ID A0A1S2VHX8_9BACT Unreviewed; 806 AA.
AC A0A1S2VHX8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, 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 ORFNames=BLX24_17250 {ECO:0000313|EMBL:OIN57845.1};
OS Arsenicibacter rosenii.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Arsenicibacter.
OX NCBI_TaxID=1750698 {ECO:0000313|EMBL:OIN57845.1, ECO:0000313|Proteomes:UP000181790};
RN [1] {ECO:0000313|EMBL:OIN57845.1, ECO:0000313|Proteomes:UP000181790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM-1 {ECO:0000313|EMBL:OIN57845.1,
RC ECO:0000313|Proteomes:UP000181790};
RA Huang K.;
RT "Arsenicibacter rosenii gen. nov., sp. nov., an efficient arsenic-
RT methylating bacterium isolated from an arsenic-contaminated paddy soil.";
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}.
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:OIN57845.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MORL01000009; OIN57845.1; -; Genomic_DNA.
DR RefSeq; WP_071504433.1; NZ_MORL01000009.1.
DR AlphaFoldDB; A0A1S2VHX8; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000181790; 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; 2.
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 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:UP000181790};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 677..758
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..781
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 806 AA; 91940 MW; 1EE64482E569DFB3 CRC64;
MRNKPKNNQY NRAQSGRSRE QSAGSPGKDR PRAGGPKSAV SFLDEMKDDL AAFFRINSEE
SFSQLQVLDH FGVGDRKMKL IMHGLIGELT DEGVLSRLDD GTYRANEAVA TLEGTVDHVN
AKFAYIVPTE NRVDRDSDIW VATEDLAGAI DGDKVRVMRY GDRPGGRSRK RTEGKVTEIV
ERGRSEIVGQ IEVWPTYGII SPDSKKLYED IYIPKDKLGA ANDGDKVIVR LTKYPDPLSK
KSRFEGEVIT VLGEAGQNDT EMHAILAEFG LPISFPPAVE EEAEQIPVKI SKRDLAKRRD
FRGITTFTID PVDAKDFDDA LSFQYLDNGN YEIGVHIADV THYVKPGSLL EEEAYKRATS
VYLVDRVVPM LPEKLSNGLC SLRPNEDKLT FSAVFEITPD ARVVSEWFGR TVIHSDRRFA
YEEAQEVIDS GNGDYVSELR ILNDLAKKLR AERFRHGAIN FETVELKFKL DEKGVPIAVY
PKIRKDAHKL IEEFMLLANK QVAEFVHRLS PKKKRGADED NANVMVYRVH ENPDDDRLRT
FADFARRFGY KLKVDDEHLS GSMNKFMDEL EGKPEQHMLQ QLAIRTMSKA RYSIEDLGHF
GLAFRRYSHF TSPIRRYPDM MAHRLLQHYL DHGKPVDAEE YEKKSRHSSE REKLATEAER
ASIKYKQVEF MSRIGTSKTF EGVISGVTEF GIFVEITENS CEGLIRMQDL NGDYYEYDRE
NYRIIGSRTK QIFTFGDKVV VRLKEANLSR RSMDFYLVSD STGKPYRTEN PKERSSAEGG
PRGGRSERPT AKVPSKLELK RRTKRR
//
