ID A0A126PES6_9BACT Unreviewed; 826 AA.
AC A0A126PES6;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=AXW84_21030 {ECO:0000313|EMBL:AMJ67624.1};
OS Hymenobacter sp. PAMC 26628.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1484118 {ECO:0000313|EMBL:AMJ67624.1, ECO:0000313|Proteomes:UP000059956};
RN [1] {ECO:0000313|EMBL:AMJ67624.1, ECO:0000313|Proteomes:UP000059956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC26628 {ECO:0000313|EMBL:AMJ67624.1,
RC ECO:0000313|Proteomes:UP000059956};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-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; CP014304; AMJ67624.1; -; Genomic_DNA.
DR RefSeq; WP_068238000.1; NZ_CP014304.1.
DR AlphaFoldDB; A0A126PES6; -.
DR STRING; 1484118.AXW84_21030; -.
DR KEGG; hyz:AXW84_21030; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000059956; Chromosome.
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; cd00164; S1_like; 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; 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:UP000059956};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 697..778
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..811
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 826 AA; 92996 MW; F4621A598AC0248F CRC64;
MEPTNPPRPA RAKREQPAPA PITQELVLRA FTDNPDKVLA YRQLSRRLGV TTKQQREEIF
GYLKKLRQLG AITLLQNDEY RLADVSVAPA PELPAKGKKT VKAGAPASHS SGREPVAEFG
QDPIVHRRRE AGFDYVGDDS RPSRDANTII GTVDLATANF AFVVPEAEGS DDIRVFTDQL
KFALQGDVVR VRMRGSRDGR PVGDVVEVLK RQRPEVVGRL QVQGTLGFVK PDNRKMYFDV
FVPPHALGDA RNGDKVLVRI VEFPEDSHRQ PVGEVVRNFG QAGGNEAEIN AIMAEFGLPF
EFPAEVEEES EAISDVIPES EVVLRRDFRN ITTFTIDPAD AKDFDDALSI EKLENGNWEI
GVHIADVTHY VRPNTELERE GKHRATSVYL VDRVIPMLPE RLSNGLCSLR PNEDKLTFSA
VFELDENGKL YESWFGKTII HSDRRFAYED AQDRIETGEG DYAEEVNMLN GIAKKLHAQR
FKQGAISFET QEVKFRLAPD GKPLGVYVKE RKDAHKLIEE FMLLANRKVA EFVFNLKKTK
PRYTMVYRTH DAPEPERLQN FALFAQKFGY TLKLDDPKKV STELNTLSEE VMGKPEQNVL
QGLAIRTMSK AIYSTEPLGH FGLAFAHYSH FTSPIRRYPD MMAHRLLEHY LLGGKNVPVA
PVEDECKHSS AREKLAANAE RASIKFKQVE FMADEIGNVF KGVVSGLTER GMYIEIESNK
CEGMVRLSDI PGDTFELDKD NYRIVGRGSK RIIQFGDELD VVVKSANLLD RTIDFDLVDN
RPDDVKRREA EERKAQRNAP RGYREHSGGG HKGGSKGGPK GGNRRR
//
