ID A0A2U3X3C7_ODORO Unreviewed; 786 AA.
AC A0A2U3X3C7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Zinc phosphodiesterase ELAC protein 2 {ECO:0000256|ARBA:ARBA00013357};
DE EC=3.1.26.11 {ECO:0000256|ARBA:ARBA00012477};
DE AltName: Full=ElaC homolog protein 2 {ECO:0000256|ARBA:ARBA00032616};
DE AltName: Full=Ribonuclease Z 2 {ECO:0000256|ARBA:ARBA00030729};
DE AltName: Full=tRNA 3 endonuclease 2 {ECO:0000256|ARBA:ARBA00032104};
DE AltName: Full=tRNase Z 2 {ECO:0000256|ARBA:ARBA00030689};
GN Name=ELAC2 {ECO:0000313|RefSeq:XP_004416668.1};
OS Odobenus rosmarus divergens (Pacific walrus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Odobenidae;
OC Odobenus.
OX NCBI_TaxID=9708 {ECO:0000313|Proteomes:UP000245340, ECO:0000313|RefSeq:XP_004416668.1};
RN [1] {ECO:0000313|RefSeq:XP_004416668.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) 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 matrix, mitochondrion nucleoid
CC {ECO:0000256|ARBA:ARBA00004436}.
CC -!- SIMILARITY: Belongs to the RNase Z family.
CC {ECO:0000256|ARBA:ARBA00007823}.
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DR RefSeq; XP_004416668.1; XM_004416611.1.
DR AlphaFoldDB; A0A2U3X3C7; -.
DR GeneID; 101379017; -.
DR CTD; 60528; -.
DR OrthoDB; 296811at2759; -.
DR Proteomes; UP000245340; Unplaced.
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 CDD; cd16296; RNaseZ_ELAC2-N-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 Mitochondrion {ECO:0000256|ARBA:ARBA00023271};
KW Mitochondrion nucleoid {ECO:0000256|ARBA:ARBA00023271};
KW Reference proteome {ECO:0000313|Proteomes:UP000245340};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..786
FT /note="Zinc phosphodiesterase ELAC protein 2"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015488933"
FT DOMAIN 57..116
FT /note="tRNase Z endonuclease"
FT /evidence="ECO:0000259|Pfam:PF13691"
FT DOMAIN 468..682
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|Pfam:PF12706"
FT REGION 750..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..786
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 786 AA; 86891 MW; 28BEC93655B5AA23 CRC64;
MWALRSVLLL RSAAGRAMSQ GPARRQRPPK DLLRHLRTRE KRGAAWEPGG PNTVYLQVVA
AGGRDVGAAL YVFSEYNRYL FNCGEGVQRL MQEHKLKVAR LDNIFLTRMH WCNVGGLCGM
ILTLKETGLP KCVLSGPPQL EKYLEAIKIF SGPLKGIDLA VRPHSAPEYK DETMTVFQIP
IYSIGQKKSG RDPSLVVAFV CKLHVKKGNF LVLKAKELGL PVGTAAIAPI IAAVKGGKSI
TYEGREILPE EICTPPDPGL AFVVVECPDE GFIQPICENA TFKRYQGNAD APVALVVHMA
PECVLADPRY QQWMERFGPA TQHLVLNESC SSVHNLRSHK IQTQLSLIHP TIFPPLATPH
SQEEHPAFFR VPTVRGECLL KYQLRPRREW QRDAVIVCNS DEFIAEALEL PNFQESVQEY
REAVQDGPAP AEKRSQYPEI VFLGTGSAIP MKIRNVSATL VNVSPDRSLL LDCGEGTFGQ
LCRHYGDEVD RVLGTLAAVF VSHLHADHHT GLLNILLQRE RALASLGKPC PPLLVVAPTQ
LKAWLQLYHN QCQQLLQHVS LIPAKCLQKG AEVSSPAVER LIGSLLGACD LAEFQTCLVR
HCKHAFGCAL VHTSGWKVVY SGDTMPCEAL VQMGKDATLL IHEATLEDGL EEEAVEKTHS
TTSQAIGVGV RMNAGFTMLN HFSQRYAKVP LFSPDFNEKV GIAFDHMKVS FGDLPTVPKL
TAPLKALFAG DIEEMEERRE KREVRLARTA LLSREQAGGP EDGTPLQKRA LTEQPQNPQS
KKVRAQ
//