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Database: UniProt
Entry: D5ATC8_RHOCB
LinkDB: D5ATC8_RHOCB
Original site: D5ATC8_RHOCB 
ID   D5ATC8_RHOCB            Unreviewed;       384 AA.
AC   D5ATC8;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 64.
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=rnd2 {ECO:0000313|EMBL:ADE85235.1};
GN   Synonyms=rnd {ECO:0000256|HAMAP-Rule:MF_01899};
GN   OrderedLocusNames=RCAP_rcc01490 {ECO:0000313|EMBL:ADE85235.1};
OS   Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodobacter.
OX   NCBI_TaxID=272942 {ECO:0000313|EMBL:ADE85235.1, ECO:0000313|Proteomes:UP000002361};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SB1003;
RA   Strnad H., Lapidus A., Vlcek C., Ulbrich P., Paces J., Maltsev N.,
RA   Kumar V., Kogan Y., Milgram A., Rebrekov D., Mazur M., Cox R., Kyrpides N.,
RA   Kolar M., Sachova J., Ridl J., Ivanova N., Kapatral V., Los T., Lykidis A.,
RA   Mikhailova N., Reznik G., Vasieva O., Fonstein M., Paces V., Haselkorn R.;
RT   "Complete genome sequence of Rhodobacter capsulatus SB1003.";
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADE85235.1, ECO:0000313|Proteomes:UP000002361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003
RC   {ECO:0000313|Proteomes:UP000002361};
RX   PubMed=20418398; DOI=10.1128/JB.00366-10;
RA   Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA   Haselkorn R.;
RT   "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT   Rhodobacter capsulatus SB 1003.";
RL   J. Bacteriol. 192:3545-3546(2010).
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; CP001312; ADE85235.1; -; Genomic_DNA.
DR   RefSeq; WP_013067214.1; NC_014034.1.
DR   AlphaFoldDB; D5ATC8; -.
DR   STRING; 272942.RCAP_rcc01490; -.
DR   GeneID; 31490371; -.
DR   KEGG; rcp:RCAP_rcc01490; -.
DR   eggNOG; COG0349; Bacteria.
DR   HOGENOM; CLU_042387_0_0_5; -.
DR   OrthoDB; 9800549at2; -.
DR   Proteomes; UP000002361; Chromosome.
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:ADE85235.1};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01899};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002361};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_01899}.
FT   DOMAIN          211..292
FT                   /note="HRDC"
FT                   /evidence="ECO:0000259|PROSITE:PS50967"
SQ   SEQUENCE   384 AA;  42826 MW;  792B30F86F793688 CRC64;
     MQTITTTDAL EQFCTRAKAA PYVTVDTEFL RERTYWSKLC LVQMALPGKE GEAVLVDPLV
     EGLSLEPLYD LFRHQATVKV FHAARQDLEI FFTEAGVFPL PLFDTQVAAM VCGFGEQVGY
     ETLVKKIAKQ SLDKTSRFTD WSRRPLTDAQ KAYALADVTH LRVIYEFLSK ELRKSGREKW
     VEEEEAILLN PETYITRPED AWERVKTRTN SGRFMAVVRE LARFRETFAQ GRNIPRSRVF
     KDDALLELAS TKPVSLDELG KSRLLLREAR RGDIADGIIA AVKAGLETKP EDFPRVPDED
     AQLQVNTALA DLLRVLLKAK SEEAGVAAKL IATASDLDRI AAGKRDVAAL NGWRLDVFGN
     DALRLAKGEI ALTASGGAVR VVQV
//
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