ID A0A0Q4BX54_9SPHN Unreviewed; 763 AA.
AC A0A0Q4BX54;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=ASE49_10345 {ECO:0000313|EMBL:KQM17444.1};
OS Novosphingobium sp. Leaf2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1735670 {ECO:0000313|EMBL:KQM17444.1, ECO:0000313|Proteomes:UP000050893};
RN [1] {ECO:0000313|EMBL:KQM17444.1, ECO:0000313|Proteomes:UP000050893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf2 {ECO:0000313|EMBL:KQM17444.1,
RC ECO:0000313|Proteomes:UP000050893};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQM17444.1, ECO:0000313|Proteomes:UP000050893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf2 {ECO:0000313|EMBL:KQM17444.1,
RC ECO:0000313|Proteomes:UP000050893};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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}.
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:KQM17444.1}.
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DR EMBL; LMJY01000018; KQM17444.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q4BX54; -.
DR STRING; 1735670.ASE49_10345; -.
DR Proteomes; UP000050893; 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 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:UP000050893};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 642..723
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 763 AA; 84152 MW; C4A48467B47899B4 CRC64;
MALPRYQPHC GTMPANNRPA PGLPTRKQIL DFIQNSPVPA GKREISREFG LKGNEKIQLK
ALLKDMAEEG LIDGKRTAFH KLGGLPKVTV LRVIDIDEGE AIAVPDTWQP EDATPPPRIR
LIEKGRGSAL KKGDRVLSRT EESGTGWRAF PMKKLELRAE QVLGVVEIDG AGKPWLAPVD
KRIRNSSPIS DLGEAKAGEL VLGVPMGRSA RPSIKVTEVL GEPLAPKAFS LIAIHKHGIP
NHFDEETLAE AQEAAKLPLS HEQREDLRHL PIVAIDPSDA RDHDDAIWAQ PDGEGGFDAL
VAIADVSFYV RPGGKIDREA RKRGNSVYFP DRVVPMLPEV LSADVCSLRS GEDRAAMACH
LKIDAAGKLV NWRFTRALVR IHEVIAYEEA QARIDEDRAE AHIRNLWACW QLLAAARKDR
DPLELELPER RVKLDDKGRI TEIAVRERLD AHRVVEDFMI AANVAAAKAL EAKTAPVVYR
IHETPGREKL TALKDYLATF DKKLALGQVI TPGLFNRMLK GITDEAEKAL IMEAVLRSQT
QAYYGPANAG HFGLALASYA HFTSPIRRYA DLLVHRSLVD AYSLEQPRPG GDIPATSGLS
ERDREDLGRV SDAISKAERR AMEAERETID RYVAAWLSSR VGEVFDTRIT GVQKFGFFAT
IIGLGGDGLV PVSTLGDERF GYDEKAQVLV GEQSSTTYAV GQILRLRLAE ANPLTGALKY
ELEEGNGRIE PRGRPQPVKK VGGYVAGQRG RPRNIRHQGR GKR
//
