ID A0A1I3MMJ8_9RHOB Unreviewed; 753 AA.
AC A0A1I3MMJ8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=SAMN05216258_111163 {ECO:0000313|EMBL:SFI97955.1};
OS Albimonas pacifica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Albimonas.
OX NCBI_TaxID=1114924 {ECO:0000313|EMBL:SFI97955.1, ECO:0000313|Proteomes:UP000199377};
RN [1] {ECO:0000313|EMBL:SFI97955.1, ECO:0000313|Proteomes:UP000199377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.11030 {ECO:0000313|EMBL:SFI97955.1,
RC ECO:0000313|Proteomes:UP000199377};
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|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; FOQH01000011; SFI97955.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3MMJ8; -.
DR STRING; 1114924.SAMN05216258_111163; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000199377; 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; 1.
DR HAMAP; MF_01895; RNase_R; 1.
DR InterPro; IPR040476; CSD2.
DR InterPro; IPR012340; NA-bd_OB-fold.
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; 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; 2.
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:UP000199377};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 633..714
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 719..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..753
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 753 AA; 82735 MW; CD3AA4E1BA7FB8C9 CRC64;
MSRVPDKDTL ADFIRLNPDK AGKRDLARAF GLKGVERVQL KDLLRELTEE GVIEKRPGKS
FAAPGHLPPV AVLVVGEPDH AGDLFATPQD WDRDEPAPKV LIQPGSRGPA PGPGDRLLTR
VTPVHGEDHA YVGKVIKKIG AGPRKILGIF RQAPDGGGRL VPVSKGDQRE WVIAARDAGE
AENGELIEAE QIGQIRRNRE LALPRARVVE RLGSPGSARS FSLIAIHEQG IPDAFPERVT
EAAAAARPVT SLKGREDLRH LPLVTIDPAD ARDHDDAVCA QPDPDPENPG GHIVWVAIAD
VAHYVRPGSP LDREARLRGN STYFPDRVVP MLPEELSADL CSLVAHEDRP CIALRMVLSE
DGTKLAHDFH RALMRSPASL TYEQVQAAAD GRPGPEVEPH LKTIADLYAA YDSAAKARER
RQPLDLDLPE RRIKLAEDGT VASVGFRDRL EAHRLIEEFM ILSNVCAAET LEAKRRPHLL
RVHEEPGQDK LDTLRDVAEG CGLTLSKSQA IRPALFNRLL HQAAGSEFAE LINLTVLRSQ
TQAYYSPDNL GHFGLNLRAY AHFTSPIRRY ADLIVHRALI SAHDWGTDGQ TGEEIEELKD
TAEHISFTER RSMTAERDTN DRYLASYLSE RVGNEFAGRV AGVARFGLFV KLDETGADGL
VPIASLGREW FRHDPETHTL TGEDSGRVIG MGQRCLVRLS EAVPVTGGLL LELLEIEGDD
APRPGRARGR APRKKLSSAT KARAKHARHK RRG
//
