ID A0A3M0BJ75_9AQUI Unreviewed; 698 AA.
AC A0A3M0BJ75;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 02-APR-2025, entry version 22.
DE RecName: Full=Ribonuclease R {ECO:0000256|HAMAP-Rule:MF_01895};
DE Short=RNase R {ECO:0000256|HAMAP-Rule:MF_01895};
DE EC=3.1.13.1 {ECO:0000256|HAMAP-Rule:MF_01895};
GN Name=rnr {ECO:0000256|HAMAP-Rule:MF_01895};
GN ORFNames=CLV39_0873 {ECO:0000313|EMBL:RMA97217.1};
OS Hydrogenothermus marinus.
OC Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales;
OC Hydrogenothermaceae; Hydrogenothermus.
OX NCBI_TaxID=133270 {ECO:0000313|EMBL:RMA97217.1, ECO:0000313|Proteomes:UP000280842};
RN [1] {ECO:0000313|EMBL:RMA97217.1, ECO:0000313|Proteomes:UP000280842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VM1 {ECO:0000313|EMBL:RMA97217.1,
RC ECO:0000313|Proteomes:UP000280842};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: 3'-5' exoribonuclease that releases 5'-nucleoside
CC monophosphates and is involved in maturation of structured RNAs.
CC {ECO:0000256|HAMAP-Rule:MF_01895}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC nucleoside 5'-phosphates.; EC=3.1.13.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001849, ECO:0000256|HAMAP-
CC Rule:MF_01895};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01895}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase R subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01895}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RMA97217.1}.
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DR EMBL; REFO01000011; RMA97217.1; -; Genomic_DNA.
DR RefSeq; WP_121923002.1; NZ_REFO01000011.1.
DR AlphaFoldDB; A0A3M0BJ75; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000280842; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:TreeGrafter.
DR CDD; cd04471; S1_RNase_R; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 2.
DR HAMAP; MF_01895; RNase_R; 1.
DR InterPro; IPR011129; CSD.
DR InterPro; IPR040476; CSD2.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR013223; RNase_B_OB_dom.
DR InterPro; IPR001900; RNase_II/R.
DR InterPro; IPR022966; RNase_II/R_CS.
DR InterPro; IPR004476; RNase_II/RNase_R.
DR InterPro; IPR011805; RNase_R.
DR InterPro; IPR050180; RNR_Ribonuclease.
DR InterPro; IPR003029; S1_domain.
DR NCBIfam; TIGR00358; 3_prime_RNase; 1.
DR NCBIfam; TIGR02063; RNase_R; 1.
DR PANTHER; PTHR23355:SF9; DIS3-LIKE EXONUCLEASE 2; 1.
DR PANTHER; PTHR23355; RIBONUCLEASE; 1.
DR Pfam; PF17876; CSD2; 1.
DR Pfam; PF08206; OB_RNB; 1.
DR Pfam; PF00773; RNB; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00357; CSP; 1.
DR SMART; SM00955; RNB; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 4.
DR PROSITE; PS01175; RIBONUCLEASE_II; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01895};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_01895};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01895};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01895};
KW Reference proteome {ECO:0000313|Proteomes:UP000280842};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 617..697
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 698 AA; 80921 MW; 7A9A78AD77246BC8 CRC64;
MEITENEILE LFRQKKKPFY IKTLLKQLGL PKTEKQNLKK MLRKLQKKKL IKYQKGKYFL
IEKKQEEDLV KGQVEAHPSG YGFLIIGDQV EDLFIPPPEM KYLFDGDIVL AKPIKKKKKD
EAKVVKVLER VVKEGVGVLK KDKTGYYVLL SDTVIPHKIY VPKKQAEKIV KGSYVVVKIK
QYPEPKKRAK GDIVEVLGKT RNTKTVAEII ARKYGLPKRH SDEALQEAEK ISSRVVISKN
RKDLTKQVCF TIDPESARDF DDAVAIEKEG ENYRLYVHIA DVSHYVKEGS AIDKEAFERG
NTYYLPENAL HMLPERLSAD LCSLKPKEKR YAFTCEMLIN PKGKVIDYDI YESVIISKAR
LTYDQALGII LGDPELSEKY PDLVEPLKYM EELAKILLKE RERRGSIDFD LPESKILFTD
TGDPYDVVPY ERHFAHRLIE EFMIIANITV AKHMEKLEQP FIYRSHEEPD IEKVIKFVDL
VAGLGYEVNY PDVITPKFIQ KILKKVAGTP EEELIRFMAL RSMKQAKYTV ENYGHFGLAL
DTYTHFTSPI RRYADLVVHR MLKKSIKNKF TKKDLQTLPI KLEEVAKQCS KMERVAEEAE
RDALEILKLR ILSNHIGEEF EGIITGVVSF GLFVEIEKYI IEGLIPISSL EGYYIYDEQN
HRLIREDKQK SYRLGDKVKV RIEKVDEDLK KLDLSMVD
//
