ID W7Z498_9BACL Unreviewed; 953 AA.
AC W7Z498;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=JCM16418_3299 {ECO:0000313|EMBL:GAF09179.1};
OS Paenibacillus pini JCM 16418.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1236976 {ECO:0000313|EMBL:GAF09179.1, ECO:0000313|Proteomes:UP000019364};
RN [1] {ECO:0000313|EMBL:GAF09179.1, ECO:0000313|Proteomes:UP000019364}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 16418 {ECO:0000313|EMBL:GAF09179.1,
RC ECO:0000313|Proteomes:UP000019364};
RA Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida Y., Hattori M.,
RA Ohkuma M.;
RT "Draft Genome Sequence of Paenibacillus pini JCM 16418T, Isolated from the
RT Rhizosphere of Pine Tree.";
RL Genome Announc. 2:e00210-14(2014).
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:GAF09179.1}.
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DR EMBL; BAVZ01000010; GAF09179.1; -; Genomic_DNA.
DR RefSeq; WP_036650382.1; NZ_BAZT01000010.1.
DR AlphaFoldDB; W7Z498; -.
DR STRING; 1236976.JCM16418_3299; -.
DR eggNOG; COG0557; Bacteria.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000019364; 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; 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:UP000019364};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 629..709
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 706..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..827
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..852
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..892
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 953 AA; 104282 MW; 299320BD44BCA869 CRC64;
MITEQTLLDW LRDPAYKPMT YQELEKHFEI RDALEFKDLI KLLNALEQDG KIIMTNGERY
GVPERLDLLR GRLQAHAKGF AFLIPDDKEH PDVYINANDL KSAMNGDTVL AKVTSQSPAG
GKLEGVVVSI VNRAVTQIVG VFQGHEAYGF VLPDDKRINR DIFVPKHAFG GAVDGDKVVA
KIVSYPEGKS AAEGAVIEIL GHKDDPGVDI LSIIRKHQLP EGFPEEVLAE AEQAPDSITE
EEIVSQGRRD LRGKNIVTID GEDAKDLDDA VNVELLPNGH FRLGVHIADV GYYVRENSEL
DKEAYSRGCS VYLVDRVIPM IPHRLSNGIC SLNPQVDRLT LSCEMEFDEQ MKVVSHDVFT
SVIKTKERMT YSNVRKILEE EDPELMERYS ELVGDFRLMK ELALKLRGRR MKRGAVDFDF
VESKVILDES GKPIDIVKRE RSIAEQIIEE FMLAANETVA EHFYWLKVPF LYRIHENPDP
EKLQNFMAFA ANFGHHVKGR GNDIHPRALQ NLLEDIQGTK EQTVISTMML RSMKQAKYAA
ETSGHFGLAA EYYSHFTSPI RRYPDLAIHR VIREVIENKN VLSDKRQEYL AARMPDIAQQ
SSERERVAVE AERDTDQLKK AEFMLDKVGE DFDGIISSVT SFGMFIELEN TVEGLIRLSS
LSDDYYHFDE SSMSLIGERT SNVYRIGDDI KIRVARVNMD DHTIDFELPD MKPRREGNRG
GGFGGRGGAG RKGGAPAREG GATRGGRGAA KGSGGERGSK AGAGKGAGAV PASRVTSAGG
RKRGGKGGAV HANAERSRTV AGDNSEATRV NNVGAAESAS PASSSEGRES KGGKRGIHAN
PKRSREGVGG KYGDPNRKGF AFGSGKGGYG AAPSSGGDTY ISPNSSAGRR KKTSENGVFI
GEGATRGRNA GGSGAGKPAG ENSGTPGEGG RKRKKKTKGE ANNSTAGFVR KNQ
//
