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RNZ1_BOVIN
ID   RNZ1_BOVIN              Reviewed;         363 AA.
AC   Q29RY4;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Zinc phosphodiesterase ELAC protein 1;
DE            EC=3.1.26.11;
DE   AltName: Full=ElaC homolog protein 1;
DE   AltName: Full=Ribonuclease Z 1;
DE            Short=RNase Z 1;
DE   AltName: Full=tRNA 3 endonuclease 1;
DE   AltName: Full=tRNase Z 1;
GN   Name=ELAC1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Zinc phosphodiesterase, which displays some tRNA 3'-
CC       processing endonuclease activity. Probably involved in tRNA maturation,
CC       by removing a 3'-trailer from precursor tRNA (By similarity).
CC       {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Nucleus
CC       {ECO:0000250}. Note=Mainly cytosolic. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RNase Z family. {ECO:0000305}.
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DR   EMBL; BC113356; AAI13357.1; -; mRNA.
DR   RefSeq; NP_001039792.1; NM_001046327.1.
DR   RefSeq; XP_005224260.1; XM_005224203.3.
DR   RefSeq; XP_005224261.1; XM_005224204.3.
DR   AlphaFoldDB; Q29RY4; -.
DR   SMR; Q29RY4; -.
DR   STRING; 9913.ENSBTAP00000007468; -.
DR   PaxDb; Q29RY4; -.
DR   Ensembl; ENSBTAT00000007468; ENSBTAP00000007468; ENSBTAG00000005683.
DR   GeneID; 532568; -.
DR   KEGG; bta:532568; -.
DR   CTD; 55520; -.
DR   VEuPathDB; HostDB:ENSBTAG00000005683; -.
DR   VGNC; VGNC:97267; ELAC1.
DR   eggNOG; KOG2121; Eukaryota.
DR   GeneTree; ENSGT00730000111224; -.
DR   HOGENOM; CLU_031317_2_2_1; -.
DR   InParanoid; Q29RY4; -.
DR   OMA; GTQRQMM; -.
DR   OrthoDB; 1387038at2759; -.
DR   TreeFam; TF324462; -.
DR   Proteomes; UP000009136; Chromosome 24.
DR   Bgee; ENSBTAG00000005683; Expressed in anterior segment of eyeball and 106 other tissues.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0042781; F:3'-tRNA processing endoribonuclease activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042779; P:tRNA 3'-trailer cleavage; IBA:GO_Central.
DR   CDD; cd07717; RNaseZ_ZiPD-like_MBL-fold; 1.
DR   Gene3D; 3.60.15.10; -; 1.
DR   HAMAP; MF_01818; RNase_Z_BN; 1.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   InterPro; IPR013471; RNase_Z/BN.
DR   Pfam; PF00753; Lactamase_B; 1.
DR   Pfam; PF12706; Lactamase_B_2; 1.
DR   SUPFAM; SSF56281; SSF56281; 1.
DR   TIGRFAMs; TIGR02651; RNase_Z; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Endonuclease; Hydrolase; Metal-binding; Nuclease; Nucleus;
KW   Reference proteome; tRNA processing; Zinc.
FT   CHAIN           1..363
FT                   /note="Zinc phosphodiesterase ELAC protein 1"
FT                   /id="PRO_0000240601"
FT   ACT_SITE        66
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   BINDING         62
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         64
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         67
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         182
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         253
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         253
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         313
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   363 AA;  39979 MW;  2A6886919D497471 CRC64;
     MSMDVTFLGT GAAYPSPTRG ASALVLRCEG ECWLFDCGEG TQTQLMKSQL KAGRITKIFI
     THLHGDHFFG LPGLLCTISL QSGSMVTKQP IEIYGPVGLR DFIWRTMELS HTELVFPYVV
     HELVPTADQC PTEELQESVQ VDKTDNPPKE GEGRTILLDS EENSYLLVDD EQFVVKAFRL
     FHRIPSFGFS VVEKKRPGKL NAQKLKDLGV PPGPAYGKLK NGISVVLENG VTISPQDVLK
     KPIVGRKICI LGDCSGVVDD AGVKLCFEAD LLIHEATLDD TQMDKAKEHG HSTPQMAATF
     AKLCQAKRLV LTHFSQRYKP VALAREGEAD GIVELKKQAE SVLDLQEVTL AEDFMVISIP
     IKK
 
 
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