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Database: UniProt
Entry: K1LUW1_9LACT
LinkDB: K1LUW1_9LACT
Original site: K1LUW1_9LACT 
ID   K1LUW1_9LACT            Unreviewed;       770 AA.
AC   K1LUW1;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 54.
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=HMPREF9707_01531 {ECO:0000313|EMBL:EKB53778.1};
OS   Falseniella ignava CCUG 37419.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Falseniella.
OX   NCBI_TaxID=883112 {ECO:0000313|EMBL:EKB53778.1, ECO:0000313|Proteomes:UP000005147};
RN   [1] {ECO:0000313|EMBL:EKB53778.1, ECO:0000313|Proteomes:UP000005147}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 37419 {ECO:0000313|EMBL:EKB53778.1,
RC   ECO:0000313|Proteomes:UP000005147};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Facklamia ignava CCUG 37419.";
RL   Submitted (JUL-2012) 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:EKB53778.1}.
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DR   EMBL; AGZE01000037; EKB53778.1; -; Genomic_DNA.
DR   RefSeq; WP_006702164.1; NZ_JH932301.1.
DR   AlphaFoldDB; K1LUW1; -.
DR   STRING; 883112.HMPREF9707_01531; -.
DR   PATRIC; fig|883112.3.peg.1528; -.
DR   eggNOG; COG0557; Bacteria.
DR   HOGENOM; CLU_002333_4_1_9; -.
DR   Proteomes; UP000005147; Unassembled WGS sequence.
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; 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; 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:UP000005147};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT   DOMAIN          638..718
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          729..770
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        735..770
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   770 AA;  88458 MW;  9041A8B0A17F4D91 CRC64;
     MSLTKKEQRI LKFLQDHQEH SYSVQELAGI FNYQGNKTYK KLVKALAYLE RIGEIEFLAN
     GRVRAFGQLQ TTLTGIYRAN DKGYGFVDYE GDSDLFIPPG YALNAMDQDK VEVTVLKQVN
     PMTGKGSEAR VERIIERHYQ QLVGEFYAYS NEEQVETGYL GYVIPQGTSG QAYTVFILPE
     GIEPVDHSIV IVKIRDYPTN ENPSTLTGYV AKEIGHRDEP GVDILAILYQ LNIPHEFPQN
     VLEEAEKFGL EINPEDVNGR VDHRNQLVMT IDGADAKDLD DAIALDQLAN GNYRLYVHIA
     DVSHYVREGS PIDREAFERG TSVYLTDRVV PMLPQRLSNG ICSLHPGVDR LTLTCAMEID
     AQGSVVDYQI YPAVINSSYR MTYEAINAIY NGDKALIEEY DPIISTLYSM RDLHHILEAK
     RHRRGAINFD TTEAIIEVDD QGHPISIKAR ERGVGERLIE SFMLVANETV AQSYHEKELP
     MIYRVHEQPD ADRMLKFAEL LTGFGIILQG HVESIQPKQL QRVMQKLKDS PYEEVVSMML
     LRSMQQAHYS EESLGHYGLA AKYYTHFTSP IRRYPDLIVH RLVHQYLIKR PNQAEIDRLE
     QRLPEIAVQS SKRERRSVEA ERETDALKKA EYMQDKIGEE FEGMISSITS FGIFVQLPNT
     VEGLVHLNKL NDDYYQYYPE QWVLIGKERG KVYRIGQSVR IVVDQVNIEE REIDFNIIDA
     ENAETDDLSH LIKRESSSKK KRKSRNQSHP VRQRKNTKAK KHSPKRRRRK
//
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