ID A0A2R8AKQ7_9RHOB Unreviewed; 386 AA.
AC A0A2R8AKQ7;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
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_1 {ECO:0000313|EMBL:SPF76474.1};
GN Synonyms=rnd {ECO:0000256|HAMAP-Rule:MF_01899};
GN ORFNames=ALP8811_01479 {ECO:0000313|EMBL:SPF76474.1};
OS Aliiroseovarius pelagivivens.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Aliiroseovarius.
OX NCBI_TaxID=1639690 {ECO:0000313|EMBL:SPF76474.1, ECO:0000313|Proteomes:UP000244911};
RN [1] {ECO:0000313|EMBL:SPF76474.1, ECO:0000313|Proteomes:UP000244911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8811 {ECO:0000313|EMBL:SPF76474.1,
RC ECO:0000313|Proteomes:UP000244911};
RA Keele B.F.;
RL Submitted (MAR-2018) 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; OMOI01000001; SPF76474.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R8AKQ7; -.
DR OrthoDB; 9800549at2; -.
DR Proteomes; UP000244911; 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:SPF76474.1};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01899};
KW Reference proteome {ECO:0000313|Proteomes:UP000244911};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_01899}.
FT DOMAIN 212..293
FT /note="HRDC"
FT /evidence="ECO:0000259|PROSITE:PS50967"
SQ SEQUENCE 386 AA; 43651 MW; 79C0CA745A260070 CRC64;
MITITTTEAL EEFCIRATSH PYVTVDTEFL RERTYYSKLC LIQLAVPGND DEDAVLVDPL
VDGLSLEPLY ELFRDERVVK VFHAARQDLE IFFVEAGVFP RPLFDTQVAA MVCGFGDQVG
YETLVRKIER AQMDKSSRFT DWSRRPLTDA QKKYAQGDVT HLRGIYEYLS KELEKSGRAH
WVQEELTSLT SPETYTIHPD DAWKRLKTRT NSGRFLGVAK ELARFREGYA QSRNIPRNRV
MKDDALLELA STKPRTIQEL GRSRLLLREA RKGEVAEEIL KAISVGLELP QDQLPKAPDR
SKEKLQVNPA LADLLRVLLK ARCEQEKVAQ KLIASAADLD ALAAGKRDVV ALTGWRAEVF
GDDALRLCEG KLALAAKGQR VEVFEV
//
