ID A0A3Q4ML57_NEOBR Unreviewed; 708 AA.
AC A0A3Q4ML57;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
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};
OS Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000013459.1, ECO:0000313|Proteomes:UP000261580};
RN [1] {ECO:0000313|Ensembl:ENSNBRP00000013459.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A3Q4ML57; -.
DR STRING; 32507.ENSNBRP00000013459; -.
DR Ensembl; ENSNBRT00000013833.1; ENSNBRP00000013459.1; ENSNBRG00000010410.1.
DR GeneTree; ENSGT00730000111191; -.
DR OMA; ERIPGWK; -.
DR Proteomes; UP000261580; Unplaced.
DR Bgee; ENSNBRG00000010410; Expressed in testis and 7 other cell types or tissues.
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 Mitochondrion {ECO:0000256|ARBA:ARBA00023271};
KW Mitochondrion nucleoid {ECO:0000256|ARBA:ARBA00023271};
KW Reference proteome {ECO:0000313|Proteomes:UP000261580};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..708
FT /note="Zinc phosphodiesterase ELAC protein 2"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018554946"
FT DOMAIN 47..106
FT /note="tRNase Z endonuclease"
FT /evidence="ECO:0000259|Pfam:PF13691"
FT DOMAIN 406..602
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|Pfam:PF12706"
FT REGION 20..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..708
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 708 AA; 78840 MW; E43F502A9C9F6AF3 CRC64;
LWAFFLLMLR KEGCAKAKQK EPLRRVKTKE NRSKRGDVHG PSTVYLQVVG AGSRDNAASV
YVFSEFNRYL FNCGEGTQRL MQEHKLKAAR LDNIFLTRLS WENVGGLSAK SRDNDRNRSH
RSGRNSPTQA TPQKADVSSA DDPGESEQAR LDMQRTAARD SSLVVAFACK LHPKKGNFLV
AQAKELGLPV GTAAIGPIIA ALKAGKSIVH EGKEIRPEQV CTPTDPGPVF IMVECPSEEF
LGALCTNQQL GRKRSALDQP LSTAFFSRLF LTSSYKCQGF IIFFPTLFLS STVEAHQGQM
WGEEKKTLLF SPAVFLQAVV CVFFTLVSFV RDAIPSCNSE EFVKEASEVP NFLAEVDECR
KICSAGSAEL SGKYPEVVFL GTGSALPMKI RNVSGTLVNI SPSQSLLLDC GEGTFGQLCR
HYGDDVDDAL SKIATVFISH LHADHHTGLV KLLYQRERAL ATLGKPFSPI FLVAPVQIMT
WLNQYHDYCE EILSHIKYVD TKTSELIRTH STSFHTCLVR HCKNAFACSF THQAGWKLAF
SGDTMPCDAF VHIGKNATLL IHEATLEDEL EEEAVEKRHS TTSQAIGIGM KMNADFIVLN
HFSQRYAKIP LFSEDFNDRV GISFDHMRIR FDDSKIIPKL IPALKTLFAE ELGEMEERRE
RREMRYPRGS SSEVTSEHKT GAPDVGRGAK RDQEETAAHV ETKRLKSS
//
