ID A0A1E3LBE3_9BACL Unreviewed; 922 AA.
AC A0A1E3LBE3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-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=vacB {ECO:0000313|EMBL:ODP30250.1};
GN Synonyms=rnr {ECO:0000256|HAMAP-Rule:MF_01895};
GN ORFNames=PTI45_00320 {ECO:0000313|EMBL:ODP30250.1};
OS Paenibacillus nuruki.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1886670 {ECO:0000313|EMBL:ODP30250.1, ECO:0000313|Proteomes:UP000094578};
RN [1] {ECO:0000313|EMBL:ODP30250.1, ECO:0000313|Proteomes:UP000094578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TI45-13ar {ECO:0000313|EMBL:ODP30250.1,
RC ECO:0000313|Proteomes:UP000094578};
RA Kim S.-J.;
RT "Genome sequencing of Paenibacillus sp. TI45-13ar, isolated from Korean
RT traditional nuruk.";
RL Submitted (AUG-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}.
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:ODP30250.1}.
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DR EMBL; MDER01000022; ODP30250.1; -; Genomic_DNA.
DR RefSeq; WP_069325811.1; NZ_MDER01000022.1.
DR AlphaFoldDB; A0A1E3LBE3; -.
DR STRING; 1886670.PTI45_00320; -.
DR PATRIC; fig|1886670.3.peg.344; -.
DR Proteomes; UP000094578; 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:UP000094578};
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..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..747
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..825
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 922 AA; 103192 MW; B35FB70B65710C5A CRC64;
MITEQQVLDV IKSIDYKPMT YQELEQQLEI QAASDFKELV KILNELERTG IIVQNKSHHY
GLPEHMDLVR GRIQAHAKGF AFLIPEEKEH GDVYINANDM GTAMNGDIVF VKVTSRSTTG
GRMEGEVVRV ITRKNTRVVG VFQGLDTYGF IIPDDKRINR DIFVPKEAFG GAVEGEKVVA
EIVSYPEGRA AAEGRIVEVL GHKDDPGVDI LSVIRKHQLP ESFPDEIMDE AQAAPDSITD
AEIVEQGRRD LRDKNIVTID GEDAKDLDDA VNVERLDNGH YRLGVHIADV GYYVKEGSKL
DIEAYNRGCS VYLVDRVIPM LPHRLSNGIC SLHPQVDRLT LSCEMEFDEH MKVVKHEVFT
SVIKTKERMT YTNVRKILED EDPELLERYA PLVEDFKLMR ELAMQLREMR ARRGAVDFDF
DEAKIILDEK GRPIDIVKRE RSVAEQIIEE FMLAANETVA EHFSTLQVPF LYRIHENPDQ
EKLQNFLAFA SNFGHVIKGT GDHIHPRALQ QLLQDIKGEK EETVISTMML RSMKQAKYSA
DSSGHFGLAA DYYSHFTSPI RRYPDLVIHR VIREVIENGG KLKPKRQDYL NSRMADIAQQ
SSERERVAVD AERDTDQLKK AEYMLDKVGE EFEGMISSVT SFGMFIELDN TVEGLIRLGM
LTDDYYHFDD KQMILLGERT SKIYRIGDAI TVRVARVNME DHTIDFELKD MPKSNRPERT
DRGARPPRGD SDRKGGRGGD RGKNKAAGKA AKFGKAAKAA KASKAPTASV APTADSGSKK
PARRKRKPST VSGQTSAVSV PNTQQPRATE NTVSASTSNS EGAPKKAKGI STHAPKSSSK
DNSRNFNFGS GKGGYNSPVE SSKKRKGSPA PRRKKIEGPV FDPEAGNIQT SSAKADPSKT
GGEVKKSRPR KRKPKPTEQK PE
//
