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Database: UniProt
Entry: A0A1M6T1N8_9AQUI
LinkDB: A0A1M6T1N8_9AQUI
Original site: A0A1M6T1N8_9AQUI 
ID   A0A1M6T1N8_9AQUI        Unreviewed;       681 AA.
AC   A0A1M6T1N8;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
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=SAMN05444391_1259 {ECO:0000313|EMBL:SHK50819.1};
OS   Thermocrinis minervae.
OC   Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Thermocrinis.
OX   NCBI_TaxID=381751 {ECO:0000313|EMBL:SHK50819.1, ECO:0000313|Proteomes:UP000189810};
RN   [1] {ECO:0000313|EMBL:SHK50819.1, ECO:0000313|Proteomes:UP000189810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19557 {ECO:0000313|EMBL:SHK50819.1,
RC   ECO:0000313|Proteomes:UP000189810};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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}.
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DR   EMBL; LT670846; SHK50819.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M6T1N8; -.
DR   STRING; 381751.SAMN05444391_1259; -.
DR   OrthoDB; 9764149at2; -.
DR   Proteomes; UP000189810; Chromosome i.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016070; P:RNA metabolic process; IEA:UniProtKB-UniRule.
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; 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; 2.
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:UP000189810};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT   DOMAIN          600..681
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
SQ   SEQUENCE   681 AA;  78820 MW;  1A2533871AFC423F CRC64;
     MEDLILELFK KAKRPLHFME IAQRLGLEKK QLKALKKALR NLKKKHLLQV VKGRYVLASE
     PIVKGTVIAF PAGFGFLHVG EGQKDIYIPP FEMQKLFSGD VIKAKVVEYK GKKEVRVLKI
     LKRAKKDIVC KIEGMYAIPV DENSFHKIVL VKKDRNKLKD GTYVVVEIIS YPSKGNPAIG
     RIKEVLGHPS ERSLIVELLI RKYELPTDYP PAVKKEAESL TILIKEDRRD LRDQVCFTID
     PERARDFDDA VAIEKIDQER FRLWVHIADV TYFVKLGSEI DKEAYRRGFT FYLPDRALHM
     LPERLSADLC SLKPNEDRLA FTCQMTFDLK GRLLDYDLYE SVIKSKARLT YNEALSLIVG
     DPALENKYPG FVEHLRLMED LYRILSKKRW ELGSIDFDLP EVELIVDEYG EPTAIIPYER
     HVAHRIIEQF MVSANETVAM HLENAGYPCL YRVHEKPDPE KVENLLEILN GLGYKTKGFS
     LEPRFFQKII EYFEGRPEEN LVRFLTLRSM KRAVYSPHNL GHFGLASEHY AHFTSPIRRY
     PDIVVHRLLK DSLMGREPTY DIEELEQMGQ YLSMREWLAE EVERTAIDLL KARYMKAHVG
     EVFEGIITGL IPAGFFVEIK EYLVEGLVKI SDLTDDEYIY DEPAHRFVGV RTGKVYRLGD
     VVRVKVVAVD EERGKLELVL V
//
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