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Database: UniProt
Entry: A0A0Q9ZA66_9FLAO
LinkDB: A0A0Q9ZA66_9FLAO
Original site: A0A0Q9ZA66_9FLAO 
ID   A0A0Q9ZA66_9FLAO        Unreviewed;       728 AA.
AC   A0A0Q9ZA66;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 51.
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=APR42_14025 {ECO:0000313|EMBL:KRG29887.1};
OS   Salegentibacter mishustinae.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Salegentibacter.
OX   NCBI_TaxID=270918 {ECO:0000313|EMBL:KRG29887.1, ECO:0000313|Proteomes:UP000051643};
RN   [1] {ECO:0000313|EMBL:KRG29887.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 12263 {ECO:0000313|EMBL:KRG29887.1};
RA   Lin W., Zheng Q.;
RT   "Draft genome sequence of Salegentibacter mishustinae KCTC 12263.";
RL   Submitted (OCT-2015) 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:KRG29887.1}.
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DR   EMBL; LKTP01000003; KRG29887.1; -; Genomic_DNA.
DR   RefSeq; WP_057480913.1; NZ_QKZW01000008.1.
DR   AlphaFoldDB; A0A0Q9ZA66; -.
DR   STRING; 270918.APR42_14025; -.
DR   OrthoDB; 9764149at2; -.
DR   Proteomes; UP000051643; 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; 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; 2.
DR   SMART; SM00955; RNB; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 3.
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:UP000051643};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT   DOMAIN          642..723
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
SQ   SEQUENCE   728 AA;  83655 MW;  9498C34B86C884F0 CRC64;
     MSKKNKNKSQ HQSNLSKSIL DILRKDAGKT FNHKQIAAKL GVNDANSRNN IIKKLAQLAA
     KKQIEEEGRG KFKIVKSNDY YRAVIDMTTK GYAYAMVDEL EDDVFISPRD LNTAFNGDEV
     EIYIYNRKRN KKSEGEVTKI LNRKRTEFVG VLDMQKDFGF VVIGDPKMYT DIFVQKNKMG
     EAKDGDKVVV ELEEWPEKAD SPFGKIIQVL GTPGEHHTEI HSILAQYGLP HEFPQEIEDF
     ANQIDTSIQP EEIKKRRDMR DVLTFTIDPA DAKDFDDALS FQKLENGNVE VGIHIADVSH
     YLQPGTVLDD EAYERATSVY LVDRVVPMLP EVLSNNACSL RPNEEKYTFS AVFEIDKNTK
     VVNEWFGRTV TYSDARFAYE EAQQIIETEK GDIPEEISIQ DKAYTVKDEI VEAVLTMNKM
     AKKMRATRMR QGAISFDKVE VKFQLDEENE PVGVYFKTAK DANKLIEEFM LLANRKVAEF
     IGKRDEKKTF IYRCHDEPDE EKLVSLNSLV SRFGHGLNLK NRKTVSSSLN QLLQDVQGKK
     EQNLVDTLAI RTMSKAYYGT ENIGHYGLAF DYYSHFTSPI RRYPDVMVHR LLQRYLDGQP
     SAKEDEYEEK CHHSSEMENL SSNAERDSIK YMQVKFMQDH QDKEFIGVIS GVTDFGIFVE
     IVENKCEGMI RLRDIKGDHY DFDADNYAIV GRKTKMVYQL GDEVIVKVKN ADLVKRHLDF
     TLIGKKEE
//
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