ID A0A5J5G5C7_9BACL Unreviewed; 911 AA.
AC A0A5J5G5C7;
DT 11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 1.
DT 02-APR-2025, entry version 21.
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 ECO:0000313|EMBL:KAA9002379.1};
GN ORFNames=F4V43_13230 {ECO:0000313|EMBL:KAA9002379.1};
OS Paenibacillus spiritus.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Paenibacillus.
OX NCBI_TaxID=2496557 {ECO:0000313|EMBL:KAA9002379.1, ECO:0000313|Proteomes:UP000367750};
RN [1] {ECO:0000313|EMBL:KAA9002379.1, ECO:0000313|Proteomes:UP000367750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MER_111 {ECO:0000313|EMBL:KAA9002379.1,
RC ECO:0000313|Proteomes:UP000367750};
RA Seuylemezian A., Vaishampayan P.;
RT "Bacillus ochoae sp. nov., Paenibacillus whitsoniae sp. nov., Paenibacillus
RT spiritus sp. nov. Isolated from the Mars Exploration Rover during
RT spacecraft assembly.";
RL Submitted (SEP-2019) 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:KAA9002379.1}.
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DR EMBL; VYKK01000017; KAA9002379.1; -; Genomic_DNA.
DR RefSeq; WP_150458724.1; NZ_VYKK01000017.1.
DR AlphaFoldDB; A0A5J5G5C7; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000367750; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:TreeGrafter.
DR CDD; cd04471; S1_RNase_R; 1.
DR FunFam; 2.40.50.140:FF:000273; Ribonuclease 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; IPR050180; RNR_Ribonuclease.
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:UP000367750};
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 711..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..721
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..766
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..782
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..830
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..851
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 911 AA; 100476 MW; A3F31E66AFFE300E CRC64;
MITQDHLLAF MRETAYKPMT YDEFVLHLNL VGSEELREFE ELLRVLEQEG RVVLTRTGRY
GVPERMDLLR GRLQAHAKGF AFLIPDDREH PDVYIHANDI KGAMNGDIVL VRVTSRSPSG
GRMEGEVVRI VRRGVQQTVG TFQSFETYGF VLPDDKRINR DIFVPKESFH GAVDGEKVVV
RIVHYPEGRA AAEGEIIEIL GHKDDPGVDI LSVIRKHQLP EGFSDEVMAE ANAAPDSITE
EEIIQQGRRD LRGLNIVTID GEDAKDLDDA VNVQLLDNGH YKLGVHIADV SYYVRENSEL
DKEAYARGCS VYLVDRVIPM LPHRLSNGIC SLNPQVDRLT MSCEMEFNEQ MKVVKHDIFT
SVIRTKERMT YTNVRKILEG EDPELLERYA PLVNDFKLMK ELAMKLRDAR MRRGAVDFDF
QESKIIVDEN GKAVDIVKRE RSVAEQIIEE FMLAANETVA EHFHWLKVPF LYRIHEDPDP
EKLQNFMAFA ANFGYQVKGR GNSVHPRALQ KLLEDIQGTK EQTVISTMML RSMKQAKYDA
ESTGHFGLAA EFYSHFTSPI RRYPDLVIHR VMREVLEGGG ALSEKRQEYL ASRMPDIAQQ
SSERERVAVE AERDTEQLKK AEYMLDKVGE EFDAMVSSVT NFGMFVELDN TVEGLIRLSH
LTDDYYHFDE THMALIGERT SKVFRIGDEV KIRVAKVNMD DHTIDFELVD MKPRQAGERR
GGGFGGRPGK KGGKGGRAGS AGAAQGGGPG KAGRGKGKPG SAGRPGGSEA AGARGGQGGG
PRGEAAGQGA ARGKRGKGRG PGEDARRAHT ALTERSGGRA PGGAEAGGPG IRFSFGSGKG
GYGAPSEGAG GSAADAISGD TKFRSREDLG GDYGGGRSGK GRRKKNTPSG VFISPDVTPG
GGEGRKRKRK K
//
