ID   A0A1N6ILX0_9FLAO        Unreviewed;       716 AA.
AC   A0A1N6ILX0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=SAMN05444409_2791 {ECO:0000313|EMBL:SIO32999.1};
OS   Epilithonimonas zeae.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Epilithonimonas.
OX   NCBI_TaxID=1416779 {ECO:0000313|EMBL:SIO32999.1, ECO:0000313|Proteomes:UP000185207};
RN   [1] {ECO:0000313|Proteomes:UP000185207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27623 {ECO:0000313|Proteomes:UP000185207};
RA   Varghese N., Submissions S.;
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; FSRK01000002; SIO32999.1; -; Genomic_DNA.
DR   RefSeq; WP_074235947.1; NZ_FSRK01000002.1.
DR   AlphaFoldDB; A0A1N6ILX0; -.
DR   STRING; 1416779.SAMN05444409_2791; -.
DR   OrthoDB; 9764149at2; -.
DR   Proteomes; UP000185207; 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; 3.
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; 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   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT   DOMAIN          634..715
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
SQ   SEQUENCE   716 AA;  81467 MW;  D07D7D4780649B9A CRC64;
     MKNKKNISHK NEQKLLDLGR TILRFMSKKT SKIYNYKQIA EGIDYKNPRQ RELVIQALHR
     LLATQKIKET EKGKYIVNLN IEGTLTGVID FNQSGNAYVK VDGINDDIFV HQKNVKDALQ
     GDKVLIVTYN FKGKKLEGSV VEVLERAKEV FVGTFQKIAD KDFGFVVLDK KKLNTDIFIS
     KNHFNGAEDG DKVIVKMLEW KPGSKNPEGE ITTVLGAPGD HETEIHSILA EYGLPYSFPP
     EVEHDADQID RSINAEEVAK RWDMRDILTF TIDPKDAKDF DDALSIRKLE SGLWEIGVHI
     ADVSHYVKPG TILDDEAYAR ATSVYMVDRV VPMLPEVLSN DVCSLRPNED KFTFSAVFEL
     DEDAKIHKQW FGRTVIHSDR RFAYEEAQEK IETKEGDLVE EILQLDKLAK IMRAERIRNG
     AITFDRSEVR FNLDENSKPI GVYFKVSKDS NHLIEEFMLL ANKKVSEFIS LNKRNEPTGN
     TFIYRIHDDP DPAKLTALRD FVGTFGYKMD LANTQKVAES LNKLLSDVKG KGEENMIETL
     AMRSMSKAVY STDPIGHYGL GFEYYSHFTS PIRRYPDLIA HRLLQHYLDG GKSPNKEEVE
     EKAKHCSAME RLASEAERES IKFMQVKFME DHVGEVFSGV ISGVAEYGFW VEIPENGAEG
     MIKLRDLVDD SYSLDAKNYA IIGSRTGNTF QLGDEVKIKV VKANLIAKQL DFKIVE
//