHVM TLRYVVINRQ PASATREAGS DEDQNQDEAT
     VDDTDYYAYE RKRETLQKPQ SEAAKTVQST NWTKREESSV MAYICKLKPR HGQLSLEQCV
     ELGVPPGPLL GQLKNGNDVT LPDGRVVRSC EVRAPDDPGP VFMFIDIPSR EYMDDFVAKA
     ELFEKYQQTA VEESDQAIFV VHFSPLDVMR CDEYRQFMDR FSASTRHIAL NEVNSFSGYI
     AAHRIQYHLN QLDGQIFPLL REENNQYADP PANDTDLVRS SSLSYMHIRP PKGIDRTLEA
     SLNPQEYLNE LELLPDFKEA LAELKQQLAQ HTVRRSAAVR AEQFPRLIFL GTGSSIPNKT
     RNVSAILILT SKQSSILLDC GEGTVGQIWR VFGKEQAEEI LRSIKMVYIS HLHADHHLGL
     IGLLQARKKL LGDNCERLTL VAPEQISYWL RLYDCRFETI HRDYVLVKNA DLLENPLQDE
     KLLAMGIKEI ATCRVRHCPH SFGVALKVAS LGTHPETNIE GDVKITYSGD TMPCESLIEL
     GRDSTVLIHE ATMEDELSAE ARIKMHSTLS QAIEQGRKMN ARYTLLTHFS QRYAKIPRLR
     PEQQQAGLGT DLGIAFDNME VTLDDLPTLC KFYPALKAMF ISHFEEMEQK AIKRGNKKLR
     LETATRSKEC SPTR
//
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