ID A0A0P1IUB1_9RHOB Unreviewed; 410 AA.
AC A0A0P1IUB1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Ribonuclease D {ECO:0000256|HAMAP-Rule:MF_01899};
DE Short=RNase D {ECO:0000256|HAMAP-Rule:MF_01899};
DE EC=3.1.13.5 {ECO:0000256|HAMAP-Rule:MF_01899};
GN Name=rnd_2 {ECO:0000313|EMBL:CUK27239.1};
GN Synonyms=rnd {ECO:0000256|HAMAP-Rule:MF_01899};
GN ORFNames=TA5114_03066 {ECO:0000313|EMBL:CUK27239.1};
OS Cognatishimia activa.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Cognatishimia.
OX NCBI_TaxID=1715691 {ECO:0000313|EMBL:CUK27239.1, ECO:0000313|Proteomes:UP000051184};
RN [1] {ECO:0000313|Proteomes:UP000051184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5114 {ECO:0000313|Proteomes:UP000051184};
RA Rodrigo-Torres Lidia, Arahal R.David.;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Exonuclease involved in the 3' processing of various
CC precursor tRNAs. Initiates hydrolysis at the 3'-terminus of an RNA
CC molecule and releases 5'-mononucleotides. {ECO:0000256|HAMAP-
CC Rule:MF_01899}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage that removes extra residues from the
CC 3'-terminus of tRNA to produce 5'-mononucleotides.; EC=3.1.13.5;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01899};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01899};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01899}.
CC -!- SIMILARITY: Belongs to the RNase D family. {ECO:0000256|HAMAP-
CC Rule:MF_01899}.
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DR EMBL; CYUE01000021; CUK27239.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P1IUB1; -.
DR STRING; 1715691.TA5113_02918; -.
DR Proteomes; UP000051184; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0033890; F:ribonuclease D activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042780; P:tRNA 3'-end processing; IEA:UniProtKB-UniRule.
DR CDD; cd06142; RNaseD_exo; 1.
DR Gene3D; 1.10.150.80; HRDC domain; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR HAMAP; MF_01899; RNase_D; 1.
DR InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR InterPro; IPR010997; HRDC-like_sf.
DR InterPro; IPR002121; HRDC_dom.
DR InterPro; IPR044876; HRDC_dom_sf.
DR InterPro; IPR006292; RNase_D.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR NCBIfam; TIGR01388; rnd; 1.
DR PANTHER; PTHR47649; RIBONUCLEASE D; 1.
DR PANTHER; PTHR47649:SF1; RIBONUCLEASE D; 1.
DR Pfam; PF01612; DNA_pol_A_exo1; 1.
DR Pfam; PF00570; HRDC; 1.
DR SMART; SM00474; 35EXOc; 1.
DR SUPFAM; SSF47819; HRDC-like; 2.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50967; HRDC; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01899};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_01899};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01899, ECO:0000313|EMBL:CUK27239.1};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01899};
KW Reference proteome {ECO:0000313|Proteomes:UP000051184};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_01899}.
FT DOMAIN 236..317
FT /note="HRDC"
FT /evidence="ECO:0000259|PROSITE:PS50967"
SQ SEQUENCE 410 AA; 46450 MW; E099B3935287D37E CRC64;
MHFNEFARKP YMGPQEIKNE DSRFMKTLTT TEELAQFCKE ARQHPYVTID TEFLRERTYY
SKLCLVQLAY PGEGDENAVL VDPLVDGLSL EPLYELFRDT NVVKVFHAAR QDLEIFFIEA
GVFPDPLFDT QVAAMVCGFG EQVGYETLVR KIARQGLDKS SRFTDWSRRP LTDAQKKYAL
GDVTHLRKIY EFLAEKLEET GRARWVKEEL TVLTSPETYI LDPEDAWKRV KTRTTTPKFL
AIVRELAKFR ERLAQSRNIP RNRVYKDDAL IELASTKPQT PQDLGRSRLL LREARKGEIA
EGILAAIKAG IECPPADMPK VKKAKDSQQV NPALADLLRV LLKSKTERSG VASKLIANAA
ELDAIASGER DVPSLKGWRR EVFGEDALRL CDGQIALSAK GSNIKIIQLS
//
