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Database: UniProt
Entry: E4WYN6_OIKDI
LinkDB: E4WYN6_OIKDI
Original site: E4WYN6_OIKDI 
ID   E4WYN6_OIKDI            Unreviewed;       295 AA.
AC   E4WYN6;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Endoribonuclease LACTB2 {ECO:0000256|ARBA:ARBA00019428};
DE   AltName: Full=Beta-lactamase-like protein 2 {ECO:0000256|ARBA:ARBA00032142};
GN   ORFNames=GSOID_T00013574001 {ECO:0000313|EMBL:CBY22800.1};
OS   Oikopleura dioica (Tunicate).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Appendicularia; Copelata;
OC   Oikopleuridae; Oikopleura.
OX   NCBI_TaxID=34765 {ECO:0000313|EMBL:CBY22800.1};
RN   [1] {ECO:0000313|EMBL:CBY22800.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21097902; DOI=10.1126/science.1194167;
RA   Denoeud F., Henriet S., Mungpakdee S., Aury J.M., Da Silva C.,
RA   Brinkmann H., Mikhaleva J., Olsen L.C., Jubin C., Canestro C.,
RA   Bouquet J.M., Danks G., Poulain J., Campsteijn C., Adamski M., Cross I.,
RA   Yadetie F., Muffato M., Louis A., Butcher S., Tsagkogeorga G., Konrad A.,
RA   Singh S., Jensen M.F., Cong E.H., Eikeseth-Otteraa H., Noel B.,
RA   Anthouard V., Porcel B.M., Kachouri-Lafond R., Nishino A., Ugolini M.,
RA   Chourrout P., Nishida H., Aasland R., Huzurbazar S., Westhof E., Delsuc F.,
RA   Lehrach H., Reinhardt R., Weissenbach J., Roy S.W., Artiguenave F.,
RA   Postlethwait J.H., Manak J.R., Thompson E.M., Jaillon O., Du Pasquier L.,
RA   Boudinot P., Liberles D.A., Volff J.N., Philippe H., Lenhard B.,
RA   Roest Crollius H., Wincker P., Chourrout D.;
RT   "Plasticity of animal genome architecture unmasked by rapid evolution of a
RT   pelagic tunicate.";
RL   Science 330:1381-1385(2010).
CC   -!- FUNCTION: Endoribonuclease; cleaves preferentially 3' to purine-
CC       pyrimidine dinucleotide motifs in single-stranded RNA. The cleavage
CC       product contains a free 3' -OH group. Has no activity with double-
CC       stranded RNA or DNA. Required for normal mitochondrial function and
CC       cell viability. {ECO:0000256|ARBA:ARBA00002153}.
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC       Glyoxalase II family. {ECO:0000256|ARBA:ARBA00006759}.
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DR   EMBL; FN653019; CBY22800.1; -; Genomic_DNA.
DR   AlphaFoldDB; E4WYN6; -.
DR   InParanoid; E4WYN6; -.
DR   Proteomes; UP000001307; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd07722; LACTB2-like_MBL-fold; 1.
DR   Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR047921; LACTB2-like_MBL-fold.
DR   InterPro; IPR041516; LACTB2_WH.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR23131; ENDORIBONUCLEASE LACTB2; 1.
DR   PANTHER; PTHR23131:SF0; ENDORIBONUCLEASE LACTB2; 1.
DR   Pfam; PF17778; BLACT_WH; 1.
DR   Pfam; PF00753; Lactamase_B; 1.
DR   SMART; SM00849; Lactamase_B; 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:UP000001307}.
FT   DOMAIN          29..210
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|SMART:SM00849"
SQ   SEQUENCE   295 AA;  33186 MW;  F5EE4C8EE8F41D25 CRC64;
     MSGLQYVKRM TPSIIRILAR NPSPMTGHGT NCYLIGNGQR RVLLDTGSPN DESIVSSLVD
     VLDSENCEID KIVISHWHFD HIGGVEAIQR QIGSEIPLYK HKRVRYPKVY KGAGEKMPSG
     LDIPVFEEQY WNFLADGDVL ETSCGSKIQV VFTPGHADDH ICLWMENERV LFSGDNILGD
     STTVIDNYKA YMKSLEKMKT FGKCQIFPGH GDEIENGLER VEFYINHRRM RETQILKQLQ
     TGQKSISDIV KVLYADVPEV LHPAASINVA MTLDLLIENK AVSIVDADGD IYCRN
//
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