ID A0A1H2XHP6_9BACI Unreviewed; 773 AA.
AC A0A1H2XHP6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=SAMN05421781_2747 {ECO:0000313|EMBL:SDW92306.1};
OS Marinococcus luteus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Marinococcus.
OX NCBI_TaxID=1122204 {ECO:0000313|EMBL:SDW92306.1, ECO:0000313|Proteomes:UP000199488};
RN [1] {ECO:0000313|EMBL:SDW92306.1, ECO:0000313|Proteomes:UP000199488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23126 {ECO:0000313|EMBL:SDW92306.1,
RC ECO:0000313|Proteomes:UP000199488};
RA de Groot N.N.;
RL Submitted (OCT-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; FNNC01000007; SDW92306.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2XHP6; -.
DR STRING; 1122204.SAMN05421781_2747; -.
DR Proteomes; UP000199488; 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:UP000199488};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 627..707
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 715..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..773
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 773 AA; 87269 MW; 7E52194F15404509 CRC64;
MNQEIKQTLL NYLKNDSAGP ATIEEIQETL QADSAEDIKR LMKTLNEMED SGDVVRTRSN
RYGISEKMNL MRGRVQSHAK GFAFIIPEEK ERDDIFVPAG EINGAMNKDT VLVRISDSSQ
GSKTEGTIIR IIERGIEKVV GTYQRYGNYG FVAADDKHIR DDIYIPQDAE NGAVDGHKVV
VELTKYPDAA SGAEGKVVNI IGHKNDPGVD ILSIIHKHGL PGDFPEEAVE QAQKTPDVID
ESEIKQRRDL RDETIVTIDG ADAKDLDDAV TVTKYNNGNY KLGVHIADVS YYVDEGTPID
VEAGERATSV YLVDRVIPMI PHRLSNGICS LNPQVDRLTL SCEMEVTPEG EVVNHEIFES
VIRTAARMTY NDVRLILEEN NQAKREEYSG LVPMFERMEE LAAILRGKRF GRGAIDFDFK
EAQVLVDETT APTDVVLRER SVAEKLIEEF MLAANETVAE HFHWMKVPFV YRIHEDPAED
KLQSFVEFVT NFGYSVKGTA NTVHPRALQE VLDAVKGEPE QAVISTVMLR SMQQAKYDPE
NAGHFGLAAD FYTHFTSPIR RYPDLVVHRL IRTYLVNKRM DDKTQQKWKN ELPEITQHSS
EMERRAIDAE REVDSMKKAQ YMKDKIGEEF TGFVSGAANF GLFVELENTI EGMVHISYLT
DDYYHYDPKQ YALIGERTAN MYRIGDQVEV RVLNVNLDEA AIDFEIVGMK RPAKARRKES
AKVIQGDKGK RPGRKEGQGE KKDGNKKDGG RKKGKSGNKK PFYSKVSKNN KKK
//
